|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
119-829 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 1302.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPasvstvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP--------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQERELFQETLE 358
Cdd:cd14930 153 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQERELFQETLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 359 SLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKA 438
Cdd:cd14930 233 SLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 439 QTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 518
Cdd:cd14930 313 QTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 519 FVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRD 598
Cdd:cd14930 393 FVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 599 QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsflgsfppsppgsaercssais 678
Cdd:cd14930 473 QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKD------------------------------ 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 679 ppgVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLR 758
Cdd:cd14930 523 ---VEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLR 599
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224831241 759 CNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14930 600 CNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
119-829 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 1278.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPasvstvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP--------GELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQ-ERELFQETL 357
Cdd:cd14920 153 DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQqDKDNFQETM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd14920 233 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 517
Cdd:cd14920 313 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 518 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLR 597
Cdd:cd14920 393 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 598 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsflgsfppsppgsaercssai 677
Cdd:cd14920 473 DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKD----------------------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 678 sppgVEGIVGLEQVSSLGDGP--PGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLD 755
Cdd:cd14920 524 ----VDRIVGLDQVTGMTETAfgSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLD 599
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224831241 756 QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14920 600 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
119-829 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 1266.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpasvstVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESG-------KKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP-CSHYRFLTNGPSSSPGQ-ERELFQET 356
Cdd:cd01377 154 GSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGdPSYYFFLSQGELTIDGVdDAEEFKLT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 357 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd01377 234 DEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSpRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 516
Cdd:cd01377 314 KGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTK-SKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 517 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPK-FQRPRH 595
Cdd:cd01377 393 HMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 596 LRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEhggfqqfsflgsFPPSPPGSAERCSS 675
Cdd:cd01377 471 KKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDY------------EESGGGGGKKKKKG 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 676 AisppgvegivgleqvsslgdgppggrprrgMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLD 755
Cdd:cd01377 539 G------------------------------SFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLH 588
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224831241 756 QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd01377 589 QLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
906-1986 |
0e+00 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 1218.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 906 TRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSEL 985
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 986 EARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDR 1065
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1066 LAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGR 1145
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1146 KEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQE 1225
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1226 LRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTAR 1305
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1306 QEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEE 1385
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1386 TRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQR 1465
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1466 LAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALS 1545
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1546 LTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEV 1625
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1626 TVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQL 1705
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1706 RKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAI 1785
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1786 LEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAG 1865
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1866 ARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLE 1945
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 224831241 1946 EAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRL 1986
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
119-829 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 1155.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPAsvstVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIA----LSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETL 357
Cdd:cd14932 157 DVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGqQDKELFAETM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd14932 237 EAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 517
Cdd:cd14932 317 AQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 518 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLR 597
Cdd:cd14932 397 MFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 598 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsflgsfppsppgsaercssai 677
Cdd:cd14932 477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKD----------------------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 678 sppgVEGIVGLEQVSSLGDGPP-GGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQ 756
Cdd:cd14932 528 ----VDRIVGLDKVAGMGESLHgAFKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQ 603
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224831241 757 LRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14932 604 LRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
119-829 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 1121.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 199 ESGAGKTENTKKVIQYLAHVASS-PKGRKEPGVPASVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkPKGSGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQET 356
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGvDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 357 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 516
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 517 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPrHL 596
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKT-DF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 597 RDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsflgsfppsppgsAErcssa 676
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKD---------------------AE----- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 677 isppgvegIVGLEQvSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQ 756
Cdd:cd14911 531 --------IVGMAQ-QALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQ 601
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224831241 757 LRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14911 602 LRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
119-829 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 1095.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpasvstvsygELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQG-----------ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETL 357
Cdd:cd14919 150 DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQdKDMFQETM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd14919 230 EAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 517
Cdd:cd14919 310 AQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 518 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLR 597
Cdd:cd14919 390 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 598 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsflgsfppsppgsaercssai 677
Cdd:cd14919 470 DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD----------------------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 678 sppgVEGIVGLEQVSSLGDGPP--GGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLD 755
Cdd:cd14919 521 ----VDRIIGLDQVAGMSETALpgAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLD 596
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224831241 756 QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14919 597 QLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
119-829 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 1089.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEpgvpASVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKD----QNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETL 357
Cdd:cd15896 157 DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQdKDLFTETM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd15896 237 EAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 517
Cdd:cd15896 317 AQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 518 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLR 597
Cdd:cd15896 397 MFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 598 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsflgsfppsppgsaercssai 677
Cdd:cd15896 477 DEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKD----------------------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 678 sppgVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQL 757
Cdd:cd15896 528 ----VDRIVGLDKVSGMSEMPGAFKTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQL 603
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224831241 758 RCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd15896 604 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
119-829 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 1081.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpasvstvsYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSI--------TGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER-ELFQETL 357
Cdd:cd14921 153 DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDdEMFQETL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd14921 233 EAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 517
Cdd:cd14921 313 AQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 518 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLR 597
Cdd:cd14921 393 MFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 598 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsflgsfppsppgsaercssai 677
Cdd:cd14921 473 DKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKD----------------------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 678 sppgVEGIVGLEQVSSLGDGP--PGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLD 755
Cdd:cd14921 524 ----VDRIVGLDQMAKMTESSlpSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLE 599
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224831241 756 QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14921 600 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
108-829 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1062.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 108 EDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQ 187
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 188 DREDQSILCTGESGAGKTENTKKVIQYLAHVASSPkgrkepgvpasvSTVSYGELERQLLQANPILEAFGNAKTVKNDNS 267
Cdd:pfam00063 82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSG------------SAGNVGRLEEQILQSNPILEAFGNAKTVRNNNS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 268 SRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-P 346
Cdd:pfam00063 150 SRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTiD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 347 G-QERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLT 425
Cdd:pfam00063 230 GiDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 426 PRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINY 505
Cdd:pfam00063 310 RRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 506 TNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQG 585
Cdd:pfam00063 390 VNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 586 GHPKFQRPRhLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEhggfqqfsflgsfPPS 665
Cdd:pfam00063 467 KHPHFQKPR-LQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDY-------------ETA 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 666 PPGSAERCSSAISPPGvegivgleqvsslgdgppggrpRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRA 745
Cdd:pfam00063 533 ESAAANESGKSTPKRT----------------------KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRA 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 746 GKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSK 825
Cdd:pfam00063 591 GVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTK 670
|
....
gi 224831241 826 IFFR 829
Cdd:pfam00063 671 IFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
100-841 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 988.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 100 NPPKFSKAEDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTE 179
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 180 GAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRkepgvpasvstvsyGELERQLLQANPILEAFGNA 259
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV--------------GSVEDQILESNPILEAFGNA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 260 KTVKNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLT 339
Cdd:smart00242 147 KTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 340 NGPSSS-PGQE-RELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNT-AAQKLCRLLGLGV 416
Cdd:smart00242 227 QGGCLTvDGIDdAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 417 TDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLN 496
Cdd:smart00242 307 EELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 497 SFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSF 576
Cdd:smart00242 386 SFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTF 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 577 VEKVAQEQGGHPKFQRPRhLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEhggfqqf 656
Cdd:smart00242 463 LEKLNQHHKKHPHFSKPK-KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 657 sflgsfppsppgsaercssaisppgvegivgLEQVSSLGdgppggrprrgMFRTVGQLYKESLSRLMATLSNTNPSFVRC 736
Cdd:smart00242 535 -------------------------------VSNAGSKK-----------RFQTVGSQFKEQLNELMDTLNSTNPHFIRC 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 737 IVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDP 816
Cdd:smart00242 573 IKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDE 652
|
730 740
....*....|....*....|....*
gi 224831241 817 NLYRVGQSKIFFRAGVLAQLEEERD 841
Cdd:smart00242 653 DEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
98-1216 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 908.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 98 RMNPPKFSKAEDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAV 177
Cdd:COG5022 59 RIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 178 TEGAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSpkgrkepgvpasvSTVSYGELERQLLQANPILEAFG 257
Cdd:COG5022 139 AEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSS-------------STVEISSIEKQILATNPILEAFG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 258 NAKTVKNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRF 337
Cdd:COG5022 206 NAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIY 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 338 LTNGPSSSPGQ--ERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNtDQATMPDNTAAQKLCRLLGLG 415
Cdd:COG5022 286 LSQGGCDKIDGidDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGID 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 416 VTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGaSFLGILDIAGFEIFQL 495
Cdd:COG5022 365 PSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEK 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 496 NSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpANPPGLLALLDEECWFPKATDKS 575
Cdd:COG5022 444 NSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDES 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 576 FVEKVAQ--EQGGHPKFQRPRhLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEhggf 653
Cdd:COG5022 522 FTSKLAQrlNKNSNPKFKKSR-FRDNK-FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDE---- 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 654 qqfsflgsfppsppgsaercssaisppgvegivglEQVSSLGdgppggrprrgMFRTVGQLYKESLSRLMATLSNTNPSF 733
Cdd:COG5022 596 -----------------------------------ENIESKG-----------RFPTLGSRFKESLNSLMSTLNSTQPHY 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 734 VRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA----IPKGFMDGKQACEKMI 809
Cdd:COG5022 630 IRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDTKNAVKSIL 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 810 QALELDPNLYRVGQSKIFFRAGVLAQLEEERDLKVTDIIVSFQAAARGYLARRAFQKRQQQQSALRVMQRNCAAYLKLRH 889
Cdd:COG5022 710 EELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDY 789
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 890 WQWWRLFTKVKPLLQVTRQDEVLQARAQELQKVQ--ELQQQSAREvgelqgrvaQLEEERARLAEQLRAEAELCaeaeet 967
Cdd:COG5022 790 ELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQktIKREKKLRE---------TEEVEFSLKAEVLIQKFGRS------ 854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 968 rgrLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQELeahleaeegARQKLQLEKVTTEAKmKKFEEDLLL 1047
Cdd:COG5022 855 ---LKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSL---------KLVNLELESEIIELK-KSLSSDLIE 921
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1048 -LEDQNSKLSKERKLLEDRlaEFSSQAAEEEEKVKSLNKLRL---KYEATIADMEDRLRKEEKGRQELEKLKRRLDGESS 1123
Cdd:COG5022 922 nLEFKTELIARLKKLLNNI--DLEEGPSIEYVKLPELNKLHEvesKLKETSEEYEDLLKKSTILVREGNKANSELKNFKK 999
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1124 ELQEQMVEQQ--QRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSlreaqaALAEAQEDLESERV-ARTKAEKQRR 1200
Cdd:COG5022 1000 ELAELSKQYGalQESTKQLKELPVEVAELQSASKIISSESTELSILKPL------QKLKGLLLLENNQLqARYKALKLRR 1073
|
1130
....*....|....*.
gi 224831241 1201 DLGEELEALRGELEDT 1216
Cdd:COG5022 1074 ENSLLDDKQLYQLEST 1089
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
119-829 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 828.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRH-EVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 198 GESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpasvstvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSA---------SSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-----PGQE-RE 351
Cdd:cd00124 152 FDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLNDYLNSSgcdriDGVDdAE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 352 LFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNI--ALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 429
Cdd:cd00124 232 EFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIefEEDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 430 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQ-GASFLGILDIAGFEIFQLNSFEQLCINYTNE 508
Cdd:cd00124 312 VGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 509 KLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHP 588
Cdd:cd00124 392 KLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 589 KFQRPRHLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTdrltaeiwkdehggfqQFsflgsfppsppg 668
Cdd:cd00124 469 RFFSKKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS----------------QF------------ 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 669 saercssaisppgvegivgleqvsslgdgppggrprrgmfrtvgqlyKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKL 748
Cdd:cd00124 520 -----------------------------------------------RSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLF 552
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 749 EPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFF 828
Cdd:cd00124 553 DPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFL 632
|
.
gi 224831241 829 R 829
Cdd:cd00124 633 R 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
119-829 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 766.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpASVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKA--QFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQET 356
Cdd:cd14927 159 GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYdYHFCSQGVTTVDNmDDGEELMAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 357 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14927 239 DHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRS-PRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 515
Cdd:cd14927 319 KGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKlPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 516 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPR 594
Cdd:cd14927 397 HHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPR 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 595 ---HLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsFLGSFPPSPP--GS 669
Cdd:cd14927 474 pdkKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYEN---------YVGSDSTEDPksGV 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 670 AERCSSAISppgvegivgleqvsslgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLE 749
Cdd:cd14927 545 KEKRKKAAS-----------------------------FQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMD 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 750 PRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK-GFMDGKQACEKMIQALELDPNLYRVGQSKIFF 828
Cdd:cd14927 596 PFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFF 675
|
.
gi 224831241 829 R 829
Cdd:cd14927 676 K 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
120-829 |
0e+00 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 740.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 200 SGAGKTENTKKVIQYLAHVASS--PKGRKEPGVPasvstvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATgdLAKKKDSKMK--------GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQE 355
Cdd:cd14913 154 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYdYPFISQGEILVASiDDAEELLA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 356 TLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDY 434
Cdd:cd14913 234 TDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 435 VQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 513
Cdd:cd14913 313 VTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDtKLPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 514 FNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQR 592
Cdd:cd14913 391 FNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFQK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 593 PRHLRDQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIwkdehggFQQFSFLGSFPPSPPGSA 670
Cdd:cd14913 468 PKVVKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHL-------YATFATADADSGKKKVAK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 671 ERCSSaisppgvegivgleqvsslgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEP 750
Cdd:cd14913 541 KKGSS--------------------------------FQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEH 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 751 RLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14913 589 SLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
119-829 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 728.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEpgvpasvsTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEA--------AKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLL-EPCSHYRFLTNGPSSSPG-QERELFQET 356
Cdd:cd14909 153 GPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNvDDGEEFSLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 357 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14909 233 DQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 516
Cdd:cd14909 313 QGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKR-QHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 517 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRH 595
Cdd:cd14909 392 HMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 596 LR---DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEHGgfqqfsflgsfPPSPPGSAEr 672
Cdd:cd14909 469 PKpgqQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAG-----------QSGGGEQAK- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 673 cssaisppGVEGIVGleqvsslgdgppggrprrGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRL 752
Cdd:cd14909 537 --------GGRGKKG------------------GGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHL 590
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224831241 753 VLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIpKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14909 591 VMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
119-829 |
0e+00 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 701.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 199 ESGAGKTENTKKVIQYLAHVASSPKgrkepgvpasVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGK----------QSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP-CSHYRFLTNGPSSSPGQER-ELFQET 356
Cdd:cd14934 151 GTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPnPKEYHWVSQGVTVVDNMDDgEELQIT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 357 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14934 231 DVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 516
Cdd:cd14934 311 KGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 517 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRH 595
Cdd:cd14934 390 HMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 596 LRD---QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEHGgfqqfsflgsfpPSPPGSAER 672
Cdd:cd14934 467 GKGkgpEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEA------------PAGSKKQKR 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 673 CSSaisppgvegivgleqvsslgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRL 752
Cdd:cd14934 535 GSS--------------------------------FMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHL 582
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224831241 753 VLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14934 583 IMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
120-829 |
0e+00 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 692.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 120 SVLHNLRERYYSG-LIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 199 ESGAGKTENTKKVIQYLAHVASSpkgrkepgvpASVSTvsygELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGS----------SSGET----QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-PG-QERELFQET 356
Cdd:cd01380 148 DKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPViDGvDDAAEFEET 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 357 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd01380 228 RKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGA-SFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 515
Cdd:cd01380 308 KPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 516 HTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPK--FQRP 593
Cdd:cd01380 388 QHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 594 RhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdehggfqqfsflgsfppsppgsaerc 673
Cdd:cd01380 464 R--FSNTAFIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNRK-------------------------------- 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 674 ssaisppgvegivgleqvsslgdgppggrprrgmfRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLV 753
Cdd:cd01380 510 -----------------------------------KTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRV 554
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224831241 754 LDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd01380 555 VQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
120-829 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 684.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 200 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASvstvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGK------GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETL 357
Cdd:cd14917 156 ATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYdYAFISQGETTVASiDDAEELMATD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14917 236 NAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 515
Cdd:cd14917 315 KGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFN 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 516 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPR 594
Cdd:cd14917 393 HHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 595 HLRD--QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsFLGSFPP--SPPGSA 670
Cdd:cd14917 470 NIKGkpEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN---------YAGADAPieKGKGKA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 671 ERCSSaisppgvegivgleqvsslgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEP 750
Cdd:cd14917 541 KKGSS--------------------------------FQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDN 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 751 RLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14917 589 PLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
119-829 |
0e+00 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 678.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpasvstvsygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKLGA-----------LEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETL 357
Cdd:cd14929 150 GARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESlDDAEELLATE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd14929 230 QAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 516
Cdd:cd14929 310 SQNIEQVTYAVGALSKSIYERMFKWLVARINRVLDaKLSRQ--FFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 517 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRH 595
Cdd:cd14929 388 HMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 596 LRD--QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIwkdehggFQQFSFLGSfpPSPPGSAERC 673
Cdd:cd14929 465 DKKkfEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASL-------FENYISTDS--AIQFGEKKRK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 674 SSAisppgvegivgleqvsslgdgppggrprrgMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLV 753
Cdd:cd14929 536 KGA------------------------------SFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLV 585
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224831241 754 LDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14929 586 LQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
121-829 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 669.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 121 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGES 200
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 201 GAGKTENTKKVIQYLAHVASSPKGRKEPgvpasvSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 280
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEE------SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 281 AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLE 358
Cdd:cd14918 157 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYdYAFVSQGEITVPSiDDQEELMATDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 359 SLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd14918 237 AIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 516
Cdd:cd14918 316 GQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 517 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQRPRH 595
Cdd:cd14918 394 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFQKPKV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 596 LRDQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdehggfqqfsflgsfppSPPGSAERC 673
Cdd:cd14918 471 VKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLF------------------STYASAEAD 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 674 SSAISPPGVEGivgleqvsslgdgppggrprrGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLV 753
Cdd:cd14918 533 SGAKKGAKKKG---------------------SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELV 591
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224831241 754 LDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14918 592 LHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
120-829 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 667.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 200 SGAGKTENTKKVIQYLAHVAS-SPKGRKEpgvpasVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKE------NPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQET 356
Cdd:cd14916 156 GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYdYAFVSQGEVSVASiDDSEELLAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 357 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNTA-AQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 435
Cdd:cd14916 236 DSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 436 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 514
Cdd:cd14916 315 TKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 515 NHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRP 593
Cdd:cd14916 393 NHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 594 RHL--RDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEHGgfqqfsflgsfppsppgsae 671
Cdd:cd14916 470 RNVkgKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYAS-------------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 672 rcssAISPPGVEGIVGLEQVSSlgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPR 751
Cdd:cd14916 530 ----ADTGDSGKGKGGKKKGSS--------------FQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNP 591
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224831241 752 LVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14916 592 LVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
120-829 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 666.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 200 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVStvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQ----GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGP-SSSPGQERELFQETL 357
Cdd:cd14912 158 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYdYPFVSQGEiSVASIDDQEELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14912 238 SAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 515
Cdd:cd14912 317 KGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 516 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQRPR 594
Cdd:cd14912 395 HHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyEQHLGKSANFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 595 HLRDQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdehgGFQQFSFLGSFPPSPPGSAER 672
Cdd:cd14912 472 VVKGKAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFS----GAQTAEGASAGGGAKKGGKKK 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 673 CSSaisppgvegivgleqvsslgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRL 752
Cdd:cd14912 548 GSS--------------------------------FQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHEL 595
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224831241 753 VLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14912 596 VLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
120-829 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 661.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 200 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVStvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQ----GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETL 357
Cdd:cd14910 158 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYdYAFVSQGEITVPSiDDQEELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14910 238 SAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 515
Cdd:cd14910 317 KGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 516 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPR 594
Cdd:cd14910 395 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 595 HLRD--QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdehggfqqfsflgsfppsppgSAER 672
Cdd:cd14910 472 PAKGkvEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLF----------------------SGAA 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 673 CSSAISPPGVEGivGLEQVSSlgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRL 752
Cdd:cd14910 530 AAEAEEGGGKKG--GKKKGSS--------------FQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHEL 593
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224831241 753 VLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14910 594 VLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
120-829 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 657.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 200 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVStvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKMQ----GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETL 357
Cdd:cd14915 158 ATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYdFAFVSQGEITVPSiDDQEELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14915 238 SAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 515
Cdd:cd14915 317 KGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 516 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPR 594
Cdd:cd14915 395 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 595 HLRDQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQStdrltaeiwkdehgGFQQFSFLgsfppsppGSAER 672
Cdd:cd14915 472 PAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKS--------------GMKTLAFL--------FSGGQ 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 673 CSSAISPPGVEGivGLEQVSSlgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRL 752
Cdd:cd14915 530 TAEAEGGGGKKG--GKKKGSS--------------FQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHEL 593
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224831241 753 VLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14915 594 VLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
120-829 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 654.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 200 SGAGKTENTKKVIQYLAHVASSPKGRKEPGvPASVStvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQQ-PGKMQ----GTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLkADLLLEPCSHYRFltngPSSSPGQ-------EREL 352
Cdd:cd14923 157 ATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDF----PFVSQGEvtvasidDSEE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 353 FQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVG 431
Cdd:cd14923 232 LLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 432 RDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKL 510
Cdd:cd14923 311 NEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 511 QQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPK 589
Cdd:cd14923 389 QQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 590 FQRPRHLRDQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTaeiwkdehggfqqfsflgSFPPSPP 667
Cdd:cd14923 466 FQKPKPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLL------------------SFLFSNY 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 668 GSAERCSSAISPPGvegivGLEQVSSlgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGK 747
Cdd:cd14923 528 AGAEAGDSGGSKKG-----GKKKGSS--------------FQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGV 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 748 LEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKI 826
Cdd:cd14923 589 MDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKV 668
|
...
gi 224831241 827 FFR 829
Cdd:cd14923 669 FFK 671
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
120-829 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 631.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 200 SGAGKTENTKKVIQYLAHVasSPKGrkepgvPASVSTVSygeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAV--SGGS------ESEVERVK-----DMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLE-PCSHYRFLTNGPSSSPG-QERELFQETL 357
Cdd:cd01378 149 FKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQrPEQYYYYSKSGCFDVDGiDDAADFKEVL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKrERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVG---RDY 434
Cdd:cd01378 229 NAMKVIGFTEEEQDSIFRILAAILHLGNIQFA-EDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 435 VQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 514
Cdd:cd01378 308 YEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 515 nhTMFVL--EQEEYQREGIPWTFLDFgLDLQPCIDLIErpANPPGLLALLDEECWFP-KATDKSFVEKVAQEQGGHPKFQ 591
Cdd:cd01378 388 --IELTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 592 RPR-HLRD-QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsflgsfpPSPPGS 669
Cdd:cd01378 463 CPSgHFELrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPE---------------GVDLDS 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 670 AERcssaisPPgvegivgleqvsslgdgppggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLE 749
Cdd:cd01378 528 KKR------PP-----------------------------TAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFD 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 750 PRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd01378 573 EELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
120-829 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 621.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRgkKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 200 SGAGKTENTKKVIQYLAHVASSPKGrkepgvpasvstvsygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG-----------------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPG-QERELFQETL 357
Cdd:cd01383 143 AAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNClTIDGvDDAKKFHELK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd01383 223 EALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 517
Cdd:cd01383 303 KLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRH 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 518 MFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRprhlR 597
Cdd:cd01383 383 LFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKG----E 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 598 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEHGGFQQfsflgsfpPSPPGSAERCSSai 677
Cdd:cd01383 456 RGGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASKMLDASRK--------ALPLTKASGSDS-- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 678 sppgvegivgleqvsslgdgppggrprrgMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQL 757
Cdd:cd01383 526 -----------------------------QKQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQL 576
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224831241 758 RCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIpKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd01383 577 RCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
120-829 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 616.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 200 SGAGKTENTKKVIQYLAHVASSPKgrkepgvpasvstvsygELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS-----------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGE--QLKADLLLEPCSHYRFLT-NGPSSSPG-QERELFQE 355
Cdd:cd14883 145 ASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNiNDKKDFDH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 356 TLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKR-ERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDY 434
Cdd:cd14883 225 LRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 435 VQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRsPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 514
Cdd:cd14883 305 TEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNP-GQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 515 NHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPR 594
Cdd:cd14883 384 NHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 595 HLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdehggfqqfsflgsfppsPPGSAERCS 674
Cdd:cd14883 461 RRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFT------------------YPDLLALTG 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 675 SAISPPGVEGIVGLEQVSSlgdgppggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVL 754
Cdd:cd14883 523 LSISLGGDTTSRGTSKGKP----------------TVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVL 586
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224831241 755 DQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14883 587 AQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
119-829 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 590.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 199 ESGAGKTENTKKVIQYLAHVAsspkGRKepgvpasvSTVsygelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAIS----GQH--------SWI-----EQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPGQ-ERELFQET 356
Cdd:cd01381 144 NKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNClTCEGRdDAAEFADI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 357 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALK-RER-NTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDY 434
Cdd:cd01381 224 RSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEaTVVdNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGET 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 435 VQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS--FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 512
Cdd:cd01381 304 VVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 513 LFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLI-ERPANppgLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQ 591
Cdd:cd01381 384 FFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 592 RPRHlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEHggfqqfsflgsfppsPPGSAE 671
Cdd:cd01381 460 KPKS-DLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDI---------------SMGSET 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 672 RCSSAisppgvegivgleqvsslgdgppggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPR 751
Cdd:cd01381 524 RKKSP---------------------------------TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRE 570
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224831241 752 LVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd01381 571 LCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
119-829 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 588.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 198 GESGAGKTENTKKVIQYLAHVAsspkGRKEPGVpASVstvsygelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG----GRAVTEG-RSV--------EQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG--QERELFQE 355
Cdd:cd01384 148 FDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDgvDDAEEYRA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 356 TLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKL---CRLLGLGVTDFSRALLTpRIKVGR 432
Cdd:cd01384 228 TRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDALCK-RVIVTP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 433 D-YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQ 511
Cdd:cd01384 307 DgIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 512 QLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQ 591
Cdd:cd01384 386 QHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFS 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 592 RPRhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIwkdehggfqqfsflgsFPPSPPGSAE 671
Cdd:cd01384 463 KPK--LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGL----------------FPPLPREGTS 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 672 RCSSaisppgvegivgleqvsslgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPR 751
Cdd:cd01384 525 SSSK--------------------------------FSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENA 572
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224831241 752 LVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAiPKGFMDGKQACEKMIQALELDPnlYRVGQSKIFFR 829
Cdd:cd01384 573 NVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
119-829 |
2.29e-176 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 551.85 E-value: 2.29e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 198 GESGAGKTENTKKVIQYLAHVASSpkgrkepgvpasvstvSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGS----------------GAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPcshyrfLTNGPSSspgqerelFQETL 357
Cdd:cd01382 145 FNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDP------LLDDVGD--------FIRMD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQA-TMPDNTAAQKL---CRLLGLGVTDF-----SRALLTPRI 428
Cdd:cd01382 211 KAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGgCNVKPKSEQSLeyaAELLGLDQDELrvsltTRVMQTTRG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 429 KVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSprqgASFLGILDIAGFEIFQLNSFEQLCINYT 506
Cdd:cd01382 291 GAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIpfETS----SYFIGVLDIAGFEYFEVNSFEQFCINYC 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 507 NEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQEQGG 586
Cdd:cd01382 367 NEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKN 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 587 HPKFQRPR------H--LRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIwkdehggfqqfsf 658
Cdd:cd01382 444 HFRLSIPRksklkiHrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSL------------- 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 659 lgsFPPSPPGSAERCSSAisppgvegivgleqvsslgdgppggrpRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIV 738
Cdd:cd01382 511 ---FESSTNNNKDSKQKA---------------------------GKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIK 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 739 PNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKgfMDGKQACEKMIQALELDPNL 818
Cdd:cd01382 561 PNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNEND 638
|
730
....*....|.
gi 224831241 819 YRVGQSKIFFR 829
Cdd:cd01382 639 FKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
119-829 |
2.83e-174 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 546.68 E-value: 2.83e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQ----DREDQS 193
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 194 ILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVSTVS--YGELERQLLQANPILEAFGNAKTVKNDNSSRFG 271
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASEAIEqtLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 272 KFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-R 350
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDdA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 351 ELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmpDNTAAQKL---CRLLGLGVTDFSRALLTPR 427
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQSLklaAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 428 IKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTN 507
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTIS-SPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 508 EKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIE-RPANPPGLLALLDeECWFPKAT--DKSFV------- 577
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVsqlhasf 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 578 ------EKVAQEQGGHPKFQRPRHLRDQaDFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdehg 651
Cdd:cd14890 476 grksgsGGTRRGSSQHPHFVHPKFDADK-QFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRR------------ 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 652 gfqqfsflgsfppsppgsaercssaisppgvegivGLEQVSslgdgppggrprrgmfrtVGQLYKESLSRLMATLSNTNP 731
Cdd:cd14890 543 -----------------------------------SIREVS------------------VGAQFRTQLQELMAKISLTNP 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 732 SFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAipkgfMDGKQACEKMIQA 811
Cdd:cd14890 570 RYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKM 644
|
730
....*....|....*...
gi 224831241 812 LELDPNLYRVGQSKIFFR 829
Cdd:cd14890 645 LGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
119-829 |
9.06e-171 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 536.67 E-value: 9.06e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 199 ESGAGKTENTKKVIQYLAHVASSPKGrkepgvpasvstvsygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG-----------------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAgeqlkadlllEPCSHYRFLTNGPSSSPGQEREL------ 352
Cdd:cd14872 144 DNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASP----------DPASRGGWGSSAAYGYLSLSGCIevegvd 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 353 ----FQETLESLRVLGFSHEEIISMLRMVSAVLQFGNI---ALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLT 425
Cdd:cd14872 214 dvadFEEVVLAMEQLGFDDADINNVMSLIAAILKLGNIefaSGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 426 PRIKV-GRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCIN 504
Cdd:cd14872 294 RLMEIkGCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCIN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 505 YTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQ 584
Cdd:cd14872 374 FTNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTH 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 585 GGHPKFQRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIwkdehggfqqfsflgsFPP 664
Cdd:cd14872 451 AAKSTFVYAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVL----------------FPP 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 665 SPPGSAERcssaisppgvegivgleQVsslgdgppggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKR 744
Cdd:cd14872 515 SEGDQKTS-----------------KV------------------TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKR 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 745 AGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILtPNAIPKGFM-DGKQACEKMIQALELDPNLYRVGQ 823
Cdd:cd14872 560 ARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGK 638
|
....*.
gi 224831241 824 SKIFFR 829
Cdd:cd14872 639 TRVLYR 644
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
120-829 |
2.62e-162 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 512.98 E-value: 2.62e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 200 SGAGKTENTKKVIQYLAHVASSPkgrkepgvpasvstvsYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKAN----------------NRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLK-ADLLLEPCSHYRFLTNGPSSSPGQE-----RELF 353
Cdd:cd01379 146 STGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDIVnnsgnREKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 354 QETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQ----ATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 429
Cdd:cd01379 226 EEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 430 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTN 507
Cdd:cd01379 306 TRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIAN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 508 EKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCID-LIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGG 586
Cdd:cd01379 386 EQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKFHNNIKS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 587 HPkFQRPRhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTaeiwkdehggfQQfsflgsfppsp 666
Cdd:cd01379 462 KY-YWRPK--SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV-----------RQ----------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 667 pgsaercssaisppgvegivgleqvsslgdgppggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAG 746
Cdd:cd01379 517 -------------------------------------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAG 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 747 KLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDgKQACEKMIQALELDPnlYRVGQSKI 826
Cdd:cd01379 554 KFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKV 630
|
...
gi 224831241 827 FFR 829
Cdd:cd01379 631 FLK 633
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
119-829 |
9.94e-162 |
|
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 512.38 E-value: 9.94e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 199 ESGAGKTENTKKVIQYLAHVASSPkgrkepgvPASVStvsygeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRR--------NNLVT--------EQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 279 DvAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSS-SPGQ-ERELFQET 356
Cdd:cd01387 145 E-GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCeIAGKsDADDFRRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 357 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTD-QATMPDNTAA--QKLCRLLGLGVTDFSRALLTPRIKVGRD 433
Cdd:cd01387 224 LAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHgQEGVSVGSDAeiQWVAHLLQISPEGLQKALTFKVTETRRE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 434 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNrALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 513
Cdd:cd01387 304 RIFTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 514 FNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRP 593
Cdd:cd01387 383 FNKHVFKLEQEEYIREQIDWTEIAFA-DNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKP 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 594 RhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEHGGFQQfsflgsfppSPPGSAERC 673
Cdd:cd01387 460 R--MPLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDK---------APPRLGKGR 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 674 SSAISPPGvegivgleqvsslgdgppggrprrgmfRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLV 753
Cdd:cd01387 529 FVTMKPRT---------------------------PTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVV 581
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224831241 754 LDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGfMDGKQACEKMIQALELDP-NLYRVGQSKIFFR 829
Cdd:cd01387 582 MAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
119-829 |
4.98e-161 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 511.54 E-value: 4.98e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 199 ESGAGKTENTKKVIQYLahVASSPKGrkepgvpasvstvsYGE-LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG--------------YGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL--TNGPSSSPGQERELFQE 355
Cdd:cd01385 145 YRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLnqSDCYTLEGEDEKYEFER 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 356 TLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRER-NTDQATMPDNTAAQKL-CRLLGLGVTDFSRALLTPRIKVGRD 433
Cdd:cd01385 225 LKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLEALTTKKTVTVGE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 434 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQGASfLGILDIAGFEIFQLNSFEQLCINYTNEK 509
Cdd:cd01385 305 TLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEH 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 510 LQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPK 589
Cdd:cd01385 384 LQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKY 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 590 FQRPRhLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEHGGFQQFSFLGSFPPSPPGS 669
Cdd:cd01385 461 YEKPQ-VMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVAVFRWAVLRAFFRAMAAF 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 670 AERCSSAIS-PPGVEGIVGLEQVSSLGDGPPGGRPRrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKL 748
Cdd:cd01385 539 REAGRRRAQrTAGHSLTLHDRTTKSLLHLHKKKKPP-----SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRF 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 749 EPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILtpnaIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFF 828
Cdd:cd01385 614 DDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFL 689
|
.
