|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
81-741 |
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: 1202.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFAESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01380 1 PAVLHNLKVRFCQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 161 GESGAGKTVSARYAMRYFATVSKSGSN-AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMST 239
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATVGGSSSGeTQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDF 319
Cdd:cd01380 161 YLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 320 QMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARD 399
Cdd:cd01380 241 QMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 400 ALAKKIYAHLFDFIVERINQALQF--SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 477
Cdd:cd01380 321 ALAKHIYAQLFDWIVDRINKALASpvKEKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNR-NPLFEKPRMSNTSFVIQHFADKVE 556
Cdd:cd01380 401 EEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTAFIVKHFADDVE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 557 YKCEGFLEKNRDTVYDMLVEILRASKFHlcanffqenptppspfgsmitvksakqviKPnskhfrtTVGSKFRSSLYLLM 636
Cdd:cd01380 481 YQVEGFLEKNRDTVSEEHLNVLKASKNR-----------------------------KK-------TVGSQFRDSLILLM 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 637 ETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKEV 716
Cdd:cd01380 525 ETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRDDKKKT 604
|
650 660
....*....|....*....|....*
gi 767984698 717 CKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd01380 605 CENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
62-752 |
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: 961.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 62 NPDILVGENDLTALSYLHEPAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVA 141
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRY-LKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 142 EEAYKQMARNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSGSNA-HVEDKVLASNPITEAVGNAKTTRNDNSSRFGK 220
Cdd:smart00242 80 DNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVgSVEDQILESNPILEAFGNAKTLRNNNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 221 YTEISFDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDR 300
Cdd:smart00242 160 FIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 301 AEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNE-RSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIV 379
Cdd:smart00242 240 EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDnAASTVKDKEELSNAAELLGVDPEELEKALTKRKIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 380 TSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKL 459
Cdd:smart00242 320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 460 QQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNRNPLFEK 538
Cdd:smart00242 400 QQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKpPGILSLLDEECRFPKGTDQTFLEKLNQHH-KKHPHFSK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 539 P-RMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQEnptppspfgsmitvksakQVIKPNS 617
Cdd:smart00242 479 PkKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS------------------GVSNAGS 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 618 KHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYS 697
Cdd:smart00242 541 KKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQ 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 767984698 698 RYGILMTKQELSFS-DKKEVCKVVLHRLIQDSNQYQFGKTKIFFRAGQVAYLEKLR 752
Cdd:smart00242 621 RYRVLLPDTWPPWGgDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
70-741 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 914.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 70 NDLTALSYLHEPAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMA 149
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYK-SDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 150 RNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSGSN---AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISF 226
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAgnvGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 227 DEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVET 306
Cdd:pfam00063 161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 307 QKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVV 386
Cdd:pfam00063 241 DKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETVS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 387 KPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQF-SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNM 465
Cdd:pfam00063 321 KPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVkTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 466 HVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNRNPLFEKPR-MSN 543
Cdd:pfam00063 401 HMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKpLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHFQKPRlQGE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 544 TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQEnptpPSPFGSMITVKSAKQVIKPNSKHFRTT 623
Cdd:pfam00063 480 THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPD----YETAESAAANESGKSTPKRTKKKRFIT 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 624 VGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILM 703
Cdd:pfam00063 556 VGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILA 635
|
650 660 670
....*....|....*....|....*....|....*....
gi 767984698 704 TK-QELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:pfam00063 636 PKtWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
12-1296 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 888.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 12 RVWIPDPEEVWKSAEIAK-DYRVGDKVLRLLLEDGtELDySVNPESLPPLR-NPDILVGENDLTALSYLHEPAVLHNLRI 89
Cdd:COG5022 11 GCWIPDEEKGWIWAEIIKeAFNKGKVTEEGKKEDG-ESV-SVKKKVLGNDRiKLPKFDGVDDLTELSYLNEPAVLHNLEK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 90 RFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTV 169
Cdd:COG5022 89 RY-NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 170 SARYAMRYFATVSKSGSN--AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYLLEKSRV 247
Cdd:COG5022 168 NAKRIMQYLASVTSSSTVeiSSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 248 VFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKIL 327
Cdd:COG5022 248 VHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKIL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 328 AAILHLGNVQITAVGNERSSVSeDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYA 407
Cdd:COG5022 328 AAILHIGNIEFKEDRNGAAIFS-DNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYS 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 408 HLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDF 487
Cdd:COG5022 407 NLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 488 YDNQPVIDLIEAK--MGILELLDEECLLPHGTDENWLQKLYNNF-VNRNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLE 564
Cdd:COG5022 487 FDNQPCIDLIEKKnpLGILSLLDEECVMPHATDESFTSKLAQRLnKNSNPKFKKSRFRDNKFVVKHYAGDVEYDVEGFLD 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 565 KNRDTVYDMLVEILRASKFHLCANFFQENptppspfgsmitvksakqvIKPNSKHFRTTVGSKFRSSLYLLMETLNATTP 644
Cdd:COG5022 567 KNKDPLNDDLLELLKASTNEFVSTLFDDE-------------------ENIESKGRFPTLGSRFKESLNSLMSTLNSTQP 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 645 HYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILM-----TKQELSFSDKKEVCKV 719
Cdd:COG5022 628 HYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSpskswTGEYTWKEDTKNAVKS 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 720 VLHRLIQDSNQYQFGKTKIFFRAGQVAYLEKLRLDKLRQSCVMVQKHMRGWLQRKKFL-------------------RER 780
Cdd:COG5022 708 ILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLqalkrikkiqviqhgfrlrRLV 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 781 RAALIIQQYFRGQQTVSL-----YQLIRMATITMQAYS--RGFLARRRYRKMLEEHKAVILQKYARAWLARRRFQSIRRF 853
Cdd:COG5022 788 DYELKWRLFIKLQPLLSLlgsrkEYRSYLACIIKLQKTikREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKE 867
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 854 VLNIQLTYRVQRLQKKLEDQNKEnhglVEKLTSLAALRAGDVEKIQKLEAELEKaaTHRRNYEEKgkryrdavEEKLAKL 933
Cdd:COG5022 868 TIYLQSAQRVELAERQLQELKID----VKSISSLKLVNLELESEIIELKKSLSS--DLIENLEFK--------TELIARL 933
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 934 QKHN--------SELETQKEQIQLKLQEKTEELKE---KMDNLTKQLfdDVQKEERQRMLLE-KSFELKTQDYEKQIQSL 1001
Cdd:COG5022 934 KKLLnnidleegPSIEYVKLPELNKLHEVESKLKEtseEYEDLLKKS--TILVREGNKANSElKNFKKELAELSKQYGAL 1011
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1002 KEEIKALKDEKMQLQHLVEGEHVTSDgLKAEVARLSKQVKTISEFEKEIELLQAQKIDVekhvqSQKREMREKMSeitkq 1081
Cdd:COG5022 1012 QESTKQLKELPVEVAELQSASKIISS-ESTELSILKPLQKLKGLLLLENNQLQARYKAL-----KLRRENSLLDD----- 1080
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1082 lLESYDIEDVRSRLSVedlehLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFRE 1161
Cdd:COG5022 1081 -KQLYQLESTENLLKT-----INVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQL 1154
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1162 ENDINESIRHEVTRLTsenmmIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNE 1241
Cdd:COG5022 1155 ELDGLFWEANLEALPS-----PPPFAALSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFSGWPRGDKLKKLISE 1229
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*..
gi 767984698 1242 IHTKEKEKlidkiQEMQEASDHLKKQFETESEVKCNFRQEASRL--TLENRDLEEEL 1296
Cdd:COG5022 1230 GWVPTEYS-----TSLKGFNNLNKKFDTPASMSNEKLLSLLNSIdnLLSSYKLEEEV 1281
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
81-741 |
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: 826.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMG-DMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd00124 1 AAILHNLRERYARDL-IYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 160 SGESGAGKTVSARYAMRYFATVSKSGSNAH------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQII 233
Cdd:cd00124 80 SGESGAGKTETTKLVLKYLAALSGSGSSKSsssassIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 234 GANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEE----FNYTRMGGNTVIEGVNDRAEMVETQKT 309
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSyyylNDYLNSSGCDRIDGVDDAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 310 FTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNE--RSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVK 387
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 388 PMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQH--TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNM 465
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 466 HVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSNT 544
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKpLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAKL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 545 SFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAskfhlcanffqenptppspfgsmitvksakqvikpnskhfrttv 624
Cdd:cd00124 480 EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS-------------------------------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 625 GSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMT 704
Cdd:cd00124 516 GSQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAP 595
|
650 660 670
....*....|....*....|....*....|....*...
gi 767984698 705 K-QELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd00124 596 GaTEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
81-741 |
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: 750.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01377 1 ASVLHNLRERY-YSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 161 GESGAGKTVSARYAMRYFATVSKSGSNAH--------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQI 232
Cdd:cd01377 80 GESGAGKTENTKKVIQYLASVAASSKKKKesgkkkgtLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 233 IGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTL 312
Cdd:cd01377 160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 313 LGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 393 QAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQ 472
Cdd:cd01377 320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 473 EEYMKEDIPWTLIDF-YDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMS--NTSFVI 548
Cdd:cd01377 400 EEYKKEGIEWTFIDFgLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKPKksEAHFIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 549 QHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFqENPTPPSPFGSMITVKSAKqvikpnskhFRtTVGSKF 628
Cdd:cd01377 480 KHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLF-KDYEESGGGGGKKKKKGGS---------FR-TVSQLH 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 629 RSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILM-TKQE 707
Cdd:cd01377 549 KEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILApNAIP 628
|
650 660 670
....*....|....*....|....*....|....
gi 767984698 708 LSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd01377 629 KGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
81-741 |
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: 705.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd01384 1 PGVLHNLKVRY-ELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 160 SGESGAGKTVSARYAMRYFATVSK--SGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANM 237
Cdd:cd01384 80 SGESGAGKTETTKMLMQYLAYMGGraVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 238 STYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKE 317
Cdd:cd01384 160 RTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 318 DFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDS---HLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd01384 240 EEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKsefHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 395 VNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEE 474
Cdd:cd01384 320 TLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 475 YMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFVNrNPLFEKPRMSNTSFVIQHFAD 553
Cdd:cd01384 400 YTKEEIDWSYIEFVDNQDVLDLIEKKPgGIIALLDEACMFPRSTHETFAQKLYQTLKD-HKRFSKPKLSRTDFTIDHYAG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 554 KVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFqenptPPSPFGSmiTVKSAKqvikpnskhFrTTVGSKFRSSLY 633
Cdd:cd01384 479 DVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLF-----PPLPREG--TSSSSK---------F-SSIGSRFKQQLQ 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 634 LLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDK 713
Cdd:cd01384 542 ELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLKGSDDE 621
|
650 660
....*....|....*....|....*...
gi 767984698 714 KEVCKVVLHRLiqDSNQYQFGKTKIFFR 741
Cdd:cd01384 622 KAACKKILEKA--GLKGYQIGKTKVFLR 647
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
81-741 |
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: 687.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDmdPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01383 1 PSVLHNLEYRY-SQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKLLDS--PHVYAVADTAYREMMRDEINQSIIIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 161 GESGAGKTVSARYAMRYFATVSkSGSNAhVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTY 240
Cdd:cd01383 78 GESGAGKTETAKIAMQYLAALG-GGSSG-IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 241 LLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQ 320
Cdd:cd01383 156 LLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKEDQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 321 MDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDA 400
Cdd:cd01383 236 EHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 401 LAKKIYAHLFDFIVERINQALQFSGKQH-TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKED 479
Cdd:cd01383 316 LAKAIYASLFDWLVEQINKSLEVGKRRTgRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 480 IPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLyNNFVNRNPLFEKPRmsNTSFVIQHFADKVEYK 558
Cdd:cd01383 396 IDWTKVDFEDNQECLDLIEKKpLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCFKGER--GGAFTIRHYAGEVTYD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 559 CEGFLEKNRDTVYDMLVEILRASKFHLcanffqenptpPSPFGSMITVKSAKQ--VIKPNSKHF-RTTVGSKFRSSLYLL 635
Cdd:cd01383 473 TSGFLEKNRDLLHSDLIQLLSSCSCQL-----------PQLFASKMLDASRKAlpLTKASGSDSqKQSVATKFKGQLFKL 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 636 METLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKE 715
Cdd:cd01383 542 MQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDPLS 621
|
650 660
....*....|....*....|....*.
gi 767984698 716 VCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd01383 622 TSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
82-741 |
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: 683.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd01378 2 AINENLKKRF-ENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 162 ESGAGKTVSARYAMRYFATVSKSGSN--AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMST 239
Cdd:cd01378 81 ESGAGKTEASKRIMQYIAAVSGGSESevERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDF 319
Cdd:cd01378 161 YLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 320 QMDVFKILAAILHLGNVQITAVGNERSSVSeDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSE---TVVKPMTRPQAVN 396
Cdd:cd01378 241 QDSIFRILAAILHLGNIQFAEDEEGNAAIS-DTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGgrsVYEVPLNVEQAAY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 397 ARDALAKKIYAHLFDFIVERINQALQFSGKQH-TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEY 475
Cdd:cd01378 320 ARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEEY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 476 MKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPH-GTDENWLQKLyNNFVNRNPLFEKP----RMSNTSFVIQ 549
Cdd:cd01378 400 VREGIEWTPIKYFNNKIICDLIEEKpPGIFAILDDACLTAGdATDQTFLQKL-NQLFSNHPHFECPsghfELRRGEFRIK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 550 HFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPtppspfgsmitvksakqviKPNSKHFRTTVGSKFR 629
Cdd:cd01378 479 HYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGV-------------------DLDSKKRPPTAGTKFK 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 630 SSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELS 709
Cdd:cd01378 540 NSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPA 619
|
650 660 670
....*....|....*....|....*....|...
gi 767984698 710 FS-DKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd01378 620 WDgTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| Myo5c_CBD |
cd15476 |
Cargo binding domain of myosin 5C; Class V myosins are well studied unconventional myosins, ... |
1341-1708 |
0e+00 |
|
Cargo binding domain of myosin 5C; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. The MyoV-CBDs directly interact with several adaptor proteins.MyoVb and myoVc areprimarily expressed in epithelial cells, and have been implicated as motors involved in recycling endosomes.
Pssm-ID: 271260 [Multi-domain] Cd Length: 332 Bit Score: 679.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1341 EDEAKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSNT 1420
Cdd:cd15476 1 EDEAKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRHADYLNDANKLKSLMNAIITGVKQVIKEHQEDFEMLSFWLSNT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1421 CHFLNCLKQYSGEEEFMKHNSPQQNKNCLNNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPiivpgmleyeslqgisgl 1500
Cdd:cd15476 81 YHFLNCLKQYSGEEEFMKHNTPRQNKNCLKNFDLSEHRQILSDLAIRIYHQFISVMENNLQP------------------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1501 kptgfrkrsssiddtdgyTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRC 1580
Cdd:cd15476 143 ------------------TISSILQQLSYFYSTMCQHGMDPELIKQAVKQLFFLIGAVTLNSIFLRKDMCSCRKGMQIRC 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1581 NISYLEEWLKDKNLQNSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPIDDFEKRVTPSFV 1660
Cdd:cd15476 205 NISYLEEWLKEKNLQNSNAKETLEPLSQAAWLLQVNKTTDDDAKEICERCTELSAVQIVKILNSYTPIDDFEKRVTPSFV 284
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 767984698 1661 RKVQALLNSREDSSQLMLDTKYLFQVTFPFTPSPHALEMIQIPSSFKL 1708
Cdd:cd15476 285 RKVQSLLQNREGSSQLMLDTKYRFQVTFPFCPSPQALEMLQVPSSLKL 332
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
82-741 |
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: 678.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 82 AVLHNLRIRFAEsKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd01381 2 GILRNLLIRYRE-KLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 162 ESGAGKTVSARYAMRYFATVSksGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYL 241
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAIS--GQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 242 LEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQM 321
Cdd:cd01381 159 LEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 322 DVFKILAAILHLGNVQITA--VGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARD 399
Cdd:cd01381 239 DIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 400 ALAKKIYAHLFDFIVERINQAL-QFSGKQH--TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYM 476
Cdd:cd01381 319 AFVKGIYGRLFIWIVNKINSAIyKPRGTDSsrTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEYD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 477 KEDIPWTLIDFYDNQPVIDLI-EAKMGILELLDEECLLPHGTDENWLQKLYNNFVNrNPLFEKPRM-SNTSFVIQHFADK 554
Cdd:cd01381 399 KEGINWQHIEFVDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGN-NKNYLKPKSdLNTSFGINHFAGV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 555 VEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENptppSPFGSmitvKSAKQVIkpnskhfrtTVGSKFRSSLYL 634
Cdd:cd01381 478 VFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNED----ISMGS----ETRKKSP---------TLSSQFRKSLDQ 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 635 LMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGIL------MTKQEL 708
Cdd:cd01381 541 LMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLvpgippAHKTDC 620
|
650 660 670
....*....|....*....|....*....|...
gi 767984698 709 SFSDKKEVCKVVLHrliqDSNqYQFGKTKIFFR 741
Cdd:cd01381 621 RAATRKICCAVLGG----DAD-YQLGKTKIFLK 648
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
82-741 |
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: 649.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14883 2 GINTNLKVRYK-KDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 162 ESGAGKTVSARYAMRYFATVSKSGSnaHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYL 241
Cdd:cd14883 81 ESGAGKTETTKLILQYLCAVTNNHS--WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 242 LEKSRVVFQSENERNYHIFYQLCASAQQS-EFKH-LKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDF 319
Cdd:cd14883 159 LEQSRITFQAPGERNYHVFYQLLAGAKHSkELKEkLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPEEM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 320 QMDVFKILAAILHLGNVQITAVGNERSSVSEDDSH-LKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNAR 398
Cdd:cd14883 239 QEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEiLKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 399 DALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKE 478
Cdd:cd14883 319 DAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 479 DIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNRNPLFEKP--RMSNTSFVIQHFADKV 555
Cdd:cd14883 399 GINWSHIVFTDNQECLDLIEKPpLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPdrRRWKTEFGVKHYAGEV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 556 EYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFF--QENPTPPSPFGSMITVKSAKQvikpnSKHFRTTVGSKFRSSLY 633
Cdd:cd14883 478 TYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtyPDLLALTGLSISLGGDTTSRG-----TSKGKPTVGDTFKHQLQ 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 634 LLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTK-QELSFSD 712
Cdd:cd14883 553 SLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRaRSADHKE 632
|
650 660
....*....|....*....|....*....
gi 767984698 713 KKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14883 633 TCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
81-741 |
0e+00 |
|
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: 612.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14872 1 AMIVHNLRKRFKNDQ-IYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 161 GESGAGKTVSARYAMRYFATVSksGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTY 240
Cdd:cd14872 80 GESGAGKTEATKQCLSFFAEVA--GSTNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 241 LLEKSRVVFQSENERNYHIFYQLCASAQQSefKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQ 320
Cdd:cd14872 158 LLEKSRVVYQIKGERNFHIFYQLLASPDPA--SRGGWGSSAAYGYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFDDADI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 321 MDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCE---LLGLESGRVAQWLCNRKI-VTSSETVVKPMTRPQAVN 396
Cdd:cd14872 236 NNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSRLMeIKGCDPTRIPLTPAQATD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 397 ARDALAKKIYAHLFDFIVERINQAL-QFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEY 475
Cdd:cd14872 316 ACDALAKAAYSRLFDWLVKKINESMrPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEALY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 476 MKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNF-VNRNPLFEKPRMSNTSFVIQHFAD 553
Cdd:cd14872 396 QSEGVKFEHIDFIDNQPVLDLIEKKQpGLMLALDDQVKIPKGSDATFMIAANQTHaAKSTFVYAEVRTSRTEFIVKHYAG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 554 KVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFqenptPPSpfgsmitvksakqviKPNSKHFRTTVGSKFRSSLY 633
Cdd:cd14872 476 DVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF-----PPS---------------EGDQKTSKVTLGGQFRKQLS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 634 LLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSF-SD 712
Cdd:cd14872 536 ALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVKTIAKRVgPD 615
|
650 660
....*....|....*....|....*....