gi 224831241 829 R 829
Cdd:cd01385 690 K 690
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
119-827 |
9.22e-159 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 503.94 E-value: 9.22e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMY------RGKKRHEVPPHVYAVTEGAYRSMLQDRE-- 190
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 191 --DQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKepgvpasvSTVSYGELERQLLQANPILEAFGNAKTVKNDNSS 268
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQ--------NATERENVRDRVLESNPILEAFGNARTNRNNNSS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 269 RFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLtngpSSSPGQ 348
Cdd:cd14901 153 RFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYL----NSSQCY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 349 ER-------ELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIA-LKRERNTDQATMPDNTAAQKLCRLLGLGVTDFS 420
Cdd:cd14901 229 DRrdgvddsVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCfVKKDGEGGTFSMSSLANVRAACDLLGLDMDVLE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 421 RALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS-FLGILDIAGFEIFQLNSFE 499
Cdd:cd14901 309 KTLCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 500 QLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgldlqP----CIDLIErpANPPGLLALLDEECWFPKATDKS 575
Cdd:cd14901 389 QLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGNDEK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 576 FVEKVAQEQGGHPKFQRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTdrltaeiwkdehggfqq 655
Cdd:cd14901 462 LANKYYDLLAKHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSS----------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 656 FSFLGSfppsppgsaercssaisppgvegivgleqvsslgdgppggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVR 735
Cdd:cd14901 525 NAFLSS------------------------------------------------TVVAKFKVQLSSLLEVLNATEPHFIR 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 736 CIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQA---- 811
Cdd:cd14901 557 CIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhse 636
|
730
....*....|....*...
gi 224831241 812 --LELDPNLYrVGQSKIF 827
Cdd:cd14901 637 lnIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
119-829 |
1.64e-158 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 502.68 E-value: 1.64e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKK-RHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 198 GESGAGKTENTKKVIQYLAHVASSPKGRkepgvpasvstvsygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDSD----------------LLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-------- 349
Cdd:cd14897 145 FTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNdseeleyy 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 350 RELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 429
Cdd:cd14897 225 RQMFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 430 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINY 505
Cdd:cd14897 305 IRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 506 TNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQG 585
Cdd:cd14897 385 SNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 586 GHPKFQRPRHlrDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIwkdehggfqqfsFLGSFpps 665
Cdd:cd14897 462 ESPRYVASPG--NRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDL------------FTSYF--- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 666 ppgsaercssaisppgvegivgleqvsslgdgppggrprrgmfrtvgqlyKESLSRLMATLSNTNPSFVRCIVPNHEKRA 745
Cdd:cd14897 525 --------------------------------------------------KRSLSDLMTKLNSADPLFVRCIKPNNFLRP 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 746 GKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAiPKGFMDGKQACEKMIQALELDPnlYRVGQSK 825
Cdd:cd14897 555 NKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTK 631
|
....
gi 224831241 826 IFFR 829
Cdd:cd14897 632 VFLK 635
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
119-829 |
2.80e-158 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 502.77 E-value: 2.80e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 198 GESGAGKTENTKKVIQYLAHVASSPKGrkepgvpasvSTVsygeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGGLND----------STI------KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLggAGEQLKADLLLEPCSHYRFL-TNGPSSSPG-QERELFQE 355
Cdd:cd14903 145 FDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLL--ASPDVEERLFLDSANECAYTgANKTIKIEGmSDRKHFAR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 356 TLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATM--PDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRD 433
Cdd:cd14903 223 TKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 434 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 513
Cdd:cd14903 303 VYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 514 FNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKVAqeqGGHPKFQR- 592
Cdd:cd14903 382 FTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQDv 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 593 ---PRHLRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdehggfqqfsfLGSFPPSPPGS 669
Cdd:cd14903 455 iefPRTSRTQ--FTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFK-----------EKVESPAAAST 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 670 AERCSSAISppgvegivgleQVSSLGDgppggrprrgmfRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLE 749
Cdd:cd14903 522 SLARGARRR-----------RGGALTT------------TTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELD 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 750 PRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAiPKGFMDGKQACEKMIQALELD-PNLYRVGQSKIFF 828
Cdd:cd14903 579 HLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYF 657
|
.
gi 224831241 829 R 829
Cdd:cd14903 658 Q 658
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
119-829 |
1.46e-154 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 492.39 E-value: 1.46e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 198 GESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVstvsygelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCV--------EQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL-TNGPSSSPG-QERELFQE 355
Cdd:cd14873 153 ICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLnQSGCVEDKTiSDQESFRE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 356 TLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKrerNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 435
Cdd:cd14873 233 VITAMEVMQFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 436 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALdrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 515
Cdd:cd14873 310 LTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 516 HTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRH 595
Cdd:cd14873 388 KHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 596 LRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQStdrltaeiwkdehggfqQFSFLGSFppsppgsaercss 675
Cdd:cd14873 464 AVNN--FGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRES-----------------RFDFIYDL------------- 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 676 aisppgvegivgLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLD 755
Cdd:cd14873 512 ------------FEHVSSRNNQDTLKCGSKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLN 579
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224831241 756 QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKqaCEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14873 580 QLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
119-791 |
1.80e-153 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 489.97 E-value: 1.80e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRgKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 198 GESGAGKTENTKKVIQYLAHVASSPKGRKepgvpasvSTVsygelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKR--------SLV-----EAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 278 FD---------VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQL----------------------LGGAGEQLKAD 326
Cdd:cd14888 147 FSklkskrmsgDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLcaaareakntglsyeendeklaKGADAKPISID 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 327 LLL-EPCSHYRFLT-NGPSSSPG-QERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNT 403
Cdd:cd14888 227 MSSfEPHLKFRYLTkSSCHELPDvDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSAS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 404 AAQKL---CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS 480
Cdd:cd14888 307 CTDDLekvASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 481 FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLA 560
Cdd:cd14888 387 FCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFC 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 561 LLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDR 640
Cdd:cd14888 464 MLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNP 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 641 LTAEIWKdehggfqqfSFLGSFPPSPPgsaercssaisppgvegivgleqvsslgdgppggrpRRGMFRTVGQLYKESLS 720
Cdd:cd14888 542 FISNLFS---------AYLRRGTDGNT------------------------------------KKKKFVTVSSEFRNQLD 576
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224831241 721 RLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 791
Cdd:cd14888 577 VLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
119-829 |
7.70e-151 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 482.34 E-value: 7.70e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEV---PPHVYAVTEGAYRSMLQDR----ED 191
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 192 QSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVSTvsygELERQLLQANPILEAFGNAKTVKNDNSSRFG 271
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHE----SIEECVLLSNLILEAFGNAKTIRNDNSSRFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 272 KFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-PGQER 350
Cdd:cd14892 157 KYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEvDGVDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 351 EL-FQETLESLRVLGFSHEEIISMLRMVSAVLQFGNiaLKRERNTDQATMP----DNTAAQKLCRLLGLGVTDFSRALLT 425
Cdd:cd14892 237 ATeFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGN--VRFEENADDEDVFaqsaDGVNVAKAAGLLGVDAAELMFKLVT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 426 PRIKVGRDYV-QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQ---------GASFLGILDIAGFEIFQL 495
Cdd:cd14892 315 QTTSTARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 496 NSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFP-KATDK 574
Cdd:cd14892 395 NSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 575 SFVEKVAQEQ-GGHPKFQRPRHLRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdehggf 653
Cdd:cd14892 472 QLLTIYHQTHlDKHPHYAKPRFECDE--FVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK-------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 654 qqfsflgsfppsppgsaercssaisppgvegivgleqvsslgdgppggrprrgmFRTvgqlykeSLSRLMATLSNTNPSF 733
Cdd:cd14892 536 ------------------------------------------------------FRT-------QLAELMEVLWSTTPSY 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 734 VRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPN-AIPKGFMDGKQACEKM---- 808
Cdd:cd14892 555 IKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkce 634
|
730 740
....*....|....*....|..
gi 224831241 809 -IQALELDPNLYRVGQSKIFFR 829
Cdd:cd14892 635 eIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
119-829 |
7.82e-148 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 474.52 E-value: 7.82e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRH--------EVPPHVYAVTEGAYRSMLQDR 189
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 190 EDQSILCTGESGAGKTENTKKVIQYL------AHVASSPKGRKEPGVPASVSTVSygeLERQLLQANPILEAFGNAKTVK 263
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLtqlsqqEQNSEEVLTLTSSIRATSKSTKS---IEQKILSCNPILEAFGNAKTVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 264 NDNSSRFGKFIRINFD-VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADL-LLEPCSHYRFLTNG 341
Cdd:cd14907 158 NDNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLgLKNQLSGDRYDYLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 342 PSSSPGQER----ELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALK-RERNTDQATMPDNTAA-QKLCRLLGLG 415
Cdd:cd14907 238 KSNCYEVDTindeKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKETlQIIAKLLGID 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 416 VTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL------DRSPRQGASF-LGILDIA 488
Cdd:cd14907 318 EEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekDQQLFQNKYLsIGLLDIF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 489 GFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTF--LDFgLDLQPCIDLIERPanPPGLLALLDEEC 566
Cdd:cd14907 398 GFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKP--PIGIFNLLDDSC 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 567 WFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIW 646
Cdd:cd14907 475 KLATGTDEKLLNKIKKQHKNNSKLIFPNKINKDT-FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 647 KDEHGGFQQFSflgsfppsppgsaercssaisppgvegivGLEQVSSLGDgppggrprrgmfRTVGQLYKESLSRLMATL 726
Cdd:cd14907 554 SGEDGSQQQNQ-----------------------------SKQKKSQKKD------------KFLGSKFRNQMKQLMNEL 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 727 SNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNaipkgfmdgkqace 806
Cdd:cd14907 593 MQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN-------------- 658
|
730 740
....*....|....*....|...
gi 224831241 807 kmiqaleldpnlYRVGQSKIFFR 829
Cdd:cd14907 659 ------------VLFGKTKIFMK 669
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
121-829 |
4.04e-139 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 449.74 E-value: 4.04e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 121 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSML----QDREDQSILC 196
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 197 TGESGAGKTENTKKVIQYLAHVAsspKGRKEpgvpasvstvsygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 276
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC---RGNSQ--------------LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 277 NFDvAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-AGEQLKADLLLEPcSHYRFLTN--GPSSSPGQERELF 353
Cdd:cd14889 146 RFR-NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGiSAEDRENYGLLDP-GKYRYLNNgaGCKREVQYWKKKY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 354 QETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALkrERNTDQA---TMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKV 430
Cdd:cd14889 224 DEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEAlkvENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 431 GRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALdrSPRQGASF----LGILDIAGFEIFQLNSFEQLCINYT 506
Cdd:cd14889 302 RGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL--APKDDSSVelreIGILDIFGFENFAVNRFEQACINLA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 507 NEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIerPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGG 586
Cdd:cd14889 380 NEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLF--LNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKG 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 587 HPKFQRPRhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTdrltaeiwkdehggfqqfsflgsfppSP 666
Cdd:cd14889 457 NSYYGKSR--SKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSA--------------------------TP 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 667 PGSAERCSSAISPPGVEGIVGLEQVSSLGDGPPGGrprrgmfRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAG 746
Cdd:cd14889 509 LLSVLFTATRSRTGTLMPRAKLPQAGSDNFNSTRK-------QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPG 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 747 KLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL--TPNaIPKgfmdGKQACEKMIQALELDPnlYRVGQS 824
Cdd:cd14889 582 QLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKT 654
|
....*
gi 224831241 825 KIFFR 829
Cdd:cd14889 655 RLFFK 659
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
120-789 |
2.19e-134 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 435.12 E-value: 2.19e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMY-----------RGKKRHEVPPHVYAVTEGAYRSM-- 185
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 186 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPkgrkepgVPASVSTVSYGE-LERQLLQANPILEAFGNAKTV 262
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNN-------LAASVSMGKSTSgIAAKVLQTNILLESFGNARTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 263 KNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKAdlllepcshyrfltngp 342
Cdd:cd14900 155 RNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK----------------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 343 ssspgqeRELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTD-QATMPDNTAAQKL------CRLLGLG 415
Cdd:cd14900 218 -------RDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 416 VTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL---DRSPRQGAS-FLGILDIAGFE 491
Cdd:cd14900 291 ATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 492 IFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKA 571
Cdd:cd14900 371 VFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 572 TDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDplndnvaaLLHQstdrltaeiwkdehg 651
Cdd:cd14900 448 SDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQ--------------- 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 652 gfqqfsflgsfppsppgsaercssaisppgvegivglEQVSslgdgppggrprrgMFRTVGQlYKESLSRLMATLSNTNP 731
Cdd:cd14900 505 -------------------------------------EAVD--------------LFVYGLQ-FKEQLTTLLETLQQTNP 532
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 224831241 732 SFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 789
Cdd:cd14900 533 HYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
119-829 |
3.85e-132 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 429.75 E-value: 3.85e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 198 GESGAGKTENTKKVIQYLAHVASspkGRKEpgvpasvSTVSygelerQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKD-------KTIA------KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS--PG-QERELFQ 354
Cdd:cd14904 145 FDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMqiPGlDDAKLFA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 355 ETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKrERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDY 434
Cdd:cd14904 225 STQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFD-KSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNES 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 435 VQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 514
Cdd:cd14904 304 VTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 515 NHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKV---AQEQGGHPKFQ 591
Cdd:cd14904 384 TTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESID 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 592 RPRHLRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdehggfqqfsflgsfppsppGSAE 671
Cdd:cd14904 460 FPKVKRTQ--FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELF---------------------GSSE 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 672 -RCSSAISPPGvegivgleqvsslgdgppggrPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEP 750
Cdd:cd14904 517 aPSETKEGKSG---------------------KGTKAPKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDK 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 751 RLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGfmDGKQACEKMIQAL-ELDPNLYRVGQSKIFFR 829
Cdd:cd14904 576 RMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
119-829 |
7.28e-130 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 422.92 E-value: 7.28e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERyySGLI----YTYSGLFCVVINPYKQLPiytEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDRE---D 191
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 192 QSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVSTVSYG--ELERQLLQANPILEAFGNAKTVKNDNSSR 269
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKRKLSvtSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 270 FGKFIRINFDVAGY-IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLT-NGPSSSPG 347
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 348 -QERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKrERNTDQ-----ATMPDNTAAQKLCRLLGLGVTDFSR 421
Cdd:cd14891 236 iDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFD-EEDTSEgeaeiASESDKEALATAAELLGVDEEALEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 422 ALLTPRIkVGRDYVQKAQ-TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRqGASFLGILDIAGFEIFQL-NSFE 499
Cdd:cd14891 315 VITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPD-PLPYIGVLDIFGFESFETkNDFE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 500 QLCINYTNEKLQQLFNHTMFVLEQEEYQREGIpwtflDFGLDLQP----CIDLIErpANPPGLLALLDEECWFPKATDKS 575
Cdd:cd14891 393 QLLINYANEALQATFNQQVFIAEQELYKSEGI-----DVGVITWPdnreCLDLIA--SKPNGILPLLDNEARNPNPSDAK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 576 FVEKVAQEQGGHPKFQRPrHLRDQAD-FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQStdrltaeiwkdehggfQ 654
Cdd:cd14891 466 LNETLHKTHKRHPCFPRP-HPKDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS----------------A 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 655 QFSflgsfppsppgsaercssaisppgvegivglEQVSSLGDgppggrprrgmfrtvgqlykeslsrlmaTLSNTNPSFV 734
Cdd:cd14891 529 KFS-------------------------------DQMQELVD----------------------------TLEATRCNFI 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 735 RCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQA-CEKMIQALE 813
Cdd:cd14891 550 RCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFR 629
|
730
....*....|....*.
gi 224831241 814 LDPNLYRVGQSKIFFR 829
Cdd:cd14891 630 VPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
119-791 |
1.09e-126 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 416.60 E-value: 1.09e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYR--------GKKRHEVPPHVYAVTEGAYRSMLQ-D 188
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 189 REDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASvstvsygELERQLLQANPILEAFGNAKTVKNDNSS 268
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAV-------EIGKRILQTNPILESFGNAQTIRNDNSS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 269 RFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL-TNGPSSSPG 347
Cdd:cd14902 154 RFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLnSYGPSFARK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 348 QER-----ELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKL---CRLLGLGVTDF 419
Cdd:cd14902 234 RAVadkyaQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHLakcAELMGVDVDKL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 420 SRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--------RSPRQGASFLGILDIAGFE 491
Cdd:cd14902 314 ETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 492 IFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPANppGLLALLDEECWFPKA 571
Cdd:cd14902 394 SLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLMPKG 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 572 TDKSFVEKVAQEQGGhpkfqrprhlRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIwkdehg 651
Cdd:cd14902 471 SNQALSTKFYRYHGG----------LGQ--FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAI------ 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 652 gfqqfsflgsfppsppGSAERCSSAISPPGVEGivgleqvsslgdgppggRPRRGMFRT--VGQLYKESLSRLMATLSNT 729
Cdd:cd14902 533 ----------------GADENRDSPGADNGAAG-----------------RRRYSMLRApsVSAQFKSQLDRLIVQIGRT 579
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224831241 730 NPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 791
Cdd:cd14902 580 EAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
119-829 |
2.00e-123 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 406.22 E-value: 2.00e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR--GKKRHE-------VPPHVYAVTEGAYRSMLQD- 188
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 189 REDQSILCTGESGAGKTENTKKVIQYLAHVasspkGRKEPGVPASVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSS 268
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTL-----GNGEEGAPNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 269 RFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKA--------DLLLEPCSHYRFLTN 340
Cdd:cd14908 156 RFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEkyefhdgiTGGLQLPNEFHYTGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 341 G--PSSSPGQERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNtDQATMPDNTAAQK----LCRLLGL 414
Cdd:cd14908 236 GgaPDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclarVAKLLGV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 415 GVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGA-SFLGILDIAGFEIF 493
Cdd:cd14908 315 DVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDIFGFECF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 494 QLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFP-KAT 572
Cdd:cd14908 395 AHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiRGS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 573 DKSFVEKV--------AQEQGGHPKFQRPRHLRDQADFSVLHYAGKVDYKANEWLM-KNMDPLNdnvaallhqstdrLTA 643
Cdd:cd14908 472 DANYASRLyetylpekNQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP-------------LTA 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 644 EIwkdehggfqqfsflgsfppsppgsaercssaisppgvegivgleqvsslgdgppggrprrgMFRTvGQLYKESLSRLM 723
Cdd:cd14908 539 DS-------------------------------------------------------------LFES-GQQFKAQLHSLI 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 724 ATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPnAIPKGFM---- 799
Cdd:cd14908 557 EMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEVVLswsm 635
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 224831241 800 ---DGKQACEKMI----------QALELDPNL----YRVGQSKIFFR 829
Cdd:cd14908 636 erlDPQKLCVKKMckdlvkgvlsPAMVSMKNIpedtMQLGKSKVFMR 682
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
117-875 |
2.11e-121 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 404.80 E-value: 2.11e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 117 NEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHE-VPPHVYAVTEGAYRSMLQDREDQSIL 195
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 196 CTGESGAGKTENTKKVIQYLAhvasspkgrkepgvpASVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 275
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---------------SSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQ 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 276 INFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQ 354
Cdd:PTZ00014 253 LQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGiDDVKDFE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 355 ETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALK-RERN--TDQAT-MPDNTAA-QKLCRLLGLGVTDFSRALLTPRIK 429
Cdd:PTZ00014 333 EVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEgKEEGglTDAAAiSDESLEVfNEACELLFLDYESLKKELTVKVTY 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 430 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrsPRQG-ASFLGILDIAGFEIFQLNSFEQLCINYTNE 508
Cdd:PTZ00014 413 AGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIE--PPGGfKVFIGMLDIFGFEVFKNNSLEQLFINITNE 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 509 KLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQEQGGHP 588
Cdd:PTZ00014 491 MLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNP 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 589 KFQRPRhlRDQ-ADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdehggfqqfsflgsfppspp 667
Cdd:PTZ00014 568 KYKPAK--VDSnKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFE-------------------- 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 668 gsaercssaisppGVE---GIVGLEQVsslgdgppggrprrgmfrtVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKR 744
Cdd:PTZ00014 626 -------------GVEvekGKLAKGQL-------------------IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKK 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 745 AGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQS 824
Cdd:PTZ00014 674 PLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKT 753
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 224831241 825 KIFFR---AGVLAQLEEERDLKVTDIIVSFQAAARGYLARRAFQKR----QQQQSALR 875
Cdd:PTZ00014 754 MVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKVRKNikslVRIQAHLR 811
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
119-829 |
1.21e-119 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 393.76 E-value: 1.21e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 199 ESGAGKTENTKKVIQYLAHVASSPKGRKepgvpasvstvsygelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQTEDR----------------LRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 279 DvAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSS--SPGQERELFQET 356
Cdd:cd14896 145 Q-HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACrlQGKEDAQDFEGL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 357 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQ--ATMPDNTAAQKLCRLLGLGvTDFSRALLTPRIKV-GRD 433
Cdd:cd14896 224 LKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVP-PERLEGAVTHRVTEtPYG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 434 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALdRSPRQGASF--LGILDIAGFEIFQLNSFEQLCINYTNEKLQ 511
Cdd:cd14896 303 RVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWL-APPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 512 QLFNHTMFVLEQEEYQREGIPWTFLDfGLDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQ 591
Cdd:cd14896 382 LFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYA 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 592 RPRhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIwkdehggFQQFSFLGSFPPSPPGSAE 671
Cdd:cd14896 459 KPQ--LPLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSL-------FQEAEPQYGLGQGKPTLAS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 672 RcssaisppgvegivgleqvsslgdgppggrprrgmfrtvgqlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPR 751
Cdd:cd14896 530 R------------------------------------------FQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVG 567
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224831241 752 LVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTpNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14896 568 HVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALG-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
119-825 |
9.21e-119 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 393.96 E-value: 9.21e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKR-HEVPPHVYAVTEGAYRSMLQDREDQSILC 196
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 197 TGESGAGKTENTKKVIQYLAHVASSPKGRKepgvpaSVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 276
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQN------NNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 277 NFDVAGYIV-GANIETYLLEKSR-AIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP-CSHYRFL-------------TN 340
Cdd:cd14906 155 EFRSSDGKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqSS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 341 GPSSSPGQEREL---FQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQAT--MPDNTAA-QKLCRLLGL 414
Cdd:cd14906 235 NKNSNHNNKTESiesFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 415 GVTDFSRALLTPRIKV-GRDYVQ-KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDR----------SPRQGASFL 482
Cdd:cd14906 315 IESVFKQALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 483 GILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALL 562
Cdd:cd14906 395 GVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 563 DEECWFPKATDKSFVEKVAQEQGGHPK-FQRPrhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRL 641
Cdd:cd14906 472 DDECIMPKGSEQSLLEKYNKQYHNTNQyYQRT---LAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFL 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 642 TAEIwkdehggFQQFSFlgsfppSPPGSAERCSSAIsppgvegivgleqvsslgdgppggrprrgmfrTVGQLYKESLSR 721
Cdd:cd14906 549 KKSL-------FQQQIT------STTNTTKKQTQSN--------------------------------TVSGQFLEQLNQ 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 722 LMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDG 801
Cdd:cd14906 584 LIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNP 663
|
730 740
....*....|....*....|....
gi 224831241 802 KQACEKMIQALELDPNLYRVGQSK 825
Cdd:cd14906 664 KLASQLILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
119-827 |
1.83e-117 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 387.81 E-value: 1.83e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRH-EVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 198 GESGAGKTENTKKVIQYLAhvasspkgrkepgvpASVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIn 277
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---------------SAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQL- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 278 fDVA--GYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQ 354
Cdd:cd14876 145 -DVAseGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGiDDVADFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 355 ETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRErntDQATMPDntAA----------QKLCRLLGLGVTDFSRALL 424
Cdd:cd14876 224 EVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEALKRELT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 425 TPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrsPRQG-ASFLGILDIAGFEIFQLNSFEQLCI 503
Cdd:cd14876 299 VKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 504 NYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQE 583
Cdd:cd14876 377 NITNEMLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 584 QGGHPKFQRPRHLRDQaDFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKD---EHGGFQQFSFLG 660
Cdd:cd14876 454 LKSNGKFKPAKVDSNI-NFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGvvvEKGKIAKGSLIG 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 661 SfppsppgsaercssaisppgvegivgleqvsslgdgppggrprrgmfrtvgQLYKeSLSRLMATLSNTNPSFVRCIVPN 740
Cdd:cd14876 533 S---------------------------------------------------QFLK-QLESLMGLINSTEPHFIRCIKPN 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 741 HEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYR 820
Cdd:cd14876 561 ETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYA 640
|
....*..
gi 224831241 821 VGQSKIF 827
Cdd:cd14876 641 IGKTMVF 647
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
120-790 |
8.00e-117 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 387.77 E-value: 8.00e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPiyteaivEMYRGKKRHE-------VPPHVYAVTEGAYRSMLQ----- 187
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 188 --DREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGrkepGVPASVSTVSYGElerQLLQANPILEAFGNAKTVKND 265
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTA----TSSSKRRRAISGS---ELLSANPILESFGNARTLRND 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 266 NSSRFGKFIRINF-----DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCS--HYRFL 338
Cdd:cd14895 148 NSSRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 339 TNG---PSSSPGQERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNI--ALKRERNTDQ-------------ATMP 400
Cdd:cd14895 228 SGGqcyQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVlfVASSEDEGEEdngaasapcrlasASPS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 401 DNTAAQKL---CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDR---- 473
Cdd:cd14895 308 SLTVQQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQrqfa 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 474 -SPRQGAS-----FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDlQPCID 547
Cdd:cd14895 388 lNPNKAANkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 548 LIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRhlRDQAD--FSVLHYAGKVDYKANEWLMKNMDP 625
Cdd:cd14895 467 MLE--QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNKDQ 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 626 LNDNVAALLHQSTDRLTAEIWKdehggFQQFSFLGSFPPSPPGSAERCSSaisppgvegivgleqVSSLGdgppggrprr 705
Cdd:cd14895 543 PNAELFSVLGKTSDAHLRELFE-----FFKASESAELSLGQPKLRRRSSV---------------LSSVG---------- 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 706 gmfrtVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 785
Cdd:cd14895 593 -----IGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQ 667
|
....*
gi 224831241 786 YEILT 790
Cdd:cd14895 668 YRLLV 672
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
119-829 |
3.99e-116 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 385.51 E-value: 3.99e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 199 ESGAGKTENTKKVIQYLAHVASSPKGRkepgvpasvstVSYGELErqllQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV-----------LSVEKLN----AALTVLEAFGNVRTALNGNATRFSQLFSLDF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPC--SHYRFLTngPSSSPGQEREL---F 353
Cdd:cd01386 146 DQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLaeSNSFGIV--PLQKPEDKQKAaaaF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 354 QETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRAL---------- 423
Cdd:cd01386 224 SKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpq 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 424 --LTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGfeiFQLN----- 496
Cdd:cd01386 304 qsTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSIT-IVDTPG---FQNPahsgs 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 497 ----SFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERP---ANPP---------GLLA 560
Cdd:cd01386 380 qrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLW 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 561 LLDEECWFPKATDKSFVEKV--AQEQGGHPKFQRPRHLRDQA-DFSVLHYAGK--VDYKANEWLMK-NMDPLNDNVAALL 634
Cdd:cd01386 460 LLDEEALYPGSSDDTFLERLfsHYGDKEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLL 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 635 HQSTDRLTAeiwkdehggfqqfsflgsfppsppgsAERCSSAIsppgvegivgleQVsslgdgppggrprrgmfrtvgql 714
Cdd:cd01386 540 QESQKETAA--------------------------VKRKSPCL------------QI----------------------- 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 715 yKESLSRLMATLSNTNPSFVRCIVPNHEkrAGKLEPR--------------LVLDQLRCNGVLEGIRICRQGFPNRILFQ 780
Cdd:cd01386 559 -KFQVDALIDTLRRTGLHFVHCLLPQHN--AGKDERStsspaagdelldvpLLRSQLRGSQLLDALRLYRQGFPDHMPLG 635
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 224831241 781 EFRQRYEILTPNAIPKGF-----MDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd01386 636 EFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
119-791 |
1.74e-107 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 359.16 E-value: 1.74e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKR-HEVPPHVYAVTEGAYRSMLQDRE--DQSI 194
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 195 LCTGESGAGKTENTKKVIQYLAHVASSPkgrkepgvpASVSTVSYGE-LERQLLQANPILEAFGNAKTVKNDNSSRFGKF 273
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASP---------TSWESHKIAErIEQRILNSNPVMEAFGNACTLRNNNSSRFGKF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 274 IRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLtngPSSSPGQERELF 353
Cdd:cd14880 152 IQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWL---PNPERNLEEDCF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 354 QETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTA---AQKLCRLLGLGVTDFSRALLTPRIKV 430
Cdd:cd14880 229 EVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTIRA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 431 GRDYV--QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNE 508
Cdd:cd14880 309 GKQQQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 509 KLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKS-FVEKVAQEQGGH 587
Cdd:cd14880 389 KLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAqLQTRIESALAGN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 588 PKFQRPRhLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIwkdehggfqqfsflgsFPPSPp 667
Cdd:cd14880 466 PCLGHNK-LSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKL----------------FPANP- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 668 gsaeRCSSAISPPGVEGIVGLEQVSSlgdgppggrprrgmfrtvgqlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGK 747
Cdd:cd14880 528 ----EEKTQEEPSGQSRAPVLTVVSK---------------------FKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQT 582
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 224831241 748 LEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 791
Cdd:cd14880 583 FLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLRR 626
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
119-829 |
1.02e-106 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 356.89 E-value: 1.02e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRH-----EVPPHVYAVTEGAYRSMLQDREDQ 192
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 193 SILCTGESGAGKTENTKKVIQYLAHVASSpkgrkepgvpasvstvSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGK 272
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHST----------------SSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 273 FIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPG-QER 350
Cdd:cd14886 145 FIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGiDDQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 351 ELFQETLESLRVLgFSHEEIISMLRMVSAVLQFGNIALKRERN--TDQATMPDNTAA-QKLCRLLGLGVTDFSRALLTPR 427
Cdd:cd14886 225 KEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 428 IKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSPRQgasFLGILDIAGFEIFQLNSFEQLCINY 505
Cdd:cd14886 304 VVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfDADARP---WIGILDIYGFEFFERNTYEQLLINY 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 506 TNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAqeqg 585
Cdd:cd14886 381 ANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFTSSCK---- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 586 ghpkfqrpRHLRD---------QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEiwkdehggfqqf 656
Cdd:cd14886 454 --------SKIKNnsfipgkgsQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNK------------ 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 657 sflgsfppsppgsaerCSSAISP--PGVEGivgleqvsslgdgppggrprrgmfRTVGQLYKESLSRLMATLSNTNPSFV 734
Cdd:cd14886 514 ----------------AFSDIPNedGNMKG------------------------KFLGSTFQLSIDQLMKTLSATKSHFI 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 735 RCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT--PNAIPKGFMDGKQACEKMIQAL 812
Cdd:cd14886 554 RCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENL 633
|
730
....*....|....*..
gi 224831241 813 ELDPNLYRVGQSKIFFR 829
Cdd:cd14886 634 GIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
119-829 |
4.51e-102 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 343.72 E-value: 4.51e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYS-GLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRG-KKRHEVPPHVYAVTEGAYRSM-LQDREDQSIL 195
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 196 CTGESGAGKTENTKKVIQYL---AHVASSPKGRKepgvpaSVSTvsygELERQLLQANPILEAFGNAKTVKNDNSSRFGK 272
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLgqlSYMHSSNTSQR------SIAD----KIDENLKWSNPVMESFGNARTVRNDNSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 273 FIRINFD-VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADL-LLEPCSHYR-------FLTNGPS 343
Cdd:cd14875 151 YIKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKclnggntFVRRGVD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 344 SSPGQERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNtDQATMPDNTAAQKLCRLLGLGVTDFSRAL 423
Cdd:cd14875 231 GKTLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 424 LtprIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrsPR---QGASFLGILDIAGFEIFQLNSFEQ 500
Cdd:cd14875 310 L---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASIT--PQgdcSGCKYIGLLDIFGFENFTRNSFEQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 501 LCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKV 580
Cdd:cd14875 385 LCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 581 AQEQGG-HPKFQRPRH-LRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdehggfqqfSF 658
Cdd:cd14875 462 WDQWANkSPYFVLPKStIPNQ--FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTD-----------------EF 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 659 LGSFPPSPPGSAERCssaisppgvegivgleqvsslgdgppggrprrgmfRTVGQLYKESLSRLMATLSNTNPSFVRCIV 738
Cdd:cd14875 523 IRTLLSTEKGLARRK-----------------------------------QTVAIRFQRQLTDLRTELESTETQFIRCIK 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 739 PNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGK--QACEKMIQALE--- 813
Cdd:cd14875 568 PNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrly 647
|
730
....*....|....*...