gi 767984698 713 KKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14872 616 DRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
81-741 |
0e+00 |
|
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: 603.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14903 1 AAILYNVKKRFL-RKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 160 SGESGAGKTVSARYAMRYFATVSkSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMST 239
Cdd:cd14903 80 SGESGAGKTETTKILMNHLATIA-GGLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEfkHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDF 319
Cdd:cd14903 159 YLLEKTRVISHERPERNYHIFYQLLASPDVEE--RLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 320 QMDVFKILAAILHLGNVQITAVGN--ERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNA 397
Cdd:cd14903 237 QEVLFEVLAGILHLGQLQIQSKPNddEKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDC 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 398 RDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 477
Cdd:cd14903 317 RDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSNTSFVIQHFADKVEY 557
Cdd:cd14903 397 EGIRWAHIDFADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSRTQFTIKHYAGPVTY 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 558 KCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGSMITVKSAKQVIKPNSKhfrTTVGSKFRSSLYLLME 637
Cdd:cd14903 477 ESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGGALTT---TTVGTQFKDSLNELMT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 638 TLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKEVC 717
Cdd:cd14903 554 TIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGRNTDVPVAERC 633
|
650 660
....*....|....*....|....*
gi 767984698 718 KVVLHRL-IQDSNQYQFGKTKIFFR 741
Cdd:cd14903 634 EALMKKLkLESPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
84-741 |
0e+00 |
|
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: 590.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 84 LHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd01382 4 LNNIRVRYSKDK-IYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 163 SGAGKTVSARYAMRYFaTVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYLL 242
Cdd:cd01382 83 SGAGKTESTKYILRYL-TESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 243 EKSRVVFQSENERNYHIFYQLCASAQQSEFKHLklgsaeefnytrmggnTVIEGVNDRAEMVETQKTFTLLGFKEDFQMD 322
Cdd:cd01382 162 EKSRICVQSKEERNYHIFYRLCAGAPEDLREKL----------------LKDPLLDDVGDFIRMDKAMKKIGLSDEEKLD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 323 VFKILAAILHLGNVQITAVGNER---SSVSEDDSH-LKVFCELLGLESGRVAQWLCNRKIVTSSE----TVVK-PMTRPQ 393
Cdd:cd01382 226 IFRVVAAVLHLGNIEFEENGSDSgggCNVKPKSEQsLEYAAELLGLDQDELRVSLTTRVMQTTRGgakgTVIKvPLKVEE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 394 AVNARDALAKKIYAHLFDFIVERINQALQFSGKQHtFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQE 473
Cdd:cd01382 306 ANNARDALAKAIYSKLFDHIVNRINQCIPFETSSY-FIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKEEQE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 474 EYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFVNrNPLFEKPRMS---------- 542
Cdd:cd01382 385 LYEKEGLGVKEVEYVDNQDCIDLIEAKLvGILDLLDEESKLPKPSDQHFTSAVHQKHKN-HFRLSIPRKSklkihrnlrd 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 543 NTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSpfgsmitvKSAKQVIKPNSKhfrt 622
Cdd:cd01382 464 DEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNK--------DSKQKAGKLSFI---- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 623 TVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGIL 702
Cdd:cd01382 532 SVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKY 611
|
650 660 670
....*....|....*....|....*....|....*....
gi 767984698 703 MTKqELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd01382 612 LPP-KLARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
84-741 |
0e+00 |
|
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: 586.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 84 LHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGES 163
Cdd:cd01385 4 LENLRARFKHGK-IYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 164 GAGKTVSARYAMRYFATVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYLLE 243
Cdd:cd01385 83 GSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 244 KSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDV 323
Cdd:cd01385 163 KSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQRQI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 324 FKILAAILHLGNVQI---TAVGNERSSVSEDDShLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDA 400
Cdd:cd01385 243 FSVLSAVLHLGNIEYkkkAYHRDESVTVGNPEV-LDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 401 LAKKIYAHLFDFIVERINQALQ----FSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYM 476
Cdd:cd01385 322 MAKCLYSALFDWIVLRINHALLnkkdLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 477 KEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKlYNNFVNRNPLFEKPRMSNTSFVIQHFADKV 555
Cdd:cd01385 402 KEGISWHNIEYTDNTGCLQLISKKpTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQVMEPAFIIAHYAGKV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 556 EYKCEGFLEKNRDTVYDMLVEILRASK-----------------------FHLCANFFQE----NPTPPSPFGSMITVKS 608
Cdd:cd01385 481 KYQIKDFREKNLDLMRPDIVAVLRSSSsafvreligidpvavfrwavlraFFRAMAAFREagrrRAQRTAGHSLTLHDRT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 609 AKQVIKPNSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPS 688
Cdd:cd01385 561 TKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSV 640
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 767984698 689 RWTYIEFYSRYGILMTKQELSfsdKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd01385 641 RYTFQEFITQFQVLLPKGLIS---SKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
82-741 |
0e+00 |
|
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: 576.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMAR----NNRNQS 156
Cdd:cd14890 2 SLLHTLRLRY-ERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 157 IIVSGESGAGKTVSARYAMRYFATVSK-----------SGSNAH------VEDKVLASNPITEAVGNAKTTRNDNSSRFG 219
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSgfaqgasgegeAASEAIeqtlgsLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 220 KYTEISFDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVND 299
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLR-GECSSIPSCDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 300 RAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVgnERSSVSEDDS---HLKVFCELLGLESGRVAQWLCNR 376
Cdd:cd14890 240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESE--NDTTVLEDATtlqSLKLAAELLGVNEDALEKALLTR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 377 KIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYAN 456
Cdd:cd14890 318 QLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 457 EKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM----GILELLDEECLLpHGTDEN--WLQKLYNNF- 529
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVngkpGIFITLDDCWRF-KGEEANkkFVSQLHASFg 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 530 -----------VNRNPLFEKPRMSNT-SFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASkfhlcanffqenptpp 597
Cdd:cd14890 477 rksgsggtrrgSSQHPHFVHPKFDADkQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQS---------------- 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 598 spfGSMITVKSakqvikpnskhfrttVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLE 677
Cdd:cd14890 541 ---RRSIREVS---------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMME 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767984698 678 TIRISAQSYPSRWTYIEFYSRYGILMTKQElsfsDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14890 603 AIQIRQQGFALREEHDSFFYDFQVLLPTAE----NIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
82-741 |
0e+00 |
|
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: 576.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd01387 2 TVLWNLKTRY-ERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 162 ESGAGKTVSARYAMRYFATVSKSGSNAhVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFdEQNQIIGANMSTYL 241
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNL-VTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAITSQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 242 LEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQM 321
Cdd:cd01387 159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 322 DVFKILAAILHLGNV-----QITAvGNERSSVSEDdSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVN 396
Cdd:cd01387 239 SIFRILASVLHLGNVyfhkrQLRH-GQEGVSVGSD-AEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 397 ARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYM 476
Cdd:cd01387 317 ARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 477 KEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNRNPLFEKPRMSNTSFVIQHFADKV 555
Cdd:cd01387 397 REQIDWTEIAFADNQPVINLISKKpVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPRMPLPEFTIKHYAGQV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 556 EYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQ------ENPTPPSPFGSMITVKsakqvikpnskhFRT-TVGSKF 628
Cdd:cd01387 476 WYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSshraqtDKAPPRLGKGRFVTMK------------PRTpTVAARF 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 629 RSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMtKQEL 708
Cdd:cd01387 544 QDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLV-ALKL 622
|
650 660 670
....*....|....*....|....*....|....*
gi 767984698 709 SFSDKKEVCKVVLHRL--IQDSNQYQFGKTKIFFR 741
Cdd:cd01387 623 PRPAPGDMCVSLLSRLctVTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
82-741 |
0e+00 |
|
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: 572.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14873 2 SIMYNLFQRYKRNQ-IYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 161 GESGAGKTVSARYAMRYFATVSK-------SGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQII 233
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQqslelslKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 234 GANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLL 313
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 314 GFKEDFQMDVFKILAAILHLGNVQ-ITAVGNERSsvseDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEfITAGGAQVS----FKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 393 QAVNARDALAKKIYAHLFDFIVERINQALQfsGKQH-TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLE 471
Cdd:cd14873 317 QAVDSRDSLAMALYARCFEWVIKKINSRIK--GKEDfKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 472 QEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNrNPLFEKPRMSNTSFVIQHF 551
Cdd:cd14873 395 QLEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHAN-NHFYVKPRVAVNNFGVKHY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 552 ADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQEnptppspfgsmITVKSAKQVIKPNSKHFRTTVGSKFRSS 631
Cdd:cd14873 474 AGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEH-----------VSSRNNQDTLKCGSKHRRPTVSSQFKDS 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 632 LYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMtKQELSFS 711
Cdd:cd14873 543 LHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLM-RNLALPE 621
|
650 660 670
....*....|....*....|....*....|
gi 767984698 712 DKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14873 622 DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
81-741 |
0e+00 |
|
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: 570.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFAESkLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01379 1 DTIVSQLQKRYSRD-QIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 161 GESGAGKTVSARYAMRYFATVSKSgSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTY 240
Cdd:cd01379 80 GESGAGKTESANLLVQQLTVLGKA-NNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 241 LLEKSRVVFQSENERNYHIFYQLCAS-AQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVND---RAEMVETQKTFTLLGFK 316
Cdd:cd01379 159 LLEKSRVVHQAIGERNFHIFYYIYAGlAEDKKLAKYKLPENKPPRYLQNDGLTVQDIVNNsgnREKFEEIEQCFKVIGFT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 317 EDFQMDVFKILAAILHLGNVQITAVGNE----RSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd01379 239 KEEVDSVYSILAAILHIGDIEFTEVESNhqtdKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 393 QAVNARDALAKKIYAHLFDFIVERINQALQFS----GKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVF 468
Cdd:cd01379 319 EATDARDAMAKALYGRLFSWIVNRINSLLKPDrsasDEPLS-IGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 469 KLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvnRNPLFEKPRMSNTSFV 547
Cdd:cd01379 398 AWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKpMGLLALLDEESRFPKATDQTLVEKFHNNI--KSKYYWRPKSNALSFG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 548 IQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASkfhlcanffqENPTppspfgsmitvksakqvikpnskhFRTTVGSK 627
Cdd:cd01379 476 IHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSS----------ENPL------------------------VRQTVATY 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 628 FRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQE 707
Cdd:cd01379 522 FRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKWN 601
|
650 660 670
....*....|....*....|....*....|....
gi 767984698 708 LSFSDKKEVCKVVLHRLIQDSnqYQFGKTKIFFR 741
Cdd:cd01379 602 EEVVANRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| Myo5_CBD |
cd15470 |
Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, ... |
1341-1707 |
0e+00 |
|
Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. The MyoV-CBDs directly interact with several adaptor proteins, in case of Myo5a, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin, and in case of Myo5b, Rab11-family interacting protein 2.
Pssm-ID: 271254 [Multi-domain] Cd Length: 332 Bit Score: 567.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1341 EDEAKLIQNLILDLKPRGVVvNMIPGLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSNT 1420
Cdd:cd15470 1 EDESRLIKNLITDLKPRGAV-GLLPGLPAYILFMCIRHADYVNDEAKVRSLLTATINAIKKVLKKHSEDFEMLSFWLVNT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1421 CHFLNCLKQYSGEEEFMKHNSPQQNKNCLNNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPiivpgmleyeslqgisgl 1500
Cdd:cd15470 80 CRLLNCLKQYSGEEEFMKHNTPKQNEHCLKNFDLSEYRQVLSDLAIQIYQQLIKRAEEILQP------------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1501 kptgfrkrsssiddtdgyTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRC 1580
Cdd:cd15470 142 ------------------TLDSLLQQLNSFHTTLTQHGLDPELIKQVFRQLFYLICASTLNNLLLRKDLCSWSKGMQIRY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1581 NISYLEEWLKDKNLQNSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPIDDFEKRVTPSFV 1660
Cdd:cd15470 204 NVSQLEEWLRDKGLQDSGARETLEPLIQAAQLLQVKKTTEEDAQSICEMCTKLTTAQIVKILNLYTPVDDFEERVTPSFI 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 767984698 1661 RKVQALLNSREDSS--QLMLDTKYLFQVTFPFTPSPHALEMIQIPSSFK 1707
Cdd:cd15470 284 RKVQARLNERADSNqlQLLMDTKYIFPVTFPFNPSPVALEELQIPPSLH 332
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
81-739 |
2.33e-180 |
|
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: 557.48 E-value: 2.33e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAY---SGQNMGD---MDPHIFAVAEEAYKQMARNNR- 153
Cdd:cd14901 1 PSILHVLRRRF-AHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehGERRAAGerkLPPHVYAVADKAFRAMLFASRg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 154 ---NQSIIVSGESGAGKTVSARYAMRYFATVS---KSGSNA----HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTE 223
Cdd:cd14901 80 qkcDQSILVSGESGAGKTETTKIIMNYLASVSsatTHGQNAtereNVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 224 ISFDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTV-IEGVNDRAE 302
Cdd:cd14901 160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDrRDGVDDSVQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 303 MVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQ-ITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTS 381
Cdd:cd14901 240 YAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCfVKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 382 SETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQF--SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKL 459
Cdd:cd14901 320 GEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYseSTGASRFIGIVDIFGFEIFATNSLEQLCINFANEKL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 460 QQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNRNPL-FE 537
Cdd:cd14901 400 QQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARpTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHASFsVS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 538 KPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCAnffqenptppspfgsmitvksakqvikpns 617
Cdd:cd14901 480 KLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS------------------------------ 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 618 khfrTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYS 697
Cdd:cd14901 530 ----STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVH 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 767984698 698 RYGILMTKQElsfSDKKEVCKVVLHR---------LIQDSNQYQFGKTKIF 739
Cdd:cd14901 606 TYSCLAPDGA---SDTWKVNELAERLmsqlqhselNIEHLPPFQVGKTKVF 653
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
81-741 |
3.19e-180 |
|
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: 556.86 E-value: 3.19e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14904 1 PSILFNLKKRFAASK-PYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 160 SGESGAGKTVSARYAMRYFATVSkSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMST 239
Cdd:cd14904 80 SGESGAGKTETTKIVMNHLASVA-GGRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYtrMGGN---TVIEGVNDRAEMVETQKTFTLLGFK 316
Cdd:cd14904 159 YLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQY--LGDSlaqMQIPGLDDAKLFASTQKSLSLIGLD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 317 EDFQMDVFKILAAILHLGNVQITAVGnERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVN 396
Cdd:cd14904 237 NDAQRTLFKILSGVLHLGEVMFDKSD-ENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 397 ARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEY 475
Cdd:cd14904 316 NRDALAKAIYSKLFDWMVVKINAAISTDDDRiKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 476 MKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNR--NPLFEKPRMSNTSFVIQHFAD 553
Cdd:cd14904 396 IREGLQWDHIEYQDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQTKkdNESIDFPKVKRTQFIINHYAG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 554 KVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGSmitvKSAKQVIKPNSkhfrttVGSKFRSSLY 633
Cdd:cd14904 476 PVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSETKEG----KSGKGTKAPKS------LGSQFKTSLS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 634 LLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGIlMTKQELSFSDK 713
Cdd:cd14904 546 QLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAI-MFPPSMHSKDV 624
|
650 660
....*....|....*....|....*....
gi 767984698 714 KEVCKVVLHRLIQDSN-QYQFGKTKIFFR 741
Cdd:cd14904 625 RRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
87-741 |
6.13e-177 |
|
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: 548.21 E-value: 6.13e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 87 LRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMD---PHIFAVAEEAYKQM----ARNNRNQSIIV 159
Cdd:cd14892 7 LRRRY-ERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATASsppPHVFSIAERAYRAMkgvgKGQGTPQSIVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 160 SGESGAGKTVSARYAMRYFATVSKSGS---------NAH--VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDE 228
Cdd:cd14892 86 SGESGAGKTEASKYIMKYLATASKLAKgastskgaaNAHesIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 229 QNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQK 308
Cdd:cd14892 166 DGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVDGVDDATEFKQLRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 309 TFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKV--FCELLGLESGRVAQWLCNRKIVTSSETVV 386
Cdd:cd14892 246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNVakAAGLLGVDAAELMFKLVTQTTSTARGSVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 387 K-PMTRPQAVNARDALAKKIYAHLFDFIVERINQALQ----------FSGKQHTFIGVLDIYGFETFDVNSFEQFCINYA 455
Cdd:cd14892 326 EiKLTAREAKNALDALCKYLYGELFDWLISRINACHKqqtsgvtggaASPTFSPFIGILDIFGFEIMPTNSFEQLCINFT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 456 NEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPH-GTDENWLQKLYNNFVNRN 533
Cdd:cd14892 406 NEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKpLGLLPLLEEQMLLKRkTTDKQLLTIYHQTHLDKH 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 534 PLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASkfhlcanffqenptppspfgsmitvksakqvi 613
Cdd:cd14892 486 PHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSS-------------------------------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 614 kpnskhfrttvgSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYI 693
Cdd:cd14892 534 ------------SKFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFE 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 767984698 694 EFYSRYGIL---MTKQELSFSDK------KEVCKVVLHRLiqDSNQYQFGKTKIFFR 741
Cdd:cd14892 602 EFYEKFWPLarnKAGVAASPDACdattarKKCEEIVARAL--ERENFQLGRTKVFLR 656
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
81-741 |
1.94e-175 |
|
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: 544.67 E-value: 1.94e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSgQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14888 1 ASILHSLNLRFDIDE-IYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 160 SGESGAGKTVSARYAMRYFATVsksGSNA-----HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQN---- 230
Cdd:cd14888 79 SGESGAGKTESTKYVMKFLACA---GSEDikkrsLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLKskrm 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 231 -----QIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQS-------EFKHLKLG----------------SAEE 282
Cdd:cd14888 156 sgdrgRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAkntglsyEENDEKLAkgadakpisidmssfePHLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 283 FNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQ-ITAVGNERSSV--SEDDSHLKVFC 359
Cdd:cd14888 236 FRYLTKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILfENNEACSEGAVvsASCTDDLEKVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 360 ELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHT-FIGVLDIYG 438
Cdd:cd14888 316 SLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLlFCGVLDIFG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 439 FETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGT 517
Cdd:cd14888 396 FECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKpLGIFCMLDEECFVPGGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 518 DENWLQKLYNNFVNrNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKfhlcanffqeNPTPP 597
Cdd:cd14888 476 DQGLCNKLCQKHKG-HKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSK----------NPFIS 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 598 SPFGSMItvkSAKQVIKPNSKHFRtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLE 677
Cdd:cd14888 545 NLFSAYL---RRGTDGNTKKKKFV-TVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQ 620
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767984698 678 TIRISAQSYPSRWTYIEFYSRYGILMTKQE-LSFSdkkevckvvlhrliqdsnQYQFGKTKIFFR 741
Cdd:cd14888 621 AVQVSRAGYPVRLSHAEFYNDYRILLNGEGkKQLS------------------IWAVGKTLCFFK 667
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
82-741 |
1.30e-167 |
|
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: 524.19 E-value: 1.30e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14920 2 SVLHNLKDRYY-SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 162 ESGAGKTVSARYAMRYFATVSKS--GSNAH-----VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIG 234
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASShkGRKDHnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 235 ANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVNDRAEMVETQKTFTLLG 314
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIMG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 315 FKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14920 240 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 395 VNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQE 473
Cdd:cd14920 320 DFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 474 EYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNRNPLFEKPRM--SNTSFV 547
Cdd:cd14920 400 EYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQE-QGSHSKFQKPRQlkDKADFC 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 548 IQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQE-NPTPPSPFGSMITVKSAKQVIKPNSKHFRtTVGS 626
Cdd:cd14920 479 IIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvDRIVGLDQVTGMTETAFGSAYKTKKGMFR-TVGQ 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 627 KFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQ 706
Cdd:cd14920 558 LYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 637
|
650 660 670
....*....|....*....|....*....|....*.
gi 767984698 707 -ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14920 638 iPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
82-741 |
1.37e-166 |
|
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: 521.44 E-value: 1.37e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14927 2 SVLHNLRRRYS-RWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 162 ESGAGKTVSARYAMRYFATVSKSGSN-------------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDE 228
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGpgkkaqflatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 229 QNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQ 307
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQI-LSGKKPELQDMLLVSMNPYDYHFCSqGVTTVDNMDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 308 KTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVK 387
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 388 PMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHV 467
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 468 FKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSN--- 543
Cdd:cd14927 400 FILEQEEYKREGIEWVFIDFgLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKkrk 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 544 --TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFqENptppspFGSMITVKSAKQVIKPNSKHFR 621
Cdd:cd14927 480 yeAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY-EN------YVGSDSTEDPKSGVKEKRKKAA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 622 T--TVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRY 699
Cdd:cd14927 553 SfqTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRY 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 767984698 700 GILMTKQ--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14927 633 RILNPSAipDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
81-741 |
5.12e-164 |
|
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: 514.21 E-value: 5.12e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14913 1 PAVLYNLKDRYT-SWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 161 GESGAGKTVSARYAMRYFATVSKSGSNAH---------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQ 231
Cdd:cd14913 80 GESGAGKTVNTKRVIQYFATIAATGDLAKkkdskmkgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 232 IIGANMSTYLLEKSRVVFQSENERNYHIFYQLCaSAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQKTF 310
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQIL-SNKKPELIELLLITTNPYDYPFISqGEILVASIDDAEELLATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 311 TLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMT 390
Cdd:cd14913 239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 391 RPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKL 470
Cdd:cd14913 319 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 471 EQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRM----SNTS 545
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVvkgrAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 546 FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFqenptppSPFGSMITVKSAKQVIKPNSKHFRtTVG 625
Cdd:cd14913 479 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY-------ATFATADADSGKKKVAKKKGSSFQ-TVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 626 SKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTK 705
Cdd:cd14913 551 ALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNAS 630
|
650 660 670
....*....|....*....|....*....|....*...
gi 767984698 706 Q--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14913 631 AipEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
81-741 |
1.24e-163 |
|
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: 512.98 E-value: 1.24e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14929 1 ASVLHTLRRRY-DHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 161 GESGAGKTVSARYAMRYFATVSKSGSN----AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGAN 236
Cdd:cd14929 80 GESGAGKTVNTKHIIQYFATIAAMIESkkklGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 237 MSTYLLEKSRVVFQSENERNYHIFYQLCASAQqsEFKHLKLGSA--EEFNYTRMGGNTViEGVNDRAEMVETQKTFTLLG 314
Cdd:cd14929 160 IDIYLLEKSRVIFQQPGERNYHIFYQILSGKK--ELRDLLLVSAnpSDFHFCSCGAVAV-ESLDDAEELLATEQAMDILG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 315 FKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14929 237 FLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 395 VNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEE 474
Cdd:cd14929 317 TYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 475 YMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSNTSFVIQ---- 549
Cdd:cd14929 397 YRKEGIDWVSIDFgLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHfelv 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 550 HFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPS--PFGSmitvksaKQVIKPNSKHfrtTVGSK 627
Cdd:cd14929 477 HYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSaiQFGE-------KKRKKGASFQ---TVASL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 628 FRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTK-- 705
Cdd:cd14929 547 HKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRtf 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 767984698 706 QELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14929 627 PKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| Myo5b_CBD |
cd15477 |
Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, ... |
1340-1711 |
6.54e-162 |
|
Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. They interact with several adaptor proteins, in case of Myo5b-CBD, Rab11-family interacting protein 2.