gi 224831241 814 --LDPNlYRVGQSKIFFR 829
Cdd:cd14875 648 gwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
119-786 |
1.91e-98 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 335.14 E-value: 1.91e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYrgKKRHEVP------------PHVYAVTEGAYRSM 185
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGY--AYDHNSQfgdrvtstdprePHLFAVARAAYIDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 186 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVS-TVSYGELERQLLQANPILEAFGNAKTVKN 264
Cdd:cd14899 79 VQNGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISPPaSPSRTTIEEQVLQSNPILEAFGNARTVRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 265 DNSSRFGKFIRINF-DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-----AGEQLKADLLLEPCSHYRFL 338
Cdd:cd14899 159 DNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 339 TNGPSSSPG---QERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIAL-----KRERNT--DQATMPDNTAA--- 405
Cdd:cd14899 239 NQSLCSKRRdgvKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 406 --QKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSP-------- 475
Cdd:cd14899 319 hfTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQAsapwgade 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 476 ------RQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLI 549
Cdd:cd14899 399 sdvddeEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 550 ERpaNPPGLLALLDEECWFPKATDKSFVEKVAQE---QGGHPKFQRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPL 626
Cdd:cd14899 478 EH--RPIGIFSLTDQECVFPQGTDRALVAKYYLEfekKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 627 NDNVAALLHQSTDRLTaeiwkdehggfqQFSFLGSFPPSPPGSAErcssaisPPGVEGIVGLEQVSSLGDGppggrprrg 706
Cdd:cd14899 556 CESAAQLLAGSSNPLI------------QALAAGSNDEDANGDSE-------LDGFGGRTRRRAKSAIAAV--------- 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 707 mfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 786
Cdd:cd14899 608 ---SVGTQFKIQLNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
120-793 |
1.70e-93 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 316.07 E-value: 1.70e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQlpIYTEAIVEMYRGKKRHeVPPHVYAVTEGAYRSMLQdREDQSILCTGE 199
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 200 SGAGKTENTKKVIQYLAHvasspkgrkepgvpasvSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14898 78 SGSGKTENAKLVIKYLVE-----------------RTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 280 vaGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLlepcsHYRFLTnGPSSSPGQERELFQETLES 359
Cdd:cd14898 141 --GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI-----DTSSTA-GNKESIVQLSEKYKMTCSA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 360 LRVLGFSHEEIISMLRMvsAVLQFGNIALKRERNTdqaTMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQ 439
Cdd:cd14898 213 MKSLGIANFKSIEDCLL--GILYLGSIQFVNDGIL---KLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFN 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 440 TKEQADFALEALAKATYERLFRWLVLRLNRALDRSprqGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 519
Cdd:cd14898 288 TLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 520 VLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGGhpkfqrprHLRDQ 599
Cdd:cd14898 365 RAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKIKKYLNG--------FINTK 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 600 AD--FSVLHYAGKVDYKANEWLMKNmdplndnvaallhqstdrltaeiwkdehggfqqfsflgsfppsppgsaeRCSSAI 677
Cdd:cd14898 433 ARdkIKVSHYAGDVEYDLRDFLDKN-------------------------------------------------REKGQL 463
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 678 SPPGVEGIVGLEQVSSLgdgppggrprrgmfrtvGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQL 757
Cdd:cd14898 464 LIFKNLLINDEGSKEDL-----------------VKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQL 526
|
650 660 670
....*....|....*....|....*....|....*.
gi 224831241 758 RCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA 793
Cdd:cd14898 527 AECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
119-829 |
1.27e-92 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 318.13 E-value: 1.27e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYS--------GLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDRE 190
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 191 DQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpasvstvsygeLERQLLQANPILEAFGNAKTVKNDNSSRF 270
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG------------LEARLLQSGPVLEAFGNAHTVLNANSSRF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 271 GKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGgaGEQLKADLLLEPCSHYRFLTNgpssspgqeR 350
Cdd:cd14887 149 GKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCN--AAVAAATQKSSAGEGDPESTD---------L 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 351 ELFQETLESLRVLGFSHEEIISMLrmvSAVLQFGNIALKRERNTDQATMPDNTA--------AQKLCRLL-------GLG 415
Cdd:cd14887 218 RRITAAMKTVGIGGGEQADIFKLL---AAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssGLK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 416 VTDFSRALLT--------PRIKVGRDYV------------QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSP 475
Cdd:cd14887 295 VTEASRKHLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 476 R-------------QGASFLGILDIAGFEIFQ---LNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGI-------- 531
Cdd:cd14887 375 KpsesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVfqnqdcsa 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 532 -PWTF-LDFGLDLQP--CIDLIERP--------ANPPGL---------LALLDEECWFPKATDKSFVEKVAQEQGGHPKF 590
Cdd:cd14887 455 fPFSFpLASTLTSSPssTSPFSPTPsfrsssafATSPSLpsslsslssSLSSSPPVWEGRDNSDLFYEKLNKNIINSAKY 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 591 --QRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQstdrltaeiwkdehggfqqfsflgsfppsppg 668
Cdd:cd14887 535 knITPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLA-------------------------------- 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 669 saerCSSAISPPGVEGIVGLEQVSSlgdgppggrprrgMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKL 748
Cdd:cd14887 583 ----CSTYTRLVGSKKNSGVRAISS-------------RRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIF 645
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 749 EPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIpKGFMDGKQACEKMIQALELDPNLYRVGQSKIFF 828
Cdd:cd14887 646 EDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFF 724
|
.
gi 224831241 829 R 829
Cdd:cd14887 725 R 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
116-828 |
2.17e-88 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 303.32 E-value: 2.17e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 116 LNEASVLHNLRERYYSGLIYTY---SGLfcVVINPYKQLPIYTEAIVEMYR-------GKKRHEVPPHVYAVTEGAYRSM 185
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 186 LQDREDQSILCTGESGAGKTENTKKVIQYLAHV-ASSPKGRKepgvpasvstvsygeLERQLLQANPILEAFGNAKTVKN 264
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLsSHSKKGTK---------------LSSQISAAEFVLDSFGNAKTLTN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 265 DNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG--- 341
Cdd:cd14879 144 PNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYgch 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 342 --PSSSPGQERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNI--ALKRERNTDqATMPDNTAA-QKLCRLLGLGV 416
Cdd:cd14879 224 plPLGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLefTYDHEGGEE-SAVVKNTDVlDIVAAFLGVSP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 417 TDFsRALLTPRIK-VGRD----YVQKAQTKEQADfaleALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFE 491
Cdd:cd14879 303 EDL-ETSLTYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 492 ifQL-----NSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPanPPGLLALLDEEC 566
Cdd:cd14879 378 --NRsstggNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK--PGGLLGILDDQT 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 567 -WFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQAD---FSVLHYAGKVDYKANEWLMKNmdplndnvaallhqstdrlt 642
Cdd:cd14879 453 rRMPKKTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERN-------------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 643 aeiwkdehggfqqfsflgsfppsppgsAERCSSAIsppgvegivgleqVSslgdgppggrprrgMFRTVGQLyKESLSRL 722
Cdd:cd14879 513 ---------------------------GDVLSPDF-------------VN--------------LLRGATQL-NAALSEL 537
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 723 MATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPnaipkgFMDGK 802
Cdd:cd14879 538 LDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAE 611
|
730 740
....*....|....*....|....*.
gi 224831241 803 QACEKMIQALELDPNLYRVGQSKIFF 828
Cdd:cd14879 612 RIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
119-829 |
3.19e-88 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 303.28 E-value: 3.19e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR---GKKRHEVPPHVYAVTEGAYRSMLQDREDQSIL 195
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 196 CTGESGAGKTENTKKVIQYLAHVASSpkgrkepgvpasvstvSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 275
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASS----------------SRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 276 INF-DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG-PSSSPGQERELF 353
Cdd:cd14878 145 LQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmREDVSTAERSLN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 354 QETL----ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 429
Cdd:cd14878 225 REKLavlkQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 430 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS---FLGILDIAGFEIFQLNSFEQLCINYT 506
Cdd:cd14878 305 FKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtlDIGILDIFGFEEFQKNEFEQLCVNMT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 507 NEKLQQLFNHTMFVLEQEEYQREGIPW----------TFLDFGLDlqpcidlierpaNPPGLLALLDEEC---W-----F 568
Cdd:cd14878 385 NEKMHHYINEVLFLQEQTECVQEGVTMetayspgnqtGVLDFFFQ------------KPSGFLSLLDEESqmiWsvepnL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 569 PK-------ATDKSFVEKVAQEQGGHPKFqrprhlRDQ-ADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDR 640
Cdd:cd14878 453 PKklqslleSSNTNAVYSPMKDGNGNVAL------KDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENV 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 641 LTAEIwkdehggFQqfsflgsfppsppgsaercssaisppgvegivgleqvSSLGdgppggrprrgmfrTVGQLYKESLS 720
Cdd:cd14878 527 VINHL-------FQ-------------------------------------SKLV--------------TIASQLRKSLA 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 721 RLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI-PKGFM 799
Cdd:cd14878 549 DIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQ 628
|
730 740 750
....*....|....*....|....*....|
gi 224831241 800 DGKQACEKMIQALELDPnlYRVGQSKIFFR 829
Cdd:cd14878 629 SAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
119-829 |
1.51e-79 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 277.28 E-value: 1.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLpiytEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 199 ESGAGKTENTKKVIQYLAhvasspKGRKEPGvpasvstvsygELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL------SGVKEDN-----------EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIEL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETL 357
Cdd:cd14937 140 DEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEiDDAKDFGNLM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 358 ESLRVLGFsHEEIISMLRMVSAVLQFGNI---ALKRERNTDQATMPDNT--AAQKLCRLLGLGVTDFSRALLTPRIKVGR 432
Cdd:cd14937 220 ISFDKMNM-HDMKDDLFLTLSGLLLLGNVeyqEIEKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIAN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 433 DYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSpRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 512
Cdd:cd14937 299 QKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNN-KELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 513 LFNHTMFVLEQEEYQREGIPWTFLDFGLDlQPCIDLIERPANppgLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQR 592
Cdd:cd14937 378 IYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKYAS 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 593 PRhlRD-QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsflgsfppsppgsae 671
Cdd:cd14937 454 TK--KDiNKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYED----------------------- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 672 rcssaisppgvegivgLEQVSSLGdgppggRPRRGMFRtvgqlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPR 751
Cdd:cd14937 509 ----------------VEVSESLG------RKNLITFK-----YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQK 561
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224831241 752 LVLDQLRCNGVLEGIRIcRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQAlELDPNLYRVGQSKIFFR 829
Cdd:cd14937 562 KVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
119-781 |
3.32e-77 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 271.78 E-value: 3.32e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHE-------VPPHVYAVTEGAYRSMLQDRE 190
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 191 DQSILCTGESGAGKTENTKKVIQYLAHVASSpkgrkepgvpasvstVSYGELERQLLQANPILEAFGNAKTVKNDNSSRF 270
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTD---------------SQMTERIDKLIYINNILESMSNATTIKNNNSSRC 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 271 GKFIRINFD---------VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-AGEQLKADLLLEPCSHYRFL-- 338
Cdd:cd14884 146 GRINLLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLnp 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 339 ------------------TNGPSSSPGQEREL-FQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKrerntdqatm 399
Cdd:cd14884 226 deshqkrsvkgtlrlgsdSLDPSEEEKAKDEKnFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK---------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 400 pdntAAqklCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL-------- 471
Cdd:cd14884 296 ----AA---AECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekde 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 472 ---DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFlDFGLDLQPCIDL 548
Cdd:cd14884 369 sdnEDIYSINEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCS-DVAPSYSDTLIF 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 549 IERpanppgLLALLDE-----ECWFPKATDKSFV-----EKVAQEQGGHPKFQRPRHLRDQAD---------FSVLHYAG 609
Cdd:cd14884 448 IAK------IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVSYGFVLNHDADGTAkkqnikkniFFIRHYAG 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 610 KVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEiwkdehggfqqfsflgsfppsppgSAERCSSaisppgvegivgle 689
Cdd:cd14884 522 LVTYRINNWIDKNSDKIETSIETLISCSSNRFLRE------------------------ANNGGNK-------------- 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 690 qvsslgdgppggrprrGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRIC 769
Cdd:cd14884 564 ----------------GNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKIL 627
|
730
....*....|..
gi 224831241 770 RQGFPNRILFQE 781
Cdd:cd14884 628 NRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
120-828 |
1.23e-66 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 239.25 E-value: 1.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYkqlpiyteaiveMYRGKKRHEVPPHVYA-------VTEGAYRSMLQDREDQ 192
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTLTSTRSSPlapqllkVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 193 SILCTGESGAGKTENTKKVIQYLAHVASspkgrkepGVPASvstvsygELERQLLQANPILEAFGNAKTVKNDNSSRFGK 272
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAG--------GGPET-------DAFKHLAAAFTVLRSLGSAKTATNSESSRIGH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 273 FIRINFdVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCS--HYRFLTNGPSSSPGQER 350
Cdd:cd14881 135 FIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAED 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 351 EL-FQETLESLRVLGFSHEEIIsmlRMVSAVLQFGNIALKrERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 429
Cdd:cd14881 214 AArFQAWKACLGILGIPFLDVV---RVLAAVLLLGNVQFI-DGGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHN 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 430 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALdrspRQGAS--------FLGILDIAGFEIFQLNSFEQL 501
Cdd:cd14881 290 ARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANSLK----RLGSTlgthatdgFIGILDMFGFEDPKPSQLEHL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 502 CINYTNEKLQQLFNHTMFVLEQEEYQREGIPwTFLDFG-LDLQPCIDLIErpANPPGLLALLDEECwFPKATDKSFVEKV 580
Cdd:cd14881 366 CINLCAETMQHFYNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKI 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 581 AQEQGGHPKFQRPRHLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTdrltaeiwkdehggfqqfsflg 660
Cdd:cd14881 442 KVQHRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN---------------------- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 661 sfppsppgsaerCSSAisppgvegivgleqvsslgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPN 740
Cdd:cd14881 499 ------------CNFG-------------------------------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSN 535
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 741 HEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQ--ALELDPNL 818
Cdd:cd14881 536 TTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPPSK 615
|
730
....*....|....*..
gi 224831241 819 -------YRVGQSKIFF 828
Cdd:cd14881 616 lssvstsWALGKRHIFL 632
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
120-829 |
1.76e-65 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 236.91 E-value: 1.76e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYrgKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 199 ESGAGKTENTKKVIQYLahvasspkgrkepgVPASVSTVSYgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14905 80 ESGSGKSENTKIIIQYL--------------LTTDLSRSKY--LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQ--ERELFQET 356
Cdd:cd14905 144 SLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESidDNRVFDRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 357 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNtdQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14905 224 KMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 437 KAqtkeqadfalEALAKATYERLFRWLVLRLNRALdrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 516
Cdd:cd14905 302 NR----------DSLARSLYSALFHWIIDFLNSKL--KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 517 TMFVLEQEEYQREGIPW-TFLDFGlDLQPCIDLIERPANppgllaLLDEECWFPKATDKSFVEKVAQEQGGHPKF-QRPR 594
Cdd:cd14905 370 TVLKQEQREYQTERIPWmTPISFK-DNEESVEMMEKIIN------LLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPN 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 595 hlrdqaDFSVLHYAGKVDYKANEWLMKNMDPLNDNvAALLHQSTdrLTAEIWKDEhGGF----------QQFSFLGSFPP 664
Cdd:cd14905 443 ------KFGIEHYFGQFYYDVRGFIIKNRDEILQR-TNVLHKNS--ITKYLFSRD-GVFninatvaelnQMFDAKNTAKK 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 665 SPPGSAE---RCSS-----AISPPGVEGIVGLEQVSSLGDGppggrprrgmfrTVGQLYKeSLSRLMATLSNTNPS--FV 734
Cdd:cd14905 513 SPLSIVKvllSCGSnnpnnVNNPNNNSGGGGGGGNSGGGSG------------SGGSTYT-TYSSTNKAINNSNCDfhFI 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 735 RCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFP----NRILFqefrQRYEILTPNAipKGFMD-GKQACEKMI 809
Cdd:cd14905 580 RCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTihynNKIFF----DRFSFFFQNQ--RNFQNlFEKLKENDI 653
|
730 740
....*....|....*....|
gi 224831241 810 QALELDPNLYRVGQSKIFFR 829
Cdd:cd14905 654 NIDSILPPPIQVGNTKIFLR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
119-794 |
9.22e-65 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 233.61 E-value: 9.22e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYrgkkrhevppHVYAVTEGAYRSMLQDRED-QSILCT 197
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 198 GESGAGKTENTKKVIQYLAhvaSSPKgrkepgvpASVSTVSYGELERqllqanpILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT---SQPK--------SKVTTKHSSAIES-------VFKSFGCAKTLKNDEATRFGCSIDLL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 278 FDvAGYIVGANIE-TYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER-ELFQE 355
Cdd:cd14874 133 YK-RNVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDvNHFKH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 356 TLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTD---QATMPDNTAAQKLCRLLgLGVtDFSR--ALLTPRIKV 430
Cdd:cd14874 212 LEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKWVAFL-LEV-DFDQlvNFLLPKSED 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 431 GrdyvqKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAsfLGILDIAGFEIFQLNSFEQLCINYTNEKL 510
Cdd:cd14874 290 G-----TTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 511 QQLFNHTMFVLEQEEYQREGIPWTF-LDFGLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPK 589
Cdd:cd14874 363 ENLFVKHSFHDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 590 FQRPRHlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIwkdehggFQQFSFlgsfppsppgs 669
Cdd:cd14874 441 YGKARN-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLL-------FESYSS----------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 670 aercssaisppgvegivgleqvsslgdgppggrPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLE 749
Cdd:cd14874 502 ---------------------------------NTSDMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFD 548
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 224831241 750 PRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI 794
Cdd:cd14874 549 IPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPGDI 593
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
120-789 |
5.78e-64 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 231.55 E-value: 5.78e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 200 SGAGKTENTKKVIQYLAHVasspkGRKEPGVPASVstvsygelerqlLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYL-----GDGNRGATGRV------------ESSIKAILALVNAGTPLNADSTRCILQYQLTFG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG--AGEQLKaDLLLEPCSHYRFLTNGPSSSPGQER------- 350
Cdd:cd14882 145 STGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLRIPPEVPPSKLKyrrddpe 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 351 ---ELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKreRNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPR 427
Cdd:cd14882 224 gnvERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFR--QNGGYAELENTEIASRVAELLRLDEKKFMWALTNYC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 428 IKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--RSPRQGASFLGILDIAGFEIFQLNSFEQLCINY 505
Cdd:cd14882 302 LIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSfpRAVFGDKYSISIHDMFGFECFHRNRLEQLMVNT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 506 TNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIErpANPPGLLALLDEECwfPKATDKSFV-EKVAQEQ 584
Cdd:cd14882 382 LNEQMQYHYNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDQLM--TKPDGLFYIIDDAS--RSCQDQNYImDRIKEKH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 585 GGHPKfqrprhLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsflgsfpp 664
Cdd:cd14882 457 SQFVK------KHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN---------------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 665 sppgsaercssaisppgvegivglEQVSSLgdgppggrprrgmfRTVGQLYKESLSRLMATLS-NTNPS---FVRCIVPN 740
Cdd:cd14882 515 ------------------------SQVRNM--------------RTLAATFRATSLELLKMLSiGANSGgthFVRCIRSD 556
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 224831241 741 HEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 789
Cdd:cd14882 557 LEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFL 605
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
122-787 |
3.55e-62 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 228.32 E-value: 3.55e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 122 LHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKR----------HEVPPHVYAVTEGAYRSMLQDRED 191
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 192 QSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEpGVPASVSTVSYGElerQLLQANPILEAFGNAKTVKNDNSSRFG 271
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPD-SEGASGVLHPIGQ---QILHAFTILEAFGNAATRQNRNSSRFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 272 KFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQ--LKADLLLEPCSH-YRFLTNGP--SSSP 346
Cdd:cd14893 160 KMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDptLRDSLEMNKCVNeFVMLKQADplATNF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 347 GQERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIAL-------KRERNTDQATMPDNTAaqklCRLLGLGVTDF 419
Cdd:cd14893 240 ALDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggKSVGGANSTTVSDAQS----CALKDPAQILL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 420 SRALLTPRIKVGRDYVQKAQ----------------TKEQADFALEALAKATYERLFRWLVLRLNRAL----DRSPR--- 476
Cdd:cd14893 316 AAKLLEVEPVVLDNYFRTRQffskdgnktvsslkvvTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKsni 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 477 ----QGasfLGILDIAGFEIF--QLNSFEQLCINYTNEKLQQLF-NHTMFV----LEQEEYQREG--IPWTFLDFGLDLQ 543
Cdd:cd14893 396 vinsQG---VHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 544 PCIDLIERPanPPGLLALLDEECWFPKATDKSFVEK---VAQEQGGhpkFQRPRHLRDQAD------------FSVLHYA 608
Cdd:cd14893 473 KCLQLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKlfsGNEAVGG---LSRPNMGADTTNeylapskdwrllFIVQHHC 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 609 GKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIwkdehgGFQQFSFLGSfpPSPPGSAERCSSAISPPGvEGIVGL 688
Cdd:cd14893 548 GKVTYNGKGLSSKNMLSISSTCAAIMQSSKNAVLHAV------GAAQMAAASS--EKAAKQTEERGSTSSKFR-KSASSA 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 689 EQVSSLGDGppggrprrgmfrTVGQLYKESLSRLMAtLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRI 768
Cdd:cd14893 619 RESKNITDS------------AATDVYNQADALLHA-LNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQA 685
|
730
....*....|....*....
gi 224831241 769 CRQGFPNRILFQEFRQRYE 787
Cdd:cd14893 686 SRSIFTVHLTYGHFFRRYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
141-283 |
1.01e-58 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 200.26 E-value: 1.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 141 FCVVINPYKQLPIYTEAIV-EMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 219
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224831241 220 SSPKGRKEPGVPASVsTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 283
Cdd:cd01363 81 FNGINKGETEGWVYL-TEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
120-827 |
5.29e-52 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 197.37 E-value: 5.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR-GKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 199 ESGAGKTENTKKVIQYLAHVASSpkGRKEPGVPASVSTVSYGELERQ---------LLQANPILEAFGNAKTVKNDNSSR 269
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKG--SRRLPTNLNDQEEDNIHNEENTdyqfnmsemLKHVNVVMEAFGNAKTVKNNNSSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 270 FGKFIRINFDvAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE 349
Cdd:cd14938 160 FSKFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 350 RE-LFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNI---------ALKRERNTDQATMPDNTAAQKL----------- 408
Cdd:cd14938 239 YSgKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkafrkkSLLMGKNQCGQNINYETILSELensediglden 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 409 -------CRLLGLGVTDFSRALLTPRIkVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--RSPRQGA 479
Cdd:cd14938 319 vknlllaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTqlQNININT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 480 SFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANpPGLL 559
Cdd:cd14938 398 NYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE-GSLF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 560 ALLDEECwFPKATDKSFVEKVAQEQGGH-PKF-QRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQS 637
Cdd:cd14938 477 SLLENVS-TKTIFDKSNLHSSIIRKFSRnSKYiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 638 tdrltaeiwkdEHGGFQQFSFLGSFPPSPPGSAERCSSAISppgvegivgleqvSSLGDGPPGGRPRRGMFRTvgqLYKE 717
Cdd:cd14938 556 -----------ENEYMRQFCMFYNYDNSGNIVEEKRRYSIQ-------------SALKLFKRRYDTKNQMAVS---LLRN 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 718 SLSRLMATLSNTNPSFVRCIVPNHEKRA-GKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIltPNAipk 796
Cdd:cd14938 609 NLTELEKLQETTFCHFIVCMKPNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDI--KNE--- 683
|
730 740 750
....*....|....*....|....*....|.
gi 224831241 797 gfmDGKQACEKMIQALELDPNLYRVGQSKIF 827
Cdd:cd14938 684 ---DLKEKVEALIKSYQISNYEWMIGNNMIF 711
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1225-1855 |
6.89e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 123.12 E-value: 6.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1225 ELRSKREQEVTELKKTLEEETRIhEAAVQELRQRhgqaLGELAEQLEQARRGKG-AWEKTRLALEA---EVSELRAELSS 1300
Cdd:COG1196 169 KYKERKEEAERKLEATEENLERL-EDILGELERQ----LEPLERQAEKAERYRElKEELKELEAELlllKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1301 LQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQE 1380
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1381 LLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAE 1460
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1461 ALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLraveereraeaegreRE 1540
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA---------------EL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1541 ARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAAnDLRAQVTELEDELTAAEDAK 1620
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA-VLIGVEAAYEAALEAALAAA 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1621 LRLEVTVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEE 1700
Cdd:COG1196 548 LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1701 AVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNL 1780
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224831241 1781 SKAAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERsfsAKAESGRQQLERQIQEL 1855
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL---EELERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1109-1741 |
2.54e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 115.03 E-value: 2.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1109 QELEKLKRRLDGESSELQEQmvEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESE 1188
Cdd:COG1196 216 RELKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1189 RVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAE 1268
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1269 QLEQARRGKGAWEKtRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELE 1348
Cdd:COG1196 374 LAEAEEELEELAEE-LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1349 NVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQ 1428
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1429 AQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKtETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQ 1508
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGR-ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1509 RKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLsskddvgksvhel 1588
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE------------- 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1589 eracRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEErK 1668
Cdd:COG1196 679 ----AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA-L 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1669 QRTLAVAARKKLEGELEELKAQMASAG-------QGKEEAVKQLRKMQAQMKELWREVEETRTSREEIfsqNRESEKRLK 1741
Cdd:COG1196 754 EELPEPPDLEELERELERLEREIEALGpvnllaiEEYEELEERYDFLSEQREDLEEARETLEEAIEEI---DRETRERFL 830
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
933-1500 |
5.99e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.88 E-value: 5.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 933 VGELQGRVAQLEEErARLAEQLRaeaelcaeaeetrgRLAARKQELELVVSELEARVGEEEEcsRQMQTEKKRLQQHIQE 1012
Cdd:COG1196 195 LGELERQLEPLERQ-AEKAERYR--------------ELKEELKELEAELLLLKLRELEAEL--EELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1013 LEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEA 1092
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1093 TIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLR 1172
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1173 EAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAV 1252
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1253 QELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVS---ELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDG 1329
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEaalEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1330 ERARAEAAEKLQRAQAELENVSGALNEAEsktirlskELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQ 1409
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVDLVAS--------DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1410 LEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDD 1489
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
|
570
....*....|.
gi 224831241 1490 ATMDLEQQRQL 1500
Cdd:COG1196 730 LEAEREELLEE 740
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1192-1770 |
1.97e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.95 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1192 RTKAEKqRRDLGEELEALRGELE-DTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQL 1270
Cdd:COG1196 209 AEKAER-YRELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1271 EQARRgkgawektrlaLEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENV 1350
Cdd:COG1196 288 AEEYE-----------LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1351 SGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLeeeaaareragrelQTAQAQ 1430
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL--------------ERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1431 LSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRK 1510
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1511 FDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDdvGKSVHELER 1590
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA--GRATFLPLD 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1591 ACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQR 1670
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1671 TLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRL 1750
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
570 580
....*....|....*....|
gi 224831241 1751 QEELAASDRARRQAQQDRDE 1770
Cdd:COG1196 741 LLEEEELLEEEALEELPEPP 760
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
125-770 |
4.60e-24 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 110.60 E-value: 4.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 125 LRERYYSGLIYTYSGLFCV-VINPYKQL------PIYTEAIVEMYRGKKRHE--VPPHVYAV------------------ 177
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIakqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 178 --TEGAYRSMLQDReDQSILCTGESGAGKTENTKKVIQYLAHVASSP--KGRKE----------PGVPASVST------- 236
Cdd:cd14894 87 psTISSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAQPAlsKGSEEtckvsgstrqPKIKLFTSStkstiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 237 ----------------------------------------------------------VSYGELERQL------------ 246
Cdd:cd14894 166 rteeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyekLEHLEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 247 ----LQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVAGY---IVGANIETYLLEKSRAIRQA------KDECSFHI 311
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 312 FYQLLGGAG-----EQLKADLLLE--PCSHYRFLTNGPSSSPG---------QERELFQETLESLRVLGFSHEEIISMLR 375
Cdd:cd14894 326 LYAMVAGVNafpfmRLLAKELHLDgiDCSALTYLGRSDHKLAGfvskedtwkKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 376 MVSAVLQFGNIALKRERNTDQATMPDN---TAAQKLCRLLGLG-VTDFSRALLTPRIKV--GRDYVQKAQTKEQADFALE 449
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGsVEKLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 450 ALAKATYERLFRWLVLRLNRAL----------------DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQql 513
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstdgnkhqmdsNASAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLY-- 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 514 fnhtmfvleQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKAT----------DKSFVEKVAQE 583
Cdd:cd14894 564 ---------AREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLFVRNIYDR 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 584 QGGH-PKFQR-----PRH---LRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEhggfQ 654
Cdd:cd14894 635 NSSRlPEPPRvlsnaKRHtpvLLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNES----S 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 655 QFSFLGSFPPSPPGSAErcsSAISppGVEGIVGleqvsslgdgppggrprrgmfrtvgqLYKESLSRLMATLSNTNPSFV 734
Cdd:cd14894 711 QLGWSPNTNRSMLGSAE---SRLS--GTKSFVG--------------------------QFRSHVNVLTSQDDKNMPFYF 759
|
810 820 830
....*....|....*....|....*....|....*.
gi 224831241 735 RCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICR 770
Cdd:cd14894 760 HCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
907-1756 |
4.83e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 107.83 E-value: 4.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 907 RQDEVLQARAQELQKVQELQQQ-SAREVGELQGRVAQLEEERARLAEQLRAEAELCAeaeetrgRLAARKQELELVVSEL 985
Cdd:TIGR02168 200 RQLKSLERQAEKAERYKELKAElRELELALLVLRLEELREELEELQEELKEAEEELE-------ELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 986 EARVGEEEECSRQMQT-------EKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKE 1058
Cdd:TIGR02168 273 RLEVSELEEEIEELQKelyalanEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1059 RKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEE 1138
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1139 LRAQ-LGRKEEELQAALARAEDEGGARAQLLKSLREaqaalaeaqedleservARTKAEKQRRDLGEELEALRGEledtL 1217
Cdd:TIGR02168 433 AELKeLQAELEELEEELEELQEELERLEEALEELRE-----------------ELEEAEQALDAAERELAQLQAR----L 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1218 DSTNAQQELRSKREQEVTELKKTleeetriheaavqelRQRHGQALGELAEQLEQArrgkgawEKTRLALEAEVSELRAE 1297
Cdd:TIGR02168 492 DSLERLQENLEGFSEGVKALLKN---------------QSGLSGILGVLSELISVD-------EGYEAAIEAALGGRLQA 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1298 L--SSLQTArqegeqrRRRLELQLQEVQGRAG----DGERARAEAAEKLQRAQaELENVSGALNEAESKTIRLSKELSST 1371
Cdd:TIGR02168 550 VvvENLNAA-------KKAIAFLKQNELGRVTflplDSIKGTEIQGNDREILK-NIEGFLGVAKDLVKFDPKLRKALSYL 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1372 EAQLHDAQELLQE-ETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAgaleagee 1450
Cdd:TIGR02168 622 LGGVLVVDDLDNAlELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKI-------- 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1451 arrraareaEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERE 1530
Cdd:TIGR02168 694 ---------AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1531 RAEAEGRErearalsltraleeeqeareelerqnraLRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELE 1610
Cdd:TIGR02168 765 ELEERLEE----------------------------AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1611 DELTAAEDAKLRLEVTVQALKTQHErDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQ 1690
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLE-DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224831241 1691 MasagqgkEEAVKQLRKMQAQMKELWREVEETRTSREEIfsqnresEKRLKGLEAEVLRLQEELAA 1756
Cdd:TIGR02168 896 L-------EELSEELRELESKRSELRRELEELREKLAQL-------ELRLEGLEVRIDNLQERLSE 947
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1026-1931 |
7.83e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 107.06 E-value: 7.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1026 KLQLEKVTTEAKMKKFEEDLLLLEDQNSKLskERKLleDRLAEFSSQAAEEEEKVKSLNKLRLKYEAtiadmeDRLRKEE 1105
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNEL--ERQL--KSLERQAEKAERYKELKAELRELELALLV------LRLEELR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1106 KGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDL 1185
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1186 ESERVARTKAEKQRRDLGEELEALRGELEDTldstnaqqelrskrEQEVTELKKTLEEEtrihEAAVQELRQRhgqaLGE 1265
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEEL--------------KEELESLEAELEEL----EAELEELESR----LEE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1266 LAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQ-----TARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKL 1340
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEdrrerLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1341 QRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEetraKLALGSRVRAMEAEA---AGLREQLEEEAAAR 1417
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN----LEGFSEGVKALLKNQsglSGILGVLSELISVD 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1418 ERAGRELQTA-----QAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATM 1492
Cdd:TIGR02168 533 EGYEAAIEAAlggrlQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDP 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1493 DLE-------QQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRaleeeqeareelerqnr 1565
Cdd:TIGR02168 613 KLRkalsyllGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILER----------------- 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1566 alRAELEallsskdDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERdLQGRDEAG 1645
Cdd:TIGR02168 676 --RREIE-------ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQL 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1646 EERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTS 1725
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1726 REEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVAngnlskaAILEEKRQLEGRLgqleeelee 1805
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE-------ALLNERASLEEAL--------- 889
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1806 eqsnsELLNDRYRKLLLQVESLttelsaersfsakaESGRQQLERQIQELRGRLGEEDAgARARHKMTIAALESKLAqAE 1885
Cdd:TIGR02168 890 -----ALLRSELEELSEELREL--------------ESKRSELRRELEELREKLAQLEL-RLEGLEVRIDNLQERLS-EE 948
|
890 900 910 920
....*....|....*....|....*....|....*....|....*.