Pssm-ID: 271261 Cd Length: 372 Bit Score: 497.08 E-value: 6.54e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1340 REDEAKLIQNLILDLKPRgVVVNMIPGLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSN 1419
Cdd:cd15477 1 KEDEALLIRNLVTDLKPQ-AVSATVPCLPAYILYMCIRHADYINDDQKVHSLLTSTINGIKKVLKKHNDDFEMTSFWLAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1420 TCHFLNCLKQYSGEEEFMKHNSPQQNKNCLNNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPIIVPGMLEYESLQGISG 1499
Cdd:cd15477 80 TCRLLHCLKQYSGDEGFMTQNTAKQNEHCLKNFDLTEYRQVLSDLSIQIYQQLIKIAEGILQPMIVSAMLENESIQGLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1500 LKPTGFRKRSSSIDDTD-GYTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQI 1578
Cdd:cd15477 160 VKPMGYRKRSSSMADGDnSYTLEALIRQLNTFHSIMCDQGLDPEIIQQVFKQLFYMINAVTLNNLLLRKDVCSWSTGMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1579 RCNISYLEEWLKDKNLQNSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPIDDFEKRVTPS 1658
Cdd:cd15477 240 RYNISQLEEWLRGRNLHQSGAAQTMEPLIQAAQLLQLKKKTSEDAEAICSLCTALSTQQIVKILNLYTPLNEFEERVTVS 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 767984698 1659 FVRKVQALLNSREDSSQLMLDTKYLFQVTFPFTPSPHALEMIQIPSSFKLGFL 1711
Cdd:cd15477 320 FIRTIQAQLQERNDPPQLLLDTKHMFPVLFPFNPSALTLDSIHIPASLNLDFL 372
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
81-741 |
1.00e-161 |
|
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: 507.84 E-value: 1.00e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14909 1 ASVLHNLRQRY-YAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 161 GESGAGKTVSARYAMRYFATVSKS-------GSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQII 233
Cdd:cd14909 80 GESGAGKTENTKKVIAYFATVGASkktdeaaKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 234 GANMSTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQKTFTL 312
Cdd:cd14909 160 GADIETYLLEKARVISQQSLERSYHIFYQI-MSGSVPGVKEMCLLSDNIYDYYIVSqGKVTVPNVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 313 LGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 393 QAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQ 472
Cdd:cd14909 319 QVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 473 EEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSNTS-----F 546
Cdd:cd14909 399 EEYKREGIDWAFIDFgMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGqqaahF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 547 VIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGsmitvkSAKQVIKPNSKHFrTTVGS 626
Cdd:cd14909 479 AIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGE------QAKGGRGKKGGGF-ATVSS 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 627 KFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQ 706
Cdd:cd14909 552 AYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAG 631
|
650 660 670
....*....|....*....|....*....|....*
gi 767984698 707 ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14909 632 IQGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| Myo5a_CBD |
cd15478 |
Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, ... |
1340-1714 |
1.97e-160 |
|
Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. They interact with several adaptor proteins, in case of Myo5a-CBD, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin. Mutations in human Myo5a (many of which map to the cargo binding domain) lead to Griscelli syndrome, a severe neurological disease.
Pssm-ID: 271262 Cd Length: 375 Bit Score: 493.01 E-value: 1.97e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1340 REDEAKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSN 1419
Cdd:cd15478 1 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1420 TCHFLNCLKQYSGEEEFMKHNSPQQNKNCLNNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPIIVPGMLEYESLQGISG 1499
Cdd:cd15478 81 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1500 LKPTGFRKRSSSIDDTDGYTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIR 1579
Cdd:cd15478 161 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1580 CNISYLEEWLKDKNLQNSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPIDDFEKRVTPSF 1659
Cdd:cd15478 241 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 767984698 1660 VRKVQALLNSREDSSQLMLDTKYLFQVTFPFTPSPHALEMIQIPSSFKLGFLNRL 1714
Cdd:cd15478 321 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 375
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
82-741 |
7.07e-155 |
|
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: 489.88 E-value: 7.07e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14911 2 SVLHNIKDRYY-SGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 162 ESGAGKTVSARYAMRYFATVS-----KSGSNAH-----------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEIS 225
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAaskpkGSGAVPHpavnpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 226 FDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVNDRAEMVE 305
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLS-NGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 306 TQKTFTLLGF-KEDFQMdVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSET 384
Cdd:cd14911 240 TVKSMNIMGMtSEDFNS-IFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 385 VVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQF 463
Cdd:cd14911 319 VTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 464 NMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFvNRNPLFEKPRMS 542
Cdd:cd14911 399 NHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFMKTDFR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 543 NTS-FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGSMITVKSAKQVIKpnsKHFR 621
Cdd:cd14911 478 GVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQFGARTRK---GMFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 622 tTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGI 701
Cdd:cd14911 555 -TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 767984698 702 LMTKQ-ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14911 634 LTPNViPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
83-741 |
1.96e-154 |
|
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: 488.39 E-value: 1.96e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP---------IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14907 3 LLINLKKRYQQDK-IFTYVGPTLIVMNPYKQIDnlfseevmqMYKEQIIQNGEYFDIKKEPPHIYAIAALAFKQLFENNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 154 NQSIIVSGESGAGKTVSARYAMRYFATVS------------------KSGSNAHVEDKVLASNPITEAVGNAKTTRNDNS 215
Cdd:cd14907 82 KQAIVISGESGAGKTENAKYAMKFLTQLSqqeqnseevltltssiraTSKSTKSIEQKILSCNPILEAFGNAKTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 216 SRFGKYTEISFDEQNQ-IIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKL---GSAEEFNYTRMGGN 291
Cdd:cd14907 162 SRFGKYVSILVDKKKRkILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLknqLSGDRYDYLKKSNC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 292 TVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQI---TAVGNERSSVSeDDSHLKVFCELLGLESGR 368
Cdd:cd14907 242 YEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFddsTLDDNSPCCVK-NKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 369 VAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQAL--QFSGKQHTF------IGVLDIYGFE 440
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpKDEKDQQLFqnkylsIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 441 TFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTL--IDFYDNQPVIDLIE-AKMGILELLDEECLLPHGT 517
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSYTDNQDVIDLLDkPPIGIFNLLDDSCKLATGT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 518 DENWLQKLYNNFvNRNPLFEKPRMSN-TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENptp 596
Cdd:cd14907 481 DEKLLNKIKKQH-KNNSKLIFPNKINkDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE--- 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 597 pspFGSMITVKSAKQVIKPNSKhfrtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVL 676
Cdd:cd14907 557 ---DGSQQQNQSKQKKSQKKDK----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVL 629
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767984698 677 ETIRISAQSYPSRWTYIEFYSRYGILmtkqelsfsdkkevckvvlhrliqdSNQYQFGKTKIFFR 741
Cdd:cd14907 630 ESIRVRKQGYPYRKSYEDFYKQYSLL-------------------------KKNVLFGKTKIFMK 669
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
81-741 |
7.79e-153 |
|
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: 484.22 E-value: 7.79e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14917 1 PAVLYNLKERYA-SWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 161 GESGAGKTVSARYAMRYFATVSKSGSNAH---------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQ 231
Cdd:cd14917 80 GESGAGKTVNTKRVIQYFAVIAAIGDRSKkdqtpgkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 232 IIGANMSTYLLEKSRVVFQSENERNYHIFYQLCaSAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQKTF 310
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYQIL-SNKKPELLDMLLITNNPYDYAFISqGETTVASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 311 TLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMT 390
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 391 RPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKL 470
Cdd:cd14917 319 VQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 471 EQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPR----MSNTS 545
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRnikgKPEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 546 FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPfgsmitVKSAKQVIKPNSKHfrTTVG 625
Cdd:cd14917 479 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAP------IEKGKGKAKKGSSF--QTVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 626 SKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTK 705
Cdd:cd14917 551 ALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 630
|
650 660 670
....*....|....*....|....*....|....*...
gi 767984698 706 Q--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14917 631 AipEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
83-741 |
3.33e-152 |
|
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: 482.10 E-value: 3.33e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 83 VLHNLRIRFAESkLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQM----ARNNRNQSII 158
Cdd:cd14889 3 LLEVLKVRFMQS-NIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMlgrlARGPKNQCIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 159 VSGESGAGKTVSARYAMRYFATVSKSgsNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFdEQNQIIGANMS 238
Cdd:cd14889 82 ISGESGAGKTESTKLLLRQIMELCRG--NSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 239 TYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKED 318
Cdd:cd14889 159 EYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYDEVCNAMDMVGFTEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 319 FQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSH-LKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNA 397
Cdd:cd14889 239 EEVDMFTILAGILSLGNITFEMDDDEALKVENDSNGwLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAEDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 398 RDALAKKIYAHLFDFIVERINQAL----QFSGKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQE 473
Cdd:cd14889 319 RDSIAKVAYGRVFGWIVSKINQLLapkdDSSVELRE-IGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLMEQK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 474 EYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNRNPLFEKPRMSNTSFVIQHFA 552
Cdd:cd14889 398 EYKKEGIDWKEITYKDNKPILDLFLNKpIGILSLLDEQSHFPQATDESFVDKLNIHF-KGNSYYGKSRSKSPKFTVNHYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 553 DKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQenpTPPSPFGSMITVKSAKQVIKPNSKHFRT-TVGSKFRSS 631
Cdd:cd14889 477 GKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFT---ATRSRTGTLMPRAKLPQAGSDNFNSTRKqSVGAQFKHS 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 632 LYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFS 711
Cdd:cd14889 554 LGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILLCEPALPGT 633
|
650 660 670
....*....|....*....|....*....|
gi 767984698 712 dkKEVCKVVLHRliQDSNQYQFGKTKIFFR 741
Cdd:cd14889 634 --KQSCLRILKA--TKLVGWKCGKTRLFFK 659
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
81-741 |
1.30e-150 |
|
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: 478.63 E-value: 1.30e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAY------SGQNM---GDMDPHIFAVAEEAYKQMARN 151
Cdd:cd14908 1 PAILHSLSRRFFRGI-IYTWTGPVLIAVNPFQRLPLYGKEILESYrqegllRSQGIespQALGPHVFAIADRSYRQMMSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 152 NR-NQSIIVSGESGAGKTVSARYAMRYFATVSKSGSNAHVE----------DKVLASNPITEAVGNAKTTRNDNSSRFGK 220
Cdd:cd14908 80 IRaSQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEgeelgklsimDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 221 YTEISFDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGS--------AEEFNYTRMGGNT 292
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDgitgglqlPNEFHYTGQGGAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 293 VIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVS---EDDSHLKVFCELLGLESGRV 369
Cdd:cd14908 240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIaeeGNEKCLARVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 370 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ--HTFIGVLDIYGFETFDVNSF 447
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKdiRSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 448 EQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEA-KMGILELLDEECLLP-HGTDENWLQKL 525
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAkKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 526 YNNFVNRNP--LFEKPRMSNTS-------FVIQHFADKVEYKCE-GFLEKNRDTVydmlveilraskfhlcanffqenpt 595
Cdd:cd14908 480 YETYLPEKNqtHSENTRFEATSiqktkliFAVRHFAGQVQYTVEtTFCEKNKDEI------------------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 596 ppspfgsmitvksakqvikPNSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGV 675
Cdd:cd14908 535 -------------------PLTADSLFESGQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGV 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 676 LETIRISAQSYPSRWTYIEFYSRYGILMT---KQELSFSDK---------KEVCKV-VLHRLIQD--------SNQYQFG 734
Cdd:cd14908 596 LEAVRVARSGYPVRLPHKDFFKRYRMLLPlipEVVLSWSMErldpqklcvKKMCKDlVKGVLSPAmvsmknipEDTMQLG 675
|
....*..
gi 767984698 735 KTKIFFR 741
Cdd:cd14908 676 KSKVFMR 682
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
83-741 |
1.45e-150 |
|
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: 476.88 E-value: 1.45e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDM-DPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14897 3 IVQTLKSRYNKDK-FYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVRSQrPPHLFWIADQAYRRLLETGRNQCILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 162 ESGAGKTVSARYAMRYFATVSKSgSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYL 241
Cdd:cd14897 82 ESGAGKTESTKYMIKHLMKLSPS-DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 242 LEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVNDRAEMVETQKTFT-------LLG 314
Cdd:cd14897 161 LEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILR-DDNRNRPVFNDSEELEYYRQMFHdltnimkLIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 315 F-KEDFQMdVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14897 240 FsEEDISV-IFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 394 AVNARDALAKKIYAHLFDFIVERINQAL----QFSGK-QHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVF 468
Cdd:cd14897 319 ANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMtRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 469 KLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLyNNFVNRNPLFEKPRMSNTSFV 547
Cdd:cd14897 399 PRERSEYEIEGIEWRDIEYHDNDDVLELFFKKpLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESPRYVASPGNRVAFG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 548 IQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFqenptppspfgsmitvksakqvikpnSKHfrttvgsk 627
Cdd:cd14897 478 IRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF--------------------------TSY-------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 628 FRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQE 707
Cdd:cd14897 524 FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFSN 603
|
650 660 670
....*....|....*....|....*....|....
gi 767984698 708 LSFSDKKEVCKVVLHrlIQDSNQYQFGKTKIFFR 741
Cdd:cd14897 604 KVRSDDLGKCQKILK--TAGIKGYQFGKTKVFLK 635
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
81-741 |
5.18e-150 |
|
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: 476.53 E-value: 5.18e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14918 1 PGVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 161 GESGAGKTVSARYAMRYFATVSKSGS---------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQ 231
Cdd:cd14918 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 232 IIGANMSTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQKTF 310
Cdd:cd14918 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQI-TSNKKPDLIEMLLITTNPYDYAFVSqGEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 311 TLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMT 390
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 391 RPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKL 470
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 471 EQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRM----SNTS 545
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVvkgkAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 546 FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFqenptppSPFGSMITVKSAKQVIKPNSKHFRtTVG 625
Cdd:cd14918 479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLF-------STYASAEADSGAKKGAKKKGSSFQ-TVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 626 SKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTK 705
Cdd:cd14918 551 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 630
|
650 660 670
....*....|....*....|....*....|....*...
gi 767984698 706 Q--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14918 631 AipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
82-741 |
7.55e-150 |
|
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: 475.67 E-value: 7.55e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14934 2 SVLDNLRQRYTNMR-IYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 162 ESGAGKTVSARYAMRYFATVSKSGSNA-----HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGAN 236
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSsdgkgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 237 MSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKL-GSAEEFNYTRMGgNTVIEGVNDRAEMVETQKTFTLLGF 315
Cdd:cd14934 161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQG-VTVVDNMDDGEELQITDVAFDVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 316 KEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAV 395
Cdd:cd14934 240 SAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 396 NARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEY 475
Cdd:cd14934 320 NSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 476 MKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKP-----RMSNTSFVIQ 549
Cdd:cd14934 400 KREGIEWVFIDFgLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPkggkgKGPEAHFELV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 550 HFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSpfgsmitvkSAKQviKPNSKHFrtTVGSKFR 629
Cdd:cd14934 480 HYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAG---------SKKQ--KRGSSFM--TVSNFYR 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 630 SSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQ-EL 708
Cdd:cd14934 547 EQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNViPQ 626
|
650 660 670
....*....|....*....|....*....|...
gi 767984698 709 SFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14934 627 GFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
82-741 |
2.98e-149 |
|
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: 474.90 E-value: 2.98e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14932 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 162 ESGAGKTVSARYAMRYFATVSKSG-----------SNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQN 230
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 231 QIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLgsaEEFNYTRM--GGNTVIEGVNDRAEMVETQK 308
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCL---EDYSKYRFlsNGNVTIPGQQDKELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 309 TFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 389 MTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHV 467
Cdd:cd14932 318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 468 FKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNFVNrNPLFEKPR--M 541
Cdd:cd14932 398 FILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQGN-NPKFQKPKklK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 542 SNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGSMITVKSAKQVIKPNSKHFR 621
Cdd:cd14932 477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHGAFKTRKGMFR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 622 tTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGI 701
Cdd:cd14932 557 -TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 767984698 702 LM-TKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14932 636 LTpNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
81-741 |
4.13e-149 |
|
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: 474.22 E-value: 4.13e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14912 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 161 GESGAGKTVSARYAMRYFATVSKSGS-----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQ 229
Cdd:cd14912 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 230 NQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQK 308
Cdd:cd14912 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-TSNKKPELIEMLLITTNPYDYPFVSqGEISVASIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 309 TFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14912 239 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 389 MTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVF 468
Cdd:cd14912 319 QTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 469 KLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRM----SN 543
Cdd:cd14912 399 VLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVvkgkAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 544 TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGSmitvKSAKQVIKPNSKHFRtT 623
Cdd:cd14912 479 AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAG----GGAKKGGKKKGSSFQ-T 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 624 VGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILM 703
Cdd:cd14912 554 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 633
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 767984698 704 TKQ--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14912 634 ASAipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
81-741 |
7.70e-149 |
|
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: 473.39 E-value: 7.70e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14916 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 161 GESGAGKTVSARYAMRYFATVSKSG----------SNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQN 230
Cdd:cd14916 80 GESGAGKTVNTKRVIQYFASIAAIGdrskkenpnaNKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 231 QIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCaSAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQKT 309
Cdd:cd14916 160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQIL-SNKKPELLDMLLVTNNPYDYAFVSqGEVSVASIDDSEELLATDSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 310 FTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPM 389
Cdd:cd14916 239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 390 TRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFK 469
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 470 LEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPR----MSNT 544
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRnvkgKQEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 545 SFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSpfGSMITVKSAKQvikpNSKHFRtTV 624
Cdd:cd14916 479 HFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADT--GDSGKGKGGKK----KGSSFQ-TV 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 625 GSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGIL-- 702
Cdd:cd14916 552 SALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILnp 631
|
650 660 670
....*....|....*....|....*....|....*....