gi 224831241 1886 EQLEQETrerilsgklvrrAEKRLKEVVLQVEEERRVADQLRDQLE 1931
Cdd:TIGR02168 949 YSLTLEE------------AEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
912-1440 |
2.79e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.02 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 912 LQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVGE 991
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 992 EEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSS 1071
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1072 QAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQ 1151
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1152 AALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQR----------------RDLGEELEALRGEL-- 1213
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavavligveaayeAALEAALAAALQNIvv 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1214 EDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARrgkgawektRLALEAEVSE 1293
Cdd:COG1196 554 EDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAR---------YYVLGDTLLG 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1294 LRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEA 1373
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224831241 1374 QLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEE 1440
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1333-1945 |
3.23e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.02 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1333 RAEAAEKLQRAQAELENVSGALNEAESKTIRLSKElsstEAQLHDAQELLQEETRAKLAL-GSRVRAMEAEAAGLREQle 1411
Cdd:COG1196 174 KEEAERKLEATEENLERLEDILGELERQLEPLERQ----AEKAERYRELKEELKELEAELlLLKLRELEAELEELEAE-- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1412 eeaaareragreLQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDAT 1491
Cdd:COG1196 248 ------------LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1492 MDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAEL 1571
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1572 EALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRrQ 1651
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA-L 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1652 LAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFS 1731
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1732 QNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDE--MADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSN 1809
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALArgAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1810 SELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALESKLAQAEEQLE 1889
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 224831241 1890 QETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLE 1945
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE 770
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1189-1988 |
1.46e-21 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 102.83 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1189 RVARTKAEKQRRDLgEELEALRGELEDTLDSTNAQ-------QELRSKREQ--------EVTELKKTLEEETRIhEAAVQ 1253
Cdd:TIGR02168 175 KETERKLERTRENL-DRLEDILNELERQLKSLERQaekaeryKELKAELRElelallvlRLEELREELEELQEE-LKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1254 ELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERAR 1333
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1334 AEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRA-------KLALGSRVRAMEAEAAGL 1406
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqlelqIASLNNEIERLEARLERL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1407 REQLEEEAAARERAGRELQTAQaqLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQE 1486
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1487 LDDATMDLEQQRQL---VSTLEKKQRKF--------DQLLAEEK-----AAVLRAVEERERAEAEGREREARAlSLTRAL 1550
Cdd:TIGR02168 491 LDSLERLQENLEGFsegVKALLKNQSGLsgilgvlsELISVDEGyeaaiEAALGGRLQAVVVENLNAAKKAIA-FLKQNE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1551 EEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAK-LRLEVTVQA 1629
Cdd:TIGR02168 570 LGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKkLRPGYRIVT 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1630 LktqhERDLQGRD--EAGEERRRQLAKQLRDAEVERDEERKQR-----TLAVAARKKLEGELEELKAQMASAGQGKEEAV 1702
Cdd:TIGR02168 650 L----DGDLVRPGgvITGGSAKTNSSILERRREIEELEEKIEEleekiAELEKALAELRKELEELEEELEQLRKELEELS 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1703 KQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVangNLSK 1782
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL---KALR 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1783 AAILEEKRQLEgrlgqleeeleeeqsnseLLNDRYRKLLLQVESLTTELSAersfsakaesgrqqLERQIQELRGRLGEE 1862
Cdd:TIGR02168 803 EALDELRAELT------------------LLNEEAANLRERLESLERRIAA--------------TERRLEDLEEQIEEL 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1863 dAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKR 1942
Cdd:TIGR02168 851 -SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 224831241 1943 QLEEAEEEASR-AQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1988
Cdd:TIGR02168 930 RLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1563-2033 |
1.64e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.16 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1563 QNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERdLQGRD 1642
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR-LEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1643 EAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEET 1722
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1723 RTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEE 1802
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1803 LEEEQSNSELLNDRYRKLLLQVESLT----TELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALE 1878
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAarllLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1879 SKLAQaEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLR--VKQLKRQLEEAEEEASRAQA 1956
Cdd:COG1196 545 AAALQ-NIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVdlVASDLREADARYYVLGDTLL 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1957 GRRRLQRELEDVTESAESMN---REVTTLRNRLRRGPLTFTTRTVRQVFRLEEGVASDEEAEEAQPGSGPSPEPEGSPPA 2033
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAgrlREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1063-1793 |
2.71e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 92.05 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1063 EDRLAEFSSQAAEEEEKVKSLNKLRLKYEaTIADMEDRLRKEE-----KGRQELEKLKRRLDGESSELQEQMVEQQQRAE 1137
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1138 ELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTK-AEKQRRDLGEELEALRGELEDT 1216
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEdAEERLAKLEAEIDKLLAEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1217 LDSTNAQQELRSKREQEVTELKKTLEE-ETRIHE--AAVQELRQRHGQalgeLAEQLEQARRGKGAWEKTRLALEAEVSE 1293
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELEDlRAELEEvdKEFAETRDELKD----YREKLEKLKREINELKRELDRLQEELQR 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1294 LRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEA 1373
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1374 QLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEE-EAAARERAGRELQ--------TAQAQLSEWRRRQEEEAGA 1444
Cdd:TIGR02169 498 QARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERyATAIEVAAGNRLNnvvveddaVAKEAIELLKRRKAGRATF 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1445 LEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATM--DLEQQRQLVS-----TLEKKqrkfdqlLAE 1517
Cdd:TIGR02169 578 LPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVveDIEAARRLMGkyrmvTLEGE-------LFE 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1518 EKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQ 1597
Cdd:TIGR02169 651 KSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1598 AANDLRAQVTELEDELTAAEDAKLRLEVTVQAL---KTQHERDL-QGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLA 1673
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIENVKSELKELearIEELEEDLhKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRI 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1674 VAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQ-------NRESEKRLKGLEAE 1746
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEleeleaaLRDLESRLGDLKKE 890
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 224831241 1747 VLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLE 1793
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
993-1793 |
1.21e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.20 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 993 EECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKE----RKLLEDRLAE 1068
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKaedaRKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1069 FSSQA-----AEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEklkrrldgesselqEQMVEQQQRAEELRaql 1143
Cdd:PTZ00121 1174 DAKKAeaarkAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAED--------------AKKAEAVKKAEEAK--- 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1144 gRKEEELQaalaRAEDEggaraqllkSLREAQAALAEAQEDLESERVARTKAEKQRRdlgeelealRGELEDTLDSTNAQ 1223
Cdd:PTZ00121 1237 -KDAEEAK----KAEEE---------RNNEEIRKFEEARMAHFARRQAAIKAEEARK---------ADELKKAEEKKKAD 1293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1224 QELRSKREQEVTELKKTLEEETRIHEAAVQ-ELRQRHGQALGELAEQLEQARRGKGAWEKTRlALEAEVSELRAELSSLQ 1302
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAA-ADEAEAAEEKAEAAEKK 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1303 TARQEGEQRrrrlELQLQEVQGRAGDGERARAE----AAEKLQRAQAELENVSGALNEAESKtiRLSKELSSTEAQLHDA 1378
Cdd:PTZ00121 1373 KEEAKKKAD----AAKKKAEEKKKADEAKKKAEedkkKADELKKAAAAKKKADEAKKKAEEK--KKADEAKKKAEEAKKA 1446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1379 QELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAARE 1458
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1459 AealtqRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLraveereraEAEGRE 1538
Cdd:PTZ00121 1527 A-----KKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA---------KKAEEA 1592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1539 REARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAED 1618
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1619 AKLRLEVTVQALKTQHERDLQGRDEAGEER-----RRQLAKQLRDAEVERDEERKQRTLAVAARKklEGELEELKAQMAS 1693
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEEAKkaeelKKKEAEEKKKAEELKKAEEENKIKAEEAKK--EAEEDKKKAEEAK 1750
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1694 AGQGKEEAVKQLRKMQAQMKELWREVEET---RTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDE 1770
Cdd:PTZ00121 1751 KDEEEKKKIAHLKKEEEKKAEEIRKEKEAvieEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDS 1830
|
810 820
....*....|....*....|...
gi 224831241 1771 MADEVAngnLSKAAILEEKRQLE 1793
Cdd:PTZ00121 1831 AIKEVA---DSKNMQLEEADAFE 1850
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1646-1956 |
1.98e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.23 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1646 EERRRQLAKQLRDA----EVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEE 1721
Cdd:COG1196 199 ERQLEPLERQAEKAeryrELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1722 TRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEE 1801
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1802 ELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRlgeedagaRARHKMTIAALESKL 1881
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER--------LERLEEELEELEEAL 430
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224831241 1882 AQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQA 1956
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
903-1514 |
5.05e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 87.82 E-value: 5.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 903 LQVTRQDEVLQAraqELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVV 982
Cdd:TIGR02169 290 LRVKEKIGELEA---EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 983 SELEARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLL 1062
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1063 EDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLD---GESSELQEQMVEQQQRAEEL 1139
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEervRGGRAVEEVLKASIQGVHGT 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1140 RAQLGRKEEELQAALARA----------EDEGGARA--QLLKSLREAQAA----LAEAQEDLESERVARTKAEKQRRDLG 1203
Cdd:TIGR02169 527 VAQLGSVGERYATAIEVAagnrlnnvvvEDDAVAKEaiELLKRRKAGRATflplNKMRDERRDLSILSEDGVIGFAVDLV 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1204 EELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAV----QELRQRHGQALGELAEqLEQARRGKGA 1279
Cdd:TIGR02169 607 EFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRMVTLEGELFEKSGAMtggsRAPRGGILFSRSEPAE-LQRLRERLEG 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1280 WEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAES 1359
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1360 KTIRLSKELSSTEAQL-----HDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEW 1434
Cdd:TIGR02169 766 RIEELEEDLHKLEEALndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1435 -------RRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTL-EK 1506
Cdd:TIGR02169 846 keqiksiEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELkAK 925
|
....*...
gi 224831241 1507 KQRKFDQL 1514
Cdd:TIGR02169 926 LEALEEEL 933
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
904-1518 |
5.76e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 87.80 E-value: 5.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 904 QVTRQDEVLQARAQEL-QKVQELQQQSAR---EVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELE 979
Cdd:TIGR02168 313 NLERQLEELEAQLEELeSKLDELAEELAEleeKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 980 LVVSELEARVGEEEecSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKER 1059
Cdd:TIGR02168 393 LQIASLNNEIERLE--ARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1060 KLLEDRLAEFSSQAAEEEEKVKSLNklrlkyeatiaDMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEEL 1139
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLE-----------RLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAI 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1140 RAQLG---------RKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEkqrrDLGEELEALR 1210
Cdd:TIGR02168 540 EAALGgrlqavvveNLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAK----DLVKFDPKLR 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1211 GELE---------DTLDSTNAQQEL----------------------------------RSKREQEVTELKKTLEEETRI 1247
Cdd:TIGR02168 616 KALSyllggvlvvDDLDNALELAKKlrpgyrivtldgdlvrpggvitggsaktnssileRRREIEELEEKIEELEEKIAE 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1248 HEAAVQELRQrhgqALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAG 1327
Cdd:TIGR02168 696 LEKALAELRK----ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1328 DGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLR 1407
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1408 EQLEEEAAARERAGRELQTAQAQLSEW--RRRQEEEAGALEAGEEARrraareaeaLTQRLAEKTETVDRLERGRRRLQQ 1485
Cdd:TIGR02168 852 EDIESLAAEIEELEELIEELESELEALlnERASLEEALALLRSELEE---------LSEELRELESKRSELRRELEELRE 922
|
650 660 670
....*....|....*....|....*....|...
gi 224831241 1486 ELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEE 1518
Cdd:TIGR02168 923 KLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1583-1988 |
9.80e-15 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 80.60 E-value: 9.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1583 KSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAgEERRRQLAKQLRDAEVE 1662
Cdd:pfam01576 201 KGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNA-LKKIRELEAQISELQED 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1663 RDEERKQRTLAVAARKKLEGELEELKAQMASAgQGKEEAVKQLR-KMQAQMKELWREVEETRTSREEIFSQNRESE-KRL 1740
Cdd:pfam01576 280 LESERAARNKAEKQRRDLGEELEALKTELEDT-LDTTAAQQELRsKREQEVTELKKALEEETRSHEAQLQEMRQKHtQAL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1741 KGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKL 1820
Cdd:pfam01576 359 EELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1821 LLQVESLTTELSAERSFSAKAESGRQQLERQIQELRgRLGEEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGK 1900
Cdd:pfam01576 439 QSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ-ELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVER 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1901 LVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVT 1980
Cdd:pfam01576 518 QLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVS 597
|
....*...
gi 224831241 1981 TLRNRLRR 1988
Cdd:pfam01576 598 NLEKKQKK 605
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1031-1911 |
1.56e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 80.02 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1031 KVTTEAKMKKFEEDLLLLEDqnSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQE 1110
Cdd:pfam02463 142 GKIEIIAMMKPERRLEIEEE--AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1111 -LEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESER 1189
Cdd:pfam02463 220 eLEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1190 VARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEtrihEAAVQELRQRhgqaLGELAEQ 1269
Cdd:pfam02463 300 SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE----EEEEEELEKL----QEKLEQL 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1270 LEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEvqgRAGDGERARAEAAEKLQRAQAELEN 1349
Cdd:pfam02463 372 EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKE---EKKEELEILEEEEESIELKQGKLTE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1350 VSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEA-----------EAAGLREQLEEEAAARE 1418
Cdd:pfam02463 449 EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQkeskarsglkvLLALIKDGVGGRIISAH 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1419 RAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLE--- 1495
Cdd:pfam02463 529 GRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLaql 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1496 QQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALL 1575
Cdd:pfam02463 609 DKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1576 SSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELT------AAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERR 1649
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVqeaqdkINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1650 RQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMasagqgKEEAVKQLRKMQAQMKELWREVEETRTSREEI 1729
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL------KEEAELLEEEQLLIEQEEKIKEEELEELALEL 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1730 FsqnrESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSN 1809
Cdd:pfam02463 843 K----EEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1810 SELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALESKLAQAEEQLE 1889
Cdd:pfam02463 919 IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKE 998
|
890 900
....*....|....*....|...
gi 224831241 1890 QETRERI-LSGKLVRRAEKRLKE 1911
Cdd:pfam02463 999 RLEEEKKkLIRAIIEETCQRLKE 1021
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1602-2017 |
1.56e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1602 LRAQVTELEDEltaAEDAKLRLEVTVQALKTQHERDLQgrdeageeRRRQLAKQLRDAEVERDEERKQRTLAVAARKKLE 1681
Cdd:COG1196 198 LERQLEPLERQ---AEKAERYRELKEELKELEAELLLL--------KLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1682 GELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRAR 1761
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1762 RQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKA 1841
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1842 ESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERR 1921
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1922 VADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAqAGRRRLQRELEDVTESAESMNREVTTLRNRlRRGPLTFTTRTVRQV 2001
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA-LEAALAAALQNIVVEDDEVAAAAIEYLKAA-KAGRATFLPLDKIRA 584
|
410
....*....|....*.
gi 224831241 2002 FRLEEGVASDEEAEEA 2017
Cdd:COG1196 585 RAALAAALARGAIGAA 600
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1333-2018 |
2.10e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 79.33 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1333 RAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEaqlhDAQELLQEETRAKLAL-GSRVRAMEAEAAGLREQLE 1411
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAE----RYKELKAELRELELALlVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1412 EEAAARERAGRELQTAQAQLSEWRRRQEEeagaleageearrrAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDAt 1491
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSE--------------LEEEIEELQKELYALANEISRLEQQKQILRERLANL- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1492 mdLEQQRQLVSTLEKKQRKFDQLLAEEKAavlraveereraeaegrerearalsLTRALEEEQEAREELERQNRALRAEL 1571
Cdd:TIGR02168 315 --ERQLEELEAQLEELESKLDELAEELAE-------------------------LEEKLEELKEELESLEAELEELEAEL 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1572 EALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHER----DLQGRDEAGEE 1647
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkELQAELEELEE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1648 RRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEavkqLRKMQAQMKELWreveetrtsre 1727
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN----LEGFSEGVKALL----------- 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1728 eifsQNRESEKRLKGLEAEVLRLQEE----LAASDRARRQAQQDRDEMADEVA-----NGNLSKAAILEEK----RQLEG 1794
Cdd:TIGR02168 513 ----KNQSGLSGILGVLSELISVDEGyeaaIEAALGGRLQAVVVENLNAAKKAiaflkQNELGRVTFLPLDsikgTEIQG 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1795 RLGQLEEELEEEQSNSELL---NDRYRKLL-------LQVESLTT------ELSAERSF-----------------SAKA 1841
Cdd:TIGR02168 589 NDREILKNIEGFLGVAKDLvkfDPKLRKALsyllggvLVVDDLDNalelakKLRPGYRIvtldgdlvrpggvitggSAKT 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1842 ESGRQQLERQIQELRGRLgEEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERR 1921
Cdd:TIGR02168 669 NSSILERRREIEELEEKI-EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1922 VADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRRGPLTFTTRTVRQV 2001
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
730
....*....|....*..
gi 224831241 2002 FRLEEGVASDEEAEEAQ 2018
Cdd:TIGR02168 828 SLERRIAATERRLEDLE 844
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
915-1523 |
2.13e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.80 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 915 RAQELQKVQELQQ-QSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSEL----EARV 989
Cdd:PTZ00121 1183 KAEEVRKAEELRKaEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIrkfeEARM 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 990 GEEEECSRQMQTEKKRLQQHIQELEAHLEAEEG--ARQKLQLEKVTTEAK-MKKFEEDLLLLEDQNSKLSKERKLLEDRL 1066
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKKAEEKKKADEAkkAEEKKKADEAKKKAEeAKKADEAKKKAEEAKKKADAAKKKAEEAK 1342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1067 AEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRrldgeSSELQEQMVEQQQRAEELRAqlgRK 1146
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK-----ADEAKKKAEEDKKKADELKK---AA 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1147 EEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERvartKAEKQRRDLGEELEAlrGELEDTLDSTNAQQEL 1226
Cdd:PTZ00121 1415 AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK----KAEEAKKKAEEAKKA--DEAKKKAEEAKKADEA 1488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1227 RSKREQ---EVTELKKTLEEETRIHEA-------AVQELRQRHGQALGELAEQLEQARRG---KGAWEKTRLALEAEVSE 1293
Cdd:PTZ00121 1489 KKKAEEakkKADEAKKAAEAKKKADEAkkaeeakKADEAKKAEEAKKADEAKKAEEKKKAdelKKAEELKKAEEKKKAEE 1568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1294 LRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGAlnEAESKTIRLSKELSSTEA 1373
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA--EEEKKKVEQLKKKEAEEK 1646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1374 QlhDAQELLQEETRAKLALGSRVRAMEAEaaglreqleeeaAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARR 1453
Cdd:PTZ00121 1647 K--KAEELKKAEEENKIKAAEEAKKAEED------------KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1454 RAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDlEQQRQLVSTLEKKQRKFDQLLAEEKAAVL 1523
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
973-1275 |
1.05e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.02 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 973 ARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKL---QLEKVTTEAKMKKFEEDLLLLE 1049
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsalRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1050 DQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLnklrlkyEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQE-- 1127
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEEL-------EAQIEQLKEELKALREALDELRAELTLLNEEAANLRErl 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1128 -----QMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDL 1202
Cdd:TIGR02168 827 eslerRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224831241 1203 GEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARR 1275
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1184-2002 |
2.06e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.33 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1184 DLESERVARTKAEkqRRDLGEELEALRGELEDtldstNAQQELRSKREQEVTELKKTLEEETRIHEA--AVQELRQRHGQ 1261
Cdd:PTZ00121 1049 DEDIDGNHEGKAE--AKAHVGQDEGLKPSYKD-----FDFDAKEDNRADEATEEAFGKAEEAKKTETgkAEEARKAEEAK 1121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1262 ALGELAEQLEQARRGkgawEKTRLALEAEVSELRAELSSLQTARqegeqrrrrlELQLQEVQGRAGDGERAR-AEAAEKL 1340
Cdd:PTZ00121 1122 KKAEDARKAEEARKA----EDARKAEEARKAEDAKRVEIARKAE----------DARKAEEARKAEDAKKAEaARKAEEV 1187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1341 QRAQaELENVSGALNEAESKtiRLSKELSSTEAQLHDAQELLQEETRAKLAlgsRVRAMEAEAAGLREQLEEEAAARERA 1420
Cdd:PTZ00121 1188 RKAE-ELRKAEDARKAEAAR--KAEEERKAEEARKAEDAKKAEAVKKAEEA---KKDAEEAKKAEEERNNEEIRKFEEAR 1261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1421 GRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDAtmdleqqRQL 1500
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKA-------DAA 1334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1501 VSTLEKKQRKFDQLLAEEKAAvlraveereraeaegrerearalsltraleeeQEAREELERQNRALRAELEALLSSKDD 1580
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAA--------------------------------ADEAEAAEEKAEAAEKKKEEAKKKADA 1382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1581 VGKSVHELERACRVAEQAANDLRA--QVTELEDELTAAEDAKLRLEVTVQA----LKTQHERDLQGRDEAGEERRRQLAK 1654
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEEDKKKadELKKAAAAKKKADEAKKKAEEKKKAdeakKKAEEAKKADEAKKKAEEAKKAEEA 1462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1655 QLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVK--QLRKMQAQMK-ELWREVEETRTSREEifs 1731
Cdd:PTZ00121 1463 KKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadEAKKAEEAKKaDEAKKAEEAKKADEA--- 1539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1732 qnRESEKRLKgleAEVLRLQEELAASDRARRQAQQDRDEmadEVANGNLSKAAIL---EEKRQLEGRLGQLEEELEEEQS 1808
Cdd:PTZ00121 1540 --KKAEEKKK---ADELKKAEELKKAEEKKKAEEAKKAE---EDKNMALRKAEEAkkaEEARIEEVMKLYEEEKKMKAEE 1611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1809 NSELLNDRyrkllLQVESLTTElSAERSFSAKAESGRQQLERQIQELRGRlgEEDAGARARHKMTIAALESKlaQAEEQL 1888
Cdd:PTZ00121 1612 AKKAEEAK-----IKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKKA--EEENKIKAAEEAKKAEEDKK--KAEEAK 1681
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1889 EQETRERILSGKLVRRAE--KRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKR----------QLEEAEEEASRAQA 1956
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEeaKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKeaeedkkkaeEAKKDEEEKKKIAH 1761
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 224831241 1957 GRRRLQRELEDVTESAESMNREVTTLRNRLRRGPLTFTTRTVRQVF 2002
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNF 1807
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
931-1294 |
6.94e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.32 E-value: 6.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 931 REVGELQGRVAQLEEERARLAEQLRaeaelcaeaeetrgRLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHI 1010
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALA--------------ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1011 QELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKY 1090
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1091 EATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEE---LQAALARAEDEGGARAQL 1167
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNErasLEEALALLRSELEELSEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1168 LKSLREAQAALAEAQEDLESERVA-RTKAEKQRRDLGEELEALRGELEDTLD----STNAQQELRSKREQEVTELKKTLE 1242
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQlELRLEGLEVRIDNLQERLSEEYSLTLEeaeaLENKIEDDEEEARRRLKRLENKIK 982
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 224831241 1243 EETRIHEAAVQELRQRHGQaLGELAEQLEQARRGKGAWEKTRLALEAEVSEL 1294
Cdd:TIGR02168 983 ELGPVNLAAIEEYEELKER-YDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
922-1406 |
9.46e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 9.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 922 VQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELV---VSELEARVGEEEECSRQ 998
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLegsKRKLEEKIRELEERIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 999 MQTEKKRLQQHIQELEAHleaeegarQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEE 1078
Cdd:PRK03918 271 LKKEIEELEEKVKELKEL--------KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1079 KVKSLNKLRLKYEAtiadMEDRLRKEEKGRQ---ELEKLKRRLDGESSELQEQMVEQQQRAEElraQLGRKEEELQAALA 1155
Cdd:PRK03918 343 LKKKLKELEKRLEE----LEERHELYEEAKAkkeELERLKKRLTGLTPEKLEKELEELEKAKE---EIEEEISKITARIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1156 RAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAE---------KQRRDLGEELEALRGELEDTLDSTNAQQEL 1226
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEytaelkrieKELKEIEEKERKLRKELRELEKVLKKESEL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1227 RskREQEVTELKKTLEEETRIH-----EAAVQELRQRHGQALGELAEQ--LEQARRGKGAWEKTRLALEAEVSELRAELS 1299
Cdd:PRK03918 496 I--KLKELAEQLKELEEKLKKYnleelEKKAEEYEKLKEKLIKLKGEIksLKKELEKLEELKKKLAELEKKLDELEEELA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1300 SLQTARQEGE-QRRRRLELQLQEVQG------RAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSstE 1372
Cdd:PRK03918 574 ELLKELEELGfESVEELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE--E 651
|
490 500 510
....*....|....*....|....*....|....
gi 224831241 1373 AQLHDAQELLQEETRAKLALGSRVRAMEAEAAGL 1406
Cdd:PRK03918 652 LEKKYSEEEYEELREEYLELSRELAGLRAELEEL 685
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1028-1774 |
1.92e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.79 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1028 QLEKVTTEaKMKKFEEDLLLLEDQNSK---LSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKE 1104
Cdd:TIGR02169 199 QLERLRRE-REKAERYQALLKEKREYEgyeLLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1105 EKgrqeleKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARaedeggaRAQLLKSLREAQAALAEAQED 1184
Cdd:TIGR02169 278 NK------KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEER-------LAKLEAEIDKLLAEIEELERE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1185 LESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQaLG 1264
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEE-LA 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1265 ELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGER------ARAEAAE 1338
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRelaeaeAQARASE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1339 KLQRAQAELENVSGALNEAESKTI--------------------RLSKELSSTEAQLHDAQELLQEET--RAKLALGSRV 1396
Cdd:TIGR02169 504 ERVRGGRAVEEVLKASIQGVHGTVaqlgsvgeryataievaagnRLNNVVVEDDAVAKEAIELLKRRKagRATFLPLNKM 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1397 RAMEAEAAGLREQLEEEAA------------------ARERAGRELQTAQAQLSEWRR-----RQEEEAGALEAGEEARR 1453
Cdd:TIGR02169 584 RDERRDLSILSEDGVIGFAvdlvefdpkyepafkyvfGDTLVVEDIEAARRLMGKYRMvtlegELFEKSGAMTGGSRAPR 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1454 RAAREAEALTQRLAEKTETVDRLERGRRRLQQE--------------LDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEK 1519
Cdd:TIGR02169 664 GGILFSRSEPAELQRLRERLEGLKRELSSLQSElrrienrldelsqeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELE 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1520 AAVLRAVEERERAEAEGREREARALSLTRALEEEQEAReelerqnralrAELEALLSskddvgksvheleracrvaeqaa 1599
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL-----------NDLEARLS----------------------- 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1600 ndlRAQVTELEDELTAAEDAKLRLEVTVQALKtQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKK 1679
Cdd:TIGR02169 790 ---HSRIPEIQAELSKLEEEVSRIEARLREIE-QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1680 LEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREeifsqnrESEKRLKGLEAEVLRLQEELAASDR 1759
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE-------KKRKRLSELKAKLEALEEELSEIED 938
|
810
....*....|....*
gi 224831241 1760 ARRQAQQDRDEMADE 1774
Cdd:TIGR02169 939 PKGEDEEIPEEELSL 953
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
907-1368 |
4.68e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.10 E-value: 4.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 907 RQDEVLQARAQELQKVQELQQQsAREVGELQGRVAQLEEERARlAEQLRAEAELCAEAEETRGRLAARKQELELVVSELE 986
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKADEAKKK-AEEDKKKADELKKAAAAKKK-ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 987 ARVGEE----EECSRQMQTEKKRLQQhiqeleahleaeegARQKLQLEKVTTEAKMKKfeEDLLLLEDQNSKLSKERKLL 1062
Cdd:PTZ00121 1456 AKKAEEakkkAEEAKKADEAKKKAEE--------------AKKADEAKKKAEEAKKKA--DEAKKAAEAKKKADEAKKAE 1519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1063 EDRLAEfSSQAAEEEEKVKSLNKLRLKYEAtiadmeDRLRKEEKGRQELEKLKrrldgesselqeqmVEQQQRAEELRAQ 1142
Cdd:PTZ00121 1520 EAKKAD-EAKKAEEAKKADEAKKAEEKKKA------DELKKAEELKKAEEKKK--------------AEEAKKAEEDKNM 1578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1143 LGRKEEELQAAlaraedeggARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNA 1222
Cdd:PTZ00121 1579 ALRKAEEAKKA---------EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1223 QQELRSKREQEV--TELKKTLEEETRIHEAAVQELRQRHGQalgelAEQLEQARRGKGAWEKTRLALEAEVSelRAElsS 1300
Cdd:PTZ00121 1650 EELKKAEEENKIkaAEEAKKAEEDKKKAEEAKKAEEDEKKA-----AEALKKEAEEAKKAEELKKKEAEEKK--KAE--E 1720
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224831241 1301 LQTARQEGEQRRRRLELQLQEVQGRAgdgERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKEL 1368
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKA---EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
851-1387 |
4.80e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.71 E-value: 4.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 851 FQAAARGYLARRAFQKRQQQQSALRVMqrncaaylKLRHWQWWRLFTKVKPLLQVTRQDEVlqaRAQELQKVQELQQ-QS 929
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEAKKDAEEAKKAE--------EERNNEEIRKFEEARMAHFARRQAAI---KAEEARKADELKKaEE 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 930 AREVGELQgrvaqlEEERARLAEQL-------RAEAELCAEAEETRGRLAARKQELELVVSELEARVGEEEECSRQMQTE 1002
Cdd:PTZ00121 1289 KKKADEAK------KAEEKKKADEAkkkaeeaKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1003 KKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKmKKFEEDLLLLEDQNSKLSK-------ERKLLEDRLAEFSSQAAE 1075
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK-KKAEEDKKKADELKKAAAAkkkadeaKKKAEEKKKADEAKKKAE 1441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1076 EEEKVKSLNKlrlKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELR--AQLGRKEEELQAA 1153
Cdd:PTZ00121 1442 EAKKADEAKK---KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKkaAEAKKKADEAKKA 1518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1154 LARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRdlgeeLEALRGELEDTLDSTNAQQELRSKREQE 1233
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK-----AEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1234 VTELKKTLEEETRIheaAVQELRQRHGQALGelAEQLEQARRGKGAWEKTRLALEAEV---SELRAELSSLQTARQEGEQ 1310
Cdd:PTZ00121 1594 IEEVMKLYEEEKKM---KAEEAKKAEEAKIK--AEELKKAEEEKKKVEQLKKKEAEEKkkaEELKKAEEENKIKAAEEAK 1668
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224831241 1311 RRRRLELQLQEVQgRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETR 1387
Cdd:PTZ00121 1669 KAEEDKKKAEEAK-KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1225-1982 |
5.25e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 71.64 E-value: 5.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1225 ELRSKREQEVTELKkTLEEETRIHEAAVQELRQRhgqaLGELAEQLEQARRGKGAWEKTRlalEAEVSELRAELSSLQTA 1304
Cdd:TIGR02169 167 EFDRKKEKALEELE-EVEENIERLDLIIDEKRQQ----LERLRREREKAERYQALLKEKR---EYEGYELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1305 RQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENV-SGALNEAESKTIRLSKELSSTEAQLHDAQELLQ 1383
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1384 --EETRAKLAlgSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRaareaea 1461
Cdd:TIGR02169 319 daEERLAKLE--AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD------- 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1462 LTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLaEEKAAVLRAveereraeaegrerea 1541
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK-EDKALEIKK---------------- 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1542 ralsLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDEL-------- 1613
Cdd:TIGR02169 453 ----QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtva 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1614 ----------TAAEDAK-LRL--------EVTVQALK------------------TQHERDLQGRDEAG----------- 1645
Cdd:TIGR02169 529 qlgsvgeryaTAIEVAAgNRLnnvvveddAVAKEAIEllkrrkagratflplnkmRDERRDLSILSEDGvigfavdlvef 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1646 EERRRQLAKQ-LRDAEVERDEERKQRTLAVAARKKLEGELEE---------------------LKAQMASAGQGKEEAVK 1703
Cdd:TIGR02169 609 DPKYEPAFKYvFGDTLVVEDIEAARRLMGKYRMVTLEGELFEksgamtggsraprggilfsrsEPAELQRLRERLEGLKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1704 QLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQ----DRDEMAD---EVA 1776
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQeienVKSELKEleaRIE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1777 NGNLSKAAILEEKRQLEGRLGQLEEELEEEQSNSelLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELR 1856
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSHSRIPEIQAELSK--LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1857 GRLGEEDAgararhkmTIAALESKLAQAEEQLEQ-ETRERILSGKLVRRAEKRlKEVVLQVEEERRVADQLRDQLEKGNL 1935
Cdd:TIGR02169 847 EQIKSIEK--------EIENLNGKKEELEEELEElEAALRDLESRLGDLKKER-DELEAQLRELERKIEELEAQIEKKRK 917
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 224831241 1936 RVKQLKRQLEEAEEEASRAQAGRRRLQRE------LEDVTESAESMNREVTTL 1982
Cdd:TIGR02169 918 RLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRAL 970
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
907-1243 |
6.59e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 71.25 E-value: 6.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 907 RQDEVLQARAQELQKVQELQqqsaREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELE 986
Cdd:TIGR02169 703 RLDELSQELSDASRKIGEIE----KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 987 ARVGEEE-----ECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKL 1061
Cdd:TIGR02169 779 EALNDLEarlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1062 LEDRLAEFSSQAAEeeekvkslnklrlkYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRA 1141
Cdd:TIGR02169 859 LNGKKEELEEELEE--------------LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1142 QLGRKEEELqAALARAEDEGGARAQLLKSLReaqaalaeaqedleservartKAEKQRRDLGEELEALRG-------ELE 1214
Cdd:TIGR02169 925 KLEALEEEL-SEIEDPKGEDEEIPEEELSLE---------------------DVQAELQRVEEEIRALEPvnmlaiqEYE 982
|
330 340
....*....|....*....|....*....