gi 767984698 703 MTKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14916 632 AAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
81-741 |
2.94e-148 |
|
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: 471.91 E-value: 2.94e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14910 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 161 GESGAGKTVSARYAMRYFATVSKSGS-----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQ 229
Cdd:cd14910 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 230 NQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQK 308
Cdd:cd14910 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-MSNKKPDLIEMLLITTNPYDYAFVSqGEITVPSIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 309 TFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14910 239 AIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 389 MTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVF 468
Cdd:cd14910 319 QTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 469 KLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSN---- 543
Cdd:cd14910 399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKgkve 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 544 TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGsmitvkSAKQVIKPNSKHFRtT 623
Cdd:cd14910 479 AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEG------GGKKGGKKKGSSFQ-T 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 624 VGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILM 703
Cdd:cd14910 552 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 631
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 767984698 704 TKQ--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14910 632 ASAipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
81-741 |
1.47e-146 |
|
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: 466.06 E-value: 1.47e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFA-ESKLIYTYSGIILVAMNPYKQLPiygDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNN---RNQS 156
Cdd:cd14891 1 AGILHNLEERSKlDNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSgrmQNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 157 IIVSGESGAGKTVSARYAMRYFATVS-----------------KSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFG 219
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAvggkkasgqdieqsskkRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 220 KYTEISF-DEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVN 298
Cdd:cd14891 158 KFMKLQFtKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 299 DRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQI----TAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLC 374
Cdd:cd14891 238 DAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFdeedTSEGEAEIASESDKEALATAAELLGVDEEALEKVIT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 375 NRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFD-VNSFEQFCIN 453
Cdd:cd14891 318 QREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLIN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 454 YANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFvNR 532
Cdd:cd14891 398 YANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPnGILPLLDNEARNPNPSDAKLNETLHKTH-KR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 533 NPLFEKPRMSNT--SFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKfhlcanffqenptppspfgsmitvksak 610
Cdd:cd14891 477 HPCFPRPHPKDMreMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASSA---------------------------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 611 qvikpnskhfrttvgsKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRW 690
Cdd:cd14891 529 ----------------KFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRV 592
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 767984698 691 TYIEFYSRYGILMTKQELSF--SDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14891 593 TYAELVDVYKPVLPPSVTRLfaENDRTLTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
81-741 |
1.66e-145 |
|
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: 464.59 E-value: 1.66e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14915 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 161 GESGAGKTVSARYAMRYFATVSKSGS-----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQ 229
Cdd:cd14915 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeaasgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 230 NQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQK 308
Cdd:cd14915 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-MSNKKPELIEMLLITTNPYDFAFVSqGEITVPSIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 309 TFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14915 239 AVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 389 MTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVF 468
Cdd:cd14915 319 QTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 469 KLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPR----MSN 543
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKpakgKAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 544 TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGsmitvkSAKQVIKPNSKHFRtT 623
Cdd:cd14915 479 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGG------GGKKGGKKKGSSFQ-T 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 624 VGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILM 703
Cdd:cd14915 552 VSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 631
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 767984698 704 TKQ--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14915 632 ASAipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
81-741 |
2.70e-145 |
|
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: 463.77 E-value: 2.70e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14923 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 161 GESGAGKTVSARYAMRYFATVSKSGS----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQN 230
Cdd:cd14923 80 GESGAGKTVNTKRVIQYFATIAVTGDkkkeqqpgkmQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 231 QIIGANMSTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQKT 309
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQI-MSNKKPELIDLLLISTNPFDFPFVSqGEVTVASIDDSEELLATDNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 310 FTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPM 389
Cdd:cd14923 239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 390 TRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFK 469
Cdd:cd14923 319 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 470 LEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPR----MSNT 544
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKpakgKAEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 545 SFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGSmitvkSAKQVIKPNSKHFRtTV 624
Cdd:cd14923 479 HFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSG-----GSKKGGKKKGSSFQ-TV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 625 GSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMT 704
Cdd:cd14923 553 SAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNA 632
|
650 660 670
....*....|....*....|....*....|....*....
gi 767984698 705 KQ--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14923 633 SAipEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
82-741 |
3.91e-144 |
|
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: 460.64 E-value: 3.91e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14921 2 SVLHNLRERYF-SGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 162 ESGAGKTVSARYAMRYFATVSKSGSN-------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIG 234
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGkkdtsitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 235 ANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLgsaEEF-NYTRMG-GNTVIEGVNDRAEMVETQKTFTL 312
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLL---EGFnNYTFLSnGFVPIPAAQDDEMFQETLEAMSI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 313 LGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd14921 238 MGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 393 QAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLE 471
Cdd:cd14921 318 QADFAIEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 472 QEEYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNFVNrNPLFEKPRM--SNTS 545
Cdd:cd14921 398 QEEYQREGIEWNFIDFgLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQGN-HPKFQKPKQlkDKTE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 546 FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQE-NPTPPSPFGSMITVKSAKQVIKPNSKHFRtTV 624
Cdd:cd14921 477 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDvDRIVGLDQMAKMTESSLPSASKTKKGMFR-TV 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 625 GSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMT 704
Cdd:cd14921 556 GQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 635
|
650 660 670
....*....|....*....|....*....|....*...
gi 767984698 705 KQ-ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14921 636 NAiPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
82-741 |
6.41e-142 |
|
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: 454.55 E-value: 6.41e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14930 2 SVLHNLRERYY-SGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 162 ESGAGKTVSARYAMRYFATVSKS-------GSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIG 234
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSpkgrkepGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 235 ANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTviEGVNDRAEMVETQKTFTLLG 314
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSS--SPGQERELFQETLESLRVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 315 FKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14930 239 FSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 395 VNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQE 473
Cdd:cd14930 319 DFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 474 EYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNRNPLFEKPR--MSNTSFV 547
Cdd:cd14930 399 EYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQE-QGGHPKFQRPRhlRDQADFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 548 IQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSpFGSMITVKSAKQVIKPNSKHFRtTVGSK 627
Cdd:cd14930 478 VLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVG-LEQVSSLGDGPPGGRPRRGMFR-TVGQL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 628 FRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQ- 706
Cdd:cd14930 556 YKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAi 635
|
650 660 670
....*....|....*....|....*....|....*
gi 767984698 707 ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14930 636 PKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
81-741 |
1.75e-139 |
|
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: 449.34 E-value: 1.75e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAY--------SGQNMGDMDPHIFAVAEEAYKQMARN 151
Cdd:cd14902 1 AALLQALSERF-EHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFGGLLKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 152 NR-NQSIIVSGESGAGKTVSARYAMRYFATV-------SKSGSNA-HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYT 222
Cdd:cd14902 80 ERrNQSILVSGESGSGKTESTKFLMQFLTSVgrdqsstEQEGSDAvEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 223 EISFDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEF----NYTRMGGNTVIEGVN 298
Cdd:cd14902 160 KIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYellnSYGPSFARKRAVADK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 299 DRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVS---EDDSHLKVFCELLGLESGRVAQWLCN 375
Cdd:cd14902 240 YAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAvtaASRFHLAKCAELMGVDVDKLETLLSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 376 RKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTF---------IGVLDIYGFETFDVNS 446
Cdd:cd14902 320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSIsdedeelatIGILDIFGFESLNRNG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 447 FEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKL 525
Cdd:cd14902 400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSnGLFSLLDQECLMPKGSNQALSTKF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 526 YNNFVNRNplfekprmsntSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCAnFFQENPTPPSPfgsmiT 605
Cdd:cd14902 480 YRYHGGLG-----------QFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVV-AIGADENRDSP-----G 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 606 VKSAKQVIKPNSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQS 685
Cdd:cd14902 543 ADNGAAGRRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHG 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 686 YPSRWTYIEFYSRYGILMTKQELSFSDKK-------------EVCKVVLHRLIQDSNQ---------------------- 730
Cdd:cd14902 623 YSVRLAHASFIELFSGFKCFLSTRDRAAKmnnhdlaqalvtvLMDRVLLEDGVEREEKnpgaltavtgdgsgtafendcr 702
|
730
....*....|....
gi 767984698 731 ---YQFGKTKIFFR 741
Cdd:cd14902 703 rkdVQVGRTLVFCK 716
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
81-741 |
4.21e-139 |
|
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: 448.25 E-value: 4.21e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDaiIHAYSGQNMGDMD--PHIFAVAEEAYKQMARNN------ 152
Cdd:cd14895 1 PAFVDYLAQRYGVDQ-VYCRSGAVLIAVNPFKHIPGLYD--LHKYREEMPGWTAlpPHVFSIAEGAYRSLRRRLhepgas 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 153 -RNQSIIVSGESGAGKTVSARYAMRYFATVSKSG--------SNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTE 223
Cdd:cd14895 78 kKNQTILVSGESGAGKTETTKFIMNYLAESSKHTtatssskrRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 224 ISF-----DEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFK--HLKLGSAEEFNYTRMGGNTVI-E 295
Cdd:cd14895 158 MFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLelQLELLSAQEFQYISGGQCYQRnD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 296 GVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVqitAVGNERSSVSEDDS---------------------H 354
Cdd:cd14895 238 GVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNV---LFVASSEDEGEEDNgaasapcrlasaspssltvqqH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 355 LKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQA---LQFSGKQHT-- 429
Cdd:cd14895 315 LDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSAspqRQFALNPNKaa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 430 ------FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MG 502
Cdd:cd14895 395 nkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRpSG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 503 ILELLDEECLLPHGTDENWLQKLYNNFVNRNPlFEKPR--MSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEIL-R 579
Cdd:cd14895 475 IFSLLDEECVVPKGSDAGFARKLYQRLQEHSN-FSASRtdQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLgK 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 580 ASKFHL--CANFFQENPTPPSPFGSMITVKSAKQVIKpnskhfrTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKL 657
Cdd:cd14895 554 TSDAHLreLFEFFKASESAELSLGQPKLRRRSSVLSS-------VGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESA 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 658 PFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKEVCKvVLHRLiqdsnQYQFGKTK 737
Cdd:cd14895 627 SDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIE-TLKVD-----HAELGKTR 700
|
....
gi 767984698 738 IFFR 741
Cdd:cd14895 701 VFLR 704
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
82-741 |
5.28e-139 |
|
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: 446.46 E-value: 5.28e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14919 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 162 ESGAGKTVSARYAMRYFATVSKSGSN----AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANM 237
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSkkdqGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 238 STYLLEKSRVVFQSENERNYHIFYQLCASAQQsefkHLKLG-SAEEFNYTRM--GGNTVIEGVNDRAEMVETQKTFTLLG 314
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGE----HLKTDlLLEPYNKYRFlsNGHVTIPGQQDKDMFQETMEAMRIMG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 315 FKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14919 237 IPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 395 VNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQE 473
Cdd:cd14919 317 DFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 474 EYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNRNPLFEKPRM--SNTSFV 547
Cdd:cd14919 397 EYQREGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQE-QGTHPKFQKPKQlkDKADFC 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 548 IQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQEnptpPSPFGSMITVKSAKQVIKPNSKHFRT----T 623
Cdd:cd14919 476 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD----VDRIIGLDQVAGMSETALPGAFKTRKgmfrT 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 624 VGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILM 703
Cdd:cd14919 552 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 631
|
650 660 670
....*....|....*....|....*....|....*....
gi 767984698 704 TKQ-ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14919 632 PNSiPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
71-791 |
6.09e-139 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 451.41 E-value: 6.09e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 71 DLTALSYLHEPAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAY-SGQNMGDMDPHIFAVAEEAYKQMA 149
Cdd:PTZ00014 100 DIGLLPHTNIPCVLDFLKHRY-LKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYrDAKDSDKLPPHVFTTARRALENLH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 150 RNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQ 229
Cdd:PTZ00014 179 GVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 230 NQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYtrMGGNTV-IEGVNDRAEMVETQK 308
Cdd:PTZ00014 259 GGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKY--INPKCLdVPGIDDVKDFEEVME 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 309 TFTLLGFKEDFQMDVFKILAAILHLGNVQITavGNERSSVSE----DDSHLKVF---CELLGLESGRVAQWLCNRKIVTS 381
Cdd:PTZ00014 337 SFDSMGLSESQIEDIFSILSGVLLLGNVEIE--GKEEGGLTDaaaiSDESLEVFneaCELLFLDYESLKKELTVKVTYAG 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 382 SETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQ 461
Cdd:PTZ00014 415 NQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQK 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 462 QFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPR 540
Cdd:PTZ00014 495 NFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGkSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKV 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 541 MSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQenptppspfGSMITV-KSAK-QVIkpnsk 618
Cdd:PTZ00014 575 DSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFE---------GVEVEKgKLAKgQLI----- 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 619 hfrttvGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSR 698
Cdd:PTZ00014 641 ------GSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQ 714
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 699 YGIL-MTKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR---AGQVAYLEKLRLDKLRQSCVMVQKHMRGWLQRK 774
Cdd:PTZ00014 715 FKYLdLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKR 794
|
730
....*....|....*..
gi 767984698 775 KFLRERRAALIIQQYFR 791
Cdd:PTZ00014 795 KVRKNIKSLVRIQAHLR 811
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
83-739 |
1.14e-138 |
|
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: 445.06 E-value: 1.14e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 83 VLHNLRIRFAESkLIYTYSGIILVAMNPYKQLP-IYGDAIIHAY-SGQNMGDMDPHIFAVAEEAYK--QMARNNRNQSII 158
Cdd:cd14880 3 VLRCLQARYTAD-TFYTNAGCTLVALNPFKPVPqLYSPELMREYhAAPQPQKLKPHIFTVGEQTYRnvKSLIEPVNQSIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 159 VSGESGAGKTVSARYAMRYFATVSKSGSN-------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQ 231
Cdd:cd14880 82 VSGESGAGKTWTSRCLMKFYAVVAASPTSweshkiaERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 232 IIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEgvnDRAEMveTQKTFT 311
Cdd:cd14880 162 MTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNLEE---DCFEV--TREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 312 LLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSS---VSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVV-- 386
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQVfk 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 387 KPMTRPQAVNARDALAKKIYAHLFDFIVERINQAL-QFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNM 465
Cdd:cd14880 317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSIcADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 466 HVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMS-N 543
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSpISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKLSrE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 544 TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTppspfgsmitvKSAKQVIKPNSKHFRTT 623
Cdd:cd14880 477 PSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPE-----------EKTQEEPSGQSRAPVLT 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 624 VGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILM 703
Cdd:cd14880 546 VVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLR 625
|
650 660 670
....*....|....*....|....*....|....*.
gi 767984698 704 TKQELSFSDKKEVCKVVLHrliqdSNQYQFGKTKIF 739
Cdd:cd14880 626 RLRPHTSSGPHSPYPAKGL-----SEPVHCGRTKVF 656
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
82-741 |
8.00e-138 |
|
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: 443.74 E-value: 8.00e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd15896 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 162 ESGAGKTVSARYAMRYFATVSKS-----------GSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQN 230
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 231 QIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLgsaEEFNYTRM--GGNTVIEGVNDRAEMVETQK 308
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLL---ENYNNYRFlsNGNVTIPGQQDKDLFTETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 309 TFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKP 388
Cdd:cd15896 238 AFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 389 MTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHV 467
Cdd:cd15896 318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 468 FKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIE---AKMGILELLDEECLLPHGTDENWLQKLYNNfVNRNPLFEKPR--M 541
Cdd:cd15896 398 FILEQEEYQREGIEWSFIDFgLDLQPCIDLIEkpaSPPGILALLDEECWFPKATDKSFVEKVLQE-QGTHPKFFKPKklK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 542 SNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSpFGSMITVKSAKQVIKPNSKHFR 621
Cdd:cd15896 477 DEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVG-LDKVSGMSEMPGAFKTRKGMFR 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 622 tTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGI 701
Cdd:cd15896 556 -TVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 634
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 767984698 702 LMTKQ-ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd15896 635 LTPNAiPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
81-739 |
2.45e-136 |
|
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: 438.65 E-value: 2.45e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSG-QNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14876 1 PCVLDFLKHRYLKNQ-IYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 160 SGESGAGKTVSARYAMRYFATVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMST 239
Cdd:cd14876 80 SGESGAGKTEATKQIMRYFASAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYtrMGGNTV-IEGVNDRAEMVETQKTFTLLGFKED 318
Cdd:cd14876 160 FLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKF--LNPKCLdVPGIDDVADFEEVLESLKSMGLTEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 319 FQMDVFKILAAILHLGNVQITA-----VGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14876 238 QIDTVFSIVSGVLLLGNVKITGkteqgVDDAAAISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 394 AVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQE 473
Cdd:cd14876 318 AEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERESK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 474 EYMKEDIPWTLIDFYDNQPVID-LIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSNTSFVIQHFA 552
Cdd:cd14876 398 LYKDEGIPTAELEYTSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVDSNINFIVVHTI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 553 DKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPtppspfgsMITVKSAK-QVIkpnskhfrttvGSKFRSS 631
Cdd:cd14876 478 GDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVV--------VEKGKIAKgSLI-----------GSQFLKQ 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 632 LYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGIL-MTKQELSF 710
Cdd:cd14876 539 LESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLdLGIANDKS 618
|
650 660
....*....|....*....|....*....
gi 767984698 711 SDKKEVCKVVLHRLIQDSNQYQFGKTKIF 739
Cdd:cd14876 619 LDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
83-741 |
1.34e-131 |
|
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: 425.45 E-value: 1.34e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMG-----DMDPHIFAVAEEAYKQMARNNRNQS 156
Cdd:cd14886 3 VIDILRDRFAKDK-IYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 157 IIVSGESGAGKTVSARYAMRYFATVSKSGSNAhVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGAN 236
Cdd:cd14886 82 CIVSGESGAGKTETAKQLMNFFAYGHSTSSTD-VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 237 MSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFK 316
Cdd:cd14886 161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKLFSK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 317 EDFQmDVFKILAAILHLGNVQ---ITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14886 241 NEID-SFYKCISGILLAGNIEfseEGDMGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 394 AVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQE 473
Cdd:cd14886 320 AEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEIQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 474 EYMKEDIPWTLIDFYDNQPVIDLIEA-KMGILELLDEECLLPHGTDENWLQKLYNNFvnRNPLFEKPRMSNTSFVIQHFA 552
Cdd:cd14886 400 EYEIEGIDHSMITFTDNSNVLAVFDKpNLSIFSFLEEQCLIQTGSSEKFTSSCKSKI--KNNSFIPGKGSQCNFTIVHTA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 553 DKVEYKCEGFLEKNRDTVYDMLVEILRASKFHlcanffqenptppspfgsmITVKSAKQVIKPNSKHFRTTVGSKFRSSL 632
Cdd:cd14886 478 ATVTYNTEEFVDKNKHKLSVDILELLMGSTNP-------------------IVNKAFSDIPNEDGNMKGKFLGSTFQLSI 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 633 YLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSF-- 710
Cdd:cd14886 539 DQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILISHNSSSQna 618
|
650 660 670
....*....|....*....|....*....|..
gi 767984698 711 -SDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14886 619 gEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
83-702 |
2.28e-130 |
|
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: 421.25 E-value: 2.28e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAY---------SGQNMGD--MDPHIFAVAEEAYKQMAR 150
Cdd:cd14900 3 ILSALETRFYAQK-IYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssSTRNKGSdpMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 151 --NNR--NQSIIVSGESGAGKTVSARYAMRYFA---------TVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSR 217
Cdd:cd14900 82 glNGVmsDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaaSVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 218 FGKYTEISFDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKhlklgsaeEFNYTRMggntviegv 297
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK--------RDMYRRV--------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 298 ndraemvetQKTFTLLGFKEDFQMDVFKILAAILHLGNVQItAVGNERSSVSEDDSHLKVFCE--------LLGLESGRV 369
Cdd:cd14900 225 ---------MDAMDIIGFTPHERAGIFDLLAALLHIGNLTF-EHDENSDRLGQLKSDLAPSSIwsrdaaatLLSVDATKL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 370 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQF--SGKQHT---FIGVLDIYGFETFDV 444
Cdd:cd14900 295 EKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMddSSKSHGglhFIGILDIFGFEVFPK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 445 NSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQ 523
Cdd:cd14900 375 NSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRpTGILSLIDEECVMPKGSDTTLAS 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 524 KLYNNFVNrNPLFEKPRMSNTS--FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAskfhlcanffqenptppspfg 601
Cdd:cd14900 455 KLYRACGS-HPRFSASRIQRARglFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVY--------------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 602 smitvksakqvikpnskhfrttvGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRI 681
Cdd:cd14900 513 -----------------------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRV 569
|
650 660
....*....|....*....|.
gi 767984698 682 SAQSYPSRWTYIEFYSRYGIL 702
Cdd:cd14900 570 ARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
81-741 |
1.06e-128 |
|
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: 417.26 E-value: 1.06e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14896 1 SSVLLCLKKRF-HLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 161 GESGAGKTVSARYAMRYFATVSKSGSNAHVE--DKVLasnPITEAVGNAKTTRNDNSSRFGKYTEISFdEQNQIIGANMS 238
Cdd:cd14896 80 GHSGSGKTEAAKKIVQFLSSLYQDQTEDRLRqpEDVL---PILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 239 TYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKED 318
Cdd:cd14896 156 HYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 319 FQMDVFKILAAILHLGNVQITAVGNERSSVSE--DDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVN 396
Cdd:cd14896 236 ELTAIWAVLAAILQLGNICFSSSERESQEVAAvsSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 397 ARDALAKKIYAHLFDFIVERINQALQFSGKQHTF--IGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEE 474
Cdd:cd14896 316 ARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEEE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 475 YMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNrNPLFEKPRMSNTSFVIQHFAD 553
Cdd:cd14896 396 CQRELLPWVPIPQPPRESCLDLLVDQpHSLLSILDDQTWLSQATDHTFLQKCHYHHGD-HPSYAKPQLPLPVFTVRHYAG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 554 KVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQEnptppspfgsmitvKSAKQVIKPNskhfRTTVGSKFRSSLY 633
Cdd:cd14896 475 TVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQE--------------AEPQYGLGQG----KPTLASRFQQSLG 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 634 LLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDK 713
Cdd:cd14896 537 DLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEALSDR 616
|
650 660
....*....|....*....|....*...
gi 767984698 714 KEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14896 617 ERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
83-734 |
2.63e-126 |
|
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: 413.22 E-value: 2.63e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 83 VLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQN-MGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14906 3 ILNNLGKRY-KSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINqNKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 161 GESGAGKTVSARYAMRYFATVSKSGS---------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQ 231
Cdd:cd14906 82 GESGSGKTEASKTILQYLINTSSSNQqqnnnnnnnNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSDG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 232 II-GANMSTYLLEKSRVVFQSENER-NYHIFYQLCASAQQSEFKHLKLGS-AEEFNY-------------TRMGGNTVIE 295
Cdd:cd14906 162 KIdGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNdPSKYRYldarddvissfksQSSNKNSNHN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 296 GVNDRAEMVE--TQKTFTLLGFKEDFQmDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVF---CELLGLESGRVA 370
Cdd:cd14906 242 NKTESIESFQllKQSMESMSINKEQCD-AIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLesvSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 371 QWLCNRKIVTSSETVV--KPMTRPQAVNARDALAKKIYAHLFDFIVERINQ-----------ALQFSGKQHTFIGVLDIY 437
Cdd:cd14906 321 QALLNRNLKAGGRGSVycRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRkfnqntqsndlAGGSNKKNNLFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 438 GFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHG 516
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKsDGILSLLDDECIMPKG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 517 TDENWLQKLYNNFVNRNPLFEKPrMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTP 596
Cdd:cd14906 481 SEQSLLEKYNKQYHNTNQYYQRT-LAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQITS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 597 PSPfgsmiTVKSAKQVIkpnskhfrtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVL 676
Cdd:cd14906 560 TTN-----TTKKQTQSN---------TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVL 625
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 767984698 677 ETIRISAQSYPSRWTYIEFYSRYGILMTKQELSfSDKKEVCKVVLHRLIQDSNQYQFG 734
Cdd:cd14906 626 NTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRK-NNNNPKLASQLILQNIQSKLKTMG 682
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
82-699 |
3.90e-116 |
|
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: 384.83 E-value: 3.90e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYS---GQNMGDM-------DPHIFAVAEEAYKQMAR 150
Cdd:cd14899 2 SILNALRLRY-ERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhNSQFGDRvtstdprEPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 151 NNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSG----------------SNAHVEDKVLASNPITEAVGNAKTTRNDN 214
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGnnnltnsesisppaspSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 215 SSRFGKYTEISF-DEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQL------CASAQQSEFKHLKLGSAEEFNYTR 287
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELlsadnnCVSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 288 MGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNER------------SSVSEDDSHL 355
Cdd:cd14899 241 SLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKGddtvfadearvmSSTTGAFDHF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 356 KVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGK--------- 426
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 427 ------QHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK 500
Cdd:cd14899 401 vddeedATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 501 -MGILELLDEECLLPHGTDENWLQKLYNNFVNR--NPLFEKPRM--SNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLV 575
Cdd:cd14899 481 pIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKnsHPHFRSAPLiqRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 576 EILRASKFHLCANFFQENPTPPSPFGSMITVKSAKQVIKPNSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDE 655
Cdd:cd14899 561 QLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 767984698 656 KLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRY 699
Cdd:cd14899 641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
83-741 |
2.55e-111 |
|
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: 369.52 E-value: 2.55e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 83 VLHNLRIRFAESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAY-SGQNMGDMDPHIFAVAEEAYKQM-ARNNRNQSIIVS 160
Cdd:cd14875 3 LLHCIKERFEKLHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 161 GESGAGKTVSARYAMRYFATVS----KSGSNAHVEDKVLA----SNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQI 232
Cdd:cd14875 83 GESGSGKTENAKMLIAYLGQLSymhsSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPTSGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 233 -IGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHL-KLGSAEEFNYTRmGGNTVI------EGVNDRAEMV 304
Cdd:cd14875 163 mVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLN-GGNTFVrrgvdgKTLDDAHEFQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 305 ETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVsEDDSHLKVFCELLGLESGRVAQWLcnrkIVTSSET 384
Cdd:cd14875 242 NVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQI-ADETPFLTACRLLQLDPAKLRECF----LVKSKTS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 385 VVKPMTRPQ-AVNARDALAKKIYAHLFDFIVERINQAL--QFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQ 461
Cdd:cd14875 317 LVTILANKTeAEGFRNAFCKAIYVGLFDRLVEFVNASItpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 462 QFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPR 540
Cdd:cd14875 397 HYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKrTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPYFVLPK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 541 MS-NTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKfhlcANFFQenptppspfgsmiTVKSAKQVikpnSKH 619
Cdd:cd14875 477 STiPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNST----DEFIR-------------TLLSTEKG----LAR 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 620 FRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRY 699
Cdd:cd14875 536 RKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYF 615
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 767984698 700 GILMTKQELSF---SDKKEVCKVVLHRLIQ----DSNQYQFGKTKIFFR 741
Cdd:cd14875 616 YLIMPRSTASLfkqEKYSEAAKDFLAYYQRlygwAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
82-740 |
2.53e-107 |
|
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: 357.63 E-value: 2.53e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 82 AVLHNLRIRFAESkLIYTY-SGIILVAMNPYKQLPIYGDAIIHAY-------SGQNMGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14879 5 AITSHLASRFRSD-LPYTRlGSSALVAVNPYKYLSSNSDASLGEYgseyydtTSGSKEPLPPHAYDLAARAYLRMRRRSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 154 NQSIIVSGESGAGKTVSARYAMRYFATVSKSGSNAH-VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQI 232
Cdd:cd14879 84 DQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKKGTkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 233 IGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYT-RMGGNTVIEGV--NDRAEMVETQKT 309
Cdd:cd14879 164 IGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLaSYGCHPLPLGPgsDDAEGFQELKTA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 310 FTLLGFKEDFQMDVFKILAAILHLGNVQIT--AVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNR-KIVtSSEtVV 386
Cdd:cd14879 244 LKTLGFKRKHVAQICQLLAAILHLGNLEFTydHEGGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTYKtKLV-RKE-LC 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 387 KPMTRP-QAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFD---VNSFEQFCINYANEKLQQ 461
Cdd:cd14879 322 TVFLDPeGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDDfATFISLLDFPGFQNRSstgGNSLDQFCVNFANERLHN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 462 QFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMG--ILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKP 539
Cdd:cd14879 402 YVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGglLGILDDQTRRMPKKTDEQMLEALRKRFGNHSSFIAVG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 540 RMSNTS----FVIQHFADKVEYKCEGFLEKNRDtvydmlveilraskfHLCANFfqenptppspfgsMITVKSAKQvikp 615
Cdd:cd14879 482 NFATRSgsasFTVNHYAGEVTYSVEGFLERNGD---------------VLSPDF-------------VNLLRGATQ---- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 616 nskhfrttvgskFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEF 695
Cdd:cd14879 530 ------------LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEF 597
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 767984698 696 YSRYGILMTKQELSFSDKKevckvVLHRLIQDSNQYQFGKTKIFF 740
Cdd:cd14879 598 CERYKSTLRGSAAERIRQC-----ARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
82-702 |
8.97e-106 |
|
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: 350.74 E-value: 8.97e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQlpIYGDAIIHAYSgQNMGDMDPHIFAVAEEAYKQMARNNrNQSIIVSG 161
Cdd:cd14898 2 ATLEILEKRYASGK-IYTKSGLVFLALNPYET--IYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVHG-NQTIVISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 162 ESGAGKTVSARYAMRYFatVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDeqNQIIGANMSTYL 241
Cdd:cd14898 77 ESGSGKTENAKLVIKYL--VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 242 LEKSRVVFQSENERNYHIFYQLCASaqqsefKHLKLGSaEEFNYTRMGGNT-VIEGVNDRAEMVETQ-KTFTLLGFKEdf 319
Cdd:cd14898 153 LEKSRVTHHEKGERNFHIFYQFCAS------KRLNIKN-DFIDTSSTAGNKeSIVQLSEKYKMTCSAmKSLGIANFKS-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 320 qmdVFKILAAILHLGNVQITavgNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARD 399
Cdd:cd14898 224 ---IEDCLLGILYLGSIQFV---NDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIRN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 400 ALAKKIYAHLFDFIVERINQALQFSGKQHtfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKED 479
Cdd:cd14898 298 SMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 480 IPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKL--YNN-FVNRNplfekprmSNTSFVIQHFADKVE 556
Cdd:cd14898 376 IEWPDVEFFDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIkkYLNgFINTK--------ARDKIKVSHYAGDVE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 557 YKCEGFLEKNRDtvydmlveilrasKFHLcanffqenptppSPFGSMITVKSAKqvikpnskhfRTTVGSKFRSSLYLLM 636
Cdd:cd14898 448 YDLRDFLDKNRE-------------KGQL------------LIFKNLLINDEGS----------KEDLVKYFKDSMNKLL 492
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767984698 637 ETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGIL 702
Cdd:cd14898 493 NSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRIL 558
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
81-741 |
1.18e-100 |
|
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: 340.86 E-value: 1.18e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFAES-------KLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14887 1 PNLLENLYQRYNKAyinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 154 NQSIIVSGESGAGKTVSARYAMRYFATVS---KSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQN 230
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSdrrHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 231 QIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSefKHLKLGSAEEFNYTrmggntviegvndrAEMVETQKTF 310
Cdd:cd14887 161 KLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAA--ATQKSSAGEGDPES--------------TDLRRITAAM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 311 TLLGFKEDFQMDVFKILAAILHLGNVQIT----------------AVGNE-----RSSVSE-------------DDSHLK 356
Cdd:cd14887 225 KTVGIGGGEQADIFKLLAAILHLGNVEFTtdqepetskkrkltsvSVGCEetaadRSHSSEvkclssglkvteaSRKHLK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 357 VFCELLGLESGRVAQWLCNRKIVTSS--ETVvKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGK-------- 426
Cdd:cd14887 305 TVARLLGLPPGVEGEEMLRLALVSRSvrETR-SFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsde 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 427 ------QHTFIGVLDIYGFETF---DVNSFEQFCINYANEKLqqqfnmHVFKLEQ----EE--YMKEDIPWTLIDFYDNQ 491
Cdd:cd14887 384 dtpsttGTQTIGILDLFGFEDLrnhSKNRLEQLCINYANERL------HCFLLEQlilnEHmlYTQEGVFQNQDCSAFPF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 492 P-------------VIDLI-EAKMGILELLDEECLLPH----------GTDENW------------LQKLYNNFVNRNPL 535
Cdd:cd14887 458 SfplastltsspssTSPFSpTPSFRSSSAFATSPSLPSslsslssslsSSPPVWegrdnsdlfyekLNKNIINSAKYKNI 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 536 FEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAskfhlCANFFQENPTPPSPFGSMITVKsakqvikp 615
Cdd:cd14887 538 TPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLA-----CSTYTRLVGSKKNSGVRAISSR-------- 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 616 nskhfRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEF 695
Cdd:cd14887 605 -----RSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVEL 679
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 767984698 696 YSRYGILMTKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 741
Cdd:cd14887 680 WRRYETKLPMALREALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
82-741 |
7.57e-94 |
|
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: 319.07 E-value: 7.57e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAY---SGQNMGDMDPHIFAVAEEAYKQMARNNRNQSII 158
Cdd:cd14878 2 SLLYEIQKRFGNNQ-IYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 159 VSGESGAGKTVSARYAMRYFATVSKSgSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISF-DEQNQIIGANM 237
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASS-SRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 238 STYLLEKSRVVFQSENERNYHIFYQLC--ASAQQSEFKHLKLGSAEEF-NYTRMGGNTVIEGVNDRAEMVETQKTFTLLG 314
Cdd:cd14878 160 YTYMLEKSRLVSQPPGQSNFLIFYLLMdgLSAEEKYGLHLNNLCAHRYlNQTMREDVSTAERSLNREKLAVLKQALNVVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 315 FKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14878 240 FSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 395 VNARDALAKKIYAHLFDFIVERINQALQ----FSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKL 470
Cdd:cd14878 320 EFYRDLLAKSLYSRLFSFLVNTVNCCLQsqdeQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 471 EQEEYMKEDIPWTLIDFYDNQP-VIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYN-------NFV-------NRNP 534
Cdd:cd14878 400 EQTECVQEGVTMETAYSPGNQTgVLDFFFQKpSGFLSLLDEESQMIWSVEPNLPKKLQSllessntNAVyspmkdgNGNV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 535 lfeKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQenptppspfgsmitvksakqvik 614
Cdd:cd14878 480 ---ALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ----------------------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 615 pnSKhfRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIE 694
Cdd:cd14878 534 --SK--LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSD 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 767984698 695 FYSRYG-----ILMTKQELSfsdKKEVCKVVLHRLIQDSnqYQFGKTKIFFR 741
Cdd:cd14878 610 FLSRYKpladtLLGEKKKQS---AEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
83-741 |
1.04e-92 |
|
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: 315.42 E-value: 1.04e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 83 VLHNLRIRFaESKLIYTYSGIILVAMNPYKQLpiygDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd14937 3 VLNMLALRY-KKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 163 SGAGKTVSARYAMRYFatVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYLL 242
Cdd:cd14937 78 SGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 243 EKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTrMGGNTVIEGVNDRAEMVETQKTFTLLGFkEDFQMD 322
Cdd:cd14937 156 ENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYI-VNKNVVIPEIDDAKDFGNLMISFDKMNM-HDMKDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 323 VFKILAAILHLGNVQITAV--GNERSSVSEDDSHLKVFCE---LLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNA 397
Cdd:cd14937 234 LFLTLSGLLLLGNVEYQEIekGGKTNCSELDKNNLELVNEisnLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 398 RDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 477
Cdd:cd14937 314 CKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYKA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSNTSFVIQHFADKVEY 557
Cdd:cd14937 394 EDILIESVKYTTNESIIDLLRGKTSIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINKNFVIKHTVSDVTY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 558 KCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQEnptppspfgsmitVKSAKQVIKPNSKHFrttvgsKFRSSLYLLME 637
Cdd:cd14937 474 TITNFISKNKDILPSNIVRLLKVSNNKLVRSLYED-------------VEVSESLGRKNLITF------KYLKNLNNIIS 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 638 TLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAqSYPSRWTYIEFYSRYGIL--MTKQELSFSDKKE 715
Cdd:cd14937 535 YLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNISF-FFQYKYTFDVFLSYFEYLdySTSKDSSLTDKEK 613
|
650 660
....*....|....*....|....*.
gi 767984698 716 VCKVVLHRLiqDSNQYQFGKTKIFFR 741
Cdd:cd14937 614 VSMILQNTV--DPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
82-740 |
6.92e-92 |
|
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: 312.82 E-value: 6.92e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 82 AVLHNLRIRFAESKLiYTYSGIILVAMNPYKQLPiygdAIIHAYSGQNMGDMdPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14881 2 AVMKCLQARFYAKEF-FTNVGPILLSVNPYRDVG----NPLTLTSTRSSPLA-PQLLKVVQEAVRQQSETGYPQAIILSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 162 ESGAGKTVSARYAMRYFATVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEqnqiiGANMST-- 239
Cdd:cd14881 76 TSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-----GALYRTki 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 240 --YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKT-FTLLGFK 316
Cdd:cd14881 151 hcYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKAcLGILGIP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 317 edFqMDVFKILAAILHLGNVQITAvGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVN 396
Cdd:cd14881 231 --F-LDVVRVLAAVLLLGNVQFID-GGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKSVCDANMSNM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 397 ARDALAKKIYAHLFDFIVERINQALQFSGKQHT-----FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLE 471
Cdd:cd14881 307 TRDALAKALYCRTVATIVRRANSLKRLGSTLGThatdgFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTHIFKSS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 472 QEEYMKEDIPWTL-IDFYDNQPVIDLIEA-KMGILELLDEECLlPHGTDENWLQKLYNNFVNRNPLFEKPRMSNTSFVIQ 549
Cdd:cd14881 387 IESCRDEGIQCEVeVDYVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAKPQDDRMFGIR 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 550 HFADKVEYKCEGFLEKNRDTVYDMLVEILRAskfHLCAnffqenptppspFGsmitvksakqvikpnskhFRTTVgSKFR 629
Cdd:cd14881 466 HFAGRVVYDASDFLDTNRDVVPDDLVAVFYK---QNCN------------FG------------------FATHT-QDFH 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 630 SSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELS 709
Cdd:cd14881 512 TRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLR 591
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 767984698 710 FSDKKEV--CKVVL-----HRLIQDSN---QYQFGKTKIFF 740
Cdd:cd14881 592 RVEEKALedCALILqfleaQPPSKLSSvstSWALGKRHIFL 632
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
83-741 |
1.51e-84 |
|
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: 293.06 E-value: 1.51e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 83 VLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd01386 3 VLHTLRQRYG-ANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 163 SGAGKTVSARYAMRYFATVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYLL 242
Cdd:cd01386 82 SGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 243 EKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRA-EMVETQKTFTLLGFKEDFQM 321
Cdd:cd01386 162 ERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKAAaAFSKLQAAMKTLGISEEEQR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 322 DVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLE-------------SGRVAQWLCNRkivTSSETVVKP 388
Cdd:cd01386 242 AIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTleelssaifkhhlSGGPQQSTTSS---GQESPARSS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 389 MTRPQ--AVNARDALAKKIYAHLFDFIVERINQALqfSGKQHTF--IGVLDIYGFEtfdvN----------SFEQFCINY 454
Cdd:cd01386 319 SGGPKltGVEALEGFAAGLYSELFAAVVSLINRSL--SSSHHSTssITIVDTPGFQ----NpahsgsqrgaTFEDLCHNY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 455 ANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDN-QPVIDLI---------------EAKMGILELLDEECLLPHGTD 518
Cdd:cd01386 393 AQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSpGALVALIdqapqqalvrsdlrdEDRRGLLWLLDEEALYPGSSD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 519 ENWLQKLYNNF----VNRNPLFEKPRMSNTSFVIQHF--ADKVEYKCEGFLeknrdtvydmlveilRASKfhlcanffqE 592
Cdd:cd01386 473 DTFLERLFSHYgdkeGGKGHSLLRRSEGPLQFVLGHLlgTNPVEYDVSGWL---------------KAAK---------E 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 593 NPTPpspfgsmitvKSAKQVIKPNSKHF----RTTVGSKFRSSLYLLMETLNATTPHYVRCIKPN------DEKLPFEFD 662
Cdd:cd01386 529 NPSA----------QNATQLLQESQKETaavkRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkdERSTSSPAA 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 663 SKRIVQ------QLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKEVC--KVVLHRLIQ----DSNQ 730
Cdd:cd01386 599 GDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLNSEVAdeRKAVEELLEeldlEKSS 678
|
730
....*....|.