gi 224831241 1215 DTLDSTNAQQELRSKREQEVTELKKTLEE 1243
Cdd:TIGR02169 983 EVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1594-1988 |
5.04e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1594 VAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEeRKQRtla 1673
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEE-RERR--- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1674 vaaRKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTsreEIFSQNRESEKRLKGLEAEVLRLQ-- 1751
Cdd:COG4913 361 ---RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA---EAEAALRDLRRELRELEAEIASLErr 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1752 ------EELAASDRARRQAQQDRDEM----------ADE-------------------VANGNLSKAAILEEKRQLEGRL 1796
Cdd:COG4913 435 ksnipaRLLALRDALAEALGLDEAELpfvgelievrPEEerwrgaiervlggfaltllVPPEHYAAALRWVNRLHLRGRL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1797 GQLEEELEEEQSNSELLNDR--YRKLLLQVESLTTELSAE--RSFS-AKAESGRQ--QLERQIQE-----LRGRLGEEDA 1864
Cdd:COG4913 515 VYERVRTGLPDPERPRLDPDslAGKLDFKPHPFRAWLEAElgRRFDyVCVDSPEElrRHPRAITRagqvkGNGTRHEKDD 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1865 ----------GARARHKmtIAALESKLAQAEEQLEQ-ETRERILSGKL-----VRRAEKRLKEV------VLQVEEERRV 1922
Cdd:COG4913 595 rrrirsryvlGFDNRAK--LAALEAELAELEEELAEaEERLEALEAELdalqeRREALQRLAEYswdeidVASAEREIAE 672
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224831241 1923 ADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1988
Cdd:COG4913 673 LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
970-1373 |
5.88e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.78 E-value: 5.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 970 RLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLqlEKVTTEAK-MKKFEEDLLLL 1048
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL--EKLEKEVKeLEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1049 EDQNSKLSKERKLLEDRLAEFSSQAAEE-------EEKVKSLNKLRLKYEATIAdMEDRLRKEEKGRQELEKLKRRLDGE 1121
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELkkeieelEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1122 SSELQEQMVEQQQRAEELRaQLGRKEEELQAALARAEDeggaRAQLLKSLREAQAalaeaqedlESERVARTKAEKQRRD 1201
Cdd:PRK03918 323 INGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEE----RHELYEEAKAKKE---------ELERLKKRLTGLTPEK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1202 LGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEE---ETRIHEAAVQELRQRH-GQALGELAEQLEQArrgk 1277
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkAKGKCPVCGRELTEEHrKELLEEYTAELKRI---- 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1278 gawEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLEL--QLQEVQgragdgERARAEAAEKLQRAQAELENVSGALN 1355
Cdd:PRK03918 465 ---EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELE------EKLKKYNLEELEKKAEEYEKLKEKLI 535
|
410
....*....|....*...
gi 224831241 1356 EAESKTIRLSKELSSTEA 1373
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEE 553
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1116-1886 |
6.84e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.24 E-value: 6.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1116 RRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKA 1195
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAE 1149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1196 EKQRRDLGEELEALRgELEDTLDSTNAQQELRSKREQEV---TELKKTlEEETRIHEA-AVQELRQRHGQALGELAEQLE 1271
Cdd:PTZ00121 1150 DAKRVEIARKAEDAR-KAEEARKAEDAKKAEAARKAEEVrkaEELRKA-EDARKAEAArKAEEERKAEEARKAEDAKKAE 1227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1272 QARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRlelqlqevqgrAGDGERARaeAAEKLQRAqaelENVS 1351
Cdd:PTZ00121 1228 AVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA-----------AIKAEEAR--KADELKKA----EEKK 1290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1352 GALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKlalgSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQl 1431
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK----KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK- 1365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1432 SEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERgRRRLQQELDDATMDLEQQRQLVSTLEKKQRKF 1511
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK-AAAAKKKADEAKKKAEEKKKADEAKKKAEEAK 1444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1512 DQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERA 1591
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA 1524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1592 --CRVAEQA--ANDLR-AQVTELEDELTAAEDAKLRLEVtvqalKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEE 1666
Cdd:PTZ00121 1525 deAKKAEEAkkADEAKkAEEKKKADELKKAEELKKAEEK-----KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1667 RKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMK---ELWREVEETRTSREEIFSQNRESEKR---- 1739
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkkaEELKKAEEENKIKAAEEAKKAEEDKKkaee 1679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1740 LKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAilEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRK 1819
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA--EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224831241 1820 LLLQVeslttelsaERSFSAKAESGRQQLERQIQElrgRLGEEDAGARARHKMTIAALESKLAQAEE 1886
Cdd:PTZ00121 1758 KIAHL---------KKEEEKKAEEIRKEKEAVIEE---ELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1107-1917 |
1.72e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 66.68 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1107 GRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSlreaqaalaeaqedle 1186
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRR---------------- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1187 sERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQElrskreqevtELKKTLEEetriHEAAVQELRQrhgqalgeL 1266
Cdd:pfam15921 136 -ESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIE----------QLRKMMLS----HEGVLQEIRS--------I 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1267 AEQLEQARrGKGAWEKTRLA------LEAEVSELraeLSSLQTARQEGEQRRRRLELQLqevqgragdgERARAEAAEK- 1339
Cdd:pfam15921 193 LVDFEEAS-GKKIYEHDSMStmhfrsLGSAISKI---LRELDTEISYLKGRIFPVEDQL----------EALKSESQNKi 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1340 ---LQRAQAELENVsgaLNEAESKTIRLSKELSSTEAQLHDAQ---ELLQEETRAKLALGSR-VRAMEAEAAGLREQLEE 1412
Cdd:pfam15921 259 ellLQQHQDRIEQL---ISEHEVEITGLTEKASSARSQANSIQsqlEIIQEQARNQNSMYMRqLSDLESTVSQLRSELRE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1413 EAAARERAGRELQT----AQAQLSEWRRRQEE---EAGALE-----------AGEEARRRAAREAEALTQRLAEKTETVD 1474
Cdd:pfam15921 336 AKRMYEDKIEELEKqlvlANSELTEARTERDQfsqESGNLDdqlqklladlhKREKELSLEKEQNKRLWDRDTGNSITID 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1475 RLERgrrrlqqELDDATMDLEQQRQLVSTLEKK-QRKFDQLLAEEKAavlraveereraeaegrerearalsltraleee 1553
Cdd:pfam15921 416 HLRR-------ELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQG--------------------------------- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1554 qeaREELERQNRALRAELEallSSKDDVGKSVHEL---ERACRVAEQAANDLRAQVTELED--ELTAAEDAKLRLEVTVQ 1628
Cdd:pfam15921 456 ---KNESLEKVSSLTAQLE---STKEMLRKVVEELtakKMTLESSERTVSDLTASLQEKERaiEATNAEITKLRSRVDLK 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1629 ALKTQHerdLQGRDEageerrrqlakQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKM 1708
Cdd:pfam15921 530 LQELQH---LKNEGD-----------HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQL 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1709 QAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEE 1788
Cdd:pfam15921 596 EKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSED 675
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1789 KRQLEGRLGQLEEELEEEQsnsellndryRKLLLQVESLTTELSAERSFSAKAESGRQQ-------LERQIQELRGRLG- 1860
Cdd:pfam15921 676 YEVLKRNFRNKSEEMETTT----------NKLKMQLKSAQSELEQTRNTLKSMEGSDGHamkvamgMQKQITAKRGQIDa 745
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224831241 1861 --------EEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVE 1917
Cdd:pfam15921 746 lqskiqflEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
932-1295 |
1.05e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 932 EVGELQGRVAQLEEERARLAEQLRAEAELCAEAeetRGRLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQ 1011
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDEL---SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1012 eleahleaeegarqklqlEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEfsSQAAEEEEKVKSLNKLRLKYE 1091
Cdd:TIGR02169 752 ------------------EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1092 ATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAqllksl 1171
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG------ 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1172 reaqaalaeaqeDLESErvaRTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAA 1251
Cdd:TIGR02169 886 ------------DLKKE---RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE 950
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 224831241 1252 -----VQELRQRHGQALGELA-------EQLEQARRGKGAWEKTRLALEAEVSELR 1295
Cdd:TIGR02169 951 lsledVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1127-1897 |
1.36e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1127 EQMVEQQQRAEELRAQLgRKEEELQAALARAEDEGGARAQLLKSLREAqaalaeaqeDLESERVARTKAEKQRRDLGEEL 1206
Cdd:COG4913 228 DALVEHFDDLERAHEAL-EDAREQIELLEPIRELAERYAAARERLAEL---------EYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1207 EALRGELEDTldstnaqqelrskrEQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLA 1286
Cdd:COG4913 298 EELRAELARL--------------EAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1287 LEAEVSELRAEL----SSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENV-SGALN-EAESK 1360
Cdd:COG4913 364 LEALLAALGLPLpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLeRRKSNiPARLL 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1361 TIR--LSKELSSTEAQLHDAQELLQ---EETR----AKLALGSRVRAM------EAEAAglreqleeEAAARERAGRELQ 1425
Cdd:COG4913 444 ALRdaLAEALGLDEAELPFVGELIEvrpEEERwrgaIERVLGGFALTLlvppehYAAAL--------RWVNRLHLRGRLV 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1426 TAQAQLS-EWRRRQEEEAGALEAGEEARRRAARE--AEALTQRLA-EKTETVDRLERGRRRLQQ-----------ELDDA 1490
Cdd:COG4913 516 YERVRTGlPDPERPRLDPDSLAGKLDFKPHPFRAwlEAELGRRFDyVCVDSPEELRRHPRAITRagqvkgngtrhEKDDR 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1491 TmDLEQQRQL-VSTLEKKQRKFDQL-LAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALR 1568
Cdd:COG4913 596 R-RIRSRYVLgFDNRAKLAALEAELaELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1569 AELEALLSSKDDVGksvhELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDlqgRDEAGEER 1648
Cdd:COG4913 675 AELERLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA---EDLARLEL 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1649 RRQLAKQLRDAEVERDEERkqrtlavaARKKLEGELEELKAQMAsagqgkeEAVKQLRKMQAQMKELWR-EVEETRTSRE 1727
Cdd:COG4913 748 RALLEERFAAALGDAVERE--------LRENLEERIDALRARLN-------RAEEELERAMRAFNREWPaETADLDADLE 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1728 EifsqNRESEKRLKGLEAEVL-RLQEELAasDRARRQAQQDRdemadevanGNLSkAAILEEKRQLEGRLGQleeeleee 1806
Cdd:COG4913 813 S----LPEYLALLDRLEEDGLpEYEERFK--ELLNENSIEFV---------ADLL-SKLRRAIREIKERIDP-------- 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1807 qsnselLNDRYRKL------LLQVESLTTELSAERSFsakaesgrqqlERQIQELRGRLGEEDAGARARHKMTIAALESK 1880
Cdd:COG4913 869 ------LNDSLKRIpfgpgrYLRLEARPRPDPEVREF-----------RQELRAVTSGASLFDEELSEARFAALKRLIER 931
|
810
....*....|....*..
gi 224831241 1881 LAQAEEQLEQETRERIL 1897
Cdd:COG4913 932 LRSEEEESDRRWRARVL 948
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1568-1986 |
1.48e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1568 RAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHErDLQGRDEAGEE 1647
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE-ELEDRDEELRD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1648 RrrqlakqLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSRE 1727
Cdd:PRK02224 329 R-------LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1728 EIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNL----------SKAAILEEKRQ----LE 1793
Cdd:PRK02224 402 DAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpecgqpvegsPHVETIEEDRErveeLE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1794 GRLGQLEEELEEEQSNSELLNDrYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARARHKM- 1872
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAa 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1873 ------------TIAALESKLAQAEEQLEQ-ETRERILSgkLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQ 1939
Cdd:PRK02224 561 aeaeeeaeeareEVAELNSKLAELKERIESlERIRTLLA--AIADAEDEIERLREKREALAELNDERRERLAEKRERKRE 638
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 224831241 1940 LKRQLeeAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRL 1986
Cdd:PRK02224 639 LEAEF--DEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEI 683
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
997-1295 |
1.66e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 63.22 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 997 RQMQTEKKRLQQH-IQELEAHLEAEEGARQKLQLEKVTTEAKMKKfeEDLLLLEDQNSKLSKERKL----LEDRLAEF-- 1069
Cdd:pfam17380 287 RQQQEKFEKMEQErLRQEKEEKAREVERRRKLEEAEKARQAEMDR--QAAIYAEQERMAMERERELerirQEERKRELer 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1070 --SSQAAEEEEKVKSLNKLRLkyeatiadmeDRLRKEEKGRQELE---KLKRRLDGESSELQEQMVEQQQ-RAEELRA-- 1141
Cdd:pfam17380 365 irQEEIAMEISRMRELERLQM----------ERQQKNERVRQELEaarKVKILEEERQRKIQQQKVEMEQiRAEQEEArq 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1142 -QLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEElealrgELEDTLDST 1220
Cdd:pfam17380 435 rEVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK------ELEERKQAM 508
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224831241 1221 NAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRgkgawEKTRL-ALEAEVSELR 1295
Cdd:pfam17380 509 IEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE-----ERSRLeAMEREREMMR 579
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
917-1220 |
3.09e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 62.06 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 917 QELQKVQELQQQSAREVGElQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAA-----------RKQELELVVSEL 985
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKME-QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAiyaeqermameRERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 986 EAR----VGEEE---ECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKE 1058
Cdd:pfam17380 358 RKRelerIRQEEiamEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1059 RKLLEDRLAEFSSQAAEEEEKVKSLNKLRlKYEATIADMEDRLRKEEKGRQELEKLKRR-LDGESSELQEQMVEQQQRae 1137
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLR-QQEEERKRKKLELEKEKRDRKRAEEQRRKiLEKELEERKQAMIEEERK-- 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1138 elRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEEL---EALRGELE 1214
Cdd:pfam17380 515 --RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIvesEKARAEYE 592
|
....*.
gi 224831241 1215 DTLDST 1220
Cdd:pfam17380 593 ATTPIT 598
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
912-1349 |
5.86e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 5.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 912 LQARAQELQKVQELQQQSAREVGELQGRVAQLE---EERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEAR 988
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKELKELKekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 989 VGEEEECSRqmqtEKKRLQQHIQELEAHLEAEEGARQKL----QLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLED 1064
Cdd:PRK03918 337 EERLEELKK----KLKELEKRLEELEERHELYEEAKAKKeeleRLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1065 RLAEFSSQAAEEEEKVKSLNK-------------------LRLKYEATIADMEDRLR----KEEKGRQELEKLKRRLDGE 1121
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkeLLEEYTAELKRIEKELKeieeKERKLRKELRELEKVLKKE 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1122 S----------------SELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDL 1185
Cdd:PRK03918 493 SeliklkelaeqlkeleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEEL 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1186 ES-ERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRS---KREQEVTELKKTLEEETRIhEAAVQELRQRHGQ 1261
Cdd:PRK03918 573 AElLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEReekELKKLEEELDKAFEELAET-EKRLEELRKELEE 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1262 ALGELAEQLEQARRGKgawektRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVqgragdgERARAEaAEKLQ 1341
Cdd:PRK03918 652 LEKKYSEEEYEELREE------YLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER-------EKAKKE-LEKLE 717
|
....*...
gi 224831241 1342 RAQAELEN 1349
Cdd:PRK03918 718 KALERVEE 725
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1050-1287 |
8.78e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 8.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1050 DQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQM 1129
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1130 VEQQQR-AEELRAQLGRKEEELQAALARAEDEGGA--RAQLLKSL-REAQAALAEAQEDLESERVARTKAEKQRrdlgEE 1205
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLALLLSPEDFLDAvrRLQYLKYLaPARREQAEELRADLAELAALRAELEAER----AE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1206 LEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRL 1285
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
..
gi 224831241 1286 AL 1287
Cdd:COG4942 256 PW 257
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1600-1982 |
9.90e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 9.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1600 NDLRAQVTELEDELTAAEDAKLRLEVTVQALK---TQHERDLQGRDEAGEERRrQLAKQLRDAEVERDEERKQRTLAVAA 1676
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIE-DLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1677 RKKLEGELEELKAQmASAGQGKEEAVKQLRK-MQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELA 1755
Cdd:PRK02224 288 LEELEEERDDLLAE-AGLDDADAEAVEARREeLEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1756 ASDRARRQAQQDRDEMADEVAngnlskaAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAER 1835
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIE-------ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1836 SFSAKAESGR---------QQLERQ-----IQELRGRLGEEDAgARARHKMTIAALESKLAQAEEQLEQETRerilsgkl 1901
Cdd:PRK02224 440 ERVEEAEALLeagkcpecgQPVEGSphvetIEEDRERVEELEA-ELEDLEEEVEEVEERLERAEDLVEAEDR-------- 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1902 VRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLEEAEEE----ASRAQAGRRR---LQRELEDVTESAES 1974
Cdd:PRK02224 511 IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAaaeaEEEAEEAREEvaeLNSKLAELKERIES 590
|
....*...
gi 224831241 1975 MNREVTTL 1982
Cdd:PRK02224 591 LERIRTLL 598
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
967-1367 |
2.07e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.70 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 967 TRGRLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLL 1046
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1047 LLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKslnklrlKYEATIADMEDRLRKEEkgrqeleklKRRLDGESSELQ 1126
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLH-------KLEEALNDLEARLSHSR---------IPEIQAELSKLE 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1127 EQMVEQQQRAEELRAQLGRKEEELQAalarAEDEggaraqllkslreaqaalaeaQEDLESERVArtkAEKQRRDLGEEL 1206
Cdd:TIGR02169 805 EEVSRIEARLREIEQKLNRLTLEKEY----LEKE---------------------IQELQEQRID---LKEQIKSIEKEI 856
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1207 EALRGELEDtldsTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRhgqaLGELAEQLEQARRGKGAWEKTRLA 1286
Cdd:TIGR02169 857 ENLNGKKEE----LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK----IEELEAQIEKKRKRLSELKAKLEA 928
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1287 LEAEVSELRAELSSLQTaRQEGEQRRRRLELQLQEVQgragdgerARAEAAEKLQ-RAQAELENVSGALNEAESKTIRLS 1365
Cdd:TIGR02169 929 LEEELSEIEDPKGEDEE-IPEEELSLEDVQAELQRVE--------EEIRALEPVNmLAIQEYEEVLKRLDELKEKRAKLE 999
|
..
gi 224831241 1366 KE 1367
Cdd:TIGR02169 1000 EE 1001
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1392-1940 |
3.50e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1392 LGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEA---GALEAGEEARRRAAREAEALTQRLAE 1468
Cdd:PRK02224 204 LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELEtleAEIEDLRETIAETEREREELAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1469 KTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEEREraeaegrerearalSLTR 1548
Cdd:PRK02224 284 LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAE--------------SLRE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1549 ALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQ 1628
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1629 ALKTqherDLQGRDEAGEERRRQLA--------KQLRDAE-VERDEERKQRtlavaaRKKLEGELEELKAQMASAGQgKE 1699
Cdd:PRK02224 430 ELEA----TLRTARERVEEAEALLEagkcpecgQPVEGSPhVETIEEDRER------VEELEAELEDLEEEVEEVEE-RL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1700 EAVKQLRKMQAQMKELwrevEETRTSREEIFSQNRES--EKRLKgleAEVLRLQ-EELAASDRARRQAQQDRDEMADEVA 1776
Cdd:PRK02224 499 ERAEDLVEAEDRIERL----EERREDLEELIAERRETieEKRER---AEELRERaAELEAEAEEKREAAAEAEEEAEEAR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1777 ngnlskaailEEKRQLEGRLGQLEEELEEEqsnsellnDRYRKLLLQVESLTTELSAERS-FSAKAESGRQQLERqIQEL 1855
Cdd:PRK02224 572 ----------EEVAELNSKLAELKERIESL--------ERIRTLLAAIADAEDEIERLREkREALAELNDERRER-LAEK 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1856 RGR---LGEEDAGARarhkmtIAALESKLAQAEEQLEQetreriLSGKLVRRAEKR--LKEVVLQVEEERRVADQLRDQL 1930
Cdd:PRK02224 633 RERkreLEAEFDEAR------IEEAREDKERAEEYLEQ------VEEKLDELREERddLQAEIGAVENELEELEELRERR 700
|
570
....*....|
gi 224831241 1931 EKGNLRVKQL 1940
Cdd:PRK02224 701 EALENRVEAL 710
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1056-1394 |
4.78e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1056 SKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQR 1135
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1136 AEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVartkaeKQRRDLGEELEALRGELED 1215
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI------PEIQAELSKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1216 TLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRgkgawektrlaLEAEVSELR 1295
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE-----------LEAALRDLE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1296 AELSSLQtarqegeQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAEsKTIRLSKELSSTEAQL 1375
Cdd:TIGR02169 882 SRLGDLK-------KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELSL 953
|
330
....*....|....*....
gi 224831241 1376 HDAQELLQEETRAKLALGS 1394
Cdd:TIGR02169 954 EDVQAELQRVEEEIRALEP 972
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1054-1513 |
5.14e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1054 KLSKERKLLEdRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEkgRQELEKLKRRLDGESSELQEQMVEQQ 1133
Cdd:COG4913 246 DAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE--LEELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1134 QRAEELRAQL----GRKEEELQAALARAEDEGGARAQLLKSL----------------------REAQAALAEAQEDLES 1187
Cdd:COG4913 323 EELDELEAQIrgngGDRLEQLEREIERLERELEERERRRARLeallaalglplpasaeefaalrAEAAALLEALEEELEA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1188 ERVARTKAEKQRRDLGEELEALRGELEdtldstnaqqELRSKR---EQEVTELKKTLEEETRIHEAAVQ------ELRQR 1258
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEAEIA----------SLERRKsniPARLLALRDALAEALGLDEAELPfvgeliEVRPE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1259 ------------HGQALGEL--AEQLEQARRgkgAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQG 1324
Cdd:COG4913 473 eerwrgaiervlGGFALTLLvpPEHYAAALR---WVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1325 -----------------------------RAG-----------DGERARAE-------AAEKLQRAQAELENVSGALNEA 1357
Cdd:COG4913 550 wleaelgrrfdyvcvdspeelrrhpraitRAGqvkgngtrhekDDRRRIRSryvlgfdNRAKLAALEAELAELEEELAEA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1358 ESKTIRLSKELSSTEAQLHDAQELLQ------------------EETRAKLALGS-RVRAMEAEAAGLREQLEEEAAARE 1418
Cdd:COG4913 630 EERLEALEAELDALQERREALQRLAEyswdeidvasaereiaelEAELERLDASSdDLAALEEQLEELEAELEELEEELD 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1419 RAGRELQTAQAQLSEWRRRQEEEAGALeaGEEARRRAAREAEALTQRLAEktETVDRLERG-RRRLQQELDDATmdlEQQ 1497
Cdd:COG4913 710 ELKGEIGRLEKELEQAEEELDELQDRL--EAAEDLARLELRALLEERFAA--ALGDAVERElRENLEERIDALR---ARL 782
|
570
....*....|....*.
gi 224831241 1498 RQLVSTLEKKQRKFDQ 1513
Cdd:COG4913 783 NRAEEELERAMRAFNR 798
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1043-1775 |
8.00e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 57.67 E-value: 8.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1043 EDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEeeKVKSLNKLRLKYEATIADMEDRLRK----EEKGRQELEKLKRRL 1118
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPC--MPDTYHERKQVLEKELKHLREALQQtqqsHAYLTQKREAQEEQL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1119 DGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQ 1198
Cdd:TIGR00618 257 KKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1199 RRDLGEELEALRGELEDTLDSTNAQQELRSKREQevteLKKTLEEETRIHeaAVQELRQRHGQALGELAEQLEQARRGKG 1278
Cdd:TIGR00618 337 QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREI----SCQQHTLTQHIH--TLQQQKTTLTQKLQSLCKELDILQREQA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1279 awekTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAE 1358
Cdd:TIGR00618 411 ----TIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQET 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1359 SKtirlskelssteAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLsewRRRQ 1438
Cdd:TIGR00618 487 RK------------KAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDV---YHQL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1439 EEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDdatMDLEQQRQLVSTLEKKQRKFDQLLA-E 1517
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTE---KLSEAEDMLACEQHALLRKLQPEQDlQ 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1518 EKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELER---ACRV 1594
Cdd:TIGR00618 629 DVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQcqtLLRE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1595 AEQAANDLRAQVTELEDELTAAedaklrlevtvqalktqhERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAV 1674
Cdd:TIGR00618 709 LETHIEEYDREFNEIENASSSL------------------GSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEV 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1675 AARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEK----RLKGLEAEVLRL 1750
Cdd:TIGR00618 771 TAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLsrleEKSATLGEITHQ 850
|
730 740
....*....|....*....|....*
gi 224831241 1751 QEELAASDRARRQAQQDRDEMADEV 1775
Cdd:TIGR00618 851 LLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1024-1793 |
2.60e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1024 RQKLQLEKVTTEAK-MKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLR 1102
Cdd:PRK03918 152 RQILGLDDYENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1103 KEEKGRQELEKLKRR---LDGESSELQEQMVEQQQRAEELRAqlgrKEEELQAALARaedeggaraqlLKSLREAQAALA 1179
Cdd:PRK03918 232 ELEELKEEIEELEKElesLEGSKRKLEEKIRELEERIEELKK----EIEELEEKVKE-----------LKELKEKAEEYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1180 EAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQ---EVTELKKTLE--EETRIHEAAVQE 1254
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHElyEEAKAKKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1255 LRQRH-GQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQegeqrrrrlelQLQEVQGRAGDGERAR 1333
Cdd:PRK03918 377 LKKRLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE-----------ELKKAKGKCPVCGREL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1334 AEAAEK--LQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLalgsrVRAMEAEAAGLREqle 1411
Cdd:PRK03918 446 TEEHRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQ-----LKELEEKLKKYNL--- 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1412 eeaaareragrelqtaqaqlsewrrrqeeeagaleageearrraareaealtQRLAEKTETVDRLERGRRRLQQELDDAT 1491
Cdd:PRK03918 518 ----------------------------------------------------EELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1492 MDLEQQRQLVSTLEKKQRKFDQLlaEEKAAVLraveereraeaegrerearalsltraleeeqeareelerqnraLRAEL 1571
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDEL--EEELAEL-------------------------------------------LKELE 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1572 EALLSSKDDVGKSVHELERACRvaeqAANDLRAQVTELEDELTAAEDAKLRLEvtvqalktQHERDLQGRDEAGEERRrq 1651
Cdd:PRK03918 581 ELGFESVEELEERLKELEPFYN----EYLELKDAEKELEREEKELKKLEEELD--------KAFEELAETEKRLEELR-- 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1652 laKQLRDAEVERDEERkqrtlavaaRKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFS 1731
Cdd:PRK03918 647 --KELEELEKKYSEEE---------YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224831241 1732 QNRESEkRLKGLEAEVLRLQEELAasDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLE 1793
Cdd:PRK03918 716 LEKALE-RVEELREKVKKYKALLK--ERALSKVGEIASEIFEELTEGKYSGVRVKAEENKVK 774
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1062-1869 |
3.44e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.89 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1062 LEDRLAEFSSQAAEEEEKVKSLNKLRLKYE----ATIADMEDRLRKEEKGRQELEKLKRRldgesselqeqmveQQQRAE 1137
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELHEKQKfylrQSVIDLQTKLQEMQMERDAMADIRRR--------------ESQSQE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1138 ELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQR------------------ 1199
Cdd:pfam15921 142 DLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKiyehdsmstmhfrslgsa 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1200 -----RDLGEELEALRGEL---EDTLDSTNAqqELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGE---LAE 1268
Cdd:pfam15921 222 iskilRELDTEISYLKGRIfpvEDQLEALKS--ESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1269 QLE----QARRGKGAWEKTRLALEAEVSELRAELsslQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAE------ 1338
Cdd:pfam15921 300 QLEiiqeQARNQNSMYMRQLSDLESTVSQLRSEL---REAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQesgnld 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1339 -KLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAAR 1417
Cdd:pfam15921 377 dQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGK 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1418 ERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQ 1497
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1498 RQLVSTLEKKQRKFDQLLAE--EKAAVLRAVEERERAEAEGREREAralsltRALEEEQEAREELERQNRALRAELEALL 1575
Cdd:pfam15921 537 KNEGDHLRNVQTECEALKLQmaEKDKVIEILRQQIENMTQLVGQHG------RTAGAMQVEKAQLEKEINDRRLELQEFK 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1576 SSKDDVGKSVHELEraCRVAE----------------QAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKtqheRDLQ 1639
Cdd:pfam15921 611 ILKDKKDAKIRELE--ARVSDlelekvklvnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLK----RNFR 684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1640 GRDEAGEERRRQLAKQLRDAEVERDEERKQ-----------RTLAVAARKKLEGELEELKAqMASAGQGKEEAVKQLRKM 1708
Cdd:pfam15921 685 NKSEEMETTTNKLKMQLKSAQSELEQTRNTlksmegsdghaMKVAMGMQKQITAKRGQIDA-LQSKIQFLEEAMTNANKE 763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1709 QAQMKElwrevEETRTSRE--EIFSQNRESEKRLKGLEAEVLRLQEELA----ASDRARRQAQQDRDEMADEVANGNLSK 1782
Cdd:pfam15921 764 KHFLKE-----EKNKLSQElsTVATEKNKMAGELEVLRSQERRLKEKVAnmevALDKASLQFAECQDIIQRQEQESVRLK 838
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1783 AAILEEKRQLEGRlGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAE-RSFSAKAESGRQQLERQIQELRGRLGE 1861
Cdd:pfam15921 839 LQHTLDVKELQGP-GYTSNSSMKPRLLQPASFTRTHSNVPSSQSTASFLSHHsRKTNALKEDPTRDLKQLLQELRSVINE 917
|
....*...
gi 224831241 1862 EDAGARAR 1869
Cdd:pfam15921 918 EPTVQLSK 925
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
904-1519 |
4.12e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 55.36 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 904 QVTRQDEVLQARaqeLQKVQELQQQSAREvGELQGRVAQLEEER---------ARLAEQLRAEAELCAEAEETRGRLAAR 974
Cdd:TIGR00618 244 YLTQKREAQEEQ---LKKQQLLKQLRARI-EELRAQEAVLEETQerinrarkaAPLAAHIKAVTQIEQQAQRIHTELQSK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 975 KQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQleKVTTEAKMKKFEEDLLLLEDQ--- 1051
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ--QHTLTQHIHTLQQQKTTLTQKlqs 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1052 -NSKLSKERKLLEDRLAEFSSQAAEEEEKV--KSLNKLRLKYEATIADMEDRLRKEEKGRQ-ELEKLKRRLDGESSELQ- 1126
Cdd:TIGR00618 398 lCKELDILQREQATIDTRTSAFRDLQGQLAhaKKQQELQQRYAELCAAAITCTAQCEKLEKiHLQESAQSLKEREQQLQt 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1127 -EQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLL-------KSLREAQAALAEAQEDLESERVARTKAEKQ 1198
Cdd:TIGR00618 478 kEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdnpgpltRRMQRGEQTYAQLETSEEDVYHQLTSERKQ 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1199 RRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIH-----EAAVQELRQRHGQALGELAEQLEQA 1273
Cdd:TIGR00618 558 RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEdmlacEQHALLRKLQPEQDLQDVRLHLQQC 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1274 RRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRlELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGA 1353
Cdd:TIGR00618 638 SQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASR-QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEY 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1354 LNEAESKTIRLSKELSSTEAQLHDAQELLQE-ETRAKLALGSRVRAMEaeaaglreQLEEEAAARERAGRELQTAQAQLS 1432
Cdd:TIGR00618 717 DREFNEIENASSSLGSDLAAREDALNQSLKElMHQARTVLKARTEAHF--------NNNEEVTAALQTGAELSHLAAEIQ 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1433 EWRRRQEEEAGALeageeaRRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFD 1512
Cdd:TIGR00618 789 FFNRLREEDTHLL------KTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
....*..
gi 224831241 1513 QLLAEEK 1519
Cdd:TIGR00618 863 QLTQEQA 869
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1033-1275 |
4.46e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1033 TTEAKMKKFEEDLLLLED-------QNSKLSKERKLLEDRLAEFS--SQAAEEEEKVKSLnklrlkyEATIADMEDRLRK 1103
Cdd:COG4913 607 DNRAKLAALEAELAELEEelaeaeeRLEALEAELDALQERREALQrlAEYSWDEIDVASA-------EREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1104 EEKGRQELEKLKRRLDG---ESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLlksLREAQAALAE 1180
Cdd:COG4913 680 LDASSDDLAALEEQLEEleaELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE---LRALLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1181 AQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSK-------REQEVTELKKTLEEEtRIHEAAVQ 1253
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETAdldadleSLPEYLALLDRLEED-GLPEYEER 835
|
250 260
....*....|....*....|....*
gi 224831241 1254 ELRQRH---GQALGELAEQLEQARR 1275
Cdd:COG4913 836 FKELLNensIEFVADLLSKLRRAIR 860
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1692-1932 |
5.23e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1692 ASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEM 1771
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1772 adevangnlsKAAILEEKRQLEGRLGQLEEELEEEqsnsellndrYRKLLLQVESLTTELSAERSFSAKAESGRQQLErQ 1851
Cdd:COG4942 96 ----------RAELEAQKEELAELLRALYRLGRQP----------PLALLLSPEDFLDAVRRLQYLKYLAPARREQAE-E 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1852 IQELRGRLGEEDAGARARHKmTIAALESKLAQAEEQLEQETRERilsGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLE 1931
Cdd:COG4942 155 LRADLAELAALRAELEAERA-ELEALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
.
gi 224831241 1932 K 1932
Cdd:COG4942 231 R 231
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1567-1988 |
7.30e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 54.74 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1567 LRAELEALLSSKDDvgkSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQ------ALKTQHERDLQG 1640
Cdd:pfam15921 329 LRSELREAKRMYED---KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHkrekelSLEKEQNKRLWD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1641 RDEAGEERRRQLAKQL--RDAEVERDEerkqrTLAVAARKKLEGELEElkaQMAsAGQGKEEAVKQLRKMQAQM---KEL 1715
Cdd:pfam15921 406 RDTGNSITIDHLRRELddRNMEVQRLE-----ALLKAMKSECQGQMER---QMA-AIQGKNESLEKVSSLTAQLestKEM 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1716 WREVEETRTSRE-----------EIFSQNRESEKRLKGLEAEV--------LRLQE-----------------------E 1753
Cdd:pfam15921 477 LRKVVEELTAKKmtlessertvsDLTASLQEKERAIEATNAEItklrsrvdLKLQElqhlknegdhlrnvqtecealklQ 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1754 LAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQsnseLLNDRYRKLLLQVESLTTELSA 1833
Cdd:pfam15921 557 MAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFK----ILKDKKDAKIRELEARVSDLEL 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1834 ERSFSAKAESGRQQLERQIQELRGRLGEEDAGARA----------------RHK-----MTIAALESKLAQAEEQLEQeT 1892
Cdd:pfam15921 633 EKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNelnslsedyevlkrnfRNKseemeTTTNKLKMQLKSAQSELEQ-T 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1893 RERIlsgKLVRRAEKRLKEVVLQVEEERRVAdqlRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESA 1972
Cdd:pfam15921 712 RNTL---KSMEGSDGHAMKVAMGMQKQITAK---RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEK 785
|
490
....*....|....*.