gi 767984698 731 YQFGKTKIFFR 741
Cdd:cd01386 679 YRIGLSQVFFR 689
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
81-732 |
1.51e-84 |
|
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: 292.97 E-value: 1.51e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYS-------GQNMGDMDPHIFAVAEEAYKQMARNN 152
Cdd:cd14884 1 PNVLQNLKNRYLKNK-IYTFHASLLLALNPYKPLKeLYDQDVMNVYLhkksnsaASAAPFPKAHIYDIANMAYKNMRGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 153 RNQSIIVSGESGAGKTVSARYAMRYFATVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQI 232
Cdd:cd14884 80 KRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVENT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 233 I---------GANMSTYLLEKSRVVFQSENERNYHIFYQL---CASAQQSE------FKHLKLGSAEEFNYTRMGGNTVI 294
Cdd:cd14884 160 QknmfngcfrNIKIKILLLEINRCIAHNFGERNFHVFYQVlrgLSDEDLARrnlvrnCGVYGLLNPDESHQKRSVKGTLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 295 EGVN----DRAEMVETQKTFTLL-------GFKEDFQMDVFKILAAILHLGNvqitavgnerssvseddSHLKVFCELLG 363
Cdd:cd14884 240 LGSDsldpSEEEKAKDEKNFVALlhglhyiKYDERQINEFFDIIAGILHLGN-----------------RAYKAAAECLQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 364 LESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQAL------------QFSGKQHTFI 431
Cdd:cd14884 303 IEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdesdneDIYSINEAII 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 432 GVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEEC 511
Cdd:cd14884 383 SILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAKIFRRLDDITKLK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 512 LLPHG-TDENWLQKLYNN-------------FVN---RNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDML 574
Cdd:cd14884 463 NQGQKkTDDHFFRYLLNNerqqqlegkvsygFVLnhdADGTAKKQNIKKNIFFIRHYAGLVTYRINNWIDKNSDKIETSI 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 575 VEILRASKFHlcanFFQENptppspfgsmitvksakqVIKPNSKHFrTTVGSKFRSSLYLLMETLNATTPHYVRCIKPND 654
Cdd:cd14884 543 ETLISCSSNR----FLREA------------------NNGGNKGNF-LSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNA 599
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767984698 655 EKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRwtyiefysrygilMTKQELSFSDKKEVCKVVLHRLIQDSNQYQ 732
Cdd:cd14884 600 KMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHK-------------IPKKETAAALKEQIAKELEKCNSNTDIEYQ 664
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
93-741 |
4.30e-82 |
|
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: 285.45 E-value: 4.30e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 93 ESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSgQNMGdMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTVSA 171
Cdd:cd14905 12 KKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN-QRRG-LPPHLFALAAKAISDMQDFRRDQLIFIGGESGSGKSENT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 172 RYAMRYFATVSKSGSNaHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYLLEKSRVVFQS 251
Cdd:cd14905 90 KIIIQYLLTTDLSRSK-YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 252 ENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAIL 331
Cdd:cd14905 169 KGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFII 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 332 HLGNVQITAvGNERSSVsEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSEtvvkpmtrpqAVNARDALAKKIYAHLFD 411
Cdd:cd14905 249 ILGNVTFFQ-KNGKTEV-KDRTLIESLSHNITFDSTKLENILISDRSMPVNE----------AVENRDSLARSLYSALFH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 412 FIVERINQALQFSGKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPW-TLIDFYDN 490
Cdd:cd14905 317 WIIDFLNSKLKPTQYSHT-LGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWmTPISFKDN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 491 QPVIDLIEAKMGILELLDEECllpHGTDENWLQKLyNNFVNRNPLF-EKPrmsnTSFVIQHFADKVEYKCEGFLEKNRDT 569
Cdd:cd14905 396 EESVEMMEKIINLLDQESKNI---NSSDQIFLEKL-QNFLSRHHLFgKKP----NKFGIEHYFGQFYYDVRGFIIKNRDE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 570 VY--------DMLVEIL--RASKFHLCAN-------FFQENPTPPSPFgSMITV------KSAKQVIKPNSKH------F 620
Cdd:cd14905 468 ILqrtnvlhkNSITKYLfsRDGVFNINATvaelnqmFDAKNTAKKSPL-SIVKVllscgsNNPNNVNNPNNNSggggggG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 621 RTTVGSKFRSSLYLLMETLNATTP------HYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIE 694
Cdd:cd14905 547 NSGGGSGSGGSTYTTYSSTNKAINnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKI 626
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 767984698 695 FYSRYGILMTKQElSFSDKKEvcKVVLHRLIQDS---NQYQFGKTKIFFR 741
Cdd:cd14905 627 FFDRFSFFFQNQR-NFQNLFE--KLKENDINIDSilpPPIQVGNTKIFLR 673
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
83-741 |
6.44e-78 |
|
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: 272.38 E-value: 6.44e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 83 VLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd14882 3 ILEELRHRY-LMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 163 SGAGKTVSARYAMRYFATVSKsgSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYLL 242
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGD--GNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 243 EKSRVVFQSENERNYHIFYQLCASAQQSE-FKHLKLGSAEEFNYTRMGGNTVIEGV----NDRAEMVETQKTFT----LL 313
Cdd:cd14882 160 EKLRVSTTDGNQSNFHIFYYFYDFIEAQNrLKEYNLKAGRNYRYLRIPPEVPPSKLkyrrDDPEGNVERYKEFEeilkDL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 314 GFKEDFQMDVFKILAAILHLGNVQItaVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14882 240 DFNEEQLETVRKVLAAILNLGEIRF--RQNGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHTTEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 394 AVNARDALAKKIYAHLFDFIVERINQALQFS----GKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFK 469
Cdd:cd14882 318 ARDARDVLASTLYSRLVDWIINRINMKMSFPravfGDKYS-ISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYNQRIFI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 470 LEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKmgilelldeecllPHG----TDENWLQKLYNNFV------NRNPlFEKP 539
Cdd:cd14882 397 SEMLEMEEEDIPTINLRFYDNKTAVDQLMTK-------------PDGlfyiIDDASRSCQDQNYImdrikeKHSQ-FVKK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 540 rMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASkfhlcanffqenptppspfgsmiTVKSAKQVIKPNSKH 619
Cdd:cd14882 463 -HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSS-----------------------LDESVKLMFTNSQVR 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 620 FRTTVGSKFRSSLYLLMETL----NATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEF 695
Cdd:cd14882 519 NMRTLAATFRATSLELLKMLsigaNSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEF 598
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 767984698 696 YSRYGILMTKQELSFSDKKEVCKVVLHRLIQDSnqYQFGKTKIFFR 741
Cdd:cd14882 599 LRRYQFLAFDFDETVEMTKDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
82-741 |
3.18e-75 |
|
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: 264.04 E-value: 3.18e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYsgqnmgdmdpHIFAVAEEAYKQMARNNRN-QSIIVS 160
Cdd:cd14874 2 GIAQNLHERF-KKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 161 GESGAGKTVSARYAMRYFATVSKSG-SNAHVEdkvlASNPITEAVGNAKTTRNDNSSRFGKYTEISFdEQNQIIGANMS- 238
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKvTTKHSS----AIESVFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLNLKy 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 239 TYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNT--VIEGVNDRAEMVETQKTftlLGFK 316
Cdd:cd14874 146 TVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTenIQSDVNHFKHLEDALHV---LGFS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 317 EDFQMDVFKILAAILHLGNVQITAVGNerSSVSED------DSHLKVFCELLGLEsgrVAQWLcnrKIVTSSETVVKPMT 390
Cdd:cd14874 223 DDHCISIYKIISTILHIGNIYFRTKRN--PNVEQDvveignMSEVKWVAFLLEVD---FDQLV---NFLLPKSEDGTTID 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 391 RPQAVNARDALAKKIYAHLFDFIVERINQALQFSgKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKL 470
Cdd:cd14874 295 LNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCP-LHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 471 EQEEYMKEDIPwtlIDF-----YDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSNT 544
Cdd:cd14874 374 QLVDYAKDGIS---VDYkvpnsIENGKTVELLFKKpYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARNKERL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 545 SFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENptppSPFGSMITVKSAKQVIKpnskhfrttv 624
Cdd:cd14874 451 EFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESY----SSNTSDMIVSQAQFILR---------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 625 GSKfrsslyLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMT 704
Cdd:cd14874 517 GAQ------EIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLP 590
|
650 660 670
....*....|....*....|....*....|....*...
gi 767984698 705 KQELSFSDKKEVCKVVLH-RLIQDSNQYQFGKTKIFFR 741
Cdd:cd14874 591 GDIAMCQNEKEIIQDILQgQGVKYENDFKIGTEYVFLR 628
|
|
| Myo5-like_CBD |
cd14945 |
Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied ... |
1341-1667 |
8.06e-70 |
|
Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5 a,b,c) in vertebrates and two (myo2 and myo4) in fungi and related to plant class XI myosins. Their C-terminal cargo binding domains is important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. MyoV-CBDs interact with several adaptor proteins that in turn interact with the cargo.
Pssm-ID: 271253 [Multi-domain] Cd Length: 288 Bit Score: 236.53 E-value: 8.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1341 EDEAKLIQNLILDLKPRGVVVnmiPGLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSNT 1420
Cdd:cd14945 1 SEEDSLLRGIVTDFEPSSGDH---KLTPAYILYLCIRHAASNGLTGQSTSLLNKVLKTIQQVVQQHNDDMQLLAFWLSNA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1421 CHFLNCLKQYSGEEEFMKHNSPQQNKNCLNNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPiivpgmleyeslqgisgl 1500
Cdd:cd14945 78 SELLYFLKQDSKLYGAAGEAPQKEEEQKLTVSDLNELKQDLEAVSIKIYQQALKYLNKNLQP------------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1501 kptgfrkrsssiddtdgyTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRC 1580
Cdd:cd14945 140 ------------------KIRDIVKFLNSFLDLLKSFHVHPEIRSQVFTQLFSFINARLFNQLITKKDALSWSRGMQIRA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1581 NISYLEEWLKDKNLqNSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPIDDFEKRVTPSFV 1660
Cdd:cd14945 202 NISRLEEWCEGRGL-EHLAVDFLSKLIQAVQLLQLKKYTQEDIEILCELCPSLNPAQLQAILTQYQPANYGESPVPKEIL 280
|
....*..
gi 767984698 1661 RKVQALL 1667
Cdd:cd14945 281 RTLAAEV 287
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
84-699 |
2.29e-61 |
|
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: 225.62 E-value: 2.29e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 84 LHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQN----------MGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14893 4 LYTLRARYRMEQ-VYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSReqtplyekdtVNDAPPHVFALAQNALRCMQDAGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 154 NQSIIVSGESGAGKTVSARYAMRYFATV-----------SKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYT 222
Cdd:cd14893 83 DQAVILLGGMGAGKSEAAKLIVQYLCEIgdeteprpdseGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 223 EISFDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQ--SEFKHLKLG-SAEEFNYTRMGGNTVIEGVND 299
Cdd:cd14893 163 SVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdpTLRDSLEMNkCVNEFVMLKQADPLATNFALD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 300 RAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQI---------------TAVGNERSSVSEDDSHLKVFCELLGL 364
Cdd:cd14893 243 ARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvggansTTVSDAQSCALKDPAQILLAAKLLEV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 365 ESGRVAQWLCNRKIVT--SSETV--VKPMTRPQAVNARDALAKKIYAHLFDFIVERINQAL-----QFSGK----QHTFI 431
Cdd:cd14893 323 EPVVLDNYFRTRQFFSkdGNKTVssLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdRYEKSniviNSQGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 432 GVLDIYGFETFD--VNSFEQFCINYANEK-----LQQQFNMHVFKLEQEEYMKED--IPWTLIDF-YDNQPVIDLIEAK- 500
Cdd:cd14893 403 HVLDMVGFENLTpsQNSFDQLCFNYWSEKvhhfyVQNTLAINFSFLEDESQQVENrlTVNSNVDItSEQEKCLQLFEDKp 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 501 MGILELLDEECLLPHGTDENWLQKLYN-------------NFVNRNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNR 567
Cdd:cd14893 483 FGIFDLLTENCKVRLPNDEDFVNKLFSgneavgglsrpnmGADTTNEYLAPSKDWRLLFIVQHHCGKVTYNGKGLSSKNM 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 568 DTVYDMLVEILRASKFHLCanffqeNPTPPSPFGSMITVKSAKQVIKPNSKH--FRTTVGSKFRSS---------LY--- 633
Cdd:cd14893 563 LSISSTCAAIMQSSKNAVL------HAVGAAQMAAASSEKAAKQTEERGSTSskFRKSASSARESKnitdsaatdVYnqa 636
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767984698 634 -LLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRY 699
Cdd:cd14893 637 dALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY 703
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
104-227 |
3.96e-44 |
|
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: 158.28 E-value: 3.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 104 ILVAMNPYKQLPIYGDA-IIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTVSARYAMRYFATVS 182
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 767984698 183 KSGSNA--------------HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFD 227
Cdd:cd01363 81 FNGINKgetegwvylteitvTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLD 139
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
81-739 |
5.03e-42 |
|
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: 166.55 E-value: 5.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQN-MGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14938 1 PSVLYHLKERF-KNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDcIEDLSLNEYHVVHNALKNLNELKRNQSIII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 160 SGESGAGKTVSARYAMRYFATVSK------SGSNAHVEDKVLAS----------------NPITEAVGNAKTTRNDNSSR 217
Cdd:cd14938 80 SGESGSGKSEIAKNIINFIAYQVKgsrrlpTNLNDQEEDNIHNEentdyqfnmsemlkhvNVVMEAFGNAKTVKNNNSSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 218 FGKYTEISFDEQnQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGv 297
Cdd:cd14938 160 FSKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFS- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 298 NDRAEMVETQKTFTLLgFKEDFQMD-VFKILAAILHLGNVQITAV---------------------------GNERSSVS 349
Cdd:cd14938 238 DYSGKILELLKSLNYI-FDDDKEIDfIFSVLSALLLLGNTEIVKAfrkksllmgknqcgqninyetilseleNSEDIGLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 350 EDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSeTVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQ---ALQFSGK 426
Cdd:cd14938 317 ENVKNLLLACKLLSFDIETFVKYFTTNYIFNDS-ILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEkctQLQNINI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 427 QHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTL-IDFYDNQPVID-LIEAKMGIL 504
Cdd:cd14938 396 NTNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNlLVGPTEGSL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 505 ELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPR---MSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAS 581
Cdd:cd14938 476 FSLLENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDditGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 582 K----FHLCANFFQENPTPPSPFGSMITVKSAKQVIKPNSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEK- 656
Cdd:cd14938 556 EneymRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESKr 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 657 LPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSrygILMTKQElsfsDKKEVCKVVLHRLIQDSNQYQFGKT 736
Cdd:cd14938 636 ELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLS---IFDIKNE----DLKEKVEALIKSYQISNYEWMIGNN 708
|
...
gi 767984698 737 KIF 739
Cdd:cd14938 709 MIF 711
|
|
| DIL |
pfam01843 |
DIL domain; The DIL domain has no known function. |
1546-1647 |
3.99e-34 |
|
DIL domain; The DIL domain has no known function.
Pssm-ID: 460359 [Multi-domain] Cd Length: 103 Bit Score: 126.94 E-value: 3.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1546 QAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRCNISYLEEWLKDKNLQnSLAKETLEPLSQAAWLLQVKKTTDSDAKE 1625
Cdd:pfam01843 1 QLFSQLFYFINAELFNRLLLRKKYCSWSKGMQIRYNLSRLEEWARSNGLE-SEARDHLAPLIQAAQLLQLRKSTLEDLDS 79
|
90 100
....*....|....*....|..
gi 767984698 1626 IYERCTSLSAVQIIKILNSYTP 1647
Cdd:pfam01843 80 ILQVCPALNPLQLHRLLTLYQP 101
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
187-703 |
5.39e-33 |
|
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: 139.11 E-value: 5.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 187 NAHVEDK---VLASNPITEAVGNAKTTRNDNSSRFGKYT--EISFDE---QNQIIGANMSTYLLEKSRVVFQ------SE 252
Cdd:cd14894 239 NPHAAKKlsiVLDSNIVLEAFGHATTSMNLNSSRFGKMTtlQVAFGLhpwEFQICGCHISPFLLEKSRVTSErgresgDQ 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 253 NERNYHIFYQLCASAQQSEF-----KHLKLGSAEEFNYTRMG-GNTVIEGV--------NDRAEMVETQKTFTLLGFKED 318
Cdd:cd14894 319 NELNFHILYAMVAGVNAFPFmrllaKELHLDGIDCSALTYLGrSDHKLAGFvskedtwkKDVERWQQVIDGLDELNVSPD 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 319 FQMDVFKILAAILHLGNVQIT--AVGNE--RSSVSEDDSHLKVfCELLGLESGRVAQWLCNRKIVT---SSETVVKPMTR 391
Cdd:cd14894 399 EQKTIFKVLSAVLWLGNIELDyrEVSGKlvMSSTGALNAPQKV-VELLELGSVEKLERMLMTKSVSlqsTSETFEVTLEK 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 392 PQAVNARDALAKKIYAHLFDFIVERINQALQFS-----GKQH------------TFIGVLDIYGFETFDVNSFEQFCINY 454
Cdd:cd14894 478 GQVNHVRDTLARLLYQLAFNYVVFVMNEATKMSalstdGNKHqmdsnasapeavSLLKIVDVFGFEDLTHNSLDQLCINY 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 455 ANEKLQQqfnmhvfKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQ-----KLY-NN 528
Cdd:cd14894 558 LSEKLYA-------REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENMNAQQeekrnKLFvRN 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 529 FVNRNP--LFEKPR-MSNTS-----------FVIQHFADKVEYKCEGFLEKNRDTVY-DMLVEILRASKFHLCANFFQEN 593
Cdd:cd14894 631 IYDRNSsrLPEPPRvLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYaNLLVGLKTSNSSHFCRMLNESS 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 594 PTPPSPFGSMITVKSAKQVIKpNSKHFrttVGsKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRAC 673
Cdd:cd14894 711 QLGWSPNTNRSMLGSAESRLS-GTKSF---VG-QFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQ 785
|
570 580 590
....*....|....*....|....*....|....
gi 767984698 674 GV---LETIRISAQSYPS-RWTYIEFYSRYGILM 703
Cdd:cd14894 786 RLirqMEICRNSSSSYSAiDISKSTLLTRYGSLL 819
|
|
| Myo5p-like_CBD_DIL_ANK |
cd15473 |
cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ... |
1341-1701 |
3.19e-24 |
|
cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ankyrin domain-containing protein are a group of fungal proteins that contain a domain homologous to the cargo binding domain of class V myosins and ankyrin repeats. Their function is unknown.
Pssm-ID: 271257 [Multi-domain] Cd Length: 316 Bit Score: 105.33 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1341 EDEAKLIQNLILDLKPRGVVVNMIPgLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSNT 1420
Cdd:cd15473 7 EDELPRILDLLITNMTPQRSPSQRP-VPANLLFLCARYAHYHCSPELLEDLLLGALDRIEDVVEANPWDMTLLAFWLSNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1421 C---HFLNCLKQYsgeeefmkhnspqqnknclnNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPIIVPGMLEYESLqgi 1497
Cdd:cd15473 86 TlllHYLKKDAGL--------------------VEATPEFQQELAELINEIFVLIIRDAERRIDKLLDASPRNITSL--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1498 sglkptgfrkrsssiddtdgytMTSVLQQLSYFYttmcqngLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQ 1577
Cdd:cd15473 143 ----------------------LSSTLYVLELYD-------VHPAIIIQALSQLFYWLGCELFNRILTNKKYLCRSKAMQ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1578 IRCNISYLEEWLKDKNLQ-------NSLAKETLEPLSQAAWLLQVKKT-TDSDA-KEIYERCTSLSAVQIIKILNSYTPi 1648
Cdd:cd15473 194 IRMNLSALEDWARSNNLQpekgespPRIARSHLAPVIQLLQWLQCLSSlDDFESlIATIQQLDALNPLQLLRAVKDYRY- 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 767984698 1649 DDFEKRVTPSFVRKVQALLNSRedssqlmLDTKYLFQVTFPFTPsphalEMIQ 1701
Cdd:cd15473 273 EVNEGRMPEECVKYLAQLQKDW-------LDSRYMLPFSLPTDT-----EMLV 313
|
|
| fMyo2p_CBD |
cd15480 |
cargo binding domain of fungal myosin 2; Yeast myosin V travels along actin cables, actin ... |
1368-1678 |
2.28e-23 |
|
cargo binding domain of fungal myosin 2; Yeast myosin V travels along actin cables, actin filaments that are bundled by fimbrin, in the presence of tropomyosin. This is in contrast to the other vertebrate class V myosins. Like other class V myosins, fungal myosin 2 and 4 contain a C-terminal cargo binding domain. Myo 2 binds to Vac17, vacuole-specific cargo adaptor, and Mmr1, mitochondria-specific cargo adaptor. Both adaptors bind competitivly at the same site.
Pssm-ID: 271264 Cd Length: 363 Bit Score: 103.81 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1368 PAHILFMCvryadsLNDanMLK--------SLMNSTINGIKQVVKEhLEDFEMLS---FWLSNTcHFLNCLKQYSgEEEF 1436
Cdd:cd15480 48 PAHLIILI------LSE--MWRlgltkeseRFLANVMQTIQQHVMS-LKGEDAIVpgaFWLSNV-HELLSFVCLA-ESDI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1437 MKHNSPqqnKNCLNNFDLSEYRQILSDV-------AIRIYHQFIIIMEKNIQPiivpgmleyeslqgisglkptgfrkrs 1509
Cdd:cd15480 117 LQGIGP---GKDMREEEWEEYERLVTVVkhdleslEYNIYHTWMKELKKRLEK--------------------------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1510 ssiddtdgyTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRCNISYLEEWL 1589
Cdd:cd15480 167 ---------TMDDILNFFNKVYKSMKSYYIEESVIRQVVTELLKLIGVTAFNDLLMRRNFLSWKRGLQINYNITRLEEWC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1590 K-----DKNLQnslaketLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTpIDDFEKRVTPSFVRKVQ 1664
Cdd:cd15480 238 KshdipEGTLQ-------LEHLMQATKLLQLKKATLEDIEIIYDVCWILTPAQIQKLISQYY-VADYENPISPEILKAVA 309
|
330
....*....|....
gi 767984698 1665 ALLNSREDSSQLML 1678
Cdd:cd15480 310 ARVKPEDKSDHLLL 323
|
|
| Myo5p-like_CBD_fungal |
cd15474 |
cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin ... |
1368-1666 |
3.89e-22 |
|
cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin cables, actin filaments that are bundled by fimbrin, in the presence of tropomyosin. This is in contrast to the other vertebrate class V myosins. Like other class V myosins, fungal myosin 2 and 4 contain a C-terminal cargo binding domain. In case of Myo4 it has been shown to bind to the adapter protein She3p (Swi5p-dependent HO expression 3), which in turn anchors myosin 4 to its cargos, zip-coded mRNP (messenger ribonucleoprotein particles) and tER (tubular endoplasmic reticulum). Myo 2 binds to Vac17, vacuole-specific cargo adaptor, and Mmr1, mitochondria-specific cargo adaptor. Both adaptors bind competitivly at the same site.
Pssm-ID: 271258 Cd Length: 352 Bit Score: 100.19 E-value: 3.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1368 PAHILFMC---VRYADSLNDANMLKSLmNSTINGIKQVVKEHLEDFEMLS--FWLSNTcH----FLNCLKQ---YSGEEE 1435
Cdd:cd15474 34 LGHVNFLIysqMWKSLLELLTQSERFL-SHVLSYIASIVDSLPKKETIPDgaFWLANL-HelrsFVVYLLSlieHSSSDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1436 FMKHNSPQQNKNclnnfdLSEYRQILSdvaiRIYHQFIIIMEKNIQPIIVPGMLEYESLQGISGlkptgFRKRSSSIDDT 1515
Cdd:cd15474 112 FSKESEEYWNTL------FDKTLKHLS----NIYSTWIDKLNKHLSPKIEGAVLVLLTSLDLSE-----LIDLNKEFFNK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1516 DGYTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRCNISYLEEWLKDKNLq 1595
Cdd:cd15474 177 PKKKMADLITFLNEVYDLLQSFSVQPELLNAIVSSTLQYINVEAFNSLITKRSALSWKRGSQISYNVSRLKEWCHQHGL- 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767984698 1596 nSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPiDDFEKRVTPSFVRKVQAL 1666
Cdd:cd15474 256 -SDANLQLEPLIQASKLLQLRKDDENDFKIILSVCYALNPAQIQKLLDKYQP-ANYEAPVPKEFLNALEKL 324
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
785-1355 |
2.43e-19 |
|
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: 95.19 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 785 IIQQYFRGQQTVSLYQLIRMATITMQAYSRGFLARRRYRKMLEE-HKAVILqkyARAWLARRRFQSIRRFVLNIQLTYRV 863
Cdd:pfam15921 303 IIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEElEKQLVL---ANSELTEARTERDQFSQESGNLDDQL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 864 QRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKaathrRNYEekgkryrdaVEEKLAKLQKHNSELETQ 943
Cdd:pfam15921 380 QKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDD-----RNME---------VQRLEALLKAMKSECQGQ 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 944 KEQIQLKLQEKTEELkEKMDNLTKQLFDD-------VQKEERQRMLLEKS------FELKTQDYEKQIQSLKEEIKALK- 1009
Cdd:pfam15921 446 MERQMAAIQGKNESL-EKVSSLTAQLESTkemlrkvVEELTAKKMTLESSertvsdLTASLQEKERAIEATNAEITKLRs 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1010 --DEKMQ-LQHL-VEGEHVTSDGLKAEVARLSkqvktISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEitKQLLES 1085
Cdd:pfam15921 525 rvDLKLQeLQHLkNEGDHLRNVQTECEALKLQ-----MAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVE--KAQLEK 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1086 yDIEDvrSRLSVEDLEHLNEdgelwfayeglKKATRVLESHFQSQkdcyekEIEALNFKVVHLSQEINHLQKLFREEND- 1164
Cdd:pfam15921 598 -EIND--RRLELQEFKILKD-----------KKDAKIRELEARVS------DLELEKVKLVNAGSERLRAVKDIKQERDq 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1165 -INE--SIRHEVTRLTSE-NMMIPDFKQQISELEKQKQDLEIRLneqaEKMKGKLEELSNQLHRSQEEEGTQRK-ALEAQ 1239
Cdd:pfam15921 658 lLNEvkTSRNELNSLSEDyEVLKRNFRNKSEEMETTTNKLKMQL----KSAQSELEQTRNTLKSMEGSDGHAMKvAMGMQ 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1240 NEIHTK--EKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTI 1317
Cdd:pfam15921 734 KQITAKrgQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
|
570 580 590
....*....|....*....|....*....|....*...
gi 767984698 1318 GKAndvhsSSGPKEYLGMLQYKREDEAKLIQNLILDLK 1355
Cdd:pfam15921 814 DKA-----SLQFAECQDIIQRQEQESVRLKLQHTLDVK 846
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
858-1328 |
2.94e-19 |
|
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: 95.12 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 858 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAV---EEKLAKLQ 934
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVaqlELQIASLN 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 935 KHNSELETQKEQIQ----------------------LKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSfELKTQ 992
Cdd:TIGR02168 400 NEIERLEARLERLEdrrerlqqeieellkkleeaelKELQAELEELEEELEELQEELERLEEALEELREELEEA-EQALD 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 993 DYEKQIQSLKEEIKALKDekMQLQHLVEGEHVT-----SDGLKAEVARLSKQVKTISEFEKEIEL-------------LQ 1054
Cdd:TIGR02168 479 AAERELAQLQARLDSLER--LQENLEGFSEGVKallknQSGLSGILGVLSELISVDEGYEAAIEAalggrlqavvvenLN 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1055 AQKIDVE--------------------KHVQSQKREMREKMSEITKQL--LESYDIE---DVRSRLS----VEDLEHLNE 1105
Cdd:TIGR02168 557 AAKKAIAflkqnelgrvtflpldsikgTEIQGNDREILKNIEGFLGVAkdLVKFDPKlrkALSYLLGgvlvVDDLDNALE 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1106 --------------DGEL----WFAYEGLKKATRVLESHFQSQKDCyEKEIEALNFKVVHLSQEINHLQKLFREendINE 1167
Cdd:TIGR02168 637 lakklrpgyrivtlDGDLvrpgGVITGGSAKTNSSILERRREIEEL-EEKIEELEEKIAELEKALAELRKELEE---LEE 712
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1168 SIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLnEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAqneihtkEK 1247
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI-AQLSKELTELEAEIEELEERLEEAEEELAEAEA-------EI 784
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1248 EKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVHSSS 1327
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
.
gi 767984698 1328 G 1328
Cdd:TIGR02168 865 E 865
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
862-1316 |
8.51e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 90.12 E-value: 8.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 862 RVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLE---AELEKAATHRRNYEEKGKRYRDaVEEKLAKLQKHNS 938
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvKELKELKEKAEEYIKLSEFYEE-YLDELREIEKRLS 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 939 ELETQKEQIQLKLQE------KTEELKEKMDNLTKQ---LFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALK 1009
Cdd:PRK03918 318 RLEEEINGIEERIKEleekeeRLEELKKKLKELEKRleeLEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1010 DEKMQLQHLVEGEHVTSDGLKAEVARLSKQV-----------------------KTISEFEKEIELLQAQKIDVEKHVQS 1066
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERK 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1067 QKREMREKMSEITKQ-----LLESYD-IEDVRSRLSVEDLEHLNEDGELwfaYEGLKKATRVLESHFQSQKD------CY 1134
Cdd:PRK03918 478 LRKELRELEKVLKKEselikLKELAEqLKELEEKLKKYNLEELEKKAEE---YEKLKEKLIKLKGEIKSLKKelekleEL 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1135 EKEIEALNFKVVHLSQEINHLQKLFREENdiNESIRHEVTRLTSenmMIPDFKQQIsELEKQKQDLEIRLNEQaEKMKGK 1214
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKELEELG--FESVEELEERLKE---LEPFYNEYL-ELKDAEKELEREEKEL-KKLEEE 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1215 LEELSNQLHRSQEEEGTQRKALEAQNEIHTKEK-EKLIDKIQEMQEASDHLKKQFETESEVkcnfRQEASRlTLEnrDLE 1293
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKR----REEIKK-TLE--KLK 700
|
490 500
....*....|....*....|...
gi 767984698 1294 EELDMKDRVIKKLQDQVKTLSKT 1316
Cdd:PRK03918 701 EELEEREKAKKELEKLEKALERV 723
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
858-1321 |
3.53e-17 |
|
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: 87.77 E-value: 3.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 858 QLTYRVQRLQKKLEdqNKENhglveKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHN 937
Cdd:TIGR04523 37 QLEKKLKTIKNELK--NKEK-----ELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 938 SELETQKEQIqLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFElKTQDYEKQIQSLKEEIKALKDEKMQLQH 1017
Cdd:TIGR04523 110 SEIKNDKEQK-NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNN-KYNDLKKQKEELENELNLLEKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1018 LVegehvtsDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSV 1097
Cdd:TIGR04523 188 NI-------DKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1098 EDLEHLNEDGELWFAYEGLKKATRVLESHFQSqkdcYEKEIEALNfkvvhlSQEINHLQKLFREE-NDINESIRHEVTRL 1176
Cdd:TIGR04523 261 EQNKIKKQLSEKQKELEQNNKKIKELEKQLNQ----LKSEISDLN------NQKEQDWNKELKSElKNQEKKLEEIQNQI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1177 TSENMMIPDFKQQISELEKQKQDLE---IRLNEQAEKMKGKLEELSNQLHRSQEEE---GTQRKALEAQNEIHTKEKEKL 1250
Cdd:TIGR04523 331 SQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEKQNEIEKLKKENQSYKQEIknlESQINDLESKIQNQEKLNQQK 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767984698 1251 IDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKAN 1321
Cdd:TIGR04523 411 DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
862-1321 |
9.29e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 86.66 E-value: 9.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 862 RVQRLQKKLEDQNKENHGLVEKLTSLAALRagdvEKIQKLEAELEKAATHRRNYEEKGKRyrdaVEEKLAKLQKHNSELE 941
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKELEELK----EEIEELEKELESLEGSKRKLEEKIRE----LEERIEELKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 942 TQKEQIQlKLQEKTEE---LKEKMDNLTKQLFDdVQKE----ERQRMLLEKSFElKTQDYEKQIQSLKEEIKALKDEKMQ 1014
Cdd:PRK03918 280 EKVKELK-ELKEKAEEyikLSEFYEEYLDELRE-IEKRlsrlEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1015 LQHLVEgEHVTSDGLKAEVARLSKQVK--TISEFEKEIELLQAQKIDVEKHVqsqkREMREKMSEITkqllesydiedvr 1092
Cdd:PRK03918 357 LEERHE-LYEEAKAKKEELERLKKRLTglTPEKLEKELEELEKAKEEIEEEI----SKITARIGELK------------- 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1093 srlsvedlehlNEDGELWFAYEGLKKATRVL--------ESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREEnd 1164
Cdd:PRK03918 419 -----------KEIKELKKAIEELKKAKGKCpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL-- 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1165 inESIRHEVTRLTSENMMIPDFKQQISELEK-QKQDLEiRLNEQAEKMKGKLEELSNQLhRSQEEEGTQRKALEaqneih 1243
Cdd:PRK03918 486 --EKVLKKESELIKLKELAEQLKELEEKLKKyNLEELE-KKAEEYEKLKEKLIKLKGEI-KSLKKELEKLEELK------ 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1244 tKEKEKLIDKIQEMQEASDHLKKQ-----FETESEVKCNFR--QEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKT 1316
Cdd:PRK03918 556 -KKLAELEKKLDELEEELAELLKEleelgFESVEELEERLKelEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEE 634
|
....*
gi 767984698 1317 IGKAN 1321
Cdd:PRK03918 635 LAETE 639
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
858-1322 |
1.04e-16 |
|
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: 86.65 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 858 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHN 937
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 938 SELETQKEQIQLkLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEkSFELKTQDYEKQIQSLKEEIKALKDEKMQLQH 1017
Cdd:TIGR02168 337 EELAELEEKLEE-LKEELESLEAELEELEAELEELESRLEELEEQLE-TLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1018 LVEGEH--VTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKqllESYDIEDVRSRL 1095
Cdd:TIGR02168 415 RRERLQqeIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA---AERELAQLQARL 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1096 -SVEDLEHLNED-----GELWFAYEGLKKATRVLESHFQSQKDcYEKEIEA-----LNFKVVHLSQE----INHLQK--- 1157
Cdd:TIGR02168 492 dSLERLQENLEGfsegvKALLKNQSGLSGILGVLSELISVDEG-YEAAIEAalggrLQAVVVENLNAakkaIAFLKQnel 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1158 ---LFREENDINESIRHEVTRLTSENmmIPDFKQQISELEKQKQDLEIRLN------------EQAEKMKGKLEEL---- 1218
Cdd:TIGR02168 571 grvTFLPLDSIKGTEIQGNDREILKN--IEGFLGVAKDLVKFDPKLRKALSyllggvlvvddlDNALELAKKLRPGyriv 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1219 ---------------------SNQLHRSQE--EEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVK 1275
Cdd:TIGR02168 649 tldgdlvrpggvitggsaktnSSILERRREieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI 728
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 767984698 1276 CNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKAND 1322
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
862-1315 |
9.29e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.65 E-value: 9.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 862 RVQRLQKKLEDQNKenhglVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELE 941
Cdd:PTZ00121 1303 KADEAKKKAEEAKK-----ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 942 TQKEQIQLKLQE--KTEELKEKMDNLTKQLfDDVQKEERQRmllEKSFELKTQDYEK----QIQSLKEEIKALKDEKMQL 1015
Cdd:PTZ00121 1378 KKADAAKKKAEEkkKADEAKKKAEEDKKKA-DELKKAAAAK---KKADEAKKKAEEKkkadEAKKKAEEAKKADEAKKKA 1453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1016 QHLVEGEHVTSdglKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHV-QSQKREMREKMSEITKQLLESYDIEDVRSR 1094
Cdd:PTZ00121 1454 EEAKKAEEAKK---KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAdEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1095 LSVEDLEHLNEDGELWFAYEgLKKATRVLESHFQSQKDCYEKEIEALNF---KVVHLSQ----EINHLQKLFREENDIN- 1166
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADE-LKKAEELKKAEEKKKAEEAKKAEEDKNMalrKAEEAKKaeeaRIEEVMKLYEEEKKMKa 1609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1167 -ESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEgtQRKALEAQNEIHTK 1245
Cdd:PTZ00121 1610 eEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED--KKKAEEAKKAEEDE 1687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1246 EK--EKLIDKIQEMQEASDHLKK---------QFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLS 1314
Cdd:PTZ00121 1688 KKaaEALKKEAEEAKKAEELKKKeaeekkkaeELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
.