gi 224831241 1973 ESMNREVTTLRNRLRR 1988
Cdd:pfam15921 786 NKMAGELEVLRSQERR 801
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1109-1399 |
8.70e-07 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 53.53 E-value: 8.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1109 QELEKLKRRLdgesSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESE 1188
Cdd:pfam19220 41 RELPQAKSRL----LELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1189 RVARTKAEKQ-------RRDLGEELEALRGEL----EDTLDSTNAQQELRSKR---EQEVTELKKTLEE---ETRIHEAA 1251
Cdd:pfam19220 117 TAQAEALERQlaaeteqNRALEEENKALREEAqaaeKALQRAEGELATARERLallEQENRRLQALSEEqaaELAELTRR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1252 VQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQtarqegeqrrrrleLQLQEVQGRAGDGER 1331
Cdd:pfam19220 197 LAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLR--------------MKLEALTARAAATEQ 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224831241 1332 ARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAM 1399
Cdd:pfam19220 263 LLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEML 330
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1647-1970 |
9.74e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.19 E-value: 9.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1647 ERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMK------------- 1713
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRqqekieryqedle 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1714 ELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARrQAQQDRdemadevangnlskaAIleEKRQLE 1793
Cdd:COG3096 358 ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQAL-DVQQTR---------------AI--QYQQAV 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1794 GRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGE---EDAGARARH 1870
Cdd:COG3096 420 QALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEverSQAWQTARE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1871 KMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEkgnlrvkQLKRQLEEAEEE 1950
Cdd:COG3096 500 LLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLA-------ELEAQLEELEEQ 572
|
330 340
....*....|....*....|
gi 224831241 1951 ASRAQAGRRRLQRELEDVTE 1970
Cdd:COG3096 573 AAEAVEQRSELRQQLEQLRA 592
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1062-1477 |
1.09e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1062 LEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRA 1141
Cdd:PRK02224 263 LRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1142 QLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTN 1221
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1222 AQQELRSKREQEVTELKKTLEEETRIHEA-----------------AVQELRQRhgqaLGELAEQLEQARRGKGAWEK-- 1282
Cdd:PRK02224 423 ELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphveTIEEDRER----VEELEAELEDLEEEVEEVEErl 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1283 TRL----ALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGD----GERARAEAAEKLQRAQAELENVS--- 1351
Cdd:PRK02224 499 ERAedlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAEleaeAEEKREAAAEAEEEAEEAREEVAeln 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1352 ---GALNEAESKTIRLSKELSSTEAQLHDAQEL---------LQEETRAKLA-LGSRVRAMEAEAAGlreqleEEAAARE 1418
Cdd:PRK02224 579 sklAELKERIESLERIRTLLAAIADAEDEIERLrekrealaeLNDERRERLAeKRERKRELEAEFDE------ARIEEAR 652
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 224831241 1419 RAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLE 1477
Cdd:PRK02224 653 EDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEALE 711
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1026-1385 |
2.14e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 52.65 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1026 KLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADME---DRLR 1102
Cdd:COG5185 177 KKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAqtsDKLE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1103 ---------KEEKGRQELEKLKR------RLDGESSELQEQMVEQQQRAEELRAQLgRKEEELQAALARAEDEGGARAQl 1167
Cdd:COG5185 257 klveqntdlRLEKLGENAESSKRlnenanNLIKQFENTKEKIAEYTKSIDIKKATE-SLEEQLAAAEAEQELEESKRET- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1168 LKSLREAQAALAEAQEDLEsERVARTKAEKQRRDLGEELEalrgELEDTLDSTNAQQElrSKREqEVTELKKTLEEETRI 1247
Cdd:COG5185 335 ETGIQNLTAEIEQGQESLT-ENLEAIKEEIENIVGEVELS----KSSEELDSFKDTIE--STKE-SLDEIPQNQRGYAQE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1248 HEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRlelqlQEVQGRAG 1327
Cdd:COG5185 407 ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEIN-----RSVRSKKE 481
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 224831241 1328 DGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEE 1385
Cdd:COG5185 482 DLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHIL 539
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
908-1300 |
2.70e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.20 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 908 QDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEA 987
Cdd:pfam07888 43 RAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 988 RVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLA 1067
Cdd:pfam07888 123 QRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1068 EFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEqMVEQQQR--AEELRAQLGR 1145
Cdd:pfam07888 203 QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSS-MAAQRDRtqAELHQARLQA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1146 KEEELQAALAR-AEDEGGAR-AQLLKSLReaqaalaeAQEDLESERVARTKAEKQRRD--LGEEL---EALRGELEDTLD 1218
Cdd:pfam07888 282 AQLTLQLADASlALREGRARwAQERETLQ--------QSAEADKDRIEKLSAELQRLEerLQEERmerEKLEVELGREKD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1219 STNAQqelRSKREQEVTELKKTLEEETRiheaaVQELRQRHGQALGELAEQLEQaRRGKGAWEKTRLALEAEVSELRAEL 1298
Cdd:pfam07888 354 CNRVQ---LSESRRELQELKASLRVAQK-----EKEQLQAEKQELLEYIRQLEQ-RLETVADAKWSEAALTSTERPDSPL 424
|
..
gi 224831241 1299 SS 1300
Cdd:pfam07888 425 SD 426
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
917-1249 |
2.70e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.72 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 917 QELQKVQELQQQsarevgeLQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVGEEEECS 996
Cdd:TIGR04523 398 SKIQNQEKLNQQ-------KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 997 RQMQTEKKRLQQhiqeleahleaeegarqklQLEKVTTEAKMKkfeedllllEDQNSKLSKERKLLEDRLAEFSSQAAEE 1076
Cdd:TIGR04523 471 KVLSRSINKIKQ-------------------NLEQKQKELKSK---------EKELKKLNEEKKELEEKVKDLTKKISSL 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1077 EEKVKSLNKLRLKYEATIADMEDRLRK--EEKGRQELEKLKRRLDGESSEL---QEQMVEQQQRAEELRAQLGRKEEELQ 1151
Cdd:TIGR04523 523 KEKIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELkqtQKSLKKKQEEKQELIDQKEKEKKDLI 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1152 AALARAEdeggaraQLLKSLREAQAALAEAQEDLESErvaRTKAEKQRRDLGEELEALRGELEDTLDSTN----AQQELR 1227
Cdd:TIGR04523 603 KEIEEKE-------KKISSLEKELEKAKKENEKLSSI---IKNIKSKKNKLKQEVKQIKETIKEIRNKWPeiikKIKESK 672
|
330 340
....*....|....*....|..
gi 224831241 1228 SKrEQEVTELKKTLEEETRIHE 1249
Cdd:TIGR04523 673 TK-IDDIIELMKDWLKELSLHY 693
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
912-1402 |
4.04e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 52.05 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 912 LQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLA-EQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVG 990
Cdd:pfam05557 53 LQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLnEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 991 EEEECSRQMQTEKKRLQQHIQELEAHleaeegarQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEdRLAEFS 1070
Cdd:pfam05557 133 ELEELQERLDLLKAKASEAEQLRQNL--------EKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELA-RIPELE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1071 SQAAEEEEKVKSLNKLR---LKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRA--QLGR 1145
Cdd:pfam05557 204 KELERLREHNKHLNENIenkLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSpeDLSR 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1146 KEEELQAALARAEDEGGARAQLLKSLReaqaalaEAQEDLESE-RVARTKAEKQRRDLgEELEALRGELEDTLDSTNAQ- 1223
Cdd:pfam05557 284 RIEQLQQREIVLKEENSSLTSSARQLE-------KARRELEQElAQYLKKIEDLNKKL-KRHKALVRRLQRRVLLLTKEr 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1224 ---QELRSKREQEVTELKKTLEEETRIHEAAvqELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSS 1300
Cdd:pfam05557 356 dgyRAILESYDKELTMSNYSPQLLERIEEAE--DMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESL 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1301 LQTARQEGEQRRRRLELQLQEvqgragdGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKE-LSSTEAQLHDAQ 1379
Cdd:pfam05557 434 ADPSYSKEEVDSLRRKLETLE-------LERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNpAAEAYQQRKNQL 506
|
490 500
....*....|....*....|...
gi 224831241 1380 ELLQEETRaklALGSRVRAMEAE 1402
Cdd:pfam05557 507 EKLQAEIE---RLKRLLKKLEDD 526
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1675-1911 |
4.17e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1675 AARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEEL 1754
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1755 AASDRAR-RQAQQDR-------DEMADEVANGNLSKAAILEEKRQLEgrlgqleeeleeeqsnsellndRYRKLLLQVES 1826
Cdd:COG4942 107 AELLRALyRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAE----------------------ELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1827 LTTELSAERsfsAKAESGRQQLERQIQELrgrlgeedAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAE 1906
Cdd:COG4942 165 LRAELEAER---AELEALLAELEEERAAL--------EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
....*
gi 224831241 1907 KRLKE 1911
Cdd:COG4942 234 AEAAA 238
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1595-2018 |
5.40e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1595 AEQA--ANDLR-AQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRRQLAKQLRDA----EVERDEER 1667
Cdd:PTZ00121 1274 AEEArkADELKkAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAkkaaEAAKAEAE 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1668 KQRTLAVAARKKLEGEleELKAQMAsagQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEK--RLKGlEA 1745
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAA--EKKKEEA---KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKadEAKK-KA 1427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1746 EVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAilEEKRQLEgrlgqleeeLEEEQSNSELLNDRYRKLLLQVE 1825
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA--EEAKKAD---------EAKKKAEEAKKADEAKKKAEEAK 1496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1826 SLTTELSAERSFSAKAESGRQQLE-RQIQELRGrlGEEDAGARARHKMTIAALESKLAQAEEQLEQETRERIlsgKLVRR 1904
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEaKKADEAKK--AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA---EEAKK 1571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1905 AEKRlKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRN 1984
Cdd:PTZ00121 1572 AEED-KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650
|
410 420 430
....*....|....*....|....*....|....
gi 224831241 1985 RLRRGPLTFTTRTVRQVFRLEEGVASDEEAEEAQ 2018
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
905-1295 |
5.81e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 905 VTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLA--EQLRAEAELCAEAEETRGRLAA--RKQELEL 980
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEelERLKKRLTGLTPEKLEKELEELekAKEEIEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 981 VVSELEARVGEeeecsrqMQTEKKRLQQHIQELEAHLEAEEGARQKLQ-------LEKVTteAKMKKFEEDLLLLEDQNS 1053
Cdd:PRK03918 406 EISKITARIGE-------LKKEIKELKKAIEELKKAKGKCPVCGRELTeehrkelLEEYT--AELKRIEKELKEIEEKER 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1054 KLSKERKLLEDRLAEFSS---------QAAEEEEKVKSLNKLRLKYEAtiadmedrlRKEEKGRQELEKLKRRLDGESSE 1124
Cdd:PRK03918 477 KLRKELRELEKVLKKESEliklkelaeQLKELEEKLKKYNLEELEKKA---------EEYEKLKEKLIKLKGEIKSLKKE 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1125 LqEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLK--------------SLREAQAALAEAQEDLESERV 1190
Cdd:PRK03918 548 L-EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEerlkelepfyneylELKDAEKELEREEKELKKLEE 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1191 ARTKAEKQRRDLGEELEALRGELEDtLDSTNAQQELRSKREqEVTELKKTLEE-ETRIHEAavQELRQRHGQALGELAEQ 1269
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEE-LEKKYSEEEYEELRE-EYLELSRELAGlRAELEEL--EKRREEIKKTLEKLKEE 702
|
410 420
....*....|....*....|....*.
gi 224831241 1270 LEQARRGKGAWEKTRLALEaEVSELR 1295
Cdd:PRK03918 703 LEEREKAKKELEKLEKALE-RVEELR 727
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1565-1781 |
6.45e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1565 RALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEA 1644
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1645 GeerRRQLAKQLRDAEVERDEERKQRTLAVAAR------KKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWRE 1718
Cdd:COG4942 117 G---RQPPLALLLSPEDFLDAVRRLQYLKYLAParreqaEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224831241 1719 VEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLS 1781
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1315-1768 |
6.75e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 6.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1315 LELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGS 1394
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1395 RVRAMEAEAagLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREA-EALTQRLAEKTETV 1473
Cdd:COG4717 131 YQELEALEA--ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1474 DRLERGRRRLQQELDDATMDLEQ-QRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEE 1552
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQlENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1553 EQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAE----QAANDLRAQVTELEDELTAAEDAKLRLEvtVQ 1628
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPdlspEELLELLDRIEELQELLREAEELEEELQ--LE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1629 ALKTQHERDLQGRDEAGEERRRQLAKQLRD-----AEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVK 1703
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEEELRAALEQAEEyqelkEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEE 446
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224831241 1704 QLRKMQAQMKELWREVEETRTSRE--EIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDR 1768
Cdd:COG4717 447 ELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1285-1510 |
6.80e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1285 LALEAEVSELRAELSSLQtarqegeQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRL 1364
Cdd:COG4942 16 AAQADAAAEAEAELEQLQ-------QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1365 SKELSSTEAQLHDAQELLQEETRAKLALGSRVRAME----AEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEE 1440
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1441 EAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRK 1510
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
847-1089 |
7.29e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 847 IIVSFQAAARGYLARRAFQKRQQQQSALRVMQRNCAAYLKlrhwqwwrlfTKVKPLLQVTRQDEVLQARAQELQKVQELQ 926
Cdd:COG4942 9 LLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKK----------EEKALLKQLAALERRIAALARRIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 927 QQSAREVGELQGRVAQLEEE----RARLAEQLRAEAELCAEAEETR-------GRLAARKQELELVVSELEARVGEEEEC 995
Cdd:COG4942 79 AALEAELAELEKEIAELRAEleaqKEELAELLRALYRLGRQPPLALllspedfLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 996 SRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAE 1075
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
250
....*....|....
gi 224831241 1076 EEEKVKSLNKLRLK 1089
Cdd:COG4942 239 AAERTPAAGFAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1751-1993 |
8.09e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 8.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1751 QEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTE 1830
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1831 LSAERSFSAKAESGRQQLERQiQELRGRLGEEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLK 1910
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQ-PPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1911 EVVLQVEEERRVADQLRDQLEKgnlRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRRGP 1990
Cdd:COG4942 178 ALLAELEEERAALEALKAERQK---LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
...
gi 224831241 1991 LTF 1993
Cdd:COG4942 255 LPW 257
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
944-1353 |
1.09e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 944 EEERARLAEQlraEAELCAEAEETRGRLAARKQELELVVSELEARVGEEEEcsrqmqtekkrLQQHIQELEahleaeegA 1023
Cdd:PRK04863 278 ANERRVHLEE---ALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESD-----------LEQDYQAAS--------D 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1024 RQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRK 1103
Cdd:PRK04863 336 HLNLVQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1104 EEKGRQELEKLKRRLDGES------SELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEdeggARAQLLKSLREAQAA 1177
Cdd:PRK04863 416 YQQAVQALERAKQLCGLPDltadnaEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFE----QAYQLVRKIAGEVSR 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1178 LAEAQEDLESERVARTKaekqrRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEetrihEAAVQELRQ 1257
Cdd:PRK04863 492 SEAWDVARELLRRLREQ-----RHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDD-----EDELEQLQE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1258 RHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAE----------LSSLQTARQEGEQRRRRLELQLQEVQGRAG 1327
Cdd:PRK04863 562 ELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARapawlaaqdaLARLREQSGEEFEDSQDVTEYMQQLLERER 641
|
410 420
....*....|....*....|....*.
gi 224831241 1328 DGERARAEAAEKLQRAQAELENVSGA 1353
Cdd:PRK04863 642 ELTVERDELAARKQALDEEIERLSQP 667
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1565-1988 |
1.11e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1565 RALRAELEALLSSKDDVGKSVHELERAcrvaEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHE-RDLQGRDE 1643
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEEL----EEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1644 AGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKL----EGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREV 1719
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1720 EETRTSREEIFSQNRESEKR-----------LKGLEAEVLRLQEELAA---------------SDRARRQAQQDRDEMAD 1773
Cdd:COG4717 230 EQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGvlflvlgllallfllLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1774 EVANGNLSKAAILEEKRQLEgrlgqleeeleeeqSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAEsgRQQLERQIQ 1853
Cdd:COG4717 310 LPALEELEEEELEELLAALG--------------LPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1854 ELRGRLG---EEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSgkLVRRAEKRLKEVVLQVEEERRVADQLRDQL 1930
Cdd:COG4717 374 ALLAEAGvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEL--LEALDEEELEEELEELEEELEELEEELEEL 451
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 224831241 1931 EKGNLRVKQLKRQLeEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1988
Cdd:COG4717 452 REELAELEAELEQL-EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
908-1441 |
1.12e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 908 QDEVLQARAQE--LQKVQELQQQSArevgELQGRVAQLEEERARLaeqlraeaelcaeaeetrgRLAARKQELELvvseL 985
Cdd:COG4913 241 HEALEDAREQIelLEPIRELAERYA----AARERLAELEYLRAAL-------------------RLWFAQRRLEL----L 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 986 EARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVtteakmKKFEEDLLLLEDQNSKLSKERKLLEDR 1065
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRL------EQLEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1066 LAEFSSQAAEEEEkvkSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRA--------- 1136
Cdd:COG4913 368 LAALGLPLPASAE---EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsniparlla 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1137 --EELRAQLGRKEEELQAAlA-----RAEDE----------GGAR----------AQLLKSLREAQAALAeaqedLESER 1189
Cdd:COG4913 445 lrDALAEALGLDEAELPFV-GelievRPEEErwrgaiervlGGFAltllvppehyAAALRWVNRLHLRGR-----LVYER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1190 VARTKAEKQRRDLGEelEALRGELEdtLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHG--------- 1260
Cdd:COG4913 519 VRTGLPDPERPRLDP--DSLAGKLD--FKPHPFRAWLEAELGRRFDYVCVDSPEELRRHPRAITRAGQVKGngtrhekdd 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1261 ---------------QALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQrrrrlELQLQEVQGR 1325
Cdd:COG4913 595 rrrirsryvlgfdnrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWD-----EIDVASAERE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1326 AGDGERARAEAAE---KLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAE 1402
Cdd:COG4913 670 IAELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
|
570 580 590
....*....|....*....|....*....|....*....
gi 224831241 1403 AAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEE 1441
Cdd:COG4913 750 LLEERFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
912-1270 |
1.15e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.72 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 912 LQARAQELQKVQE-LQQQsarevGELQGRVAQLEEERARLAEQlraeAELCAEAEETRGRLAARKQELELVVSELEARVG 990
Cdd:COG3096 329 YQAASDHLNLVQTaLRQQ-----EKIERYQEDLEELTERLEEQ----EEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 991 EEEECSRQMQTEKKRLQQHIQELEAhleaeegARQKLQLEKVTTEAkmkkFEEDLLLLEDQNSKLSKERKLLEDRLAeFS 1070
Cdd:COG3096 400 DYQQALDVQQTRAIQYQQAVQALEK-------ARALCGLPDLTPEN----AEDYLAAFRAKEQQATEEVLELEQKLS-VA 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1071 SQAAEEEEKVkslnklrlkYEA--TIADMEDRLRKEEKGRQ------ELEKLKRRLDGESSELQE--QMVEQQQRAEELR 1140
Cdd:COG3096 468 DAARRQFEKA---------YELvcKIAGEVERSQAWQTAREllrryrSQQALAQRLQQLRAQLAEleQRLRQQQNAERLL 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1141 AQLGRK-------EEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGEL 1213
Cdd:COG3096 539 EEFCQRigqqldaAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQS 618
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224831241 1214 EDTLDSTNAQQELRSK---REQEVTELKKTLEEETRIHEAAVQELRQRHGQA---LGELAEQL 1270
Cdd:COG3096 619 GEALADSQEVTAAMQQlleREREATVERDELAARKQALESQIERLSQPGGAEdprLLALAERL 681
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1565-1714 |
1.31e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1565 RALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHE-RDLQGRDE 1643
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224831241 1644 AGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKE 1714
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
997-1213 |
1.32e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 997 RQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEE 1076
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1077 EEKVKSLNKL------------------------RLKYEATIAD-MEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVE 1131
Cdd:COG4942 103 KEELAELLRAlyrlgrqpplalllspedfldavrRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1132 QQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALaeaqedlesERVARTKAEKQRRDLGEELEALRG 1211
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI---------ARLEAEAAAAAERTPAAGFAALKG 253
|
..
gi 224831241 1212 EL 1213
Cdd:COG4942 254 KL 255
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1195-1970 |
1.38e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1195 AEKQRRDLGEELEALRGELEDTLDSTNAQQELR---SKREQEVTELKKTLEEE---TRIHEAAVQE-LRQ-----RHGQA 1262
Cdd:PRK04863 277 HANERRVHLEEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDyqaASDHLNLVQTaLRQqekieRYQAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1263 LGELAEQLEQ-------ARRGKGAWEKTRLALEAEVSELRAELSSLQTArqegeqrrrrLELQlqevQGRAG---DGERA 1332
Cdd:PRK04863 357 LEELEERLEEqnevveeADEQQEENEARAEAAEEEVDELKSQLADYQQA----------LDVQ----QTRAIqyqQAVQA 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1333 RAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLR-EQLE 1411
Cdd:PRK04863 423 LERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVaRELL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1412 EEAAARERAGRELQTAQAQLSEWRRRQEEEAGAleageearrraAREAEALTQRLAEKTETVDRLERGRRRLQQELDDAT 1491
Cdd:PRK04863 503 RRLREQRHLAEQLQQLRMRLSELEQRLRQQQRA-----------ERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1492 MDLEQQRQLVSTLEKKQRKFDQLLAEEKAavlraveereraeaegrerearalsltraleeeqeareeLERQNRALRAEL 1571
Cdd:PRK04863 572 ESVSEARERRMALRQQLEQLQARIQRLAA---------------------------------------RAPAWLAAQDAL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1572 EALLS-SKDDVGKSvheleracrvaeQAANDLRAQVTELEDELTAAEDaklRLEVTVQALKTQHERdLQGRDEAGEERRR 1650
Cdd:PRK04863 613 ARLREqSGEEFEDS------------QDVTEYMQQLLERERELTVERD---ELAARKQALDEEIER-LSQPGGSEDPRLN 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1651 QLAK---------------------------QLRDAEVERDEERKQRTLAvaarkKLEGELEEL------KAQMASAGQG 1697
Cdd:PRK04863 677 ALAErfggvllseiyddvsledapyfsalygPARHAIVVPDLSDAAEQLA-----GLEDCPEDLyliegdPDSFDDSVFS 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1698 KEEAVKQLrkmqaQMKELWREVEETRTSREEIFSQnRESEKRLKGLEAEVLRLQEELAASDRaRRQAQQDRDEMADEVAN 1777
Cdd:PRK04863 752 VEELEKAV-----VVKIADRQWRYSRFPEVPLFGR-AAREKRIEQLRAEREELAERYATLSF-DVQKLQRLHQAFSRFIG 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1778 GNLSKA------AILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELS--AERSFSAKAESGRQQLE 1849
Cdd:PRK04863 825 SHLAVAfeadpeAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNllADETLADRVEEIREQLD 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1850 RqiqelrgrlGEEDAGARARHKMTIAALE---SKLAQAEEQLEQETRERILSGKLVRRAEKR---LKEVVlqveeERRVA 1923
Cdd:PRK04863 905 E---------AEEAKRFVQQHGNALAQLEpivSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQafaLTEVV-----QRRAH 970
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 224831241 1924 ---DQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTE 1970
Cdd:PRK04863 971 fsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQ 1020
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1094-1278 |
1.56e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1094 IADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDeggARAQL--LKSL 1171
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK---YEEQLgnVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1172 REAQAALAeaqeDLESERVARTKAEKQRRDLGEELEALRGELEDTldstnaqQELRSKREQEVTELKKTLEEETRIHEAA 1251
Cdd:COG1579 89 KEYEALQK----EIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAE 157
|
170 180 190
....*....|....*....|....*....|.
gi 224831241 1252 VQELRQRHGQALGELAEQL----EQARRGKG 1278
Cdd:COG1579 158 LEELEAEREELAAKIPPELlalyERIRKRKN 188
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1023-1357 |
1.60e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 49.68 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1023 ARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLN------KLRLK-YEATIA 1095
Cdd:pfam19220 42 ELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEaakeelRIELRdKTAQAE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1096 DMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEG------GAR-AQLL 1168
Cdd:pfam19220 122 ALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAaelaelTRRlAELE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1169 KSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIH 1248
Cdd:pfam19220 202 TQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1249 EAAVQEL---RQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGR 1325
Cdd:pfam19220 282 ERRLKEAsieRDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKR 361
|
330 340 350
....*....|....*....|....*....|....*.
gi 224831241 1326 ----AGDGERARAEAAEKLQRAQAELENVSGALNEA 1357
Cdd:pfam19220 362 feveRAALEQANRRLKEELQRERAERALAQGALEIA 397
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1088-1209 |
1.73e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.83 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1088 LKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLgrkEEELQAALARAEDEGgarAQL 1167
Cdd:PRK00409 516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKEAKKEA---DEI 589
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 224831241 1168 LKSLReaqaalaeAQEDLESERVARTKAEKQRRDLGEELEAL 1209
Cdd:PRK00409 590 IKELR--------QLQKGGYASVKAHELIEARKRLNKANEKK 623
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1184-1404 |
2.14e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1184 DLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQAL 1263
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1264 GELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRA 1343
Cdd:COG4942 104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224831241 1344 QAELENVSGALNEAESKTIRLSKELSSTEAQLhdaQELLQEETRAKLALGSRVRAMEAEAA 1404
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAEL---AELQQEAEELEALIARLEAEAAAAAE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1565-1988 |
2.28e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1565 RALRAELEALLSSKDDVGKSVHELERACRVAEQAAND--------LRAQVTELEDELTAAEDAKLRLEVTVQALKTQHER 1636
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1637 DLqgrdEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGK---EEAVKQLRKMQA--- 1710
Cdd:COG4913 378 SA----EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsniPARLLALRDALAeal 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1711 --------------QMKEL---WRE--------------------------VEET------RTSREEIFSQNRESEKRLK 1741
Cdd:COG4913 454 gldeaelpfvgeliEVRPEeerWRGaiervlggfaltllvppehyaaalrwVNRLhlrgrlVYERVRTGLPDPERPRLDP 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1742 G----------------LEAEVLRL--------QEELAASDRA-----------RRQAQQDRDEMADEVANG--NLSKAA 1784
Cdd:COG4913 534 DslagkldfkphpfrawLEAELGRRfdyvcvdsPEELRRHPRAitragqvkgngTRHEKDDRRRIRSRYVLGfdNRAKLA 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1785 ILEEKR-QLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAersfsakaesgrQQLERQIQELRGRLGEED 1863
Cdd:COG4913 614 ALEAELaELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV------------ASAEREIAELEAELERLD 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1864 AGararhKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGnlRVKQLKRQ 1943
Cdd:COG4913 682 AS-----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE--LRALLEER 754
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 224831241 1944 LEEAEEEASRAQAgRRRLQRELEDVTESAESMNREVTTLRNRLRR 1988
Cdd:COG4913 755 FAAALGDAVEREL-RENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
856-1270 |
2.91e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 856 RGYLARRAFQKRQQQQSALRVMQRNCAAYLKLRHwqwwRLFTKVKPLLQVTRQDEVLQARAQELQKVQELQ------QQS 929
Cdd:COG4717 62 QGRKPELNLKELKELEEELKEAEEKEEEYAELQE----ELEELEEELEELEAELEELREELEKLEKLLQLLplyqelEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 930 AREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELV----VSELEARVGEEEECSRQMQTEKKR 1005
Cdd:COG4717 138 EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAteeeLQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1006 LQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLL--------------------------LLEDQNSKLSKER 1059
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALlallglggsllsliltiagvlflvlgLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1060 KLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRA--- 1136
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAlla 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1137 -------EELRAQLGRKEE--ELQAALARAEDEGGARAQLLKSLrEAQAALAEAQEDLESERVARTKAEKQRRDLGEELE 1207
Cdd:COG4717 378 eagvedeEELRAALEQAEEyqELKEELEELEEQLEELLGELEEL-LEALDEEELEEELEELEEELEELEEELEELREELA 456
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224831241 1208 ALRGELEDtLDSTNAQQELRSKREQEVTELKKTLEEETRIH------EAAVQELRQRHGQALGELAEQL 1270
Cdd:COG4717 457 ELEAELEQ-LEEDGELAELLQELEELKAELRELAEEWAALKlalellEEAREEYREERLPPVLERASEY 524
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1126-1380 |
3.20e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1126 QEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLReaqaalaeaqedleservartKAEKQRRDLGEE 1205
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA---------------------ALARRIRALEQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1206 LEALRGELEDTldsTNAQQELRSKREQEVTELKKTLeeetriheAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRL 1285
Cdd:COG4942 78 LAALEAELAEL---EKEIAELRAELEAQKEELAELL--------RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1286 ALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLS 1365
Cdd:COG4942 147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250
....*....|....*
gi 224831241 1366 KELSSTEAQLHDAQE 1380
Cdd:COG4942 227 ALIARLEAEAAAAAE 241
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1633-1943 |
3.40e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1633 QHERDLQGRDEAGEERRRQL--AKQLRDAEVERDEE-RKQRTLAVAARKKLEGELEELKAQMASAgQGKEEAVKQLRKMQ 1709
Cdd:PRK04863 276 RHANERRVHLEEALELRRELytSRRQLAAEQYRLVEmARELAELNEAESDLEQDYQAASDHLNLV-QTALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1710 AQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRA----------RRQAQQDRDEM-----ADE 1774
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQAldvqqtraiqYQQAVQALERAkqlcgLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1775 VANGNLSkaAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSF-----------SAKAES 1843
Cdd:PRK04863 435 LTADNAE--DWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWdvarellrrlrEQRHLA 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1844 GR-QQLERQIQELRGRLGEEdagararhkmtiAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRV 1922
Cdd:PRK04863 513 EQlQQLRMRLSELEQRLRQQ------------QRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARER 580
|
330 340
....*....|....*....|.
gi 224831241 1923 ADQLRDQLEKGNLRVKQLKRQ 1943
Cdd:PRK04863 581 RMALRQQLEQLQARIQRLAAR 601
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1148-1517 |
4.24e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1148 EELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLES--ERVARTKAEKQRRDLGEELEALRGELEDT---LDSTNA 1222
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElrEELEKLEKLLQLLPLYQELEALEAELAELperLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1223 QQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQ 1302
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1303 TARQEGEQRRRRLELQ-----------LQEVQGRAGDGERARAEAA-----------EKLQRAQAELENVSGALNEAESK 1360
Cdd:COG4717 234 NELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGVLflvlgllallfLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1361 TIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQE- 1439
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEq 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1440 --------------EEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQlVSTLE 1505
Cdd:COG4717 394 aeeyqelkeeleelEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE-DGELA 472
|
410
....*....|..
gi 224831241 1506 KKQRKFDQLLAE 1517
Cdd:COG4717 473 ELLQELEELKAE 484
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1563-1754 |
4.78e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1563 QNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKtQHERDLQGRD 1642
Cdd:COG1340 51 QVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIE-RLEWRQQTEV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1643 EAGEERRR------QLAKQLRDAEVERDEERKQRTLavaarkklEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELW 1716
Cdd:COG1340 130 LSPEEEKElvekikELEKELEKAKKALEKNEKLKEL--------RAELKELRKEAEEIHKKIKELAEEAQELHEEMIELY 201
|
170 180 190
....*....|....*....|....*....|....*...
gi 224831241 1717 REVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEEL 1754
Cdd:COG1340 202 KEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
859-1390 |
5.55e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.58 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 859 LARRAFQKRQQQ---QSALRVMQRNCAAYLKLRHWQWWRLFTKVKPLlqvtrQDEVLQARAQELQKVQELQQQ---SARE 932
Cdd:pfam15921 283 LTEKASSARSQAnsiQSQLEIIQEQARNQNSMYMRQLSDLESTVSQL-----RSELREAKRMYEDKIEELEKQlvlANSE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 933 VGELQGRVAQLEEERARLAEQLRAEAELcaeaeetrgrLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQE 1012
Cdd:pfam15921 358 LTEARTERDQFSQESGNLDDQLQKLLAD----------LHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNME 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1013 LEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLrlkyea 1092
Cdd:pfam15921 428 VQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDL------ 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1093 tIADMEDRLRKEEKGRQELEKLKRRLDGESSELQE--------------------QMVEQQQRAEELRAQL--------- 1143
Cdd:pfam15921 502 -TASLQEKERAIEATNAEITKLRSRVDLKLQELQHlknegdhlrnvqtecealklQMAEKDKVIEILRQQIenmtqlvgq 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1144 -GRKEEELQAALARAEDEGGARAQLLKSLR-------EAQAALAEAQEDLESERVARTKAEKQR----RDLGEELEALRG 1211
Cdd:pfam15921 581 hGRTAGAMQVEKAQLEKEINDRRLELQEFKilkdkkdAKIRELEARVSDLELEKVKLVNAGSERlravKDIKQERDQLLN 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1212 ELEDTLDSTNAQQElrskrEQEVteLKKTLEEETRIHEAAVQELRQRHGQALGELAE---QLEQARRGKGAWEKTRLALE 1288
Cdd:pfam15921 661 EVKTSRNELNSLSE-----DYEV--LKRNFRNKSEEMETTTNKLKMQLKSAQSELEQtrnTLKSMEGSDGHAMKVAMGMQ 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1289 AEVSELRAELSSLQTarqegeqRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKEL 1368
Cdd:pfam15921 734 KQITAKRGQIDALQS-------KIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKV 806
|
570 580 590
....*....|....*....|....*....|...
gi 224831241 1369 SSTEAQLHDA-----------QELLQEETRAKL 1390
Cdd:pfam15921 807 ANMEVALDKAslqfaecqdiiQRQEQESVRLKL 839
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
927-1392 |
7.68e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.91 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 927 QQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVGEeeecsrqmqtekkrl 1006
Cdd:pfam12128 237 MKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKE--------------- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1007 qqhiqeleahleaeegARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKER----KLLEDRLAEFSSQAAEEEEKVKS 1082
Cdd:pfam12128 302 ----------------KRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADietaAADQEQLPSWQSELENLEERLKA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1083 L----NKLRLKYEATIAdmedrLRKEEKGRqELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLgrkEEELQAALARAE 1158
Cdd:pfam12128 366 LtgkhQDVTAKYNRRRS-----KIKEQNNR-DIAGIKDKLAKIREARDRQLAVAEDDLQALESEL---REQLEAGKLEFN 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1159 DEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRrdlgEELEALRGELEdtlDSTNAQQELRSKREQEVTELk 1238
Cdd:pfam12128 437 EEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAR----EEQEAANAEVE---RLQSELRQARKRRDQASEAL- 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1239 ktleeetRIHEAAVQELRQRHGQALGELAEQ----LEQARRGKGAWEKTRLALEAEVSELRAELS-SLQTARQEGEQRRR 1313
Cdd:pfam12128 509 -------RQASRRLEERQSALDELELQLFPQagtlLHFLRKEAPDWEQSIGKVISPELLHRTDLDpEVWDGSVGGELNLY 581
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224831241 1314 RLELQLQEVQgragdgeraRAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQellQEETRAKLAL 1392
Cdd:pfam12128 582 GVKLDLKRID---------VPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKAS---REETFARTAL 648
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1596-1735 |
8.84e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.88 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1596 EQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALK-----TQHERD-LQGRDEAGEERRRQLAKQLRDAEVERDEERKQ 1669
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRaslsaAEAERSrLQALLAELAGAGAAAEGRAGELAQELDSEKQV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224831241 1670 RTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWR--------EVEETRTSREEIFSQNRE 1735
Cdd:PRK09039 132 SARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRrlnvalaqRVQELNRYRSEFFGRLRE 205
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1738-1988 |
1.00e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1738 KRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADevangnlskaaiLEEKRQLEGRLgqleeELEEEQSNSELLNDRY 1817
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAARER------------LAELEYLRAAL-----RLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1818 RKLLLQVESLTTELSAersfsakAESGRQQLERQIQELRGRLgEEDAGARarhkmtIAALESKLAQAEEQLEQETRERil 1897
Cdd:COG4913 298 EELRAELARLEAELER-------LEARLDALREELDELEAQI-RGNGGDR------LEQLEREIERLERELEERERRR-- 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1898 sgklvRRAEKRLKEVVLQVEEER----RVADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAE 1973
Cdd:COG4913 362 -----ARLEALLAALGLPLPASAeefaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
250
....*....|....*
gi 224831241 1974 SMNREVTTLRNRLRR 1988
Cdd:COG4913 437 NIPARLLALRDALAE 451
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1366-1988 |
1.01e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1366 KELSSTEAQLHDAQEllQEETRAKL-ALGSRVRAMEAEAAGLREQLEEEAAARERAGRELqtAQAQLSEWRRRQEEEAGA 1444
Cdd:COG4913 235 DDLERAHEALEDARE--QIELLEPIrELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1445 LEAGEEARRRAAREAEALTQRLAE-KTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEkkqrkfdqLLAEEKAAVL 1523
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEALLAALG--------LPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1524 RAVEERERAEAEGREREARALSLTRALEEEQEAREELerQNRALRAELEALLSSKDDVGKSVHEL-ERACRVAEQAANDL 1602
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRR--ELRELEAEIASLERRKSNIPARLLALrDALAEALGLDEAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1603 RA-----QVTELEDE--------------------------LTAAEDAKLRLEVTVQALKTQHERDLQGRDEAG------ 1645
Cdd:COG4913 461 PFvgeliEVRPEEERwrgaiervlggfaltllvppehyaaaLRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDslagkl 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1646 --------EERRRQLAKQLRDAEVERDEERKQRTLAV--------------------------------AARKKLEGELE 1685
Cdd:COG4913 541 dfkphpfrAWLEAELGRRFDYVCVDSPEELRRHPRAItragqvkgngtrhekddrrrirsryvlgfdnrAKLAALEAELA 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1686 ELKAQMASAGQGKEEAVKQLRKMQAQmKELWREVEETRtsreeifsqnrESEKRLKGLEAEVLRLQEELAASDRArrqaQ 1765
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQER-REALQRLAEYS-----------WDEIDVASAEREIAELEAELERLDAS----S 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1766 QDRDEMADEVAngnlskaAILEEKRQLEGRLGQleeeleeeqsnselLNDRYRKLLLQVESLTTEL-SAERSFSAKAESG 1844
Cdd:COG4913 685 DDLAALEEQLE-------ELEAELEELEEELDE--------------LKGEIGRLEKELEQAEEELdELQDRLEAAEDLA 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1845 RQQLERQIQELRGRLGEEDAGARARHKMT--IAALESKLAQAEEQLEQETRErilsgkLVRRAEKRLKEVVLQVEEERRV 1922
Cdd:COG4913 744 RLELRALLEERFAAALGDAVERELRENLEerIDALRARLNRAEEELERAMRA------FNREWPAETADLDADLESLPEY 817
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224831241 1923 ADQLrDQLEKGNLRVKqlkrqleeaeeeasRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1988
Cdd:COG4913 818 LALL-DRLEEDGLPEY--------------EERFKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1731-1966 |
1.17e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1731 SQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEvangnlskaailEEKRQLEGRLGQLEEELEEEQSNS 1810
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS------------EEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1811 ELLNDRYRKLLLQVESLTTELSAersfsAKAESGRQQLERQIQELRGRLGEEDAGARARHKmTIAALESKLAQAEEQLEQ 1890
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPE-----LLQSPVIQQLRAQLAELEAELAELSARYTPNHP-DVIALRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224831241 1891 ETRerilsgklvrraeKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLkrqleeaeeeaSRAQAGRRRLQRELE 1966
Cdd:COG3206 310 EAQ-------------RILASLEAELEALQAREASLQAQLAQLEARLAEL-----------PELEAELRRLEREVE 361
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1462-1695 |
1.34e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1462 LTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEekaavlraveereraeaegREREA 1541
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-------------------LEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1542 RALSLTRALEEEQEAREELERQNRALRAELEALLSSKD--DVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDA 1619
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224831241 1620 KLRLEVTVQALKTQHERdLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAG 1695
Cdd:COG4942 173 RAELEALLAELEEERAA-LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1198-1517 |
1.41e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.25 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1198 QRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAV------------QELRQRHGQALGE 1265
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASdhlnlvqtalrqQEKIERYQEDLEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1266 LAEQLEQ-------ARRGKGAWEKTRLALEAEVSELRAELSSLQTArqegeqrrrrlelqLQEVQGRAGDGERAR---AE 1335
Cdd:COG3096 359 LTERLEEqeevveeAAEQLAEAEARLEAAEEEVDSLKSQLADYQQA--------------LDVQQTRAIQYQQAVqalEK 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1336 AAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAA-GLREQLEEEA 1414
Cdd:COG3096 425 ARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAwQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1415 AARERAGRELQTAQAQLSEWRRRQEEEAGAleageearrraAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDL 1494
Cdd:COG3096 505 RSQQALAQRLQQLRAQLAELEQRLRQQQNA-----------ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQA 573
|
330 340
....*....|....*....|...
gi 224831241 1495 EQQRQLVSTLEKKQRKFDQLLAE 1517
Cdd:COG3096 574 AEAVEQRSELRQQLEQLRARIKE 596
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1048-1160 |
1.47e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1048 LEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRK-----------------------E 1104
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqlgnvrnnkeyealqkeiesL 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 224831241 1105 EKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDE 1160
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
715-739 |
2.36e-04 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 43.87 E-value: 2.36e-04
10 20
....*....|....*....|....*
gi 224831241 715 YKESLSRLMATLSNTNPSFVRCIVP 739
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
903-1128 |
2.44e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 903 LQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAAR-------- 974
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQlkvlsrsi 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 975 ---KQELELVVSELEARVGEEEECSRQmqteKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQ 1051
Cdd:TIGR04523 478 nkiKQNLEQKQKELKSKEKELKKLNEE----KKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1052 N----------------SKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLK 1115
Cdd:TIGR04523 554 LkkenlekeideknkeiEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
250
....*....|...
gi 224831241 1116 RRLDGESSELQEQ 1128
Cdd:TIGR04523 634 KNIKSKKNKLKQE 646
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1669-1939 |
2.46e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.44 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1669 QRTLA-VAARKKLEGELEELKAQMAsagqgkeEAVKQLRKMQAQMKELWREVEETRTSREEIFSqNRESEKRLKGLEAEV 1747
Cdd:PRK11281 66 EQTLAlLDKIDRQKEETEQLKQQLA-------QAPAKLRQAQAELEALKDDNDEETRETLSTLS-LRQLESRLAQTLDQL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1748 LRLQEELA-----------ASDRARRQ---AQQDRDEMADEVANGNLSKAAILEEKRQLegrlgqleeeleeEQSNSELL 1813
Cdd:PRK11281 138 QNAQNDLAeynsqlvslqtQPERAQAAlyaNSQRLQQIRNLLKGGKVGGKALRPSQRVL-------------LQAEQALL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1814 N--DRYRKLLLQVESLTTELSAERSFSAKAESgrQQLERQIQELRGRLGEEDagararhkmtiaaLESKLAQAEEQLEQE 1891
Cdd:PRK11281 205 NaqNDLQRKSLEGNTQLQDLLQKQRDYLTARI--QRLEHQLQLLQEAINSKR-------------LTLSEKTVQEAQSQD 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 224831241 1892 TRERILSGKLVRRaekrlkevvlQVEEERRVADQLRDQLEKGN------LRVKQ 1939
Cdd:PRK11281 270 EAARIQANPLVAQ----------ELEINLQLSQRLLKATEKLNtltqqnLRVKN 313
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
900-1212 |
2.48e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.01 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 900 KPLLQVTRQDEVLQARAQElqKVQELQQQSAREVGELQG---RVAQLEEERA-RLAEQLRAEAELCAEAEETRGRLAARK 975
Cdd:pfam02029 27 EPSGQVTESVEPNEHNSYE--EDSELKPSGQGGLDEEEAfldRTAKREERRQkRLQEALERQKEFDPTIADEKESVAERK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 976 ---QELELVVSELEARVGEEEECSRQMQTEK--KRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLE- 1049
Cdd:pfam02029 105 ennEEEENSSWEKEEKRDSRLGRYKEEETEIreKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKi 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1050 DQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQE----LEKLKRRLDGESSEL 1125
Cdd:pfam02029 185 KKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEaeqkLEELRRRRQEKESEE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1126 QEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARaqllkslreaqaalaeaqedlESERVARTKAEKQRrdLGEE 1205
Cdd:pfam02029 265 FEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQE---------------------EAERKLREEEEKRR--MKEE 321
|
....*..
gi 224831241 1206 LEALRGE 1212
Cdd:pfam02029 322 IERRRAE 328
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1025-1374 |
2.68e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1025 QKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKE 1104
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1105 EKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEElqaalaraedeggaraqlLKSLREAQAALAEAQED 1184
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE------------------IKDLTNQDSVKELIIKN 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1185 LEServARTKAEKQRRDLGEELEALRGELEDTldstnaQQELRSKreqeVTELKKtLEEETRIHEAAVQELRQRHGQaLG 1264
Cdd:TIGR04523 459 LDN---TRESLETQLKVLSRSINKIKQNLEQK------QKELKSK----EKELKK-LNEEKKELEEKVKDLTKKISS-LK 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1265 ELAEQLEQarrgkgawEKTRlaLEAEVSELRAELSSLQTARQEGEQRRRRLELQ--LQEVQGRAGDGERARAEAAEKLQR 1342
Cdd:TIGR04523 524 EKIEKLES--------EKKE--KESKISDLEDELNKDDFELKKENLEKEIDEKNkeIEELKQTQKSLKKKQEEKQELIDQ 593
|
330 340 350
....*....|....*....|....*....|..
gi 224831241 1343 AQAELENVSGALNEAESKTIRLSKELSSTEAQ 1374
Cdd:TIGR04523 594 KEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1649-1794 |
2.87e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.63 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1649 RRQLAKQLRDAEVERDEERKQRTLAVAARKKlEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKelwREVEETRTSREE 1728
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIAQANR-EAEEAELEQEREIETARIAEAEAELAKKKAEER---REAETARAEAEA 266
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224831241 1729 IFSQNRESEKRLKGLEAEVLRLQE--ELAASDRARRQAQQDRDEMADEVANgnlSKAAILEEKRQLEG 1794
Cdd:COG2268 267 AYEIAEANAEREVQRQLEIAEREReiELQEKEAEREEAELEADVRKPAEAE---KQAAEAEAEAEAEA 331
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1651-1939 |
3.09e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1651 QLAKQLRDAEVERDEERKQRTlAVAARKKLEGELEELKAQMASAgqgkEEAVKQLRKmqaqmkelwreveetrtsREEIF 1730
Cdd:COG3206 152 AVANALAEAYLEQNLELRREE-ARKALEFLEEQLPELRKELEEA----EAALEEFRQ------------------KNGLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1731 SqnreSEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEekrqlegrlgqleeeleeeqsns 1810
Cdd:COG3206 209 D----LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ----------------------- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1811 ellNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALESKLAQAEEQLEQ 1890
Cdd:COG3206 262 ---SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQ 338
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 224831241 1891 eTRERILSgklVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQ 1939
Cdd:COG3206 339 -LEARLAE---LPELEAELRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
777-1258 |
3.26e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.12 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 777 ILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFRAGVLAQLEEERDLKVTDIIVSFQAAAR 856
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 857 GYLARRAFQKRQQQQSalrvmqRNCAAYLKLRHWQWWRLFTKVKPLLQVTRQDEVLQARAQELQKVQELQQQSAREVGEL 936
Cdd:pfam02463 605 LAQLDKATLEADEDDK------RAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEI 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 937 QGRVAQLEEERARLAEQLRAEAELcaeaeetrgrLAARKQELELVVSELEARVGEEEECSRQMqtekKRLQQHIQELEAH 1016
Cdd:pfam02463 679 QELQEKAESELAKEEILRRQLEIK----------KKEQREKEELKKLKLEAEELLADRVQEAQ----DKINEELKLLKQK 744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1017 LEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQnsKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIAD 1096
Cdd:pfam02463 745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEE--REKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQL 822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1097 MEDRL---RKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEG----GARAQLLK 1169
Cdd:pfam02463 823 LIEQEekiKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESkeekEKEEKKEL 902
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1170 SLREAQAALAEAQEDLESERVARTKAEKQR-RDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIH 1248
Cdd:pfam02463 903 EEESQKLNLLEEKENEIEERIKEEAEILLKyEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEE 982
|
490
....*....|
gi 224831241 1249 EAAVQELRQR 1258
Cdd:pfam02463 983 FEEKEERYNK 992
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
980-1433 |
3.50e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.87 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 980 LVVSELEARVGEEEECSRqmqTEKKRLQQHIQELEAHLEAEEgaRQKLQLEKVTTEAKMKKFE-EDLLLLEDQNSKLSKE 1058
Cdd:pfam05483 349 FVVTEFEATTCSLEELLR---TEQQRLEKNEDQLKIITMELQ--KKSSELEEMTKFKNNKEVElEELKKILAEDEKLLDE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1059 RKLLEDRLAEFSSQAAEE----EEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRR---LDGESSELQEQMVE 1131
Cdd:pfam05483 424 KKQFEKIAEELKGKEQELifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKnieLTAHCDKLLLENKE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1132 QQQRAEELRAQLGRKEEELQAALARAEdeggaraQLLKSLREAQAALAEAQEDLESERvartKAEKQRRDlgeELEALRG 1211
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCKKQEE-------RMLKQIENLEEKEMNLRDELESVR----EEFIQKGD---EVKCKLD 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1212 ELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHgqalgelaeqleQARRGKGAWEKTRL-ALEAE 1290
Cdd:pfam05483 570 KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEN------------KALKKKGSAENKQLnAYEIK 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1291 VSELRAELSSL-QTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAE--KLQ-----RAQAELENVSGALNEAESKTI 1362
Cdd:pfam05483 638 VNKLELELASAkQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEavKLQkeidkRCQHKIAEMVALMEKHKHQYD 717
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224831241 1363 RLSKELSStEAQLHDAQEllQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSE 1433
Cdd:pfam05483 718 KIIEERDS-ELGLYKNKE--QEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
940-1342 |
3.68e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.24 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 940 VAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVGEEEE--CSRQMQTEKKRLQQHIQELEAhl 1017
Cdd:pfam02029 7 AARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEeaFLDRTAKREERRQKRLQEALE-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1018 eaeegaRQKlQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLlEDRLAEfssqAAEEEEKVKSLNKLRLKYEATIADM 1097
Cdd:pfam02029 85 ------RQK-EFDPTIADEKESVAERKENNEEEENSSWEKEEKR-DSRLGR----YKEEETEIREKEYQENKWSTEVRQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1098 EDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAA 1177
Cdd:pfam02029 153 EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1178 LAEAQEDLESERVARTKAEKQRRDLGE----ELEALRGEledtldstnaQQElrskREQEVTELKKTLEEETRIHEAavq 1253
Cdd:pfam02029 233 SQEREEEAEVFLEAEQKLEELRRRRQEkeseEFEKLRQK----------QQE----AELELEELKKKREERRKLLEE--- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1254 ELRQRhgqalgelaEQLEQARRGKGAWEKTRLALEAEvselraelsslqtarqegeqrrrrlelqlqevqgragdgeRAR 1333
Cdd:pfam02029 296 EEQRR---------KQEEAERKLREEEEKRRMKEEIE----------------------------------------RRR 326
|
....*....
gi 224831241 1334 AEAAEKLQR 1342
Cdd:pfam02029 327 AEAAEKRQK 335
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
829-1124 |
4.03e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 829 RAGVLAQLEEERDLKVTDIIVSFQAAargylarRAFQKRQQQQSALRVMQRNCAAYLKLRHWQWWRLFTK-VKPLLQVTR 907
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKM-------KAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEeKKKAEELKK 1654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 908 QDEVLQARAQELQKVQELQQQSAREvgelqgrVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEA 987
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEE-------AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 988 RVGEEEECSRQMQTEKKRLQQhiqeleahLEAEEGARQKLQLEKVTTEAKMKKF--EEDLLLLEDQNSKLSKERKLLEDR 1065
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEE--------AKKDEEEKKKIAHLKKEEEKKAEEIrkEKEAVIEEELDEEDEKRRMEVDKK 1799
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224831241 1066 LAEFSSQAAEEEEKVKS----LNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSE 1124
Cdd:PTZ00121 1800 IKDIFDNFANIIEGGKEgnlvINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGE 1862
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1332-1521 |
4.63e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1332 ARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLE 1411
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1412 EEAAARERAGRELQT-----------AQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGR 1480
Cdd:COG4942 101 AQKEELAELLRALYRlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 224831241 1481 RRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAA 1521
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1059-1241 |
5.11e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1059 RKLLEdrLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEqmveqqqRAEE 1138
Cdd:COG1579 7 RALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA-------RIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1139 LRAQLG--RKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDT 1216
Cdd:COG1579 78 YEEQLGnvRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170 180
....*....|....*....|....*
gi 224831241 1217 LDstnaqqELRSKREQEVTELKKTL 1241
Cdd:COG1579 158 LE------ELEAEREELAAKIPPEL 176
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1585-1864 |
5.63e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.33 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1585 VHELERACRVAEQAANDLRAQVTELEDELTAAED----AKLRLEVTVQALKTQHERDLQ--------------------- 1639
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEevdsLKSQLADYQQALDVQQTRAIQyqqavqalekaralcglpdlt 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1640 ------------GRDEAGEERRRQLAKQLRDAEVERDEERKqrtlAVAARKKLEGE-------------LEELKAQMASA 1694
Cdd:COG3096 436 penaedylaafrAKEQQATEEVLELEQKLSVADAARRQFEK----AYELVCKIAGEversqawqtarelLRRYRSQQALA 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1695 GQGK---------EEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQ 1765
Cdd:COG3096 512 QRLQqlraqlaelEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLR 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1766 QDRDEMADeVANGNLSKAAILEekrQLEGRLGQLEEELEEEqsnsellnDRYRKLLLQVEsltTELSAERSFSAKAesgR 1845
Cdd:COG3096 592 ARIKELAA-RAPAWLAAQDALE---RLREQSGEALADSQEV--------TAAMQQLLERE---REATVERDELAAR---K 653
|
330
....*....|....*....
gi 224831241 1846 QQLERQIQELRGRLGEEDA 1864
Cdd:COG3096 654 QALESQIERLSQPGGAEDP 672
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1566-1988 |
5.85e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1566 ALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELED------ELTAAEDAKLRLEVTVQALKtQHERDLQ 1639
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYL-DELREIE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1640 GRDEAGEERRRQLAKQLRDAE--VERDEERKQRtlavaaRKKLEGELEELK--AQMASAGQGKEEAVKQLRKMQA--QMK 1713
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEekEERLEELKKK------LKELEKRLEELEerHELYEEAKAKKEELERLKKRLTglTPE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1714 ELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSK-----AAILEE 1788
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEytaelKRIEKE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1789 KRQLEGRLgqLEEELEEEQSNSELLNDR----YRKLLLQVESLTTELSA--ERSFSAKAESGRQQLERQIqELRGRLG-- 1860
Cdd:PRK03918 468 LKEIEEKE--RKLRKELRELEKVLKKESelikLKELAEQLKELEEKLKKynLEELEKKAEEYEKLKEKLI-KLKGEIKsl 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1861 EEDAGARARHKMTIAALESKLAQAEEQLEQETRE---------RILSGKL------------VRRAEKRLKEVVLQVEEE 1919
Cdd:PRK03918 545 KKELEKLEELKKKLAELEKKLDELEEELAELLKEleelgfesvEELEERLkelepfyneyleLKDAEKELEREEKELKKL 624
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224831241 1920 RRVADQLRDQLEKGNLRVKQLKRQLEeaeeeasraQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1988
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELE---------ELEKKYSEEEYEELREEYLELSRELAGLRAELEE 684
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1072-1279 |
6.07e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 44.93 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1072 QAAEEEEKVKSLNKLRLKY---EATIADMEDRLRKE-EKGRQELEKLKRRLDGE---SSELQEQM---VEQQQRAEELRA 1141
Cdd:PLN03188 1038 PESTDESPEKKLEQERLRWteaESKWISLAEELRTElDASRALAEKQKHELDTEkrcAEELKEAMqmaMEGHARMLEQYA 1117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1142 QLGRKEEELQAALARAED------EGGARAQLLKSLREAQAALAEAQEDLESERvartkaEKQRRDLGEELEALRGELED 1215
Cdd:PLN03188 1118 DLEEKHIQLLARHRRIQEgiddvkKAAARAGVRGAESKFINALAAEISALKVER------EKERRYLRDENKSLQAQLRD 1191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1216 TLDSTNAQQEL--RSKREQE--VTELKKTLEEETRIHEA--AVQELRQRHGQALGELAEQLEQARRGKGA 1279
Cdd:PLN03188 1192 TAEAVQAAGELlvRLKEAEEalTVAQKRAMDAEQEAAEAykQIDKLKRKHENEISTLNQLVAESRLPKEA 1261
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1783-1988 |
6.26e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1783 AAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEe 1862
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1863 dagARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKR 1942
Cdd:COG4942 95 ---LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 224831241 1943 QLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1988
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1338-1886 |
6.47e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1338 EKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRvramEAEAAGLREQLEEEAAAR 1417
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESL----EGSKRKLEEKIRELEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1418 ERAGRELQtaqaQLSEWRRRQEEeagaLEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQ 1497
Cdd:PRK03918 269 EELKKEIE----ELEEKVKELKE----LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1498 RQLVSTLEKKQRKFDQLlaeEKAAVLRAVEERERAEAEGREREARALSLTRaleeeqeareelerqnraLRAELEALLSS 1577
Cdd:PRK03918 341 EELKKKLKELEKRLEEL---EERHELYEEAKAKKEELERLKKRLTGLTPEK------------------LEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1578 KDDVGKSVHELERACRVAEQAANDLRAQVTELEDeltaaedAKLRLEVTVQALKTQHERDLQGRDEAG-----------E 1646
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKK-------AKGKCPVCGRELTEEHRKELLEEYTAElkriekelkeiE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1647 ERRRQLAKQLRDAEVERDEER---KQRTLA---VAARKKLEG-ELEELKAQMASAGQGKEEAVKqLRKMQAQMKELWREV 1719
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESeliKLKELAeqlKELEEKLKKyNLEELEKKAEEYEKLKEKLIK-LKGEIKSLKKELEKL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1720 EETRTSREEIFSQNRESEKRLKGLEAEVL------------RLQE---------ELAASDRARRQAQQDRDEMADEVANG 1778
Cdd:PRK03918 552 EELKKKLAELEKKLDELEEELAELLKELEelgfesveeleeRLKElepfyneylELKDAEKELEREEKELKKLEEELDKA 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1779 NLSKAAILEEKRQLEGRLGQLEEELEEeqsnsellnDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGR 1858
Cdd:PRK03918 632 FEELAETEKRLEELRKELEELEKKYSE---------EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
570 580
....*....|....*....|....*...
gi 224831241 1859 LGEedagaRARHKMTIAALESKLAQAEE 1886
Cdd:PRK03918 703 LEE-----REKAKKELEKLEKALERVEE 725
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1092-1359 |
6.56e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1092 ATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEE---LQAALARAEDEGGARAQLL 1168
Cdd:COG3883 9 PTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEidkLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1169 KSLREAQAALAEAQEDLE------------SERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTE 1236
Cdd:COG3883 89 GERARALYRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1237 LKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAweKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLE 1316
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA--AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 224831241 1317 LQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAES 1359
Cdd:COG3883 247 AGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGA 289
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
935-1200 |
6.57e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 935 ELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQELE 1014
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1015 AHLEAEEGARQKLQLEKVTTEAKMKKFEEdlLLLEDQNSKLSKERkllEDRLAEFSSQAAEEEEKVKSLNKLRLKyeatI 1094
Cdd:COG1340 92 EELDELRKELAELNKAGGSIDKLRKEIER--LEWRQQTEVLSPEE---EKELVEKIKELEKELEKAKKALEKNEK----L 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1095 ADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREA 1174
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELREL 242
|
250 260
....*....|....*....|....*.
gi 224831241 1175 QAALAEAQEDLESERVARTKAEKQRR 1200
Cdd:COG1340 243 RKELKKLRKKQRALKREKEKEELEEK 268
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1054-1404 |
7.63e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1054 KLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADME--DRLRKEEKGRQELEKLKRRLDGESSELQ--EQM 1129
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLEelEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1130 VEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQllkslreaqAALAEAQEDLESERVARTKAEKQRRDLGEELEAL 1209
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATE---------EELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1210 RGELEDTLDSTNAQQELRSKREQEVT------------ELKKTLEEETRIHEAA---------VQELRQRHGQALGELAE 1268
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLLlliaaallallgLGGSLLSLILTIAGVLflvlgllalLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1269 QLEQARRGKG----AWEKTRLALE-------AEVSELRAELSSLQTARQEGEQRRRRLELQ---------LQEVQGRAGD 1328
Cdd:COG4717 306 ELQALPALEEleeeELEELLAALGlppdlspEELLELLDRIEELQELLREAEELEEELQLEeleqeiaalLAEAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1329 GERARAEAAEKLQRAQAELENVSGALNEAESKTI---------RLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAM 1399
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELEEQLEELLGELEellealdeeELEEELEELEEELEELEEELEELREELAELEAELEQL 465
|
....*
gi 224831241 1400 EAEAA 1404
Cdd:COG4717 466 EEDGE 470
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1194-1920 |
7.86e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1194 KAEKQRRDLGEELEALRGELEDTLdstnaqqelrsKREQEVTELKKTLEEETRIHEAAVQELRQRhgqaLGELAEQLEQA 1273
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFI-----------KRTENIEELIKEKEKELEEVLREINEISSE----LPELREELEKL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1274 RRGKGAWEKTRlaleAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAaEKLQRAQAELENVSGA 1353
Cdd:PRK03918 227 EKEVKELEELK----EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1354 LNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKlalgSRVRAMEAEAAGLREQLEEEAAARERagreLQTAQAQLSE 1433
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE----ERLEELKKKLKELEKRLEELEERHEL----YEEAKAKKEE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1434 WRRRQEEEAGaleageEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELddatmdlEQQRQLVSTLEKKQRKFD- 1512
Cdd:PRK03918 374 LERLKKRLTG------LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEI-------KELKKAIEELKKAKGKCPv 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1513 ---QLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGK-SVHEL 1588
Cdd:PRK03918 441 cgrELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKyNLEEL 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1589 ERACRVAE---QAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQherdlqgrdeagEERRRQLAKQLRD---AEVE 1662
Cdd:PRK03918 521 EKKAEEYEklkEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDEL------------EEELAELLKELEElgfESVE 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1663 RDEERKQRTLAVAAR----KKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETrtsreeifsQNRESEK 1738
Cdd:PRK03918 589 ELEERLKELEPFYNEylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL---------EKKYSEE 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1739 RLKGLEAEVLRLQEELAASDRARRQAQQDRDEMadevangnlsKAAILEEKRQLEGRlgqleeeleeeqsnsellnDRYR 1818
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAELEELEKRREEI----------KKTLEKLKEELEER-------------------EKAK 710
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1819 KlllQVESLTTELSaersfsakaesgrqqlerQIQELRGRLgeedagARARHKMTIAALeSKLAQAEEQLEQETRERILS 1898
Cdd:PRK03918 711 K---ELEKLEKALE------------------RVEELREKV------KKYKALLKERAL-SKVGEIASEIFEELTEGKYS 762
|
730 740
....*....|....*....|..
gi 224831241 1899 GKLVRRAEKRLKEVVLQVEEER 1920
Cdd:PRK03918 763 GVRVKAEENKVKLFVVYQGKER 784
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
999-1714 |
8.67e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.33 E-value: 8.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 999 MQTEKKRLQQHIQELEAHLEAEEGARQKLQLEkvtTEAKMKKFEEDLllleDQNSKLSKERKLLEDRLAEFSSQAAEEEE 1078
Cdd:pfam05483 97 IEAELKQKENKLQENRKIIEAQRKAIQELQFE---NEKVSLKLEEEI----QENKDLIKENNATRHLCNLLKETCARSAE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1079 KVKSLNKLRLKYEATIADMEDRLRKEEKGRQELeklkrRLDGESS------ELQEQMVEQQQRAEELRAQLGRKEEELQA 1152
Cdd:pfam05483 170 KTKKYEYEREETRQVYMDLNNNIEKMILAFEEL-----RVQAENArlemhfKLKEDHEKIQHLEEEYKKEINDKEKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1153 ALARAEDeggaRAQLLKSLREAQAALAEAQEDLESERVARTKAEKQrrdLGEELEALRGELEDTLDSTnaqqelrskreQ 1232
Cdd:pfam05483 245 LLIQITE----KENKMKDLTFLLEESRDKANQLEEKTKLQDENLKE---LIEKKDHLTKELEDIKMSL-----------Q 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1233 EVTELKKTLEEETRIHEAAVQELRQrhgqalgELAEQLEQArrgkgawEKTRLALEAEVSELRAELSSlqtarqegeqrr 1312
Cdd:pfam05483 307 RSMSTQKALEEDLQIATKTICQLTE-------EKEAQMEEL-------NKAKAAHSFVVTEFEATTCS------------ 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1313 rrLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQ--ELLQEETRAK- 1389
Cdd:pfam05483 361 --LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKqfEKIAEELKGKe 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1390 LALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEK 1469
Cdd:pfam05483 439 QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKH 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1470 TETVDRLERGRRRLQQELDDATmdlEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARAL----- 1544
Cdd:pfam05483 519 QEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKilenk 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1545 --SLTRALEEEQEAREELERQNRALR----AELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTEL----EDELT 1614
Cdd:pfam05483 596 cnNLKKQIENKNKNIEELHQENKALKkkgsAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKkiseEKLLE 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1615 AAEDAKLRLEvtvQALKTQHERDLQGRDEAG------EERRRQLAK--QLRDAEVERDEERKQRTlaVAARKKLEGELEE 1686
Cdd:pfam05483 676 EVEKAKAIAD---EAVKLQKEIDKRCQHKIAemvalmEKHKHQYDKiiEERDSELGLYKNKEQEQ--SSAKAALEIELSN 750
|
730 740
....*....|....*....|....*...
gi 224831241 1687 LKAQMASAGQGKEEAVKQLRKMQAQMKE 1714
Cdd:pfam05483 751 IKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1242-1796 |
9.68e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 44.46 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1242 EEETRIHEAAVQELRQRHGQA----LGELAEQLEQARRGKGAWE---------KTRLALEAEVSELRAELSSLqtARQEG 1308
Cdd:COG3899 663 EERRALHRRIARALEARGPEPleerLFELAHHLNRAGERDRAARlllraarraLARGAYAEALRYLERALELL--PPDPE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1309 EQRRRRLELQLQEVQGRAGDGERARaEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRA 1388
Cdd:COG3899 741 EEYRLALLLELAEALYLAGRFEEAE-ALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALAL 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1389 KLALGSRV-----------------RAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEA 1451
Cdd:COG3899 820 AERLGDRRlearalfnlgfilhwlgPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAA 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1452 RRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERER 1531
Cdd:COG3899 900 AAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAA 979
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1532 AEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELED 1611
Cdd:COG3899 980 AAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAA 1059
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1612 ELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQM 1691
Cdd:COG3899 1060 AALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLA 1139
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1692 ASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEM 1771
Cdd:COG3899 1140 AALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEA 1219
|
570 580
....*....|....*....|....*
gi 224831241 1772 ADEVANGNLSKAAILEEKRQLEGRL 1796
Cdd:COG3899 1220 AALLLLLLLAALALAAALLALRLLA 1244
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
935-1389 |
9.84e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.33 E-value: 9.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 935 ELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSE----------LEARVGEEEECSRQMQTEKK 1004
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnatrhlcnlLKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1005 RLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMK-KFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSL 1083
Cdd:pfam05483 180 ETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1084 NKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSE----LQEQMVEQQQRAEELRAQLGRKEEELQAALARAED 1159
Cdd:pfam05483 260 TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDikmsLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1160 EGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNaqqelrsKREQEVTELKK 1239
Cdd:pfam05483 340 LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKN-------NKEVELEELKK 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1240 TLEEEtrihEAAVQELRQrhgqaLGELAEQLEQARRGKGAWEKTRlalEAEVSELRAELSSLQTARQEGEQRRRRLELQL 1319
Cdd:pfam05483 413 ILAED----EKLLDEKKQ-----FEKIAEELKGKEQELIFLLQAR---EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1320 QEVQGR----AGDGERARAEAAEKLQRAQ---AELENVSGALNEAESKTIRLSKE---LSSTEAQLHDAQELLQEETRAK 1389
Cdd:pfam05483 481 EKEKLKnielTAHCDKLLLENKELTQEASdmtLELKKHQEDIINCKKQEERMLKQienLEEKEMNLRDELESVREEFIQK 560
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1075-1348 |
1.15e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1075 EEEEKVKSLNKLRLKYEAtiadmEDRLRKEEKGRQELEKLKRR---LDGESSELQEQMVEQQQRAEEL-RAQLGRKEEEL 1150
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEK-----EEKAREVERRRKLEEAEKARqaeMDRQAAIYAEQERMAMERERELeRIRQEERKREL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1151 QAALARAEDEGGARAQLLKSLREAQAALAEA-QEDLESERVARTKAEKQRRDLGE---ELEALRGELEDTldstnAQQEL 1226
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELERLQMERQQKNERvRQELEAARKVKILEEERQRKIQQqkvEMEQIRAEQEEA-----RQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1227 RSKREQEVTELKKTLEEETRiHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRaelsslqTARQ 1306
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQE-RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERK-------QAMI 509
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 224831241 1307 EGEQRRRRLELQLQEVQGRAGDGERARaeAAEKLQRAQAELE 1348
Cdd:pfam17380 510 EEERKRKLLEKEMEERQKAIYEEERRR--EAEEERRKQQEME 549
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
837-1223 |
1.25e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 837 EEERDLKVTDIIVSfQAAARGYLARRAFQKRQQQQSALRVMQRNCAAyLKLrhwqwwrlftkvkpllQVTRQDEVLQARA 916
Cdd:pfam15921 507 EKERAIEATNAEIT-KLRSRVDLKLQELQHLKNEGDHLRNVQTECEA-LKL----------------QMAEKDKVIEILR 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 917 QELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRaeaelcaeaeetrgRLAARKQELELVVSELEARVGEeeecs 996
Cdd:pfam15921 569 QQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQ--------------EFKILKDKKDAKIRELEARVSD----- 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 997 rqMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEE 1076
Cdd:pfam15921 630 --LELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSE 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1077 EEKVKSLNKlrlkyeaTIADMEDRLRKEEKGRQELEKLKR-RLDGESSELQeQMVEQQQRAEELRAQLGRKEEELQAALA 1155
Cdd:pfam15921 708 LEQTRNTLK-------SMEGSDGHAMKVAMGMQKQITAKRgQIDALQSKIQ-FLEEAMTNANKEKHFLKEEKNKLSQELS 779
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1156 RAEDEGGARAQLLKSLREAQAALAEAQEDLES--ERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQ 1223
Cdd:pfam15921 780 TVATEKNKMAGELEVLRSQERRLKEKVANMEValDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1059-1299 |
1.27e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.53 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1059 RKLLeDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEE---KGRQELEKLKRRlDGESSELQEQmVEQQQR 1135
Cdd:COG0497 144 RELL-DAFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELDllrFQLEELEAAALQ-PGEEEELEEE-RRRLSN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1136 AEELRAQLGrkeeelQAALARAEDEGGArAQLLKSLREAQAALAEAQEDLE--SERVARTKAEKQrrDLGEELEALRGEL 1213
Cdd:COG0497 221 AEKLREALQ------EALEALSGGEGGA-LDLLGQALRALERLAEYDPSLAelAERLESALIELE--EAASELRRYLDSL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1214 E---DTLDSTNA-QQELRS-KR-----EQEVTELKKTLEEE--------TRIH--EAAVQELRQrhgqALGELAEQLEQA 1273
Cdd:COG0497 292 EfdpERLEEVEErLALLRRlARkygvtVEELLAYAEELRAElaelensdERLEelEAELAEAEA----ELLEAAEKLSAA 367
|
250 260
....*....|....*....|....*.
gi 224831241 1274 RRgkgaweKTRLALEAEVSELRAELS 1299
Cdd:COG0497 368 RK------KAAKKLEKAVTAELADLG 387
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1627-1986 |
1.36e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1627 VQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERdeeRKQRTLAVAARkklEGELEELKAQMASAGQGKEEAVKQLR 1706
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVER---RRKLEEAEKAR---QAEMDRQAAIYAEQERMAMERERELE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1707 KMQAQMKElwREVEETRtsREEIFSQnresEKRLKGLEaevlRLQEElaasdrarRQAQQDRDEMADEVANgnlsKAAIL 1786
Cdd:pfam17380 352 RIRQEERK--RELERIR--QEEIAME----ISRMRELE----RLQME--------RQQKNERVRQELEAAR----KVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1787 EEKRQLEGRLGQLEEELEEEQSNsellNDRYRKLLLQVESLTTELSAERsfsakaesgRQQLERQIQELRGRLGEEDaga 1866
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQE----EARQREVRRLEEERAREMERVR---------LEEQERQQQVERLRQQEEE--- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1867 RARHKMTIAALESKLAQAEEQleqetRERILSGKLVRRAEKRLkevvlqvEEERRvadqlRDQLEKgnlrvKQLKRQLEE 1946
Cdd:pfam17380 472 RKRKKLELEKEKRDRKRAEEQ-----RRKILEKELEERKQAMI-------EEERK-----RKLLEK-----EMEERQKAI 529
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 224831241 1947 AEEEASRAQAGRRRLQRELEDVTESAESMnREVTTLRNRL 1986
Cdd:pfam17380 530 YEEERRREAEEERRKQQEMEERRRIQEQM-RKATEERSRL 568
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
906-1164 |
1.36e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 906 TRQDEVLQARAQELQ----KVQELQQQSAREVGELQGR----------------VAQLEEERARLAEQLRAEAELCAEAE 965
Cdd:COG4913 609 RAKLAALEAELAELEeelaEAEERLEALEAELDALQERrealqrlaeyswdeidVASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 966 ETRGRLAARKQELELVVSELEARVGEEEECSRQmQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDL 1045
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKE-LEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1046 LL-LEDQNSKLSKERKLLEDRLaefssqaaeeeekVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRrldgesse 1124
Cdd:COG4913 768 REnLEERIDALRARLNRAEEEL-------------ERAMRAFNREWPAETADLDADLESLPEYLALLDRLEE-------- 826
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 224831241 1125 lqEQMVEQQQRAEELRAQL-GRKEEELQAALARAEDEGGAR 1164
Cdd:COG4913 827 --DGLPEYEERFKELLNENsIEFVADLLSKLRRAIREIKER 865
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1566-1965 |
1.39e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1566 ALRAELEALLSSKDD-VGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKL--------RLEVTVQALKTQHER 1636
Cdd:pfam12128 283 ETSAELNQLLRTLDDqWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIetaaadqeQLPSWQSELENLEER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1637 -----DLQGRDEAGEERRRQLAKQLRDAEVERDEER---------KQRTLAVAARKKLEGEL-EELKAQMASAGQGK--- 1698
Cdd:pfam12128 363 lkaltGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKlakireardRQLAVAEDDLQALESELrEQLEAGKLEFNEEEyrl 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1699 EEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRlkglEAEVLRLQEELAASDRARRQAQqdrDEMADEVANG 1778
Cdd:pfam12128 443 KSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAA----NAEVERLQSELRQARKRRDQAS---EALRQASRRL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1779 NLSKAAILEEKRQLEGRLGQLEEELEEEQSnseLLNDRYRKLLLQVESLTTELSAERSFSAKAESGR------------- 1845
Cdd:pfam12128 516 EERQSALDELELQLFPQAGTLLHFLRKEAP---DWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNlygvkldlkridv 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1846 ---QQLERQIQELRGRLGEEDAGARARHkmtiAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVE-EERR 1921
Cdd:pfam12128 593 pewAASEEELRERLDKAEEALQSAREKQ----AAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQsEKDK 668
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 224831241 1922 VADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQREL 1965
Cdd:pfam12128 669 KNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREA 712
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1602-1988 |
1.45e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1602 LRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLE 1681
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1682 GELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEI---FSQNRESEKRLKGLEAEVLRLQEELAASD 1758
Cdd:pfam02463 328 KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELlakKKLESERLSSAAKLKEEELELKSEEEKEA 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1759 RARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEgRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFS 1838
Cdd:pfam02463 408 QLLLELARQLEDLLKEEKKEELEILEEEEESIELK-QGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQL 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1839 AKAESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEE 1918
Cdd:pfam02463 487 ELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKL 566
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224831241 1919 ERRVADQLRD----QLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1988
Cdd:pfam02463 567 VRALTELPLGarklRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKES 640
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1060-1382 |
1.64e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.99 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1060 KLLEDRLAEFSsqaaeeeEKVKSLnklrlkyEATIADMEDRLR-KEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEE 1138
Cdd:pfam00038 7 QELNDRLASYI-------DKVRFL-------EQQNKLLETKISeLRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1139 LRAQLGRKEEELQAALARAEDEGGARaqllkslREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGEledtld 1218
Cdd:pfam00038 73 LQLELDNLRLAAEDFRQKYEDELNLR-------TSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKN------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1219 stnaqqelrskREQEVTELKKTLEEETRIHE---AAVQELrqrhGQALGELAEQLE-QARRGKG---AWEKTRLA-LEAE 1290
Cdd:pfam00038 140 -----------HEEEVRELQAQVSDTQVNVEmdaARKLDL----TSALAEIRAQYEeIAAKNREeaeEWYQSKLEeLQQA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1291 VSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEklqRAQAELENVSGALNEAESKTIRLSKELss 1370
Cdd:pfam00038 205 AARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEE---RYELQLADYQELISELEAELQETRQEM-- 279
|
330
....*....|..
gi 224831241 1371 tEAQLHDAQELL 1382
Cdd:pfam00038 280 -ARQLREYQELL 290
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1036-1398 |
1.71e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1036 AKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSS--QAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEK 1113
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1114 LKRRLDGESSELQEqmvEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVART 1193
Cdd:COG4717 161 LEEELEELEAELAE---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1194 KAEKQRR-----------DLGEELEALRGELEDTLDS------------TNAQQELRSKREQEVTELKKT--LEEETRIH 1248
Cdd:COG4717 238 AAALEERlkearlllliaAALLALLGLGGSLLSLILTiagvlflvlgllALLFLLLAREKASLGKEAEELqaLPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1249 EAAVQELRQRHG-------QALGELAEQLEQARRGKGAWEKtrLALEAEVSELRAELSSL-------------QTARQEG 1308
Cdd:COG4717 318 EEELEELLAALGlppdlspEELLELLDRIEELQELLREAEE--LEEELQLEELEQEIAALlaeagvedeeelrAALEQAE 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1309 EQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDA------QELL 1382
Cdd:COG4717 396 EYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLeedgelAELL 475
|
410
....*....|....*.
gi 224831241 1383 QEETRAKLALGSRVRA 1398
Cdd:COG4717 476 QELEELKAELRELAEE 491
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1134-1638 |
2.45e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 42.92 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1134 QRAEELRAQLGRKEEELQAALARAEDEGGAR---------AQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGE 1204
Cdd:COG3899 729 ERALELLPPDPEEEYRLALLLELAEALYLAGrfeeaeallERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEE 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1205 ELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTR 1284
Cdd:COG3899 809 AYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAA 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1285 LALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRL 1364
Cdd:COG3899 889 AAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAA 968
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1365 SKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGA 1444
Cdd:COG3899 969 AAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAA 1048
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1445 LEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLR 1524
Cdd:COG3899 1049 LAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAA 1128
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1525 AVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRA 1604
Cdd:COG3899 1129 ARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAA 1208
|
490 500 510
....*....|....*....|....*....|....
gi 224831241 1605 QVTELEDELTAAEDAKLRLEVTVQALKTQHERDL 1638
Cdd:COG3899 1209 LLALALLALEAAALLLLLLLAALALAAALLALRL 1242
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1231-1406 |
2.47e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1231 EQEVTELKKTLEEetriHEAAVQELRQRHGqaLGELAEQLEQarrgkgawektrlaLEAEVSELRAELSSLQTARQEGEQ 1310
Cdd:COG3206 181 EEQLPELRKELEE----AEAALEEFRQKNG--LVDLSEEAKL--------------LLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1311 RRRRLELQLQEVQGRAGD--GERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRA 1388
Cdd:COG3206 241 RLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEA 320
|
170
....*....|....*....
gi 224831241 1389 KL-ALGSRVRAMEAEAAGL 1406
Cdd:COG3206 321 ELeALQAREASLQAQLAQL 339
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1129-1299 |
2.90e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1129 MVEQQQRAEEL------RAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESE-RVARTKAEKQRRD 1201
Cdd:COG1579 2 MPEDLRALLDLqeldseLDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEiEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1202 LGE-----ELEALRGELEdtldstnAQQELRSKREQEVTELKKTLEEetriHEAAVQELRQRHGQALGELAEQLEQARRG 1276
Cdd:COG1579 82 LGNvrnnkEYEALQKEIE-------SLKRRISDLEDEILELMERIEE----LEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|...
gi 224831241 1277 KGAWEKTRLALEAEVSELRAELS 1299
Cdd:COG1579 151 LAELEAELEELEAEREELAAKIP 173
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1085-1202 |
2.93e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1085 KLRLKYEATIADMEDRLRKEEKGRQELEKLKRrldgesselqEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEgGAR 1164
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKK----------EQDEASFERLAELRDELAELEEELEALKARWEAE-KEL 469
|
90 100 110
....*....|....*....|....*....|....*...
gi 224831241 1165 AQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDL 1202
Cdd:COG0542 470 IEEIQELKEELEQRYGKIPELEKELAELEEELAELAPL 507
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1646-1791 |
3.63e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1646 EERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQA--QMKELWREVEETR 1723
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224831241 1724 TSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANgnlsKAAILEEKRQ 1791
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA----ELEELEAERE 166
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1074-1406 |
4.11e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1074 AEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAA 1153
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1154 LARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQE 1233
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1234 VTELKKTLEEETRIH-EAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRR 1312
Cdd:COG4372 166 LAALEQELQALSEAEaEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1313 RRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLAL 1392
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330
....*....|....
gi 224831241 1393 GSRVRAMEAEAAGL 1406
Cdd:COG4372 326 KKLELALAILLAEL 339
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1110-1985 |
4.13e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1110 ELEKLKRRLDGESSelQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLreaqaalAEAQEDLESER 1189
Cdd:TIGR00606 167 EGKALKQKFDEIFS--ATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQI-------TSKEAQLESSR 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1190 VARTKAEKQRRDLGE---ELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGEL 1266
Cdd:TIGR00606 238 EIVKSYENELDPLKNrlkEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1267 AEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRA-------------------- 1326
Cdd:TIGR00606 318 ERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLeldgfergpfserqiknfht 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1327 ----GDGERAR------AEAAEKLQRAQAELENV----SGALNEAESKTIRLSKELSSTEaqlHDAQELLQEETRAKLAL 1392
Cdd:TIGR00606 398 lvieRQEDEAKtaaqlcADLQSKERLKQEQADEIrdekKGLGRTIELKKEILEKKQEELK---FVIKELQQLEGSSDRIL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1393 GSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEaltqrlaEKTET 1472
Cdd:TIGR00606 475 ELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTK-------DKMDK 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1473 VDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLlaEEKAAVLRAVEEreraeaegrerearalSLTRALEE 1552
Cdd:TIGR00606 548 DEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQT--RDRLAKLNKELA----------------SLEQNKNH 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1553 EQEAREELERQNRALRAELEALLSSKD---DVGKSVHELERAC--RVAEQAANDLRAQ-VTELEDELTAAEDAKLRLEVT 1626
Cdd:TIGR00606 610 INNELESKEEQLSSYEDKLFDVCGSQDeesDLERLKEEIEKSSkqRAMLAGATAVYSQfITQLTDENQSCCPVCQRVFQT 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1627 VQALKtQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKaqmasagqgkeeavKQLR 1706
Cdd:TIGR00606 690 EAELQ-EFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELR--------------NKLQ 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1707 KMQAQMKELWREVEETRTSREEIFSQnRESEKRLKGLEAEVLRLQEELaaSDRARRQAQQDRDEmadEVANGNLSKAAIL 1786
Cdd:TIGR00606 755 KVNRDIQRLKNDIEEQETLLGTIMPE-EESAKVCLTDVTIMERFQMEL--KDVERKIAQQAAKL---QGSDLDRTVQQVN 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1787 EEKRQLEGRLgqlEEELEEEQSNSELLNDRyRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGE---ED 1863
Cdd:TIGR00606 829 QEKQEKQHEL---DTVVSKIELNRKLIQDQ-QEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSlirEI 904
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1864 AGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEE-ERRVADQLRDQLEKGNLRVKQLKR 1942
Cdd:TIGR00606 905 KDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDiENKIQDGKDDYLKQKETELNTVNA 984
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 224831241 1943 QLEEAEEEASRAQAGRRRLQRELeDVTESAESMNREVTTLRNR 1985
Cdd:TIGR00606 985 QLEECEKHQEKINEDMRLMRQDI-DTQKIQERWLQDNLTLRKR 1026
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1696-1988 |
4.19e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1696 QGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELaaSDRARRQAQQDRDEMADEV 1775
Cdd:COG5185 236 KGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENT--KEKIAEYTKSIDIKKATES 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1776 ANGNLSKAAILE--EKRQLEGRLGQLEEELEEEQSNSELLnDRYRKLLLQVESLTTELSAERSfSAKAESGRQQLERQIQ 1853
Cdd:COG5185 314 LEEQLAAAEAEQelEESKRETETGIQNLTAEIEQGQESLT-ENLEAIKEEIENIVGEVELSKS-SEELDSFKDTIESTKE 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1854 ELRGRLGEedagARARHKMTIAALESKLAQAEEQLEQETRErilsgklvrraekrLKEVVLQVEEERRVADQLRDQLEKG 1933
Cdd:COG5185 392 SLDEIPQN----QRGYAQEILATLEDTLKAADRQIEELQRQ--------------IEQATSSNEEVSKLLNELISELNKV 453
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 224831241 1934 NLRVKQL--KRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1988
Cdd:COG5185 454 MREADEEsqSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLER 510
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1654-1754 |
4.30e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.41 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1654 KQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLR-KMQAQMKELWREVEETRTSREeifsq 1732
Cdd:cd16269 191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKeKMEEERENLLKEQERALESKL----- 265
|
90 100
....*....|....*....|...
gi 224831241 1733 nRESEKRLK-GLEAEVLRLQEEL 1754
Cdd:cd16269 266 -KEQEALLEeGFKEQAELLQEEI 287
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1048-1257 |
4.41e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1048 LEDQNSKLSKERKLLEDRLAEF---------SSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRL 1118
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFrqknglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1119 --DGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARaedeggaRAQLLKSLREAQAALaeaqedLESERVARTKAE 1196
Cdd:COG3206 260 lqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ-------IAALRAQLQQEAQRI------LASLEAELEALQ 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224831241 1197 KQRRDLGEELEALRGELEDTldstnaqqelrSKREQEVTELKKTLEEETRIHEAAVQELRQ 1257
Cdd:COG3206 327 AREASLQAQLAQLEARLAEL-----------PELEAELRRLEREVEVARELYESLLQRLEE 376
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1131-1523 |
4.58e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 41.82 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1131 EQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALR 1210
Cdd:COG5278 104 EQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1211 GELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAE 1290
Cdd:COG5278 184 ALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1291 VSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSS 1370
Cdd:COG5278 264 AAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAA 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1371 TEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEE 1450
Cdd:COG5278 344 LALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALE 423
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224831241 1451 ARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVL 1523
Cdd:COG5278 424 LAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAA 496
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1833-1928 |
4.88e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1833 AERSFSAKAESGRQQLERQIQELRGR--LGEEDAGARARHKMTIAALESKLAQAEEQLEQ-------ETRERILsgKLVR 1903
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSqaLAEAQQQELVALEGLAAELEEKQQELEAQLEQlqekaaeTSQERKQ--KRKE 220
|
90 100
....*....|....*....|....*.
gi 224831241 1904 RAEKRLKEVVLQVEEERRVAD-QLRD 1928
Cdd:PRK11448 221 ITDQAAKRLELSEEETRILIDqQLRK 246
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1048-1384 |
4.89e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1048 LEDQNSKLSKERKLLEDRLAEFSSQAAEEEE-------KVKSLNKLRLKYEATIADM---------EDRLRKE-EKGRQE 1110
Cdd:TIGR00606 575 LEDWLHSKSKEINQTRDRLAKLNKELASLEQnknhinnELESKEEQLSSYEDKLFDVcgsqdeesdLERLKEEiEKSSKQ 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1111 LEKLKRRLDGESSELQEQMVEQQ------QRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQED 1184
Cdd:TIGR00606 655 RAMLAGATAVYSQFITQLTDENQsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPG 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1185 LESE--------RVARTKAEKQRRDLGEELEALRgELEDTLDSTNAQQELRSKREQEVTELKKTLEE----ETRIHEAA- 1251
Cdd:TIGR00606 735 RQSIidlkekeiPELRNKLQKVNRDIQRLKNDIE-EQETLLGTIMPEEESAKVCLTDVTIMERFQMElkdvERKIAQQAa 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1252 ----------VQELRQR---HGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQ 1318
Cdd:TIGR00606 814 klqgsdldrtVQQVNQEkqeKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVEL 893
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224831241 1319 LQEVQGRAGDGERAR------AEAAEKLQRAQAELENVSGALNE-AESKTIRLSKELSSTEAQLHDAQELLQE 1384
Cdd:TIGR00606 894 STEVQSLIREIKDAKeqdsplETFLEKDQQEKEELISSKETSNKkAQDKVNDIKEKVKNIHGYMKDIENKIQD 966
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1023-1239 |
4.98e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1023 ARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYE---------AT 1093
Cdd:PHA02562 214 NIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQ 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1094 IADMEDRLRK-EEKGRQ---ELEKLKRRLDgessELQEQMVE---QQQRAEELRAQLGRKEEELQAALARAEDeggARAQ 1166
Cdd:PHA02562 294 ISEGPDRITKiKDKLKElqhSLEKLDTAID----ELEEIMDEfneQSKKLLELKNKISTNKQSLITLVDKAKK---VKAA 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224831241 1167 LlkslreaqaalaeaqedleservarTKAEKQRRDLGEELEALRGELEDtLDSTNAQQELRSKREQEVTELKK 1239
Cdd:PHA02562 367 I-------------------------EELQAEFVDNAEELAKLQDELDK-IVKTKSELVKEKYHRGIVTDLLK 413
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1605-1984 |
5.17e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1605 QVTELEDELTAAEDAKLRLEVTVQALKtqheRDLQGRDEAGEERRRQLAKQLRDAE-VERDEERKQRTLavaarKKLEGE 1683
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQLNEQISQLK----KELTNSESENSEKQRELEEKQNEIEkLKKENQSYKQEI-----KNLESQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1684 LEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSRE-------EIFSQNRESEKRLKGLEAEVLRLQEELAA 1756
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIknnseikDLTNQDSVKELIIKNLDNTRESLETQLKV 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1757 SDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQleeeleeeqsnselLNDRYRKLLLQVESLTTELSaers 1836
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD--------------LTKKISSLKEKIEKLESEKK---- 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1837 fsakaesgrqQLERQIQELRGRLGEEDAGararhkMTIAALESKLAQAEEQLEQETRERilsgKLVRRAEKRLKEVVLQV 1916
Cdd:TIGR04523 535 ----------EKESKISDLEDELNKDDFE------LKKENLEKEIDEKNKEIEELKQTQ----KSLKKKQEEKQELIDQK 594
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224831241 1917 EEERrvaDQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRN 1984
Cdd:TIGR04523 595 EKEK---KDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1194-1430 |
6.37e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1194 KAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEtrihEAAVQELRQRHGQALGELAEQLEQA 1273
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1274 RRGKGAWEKTRLALEAE-VSELRAELSSLQTARQEGEQRRRRLELQLQEVqgragdgERARAEAAEKLQRAQAELENVSG 1352
Cdd:COG3883 96 YRSGGSVSYLDVLLGSEsFSDFLDRLSALSKIADADADLLEELKADKAEL-------EAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224831241 1353 ALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQ 1430
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1261-1395 |
6.96e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1261 QALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKL 1340
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVS 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 224831241 1341 QRAQAELEnvsgALNEAESKtirLSKELSSTEAQLhDAQELLQEETRAKLA-LGSR 1395
Cdd:PRK09039 133 ARALAQVE----LLNQQIAA---LRRQLAALEAAL-DASEKRDRESQAKIAdLGRR 180
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1563-1778 |
7.51e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1563 QNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRD 1642
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1643 EAGEE-----------------RRRQLAKQLRDAEVER-DEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQ 1704
Cdd:COG3883 97 RSGGSvsyldvllgsesfsdflDRLSALSKIADADADLlEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224831241 1705 LRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANG 1778
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1252-1630 |
8.16e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 41.16 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1252 VQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGER 1331
Cdd:COG3903 561 LREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAA 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1332 ARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLE 1411
Cdd:COG3903 641 AAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAA 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1412 EEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDAT 1491
Cdd:COG3903 721 AAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAA 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1492 MDLEQQRQLVSTLEkkqrkfDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAEL 1571
Cdd:COG3903 801 AAAAAAAAAAAAAA------ALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAA 874
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 224831241 1572 EALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQAL 1630
Cdd:COG3903 875 AAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1070-1195 |
8.40e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1070 SSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEE 1149
Cdd:COG2433 377 SIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE 456
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 224831241 1150 LQAALaRAEDEGGARAQLLKSLREAQAALAEAQEDLEsERVARTKA 1195
Cdd:COG2433 457 ERREI-RKDREISRLDREIERLERELEEERERIEELK-RKLERLKE 500
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1660-1846 |
8.56e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.51 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1660 EVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKElwrEVEETRTSREEIfsqnresEKR 1739
Cdd:pfam09787 46 TLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEE---QLATERSARREA-------EAE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1740 LKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRK 1819
Cdd:pfam09787 116 LERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQLTETLIQKQTMLEALSTEKNS 195
|
170 180
....*....|....*....|....*..
gi 224831241 1820 LLLQVESLTTELSaersfSAKAESGRQ 1846
Cdd:pfam09787 196 LVLQLERMEQQIK-----ELQGEGSNG 217
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1043-1879 |
8.69e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1043 EDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLnklrlkyEATIADMEDRLRKEEKGRQELEKLKRRLDgES 1122
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDL-------EQDYQAASDHLNLVQTALRQQEKIERYQE-DL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1123 SELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLreaqaalaeaqedleSERVARTKAEKQRRDL 1202
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQAL---------------DVQQTRAIQYQQAVQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1203 GEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHgQALGELAEQLEQARrgkgAWEK 1282
Cdd:COG3096 422 LEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAY-ELVCKIAGEVERSQ----AWQT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1283 TRLALE---------AEVSELRAELSSLQtarqEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGA 1353
Cdd:COG3096 497 ARELLRryrsqqalaQRLQQLRAQLAELE----QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQ 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1354 LNEAESKTIRLSKELSSTEAQ-------------LHDAQELLQEETRAKLALGSRVRAMEAEAAglreqleeeaaareRA 1420
Cdd:COG3096 573 AAEAVEQRSELRQQLEQLRARikelaarapawlaAQDALERLREQSGEALADSQEVTAAMQQLL--------------ER 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1421 GRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAreaealtQRLAEK------TE----------------------- 1471
Cdd:COG3096 639 EREATVERDELAARKQALESQIERLSQPGGAEDPRL-------LALAERlggvllSEiyddvtledapyfsalygparha 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1472 -TVDRLERGRRRLQQeLDDATMDLeqqrqlvSTLEKKQRKFDQLL---AEEKAAVLRAVEEREraeaegrerearaLSLT 1547
Cdd:COG3096 712 iVVPDLSAVKEQLAG-LEDCPEDL-------YLIEGDPDSFDDSVfdaEELEDAVVVKLSDRQ-------------WRYS 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1548 RALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERA-----------CRVA-----EQAANDLRAQVTELED 1611
Cdd:COG3096 771 RFPEVPLFGRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLhqafsqfvgghLAVAfapdpEAELAALRQRRSELER 850
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1612 ELTAAEDAKLRLEVTVQALKTQHE--RDLQGR-----DEAGEERRRQLAKQLRDAEVERDEERKQRtlavAARKKLEGEL 1684
Cdd:COG3096 851 ELAQHRAQEQQLRQQLDQLKEQLQllNKLLPQanllaDETLADRLEELREELDAAQEAQAFIQQHG----KALAQLEPLV 926
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1685 EELK---AQMASAGQGKEEAVKQLRKMQAQMKELwREVEETRT-----SREEIFSQNRESEKRLKgleAEVLRLQEELAA 1756
Cdd:COG3096 927 AVLQsdpEQFEQLQADYLQAKEQQRRLKQQIFAL-SEVVQRRPhfsyeDAVGLLGENSDLNEKLR---ARLEQAEEARRE 1002
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1757 SDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSNSEllndRYRKlllqvESLTTELSAERS 1836
Cdd:COG3096 1003 AREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERA----RIRR-----DELHEELSQNRS 1073
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 224831241 1837 FSAKAESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALES 1879
Cdd:COG3096 1074 RRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAG 1116
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
986-1212 |
8.70e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 986 EARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLlllEDQNSKLSKERKLLEDR 1065
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---AEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1066 LAefssQAAEEEEKVKSLNKL-----------RLKYEATIADMEDRLRKE-EKGRQELEKLKRRLDGESSELQEQMVEQQ 1133
Cdd:COG3883 92 AR----ALYRSGGSVSYLDVLlgsesfsdfldRLSALSKIADADADLLEElKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224831241 1134 QRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGE 1212
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| DUF3498 |
pfam12004 |
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ... |
1075-1149 |
9.28e-03 |
|
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 433 to 538 amino acids in length. This domain is found associated with pfam00616, pfam00168. This domain has two conserved sequence motifs: DLQ and PLSFQNP.
Pssm-ID: 463427 [Multi-domain] Cd Length: 511 Bit Score: 40.90 E-value: 9.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224831241 1075 EEEEKVKSLNKLRL--KYEATIADMEDRLRKEEKgrqELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEE 1149
Cdd:pfam12004 373 EESSGPESREELKQaeKYEQEISKLKERLRVSNR---KLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEE 446
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
912-1266 |
9.75e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 9.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 912 LQARAQELQKVQE-LQQQsarevGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRgrlaARKQELELVVSELEARVG 990
Cdd:PRK04863 330 YQAASDHLNLVQTaLRQQ-----EKIERYQADLEELEERLEEQNEVVEEADEQQEENE----ARAEAAEEEVDELKSQLA 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 991 EEEECSRQMQTEKKRLQQHIQELEAhleaeegARQKLQLEKVTTEakmkKFEEDLLLLEDQNSKLSKERKLLEDRLAefS 1070
Cdd:PRK04863 401 DYQQALDVQQTRAIQYQQAVQALER-------AKQLCGLPDLTAD----NAEDWLEEFQAKEQEATEELLSLEQKLS--V 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1071 SQAAEEE-EKVKSLNKlrlkyeaTIADMEDRLRKEEKGRQELEKLK--RRLDGESSELQ------EQMVEQQQRAEELRA 1141
Cdd:PRK04863 468 AQAAHSQfEQAYQLVR-------KIAGEVSRSEAWDVARELLRRLReqRHLAEQLQQLRmrlselEQRLRQQQRAERLLA 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1142 QLGRK-------EEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELE 1214
Cdd:PRK04863 541 EFCKRlgknlddEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSG 620
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 224831241 1215 DTLDSTNA-----QQELRskREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGEL 1266
Cdd:PRK04863 621 EEFEDSQDvteymQQLLE--RERELTVERDELAARKQALDEEIERLSQPGGSEDPRL 675
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1249-2018 |
9.77e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 9.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1249 EAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGD 1328
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1329 GERARAEAAEKLQRAQAELENVSGALNEAESKTIRLS-KELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLR 1407
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEeKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1408 EQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEagaleageearrraAREAEALTQRLAEKTETVDRLERGRRRLQQEL 1487
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELEIKREAE--------------EEEEEELEKLQEKLEQLEEELLAKKKLESERL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1488 DDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARAlsltraleeeqeaREELERQNRAL 1567
Cdd:pfam02463 387 SSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELK-------------QGKLTEEKEEL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1568 RAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEE 1647
Cdd:pfam02463 454 EKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1648 RRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQ----AQMKELWREVEETR 1723
Cdd:pfam02463 534 LGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvleiDPILNLAQLDKATL 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1724 TSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEEL 1803
Cdd:pfam02463 614 EADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEE 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1804 EEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRgrLGEEDAGARARHKMTIAALESKlaq 1883
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKID--EEEEEEEKSRLKKEEKEEEKSE--- 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224831241 1884 aEEQLEQETRERIL-SGKLVRRAEKRLKEVVLQVEEERRVADQLRD---QLEKGNLRVKQLKRQLEEAEEEASRAQAGRR 1959
Cdd:pfam02463 769 -LSLKEKELAEEREkTEKLKVEEEKEEKLKAQEEELRALEEELKEEaelLEEEQLLIEQEEKIKEEELEELALELKEEQK 847
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 224831241 1960 RLQRELEDVTESAESMNREVTTLRNRLRRGPLTFTTRTVRQVFRLEEGVASDEEAEEAQ 2018
Cdd:pfam02463 848 LEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEES 906
|
|
| |