gi 767984698 1315 K 1315
Cdd:PTZ00121 1768 K 1768
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
826-1257 |
5.18e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.88 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 826 LEEHKAVILQKYARAWLARRRFQSIRrfvlniQLTYRVQRLQKKLEDQNKENhgLVEKLTSLAalragdvEKIQKLEAEL 905
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEEAK------AKKEELERLKKRLTGLTPEK--LEKELEELE-------KAKEEIEEEI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 906 EKAATHRRNYEEKGKRYRDAVEE-KLAKLQ--KHNSEL-ETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRM 981
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEElKKAKGKcpVCGRELtEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 982 LLEKSFEL-KTQDYEKQIQSLKEEIKALKDEKM-QLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLqaqkid 1059
Cdd:PRK03918 488 VLKKESELiKLKELAEQLKELEEKLKKYNLEELeKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL------ 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1060 vekhvQSQKREMREKMSEITKQLLES--YDIEDVRSRLsvEDLEhlnedgELWFAYEGLKKATRVLESHFQSQKDCYE-- 1135
Cdd:PRK03918 562 -----EKKLDELEEELAELLKELEELgfESVEELEERL--KELE------PFYNEYLELKDAEKELEREEKELKKLEEel 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1136 ----KEIEALNFKVVHLSQEINHLQKLFREENdiNESIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEirlnEQAEKM 1211
Cdd:PRK03918 629 dkafEELAETEKRLEELRKELEELEKKYSEEE--YEELREEYLELSRE---LAGLRAELEELEKRREEIK----KTLEKL 699
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 767984698 1212 KGKLEELSnqlhRSQEEEGTQRKALEAQNEIHTK-------EKEKLIDKIQEM 1257
Cdd:PRK03918 700 KEELEERE----KAKKELEKLEKALERVEELREKvkkykalLKERALSKVGEI 748
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
896-1259 |
1.46e-14 |
|
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: 79.73 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 896 EKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKEKMDNLtkqlfdDVQK 975
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE-KLKERLEELEEDLSSL------EQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 976 EERQRMLleKSFELKTQDYEKQIQSLKEEIKALKDekMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQA 1055
Cdd:TIGR02169 754 ENVKSEL--KELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1056 QKIDVEKHVQSQKREMREKMSEITKQLLESY-DIEDVRSRLSvedlEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCY 1134
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNgKKEELEEELE----ELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1135 EKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTrLTSENMMIPDFKQQISELEKqkqdlEIRlneqaekmkgK 1214
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE-IPEEELSLEDVQAELQRVEE-----EIR----------A 969
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 767984698 1215 LEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQE 1259
Cdd:TIGR02169 970 LEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
867-1297 |
1.48e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.31 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 867 QKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYR------DAVEEKLAKLQKHNSEL 940
Cdd:PRK02224 191 QLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEerreelETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 941 ETQKEQIQLKLQEKTEELKEKMDNLTKQL----FDDV--------------QKEERQRMLLEKSfeLKTQDYEKQIQSLK 1002
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDLLaeagLDDAdaeavearreeledRDEELRDRLEECR--VAAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1003 EEIKALKDEKMQLQHlvEGEHVTSDGLKAEVArLSKQVKTISEFEKEIELLQAQKIDVE---KHVQSQKREMREKMSEIT 1079
Cdd:PRK02224 349 EDADDLEERAEELRE--EAAELESELEEAREA-VEDRREEIEELEEEIEELRERFGDAPvdlGNAEDFLEELREERDELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1080 KQLLE-SYDIEDVRSRlsVEDLEHLNEDG---ELWFAYEGLKKATRVLEShfQSQKDCYEKEIEALNFKVVHLSQEINHL 1155
Cdd:PRK02224 426 EREAElEATLRTARER--VEEAEALLEAGkcpECGQPVEGSPHVETIEED--RERVEELEAELEDLEEEVEEVEERLERA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1156 QKLFREENDIN--ESIRHEVTRLTSENMMIPDFKQ-QISELEKQKQDLEirlNEQAEKmkgklEELSNQLHRSQEEEGTQ 1232
Cdd:PRK02224 502 EDLVEAEDRIErlEERREDLEELIAERRETIEEKReRAEELRERAAELE---AEAEEK-----REAAAEAEEEAEEAREE 573
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767984698 1233 RKALEAQNEIHTKEKEKLiDKIQEMQEASDHLKKQFETESEVKCNF--RQEASRLTLEN-----RDLEEELD 1297
Cdd:PRK02224 574 VAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALaeLNDERRERLAEkrerkRELEAEFD 644
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
862-1309 |
3.75e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.64 E-value: 3.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 862 RVQRLQKKLEDQNKenhglVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKR---YRDAVEEKLAKLQKHNS 938
Cdd:PTZ00121 1379 KADAAKKKAEEKKK-----ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAdeaKKKAEEAKKADEAKKKA 1453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 939 ELETQKEQIQLKLQE--KTEELKEKMDNLTKQlfDDVQKEERQRMllEKSFELKTQDYEKQiqslKEEIKALKDEKMQLQ 1016
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEakKADEAKKKAEEAKKA--DEAKKKAEEAK--KKADEAKKAAEAKK----KADEAKKAEEAKKAD 1525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1017 HLVEGEhvtsDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDV--EKHVQSQKREMREKMSEITKQLlESYDIEDVRSR 1094
Cdd:PTZ00121 1526 EAKKAE----EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKaeEAKKAEEDKNMALRKAEEAKKA-EEARIEEVMKL 1600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1095 LSVEDL---EHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDinesirh 1171
Cdd:PTZ00121 1601 YEEEKKmkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED------- 1673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1172 evtrltsenmmipdfKQQISELEKQKQDLeiRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLI 1251
Cdd:PTZ00121 1674 ---------------KKKAEEAKKAEEDE--KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767984698 1252 DKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRD----LEEELDMKDRVIKKLQDQ 1309
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEkeavIEEELDEEDEKRRMEVDK 1798
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
751-1350 |
1.42e-13 |
|
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: 76.31 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 751 LRLDKLRQSCVMVQKHMRGWLQRKKFLRERRAALIIQQYFRGQQtvsLYQLIRMATITMQAYSRGFlarrryRKMLEEHK 830
Cdd:pfam15921 160 LKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKK---IYEHDSMSTMHFRSLGSAI------SKILRELD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 831 AVILQKYARAWLARRRFQSIRRFVLN---IQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAAlragdveKIQKLEAELEK 907
Cdd:pfam15921 231 TEISYLKGRIFPVEDQLEALKSESQNkieLLLQQHQDRIEQLISEHEVEITGLTEKASSARS-------QANSIQSQLEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 908 AATHRRNYEEKGKRyrdaveeKLAKLQKHNSELETQKEQIQLKLQEKTEELKEK------------------------MD 963
Cdd:pfam15921 304 IQEQARNQNSMYMR-------QLSDLESTVSQLRSELREAKRMYEDKIEELEKQlvlanseltearterdqfsqesgnLD 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 964 NLTKQLFDDVQKEERQrMLLEKS------------------FELKTQDYEKQIQSLKEEIKALKDE-KMQLQHLVEGEHV 1024
Cdd:pfam15921 377 DQLQKLLADLHKREKE-LSLEKEqnkrlwdrdtgnsitidhLRRELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQG 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1025 TSDGLKaEVARLSKQVKTISE-FEKEIELLQAQKI----------DVEKHVQSQKREMREKMSEITKqllesydiedVRS 1093
Cdd:pfam15921 456 KNESLE-KVSSLTAQLESTKEmLRKVVEELTAKKMtlessertvsDLTASLQEKERAIEATNAEITK----------LRS 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1094 R--LSVEDLEHLNEDGElwfayeglkkatrvlesHFQS-QKDCYEKEIE-ALNFKVVH-LSQEINHLQKLFREENDINES 1168
Cdd:pfam15921 525 RvdLKLQELQHLKNEGD-----------------HLRNvQTECEALKLQmAEKDKVIEiLRQQIENMTQLVGQHGRTAGA 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1169 IRHEVTRLTSE----NMMIPDFK-------QQISELEKQKQDLEIR----LNEQAEKMKGkLEELSNQLHRSQEEEGTQR 1233
Cdd:pfam15921 588 MQVEKAQLEKEindrRLELQEFKilkdkkdAKIRELEARVSDLELEkvklVNAGSERLRA-VKDIKQERDQLLNEVKTSR 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1234 KALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFET-ESEVkcnfrqEASRLTLENRD------------LEEELDMKD 1300
Cdd:pfam15921 667 NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSaQSEL------EQTRNTLKSMEgsdghamkvamgMQKQITAKR 740
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 767984698 1301 RVIKKLQDQVKTLSKTIGKANDvhsssgPKEYLgmlqykREDEAKLIQNL 1350
Cdd:pfam15921 741 GQIDALQSKIQFLEEAMTNANK------EKHFL------KEEKNKLSQEL 778
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
866-1319 |
2.13e-13 |
|
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: 75.44 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 866 LQKKLEDQNKENHGLVEKLTSLAalragdvEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKE 945
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQ-------QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 946 QIQlKLQEKTEELK-EKMDNLTKQLFDDVQKEERQRMLLEKsfelKTQDYEKQIQSLKEEIKALKDEKMQLqhlvEGEHV 1024
Cdd:TIGR04523 289 QLN-QLKSEISDLNnQKEQDWNKELKSELKNQEKKLEEIQN----QISQNNKIISQLNEQISQLKKELTNS----ESENS 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1025 TSDG-LKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVE----- 1098
Cdd:TIGR04523 360 EKQReLEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETiiknn 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1099 ----DLEhlNEDGELWFAYEGLKKATRVLESHFQSQKDCY-----------------EKEIEALNFKVVHLSQEINHL-- 1155
Cdd:TIGR04523 440 seikDLT--NQDSVKELIIKNLDNTRESLETQLKVLSRSInkikqnleqkqkelkskEKELKKLNEEKKELEEKVKDLtk 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1156 ---------QKLFREEN-------DINESIRHEVTRLTSENM--MIPDFKQQISELeKQKQDLEIRLNEQAEKMKGKLEE 1217
Cdd:TIGR04523 518 kisslkekiEKLESEKKekeskisDLEDELNKDDFELKKENLekEIDEKNKEIEEL-KQTQKSLKKKQEEKQELIDQKEK 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1218 LSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELd 1297
Cdd:TIGR04523 597 EKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI- 675
|
490 500
....*....|....*....|..
gi 767984698 1298 mkDRVIKKLQDQVKTLSKTIGK 1319
Cdd:TIGR04523 676 --DDIIELMKDWLKELSLHYKK 695
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
894-1324 |
3.77e-13 |
|
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: 74.76 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 894 DVEKIQKLEAELEKAAThrrNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTE-------ELKEKMDNLT 966
Cdd:pfam05483 220 DHEKIQHLEEEYKKEIN---DKEKQVSLLLIQITEKENKMKDLTFLLEESRDKAN-QLEEKTKlqdenlkELIEKKDHLT 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 967 KQLfDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDE--KMQLQH-LVEGEHVTS-----DGLKAEVARLSK 1038
Cdd:pfam05483 296 KEL-EDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEElnKAKAAHsFVVTEFEATtcsleELLRTEQQRLEK 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1039 ---QVKTIS-EFEKEI-ELLQAQKIDVEKHVQSQkrEMREKMSEITKQLLESYDIEDVRSRLSvedlehlNEDGELWFAY 1113
Cdd:pfam05483 375 nedQLKIITmELQKKSsELEEMTKFKNNKEVELE--ELKKILAEDEKLLDEKKQFEKIAEELK-------GKEQELIFLL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1114 EGLKK----------ATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHL----QKLFREENDINESIRHEVTRLTSE 1179
Cdd:pfam05483 446 QAREKeihdleiqltAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLllenKELTQEASDMTLELKKHQEDIINC 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1180 NMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEeegtqrKALEAQNEIHTKEKEKLIdkiqeMQE 1259
Cdd:pfam05483 526 KKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEE------NARSIEYEVLKKEKQMKI-----LEN 594
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767984698 1260 ASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVH 1324
Cdd:pfam05483 595 KCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNY 659
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
858-1256 |
4.30e-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: 74.71 E-value: 4.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 858 QLTYRVQRLQKKLEDQNKEnhgLVEKLTSLAALRAgDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHN 937
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKA---LAELRKELEELEE-ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 938 SELETQKEQIQLKLQEKTEELKEKMDNLTKQlfddvqkeerqrmlleksfELKTQDYEKQIQSLKEEIKALKDEKMQLQh 1017
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEEL-------------------EAQIEQLKEELKALREALDELRAELTLLN- 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1018 lvEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEkHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSV 1097
Cdd:TIGR02168 817 --EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA-AEIEELEELIEELESELEALLNERASLEEALALLR 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1098 EDLEHLNEDgelwfayeglkkaTRVLESHFQSQKDCYE---KEIEALNFKVVHLSQEINHLQKLFREENDIN--ESIRHE 1172
Cdd:TIGR02168 894 SELEELSEE-------------LRELESKRSELRRELEelrEKLAQLELRLEGLEVRIDNLQERLSEEYSLTleEAEALE 960
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1173 VTRLTSENmmipDFKQQISELEKQKQDL-EIRLN--EQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEK 1249
Cdd:TIGR02168 961 NKIEDDEE----EARRRLKRLENKIKELgPVNLAaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKD 1036
|
....*..
gi 767984698 1250 LIDKIQE 1256
Cdd:TIGR02168 1037 TFDQVNE 1043
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
863-1313 |
1.73e-12 |
|
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: 72.90 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 863 VQRLQKKLEdQNKENHGLVEKltSLAALRAGDVEkiqkLEAELEKAATHRRNYEEKGKRyrdaVEEKLAKLQKHNSELET 942
Cdd:pfam01576 358 LEELTEQLE-QAKRNKANLEK--AKQALESENAE----LQAELRTLQQAKQDSEHKRKK----LEGQLQELQARLSESER 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 943 QKEQiqlkLQEKTEELKEKMDNLTKQLfddvQKEERQRMLLEK---SFELKTQDYEKQIQ-------SLKEEIKALKDEK 1012
Cdd:pfam01576 427 QRAE----LAEKLSKLQSELESVSSLL----NEAEGKNIKLSKdvsSLESQLQDTQELLQeetrqklNLSTRLRQLEDER 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1013 MQLQHLVEGEHVTSDGLKAEVARLSKQV----KTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITK-------- 1080
Cdd:pfam01576 499 NSLQEQLEEEEEAKRNVERQLSTLQAQLsdmkKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKlektknrl 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1081 -QLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKAtRVLESHFQSQKDCYEKEIEALNfkvvhLSQEINHLQKLF 1159
Cdd:pfam01576 579 qQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISA-RYAEERDRAEAEAREKETRALS-----LARALEEALEAK 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1160 REENDINESIRHEVTRLTSENmmiPDFKQQISELEKQKQDLEirlnEQAEKMKGKLEELSNQLHRSQE-----EEGTQrk 1234
Cdd:pfam01576 653 EELERTNKQLRAEMEDLVSSK---DDVGKNVHELERSKRALE----QQVEEMKTQLEELEDELQATEDaklrlEVNMQ-- 723
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1235 ALEAQNE--IHTKE------KEKLIDKIQEMQEASDHLKKQFETESEVKcnfrqeaSRLTLENRDLEEELDM----KDRV 1302
Cdd:pfam01576 724 ALKAQFErdLQARDeqgeekRRQLVKQVRELEAELEDERKQRAQAVAAK-------KKLELDLKELEAQIDAankgREEA 796
|
490
....*....|....
gi 767984698 1303 IK---KLQDQVKTL 1313
Cdd:pfam01576 797 VKqlkKLQAQMKDL 810
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
851-1260 |
1.87e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.11 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 851 RRFVLNIQltyRVQRLQKKLEDQNKENHGLVEKLTSLAALRagdvEKIQKLEAELEKAATHRRNYEEKGKRYRDAveEKL 930
Cdd:COG4717 64 RKPELNLK---ELKELEEELKEAEEKEEEYAELQEELEELE----EELEELEAELEELREELEKLEKLLQLLPLY--QEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 931 AKLQKHNSELETQKEQIQLKLQEkTEELKEKMDNLTKQLfddvQKEERQrmlLEKSFELKTQDYEKQIQSLKEEIKALKD 1010
Cdd:COG4717 135 EALEAELAELPERLEELEERLEE-LRELEEELEELEAEL----AELQEE---LEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1011 EKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEK-------------------------------------EIELL 1053
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaallallglggsllsliltiagvlflVLGLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1054 QAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHF-QSQKD 1132
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEeELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1133 CYEKEIEAL-NFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENmmiPDFKQQISELEKQkqdleiRLNEQAEKM 1211
Cdd:COG4717 367 ELEQEIAALlAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELL---GELEELLEALDEE------ELEEELEEL 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 767984698 1212 KGKLEELSNQLHRSQEEEGT---QRKALEAQNEIHTK--EKEKLIDKIQEMQEA 1260
Cdd:COG4717 438 EEELEELEEELEELREELAEleaELEQLEEDGELAELlqELEELKAELRELAEE 491
|
|
| Myo5p-like_CBD_afadin |
cd15471 |
cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and ... |
1368-1674 |
2.43e-12 |
|
cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and Rap1 small G protein-binding protein, found in cadherin-based adherens junctions in epithelial cells, endothelial cells, and fibroblasts. It interacts with cell adhesion molecules and signaling molecules and plays a role in the formation of cell junctions, cell polarization, migration, survival, proliferation, and differentiation. Afadin is a multi domain protein, that contains beside a myosin5-like CBD, two Ras-associated domains, a forkhead-associated domain, a PDZ domain, three proline-rich domains, and an F-actin-binding domain.
Pssm-ID: 271255 Cd Length: 322 Bit Score: 70.03 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1368 PAHILFMCVRYADSLND---------ANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSNTCHFLNCLKQysgeeefmk 1438
Cdd:cd15471 25 PAYTLYLAARYRLSTHYrpeltpterAHKLTAFLNKIASLIQQVIQEQRNIAGALAFWMANASELLNFLKQ--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1439 hnspqqnknclnNFDLSEYR----QILSDVAIRIYHQFIIIMEKNIQPIIVPGMLEYESLQGISGlkptgfrkrsssIDD 1514
Cdd:cd15471 96 ------------DRDLSAFSvqaqDVLAEAVQSAFSYLVRCLQEELERSLPAFLDSLVSLDDEPA------------IGD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1515 tdgytmtsVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKD--MCSCRKGMQIRCNISYLEEWLKDK 1592
Cdd:cd15471 152 --------VLHTLSSAMRLLRRCRVNAALTIQLFSQLFHFINAWLFNSLVSNPDsgLCTRYWGKRLRQRLAHVEAWAERQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1593 NLQnsLAKET-LEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPiDDFEKRVTPSFVRKVQALLNSRE 1671
Cdd:cd15471 224 GLE--LAADChLDRIVQAANLLTAPKYSAEDVANLSSTCFKLNSLQLRALLSHYQP-PPGEPPIPPDLIERVVRLAESQA 300
|
...
gi 767984698 1672 DSS 1674
Cdd:cd15471 301 DEL 303
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
886-1259 |
2.46e-12 |
|
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: 72.40 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 886 SLAALRAGDVEKI-----QKLEAELEKAA---THRRNYEEKGKRYRDAvEEKLAKLQKHNSELETQKEQIQL------KL 951
Cdd:TIGR02168 137 SYSIIEQGKISEIieakpEERRAIFEEAAgisKYKERRKETERKLERT-RENLDRLEDILNELERQLKSLERqaekaeRY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 952 QEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKA 1031
Cdd:TIGR02168 216 KELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1032 EVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLE-SYDIEDVRSRLSVedlehlnedgelw 1110
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElKEELESLEAELEE------------- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1111 fayegLKKATRVLESHFQSQkdcyEKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSEnmmIPDFKQQI 1190
Cdd:TIGR02168 363 -----LEAELEELESRLEEL----EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE---IEELLKKL 430
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767984698 1191 SELEKQKQDLEI-RLNEQAEKMKGKLEELSNQLHRSQEE-EGTQRKALEAQNEIHTKEKEklIDKIQEMQE 1259
Cdd:TIGR02168 431 EEAELKELQAELeELEEELEELQEELERLEEALEELREElEEAEQALDAAERELAQLQAR--LDSLERLQE 499
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
847-1268 |
5.28e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.95 E-value: 5.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 847 FQSIRRFVLNIQLTYRVQRLQKK-----------LEDQNKENHGLVEKLTSLAALRagdvEKIQKLEAELEKAATHRRNY 915
Cdd:COG4717 39 LLAFIRAMLLERLEKEADELFKPqgrkpelnlkeLKELEEELKEAEEKEEEYAELQ----EELEELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 916 EEKGKRYRDAVE--EKLAKLQKHNSELETQKEQIQlKLQEKTEELKEKMDNLtKQLFDDVQKEERQrmlLEKSFELKTQD 993
Cdd:COG4717 115 REELEKLEKLLQllPLYQELEALEAELAELPERLE-ELEERLEELRELEEEL-EELEAELAELQEE---LEELLEQLSLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 994 YEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEK------------------------- 1048
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaallallglggsll 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1049 ------------EIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGL 1116
Cdd:COG4717 270 sliltiagvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1117 KKATRVLESHF-QSQKDCYEKEIEAL-NFKVVHLSQEINHLQKLFREENDINE---SIRHEVTRLTSENMMIPDF----- 1186
Cdd:COG4717 350 QELLREAEELEeELQLEELEQEIAALlAEAGVEDEEELRAALEQAEEYQELKEeleELEEQLEELLGELEELLEAldeee 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1187 -KQQISELEKQKQDLEIRLNEQAEKmKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQE--MQEASDH 1263
Cdd:COG4717 430 lEEELEELEEELEELEEELEELREE-LAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALelLEEAREE 508
|
....*
gi 767984698 1264 LKKQF 1268
Cdd:COG4717 509 YREER 513
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
864-1350 |
1.11e-11 |
|
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: 70.00 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 864 QRLQKKLEDQNKENHGLVEKLTSLaalragdvEKIQKLEAELEKAaTHRRNYEEKGKRY---RDAVEEKLAKLQKHNSEL 940
Cdd:TIGR00618 246 TQKREAQEEQLKKQQLLKQLRARI--------EELRAQEAVLEET-QERINRARKAAPLaahIKAVTQIEQQAQRIHTEL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 941 ETQKEQIQLKLQEKTEELKEKMD-----NLTKQLF---------DDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIK 1006
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKQQSSieeqrRLLQTLHsqeihirdaHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQ 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1007 ALKDEKMQL---QHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLL 1083
Cdd:TIGR00618 397 SLCKELDILqreQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1084 ESYDIEDVRSRLSVEDLEHLNEDGELwfaYEGLKKATRVLESHFQ----SQKDC---------YEKEIEALNFKVVHLSQ 1150
Cdd:TIGR00618 477 TKEQIHLQETRKKAVVLARLLELQEE---PCPLCGSCIHPNPARQdidnPGPLTrrmqrgeqtYAQLETSEEDVYHQLTS 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1151 EINHLQKLFREEndinESIRHEVTRLTSenmMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEG 1230
Cdd:TIGR00618 554 ERKQRASLKEQM----QEIQQSFSILTQ---CDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1231 TQRKALEAQNEIHTKEKEKL------IDKIQEMQEASDHLKKQFETES-EVKCNFRQEASRLTLENRDLEEELDMKDRVI 1303
Cdd:TIGR00618 627 LQDVRLHLQQCSQELALKLTalhalqLTLTQERVREHALSIRVLPKELlASRQLALQKMQSEKEQLTYWKEMLAQCQTLL 706
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 767984698 1304 KKLQDQVKTLSKTIGKANDVHSSSGPKeylgmLQYKREDEAKLIQNL 1350
Cdd:TIGR00618 707 RELETHIEEYDREFNEIENASSSLGSD-----LAAREDALNQSLKEL 748
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
934-1322 |
2.43e-11 |
|
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: 68.93 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 934 QKHNSELETQKEQiqLKLQEKTEELKEKMDNLTKQLfDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKM 1013
Cdd:TIGR02168 667 KTNSSILERRREI--EELEEKIEELEEKIAELEKAL-AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1014 QLQHLVEGEHVTSDGLKAEV----ARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITkqlLESYDIE 1089
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIeeleERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT---LLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1090 DVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLEShfqsqkdcYEKEIEALNFKVVHLSQEINHLQKLFREENDINESI 1169
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIES--------LAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1170 RHEVTRLTSEnmmipdfkqqISELEKQKQDLE---IRLNEQAEKMKGKLEELSNQLhRSQEEEGTQRKALEAqnEIHTKE 1246
Cdd:TIGR02168 893 RSELEELSEE----------LRELESKRSELRrelEELREKLAQLELRLEGLEVRI-DNLQERLSEEYSLTL--EEAEAL 959
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767984698 1247 KEKLIDKIQEMQEASDHLKKQFETESEVkcNFRQEAsrltlENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKAND 1322
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRLENKIKELGPV--NLAAIE-----EYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
845-1109 |
4.61e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 845 RRFQSIRRFVLNIQLTYRVQRLQKKLEDQNKENhglvEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRD 924
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELE----AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 925 AVEEKLAKLQKHNSELETQKEQIQ------LKLQEKTEELKEKMDNLTKQL---FDDVQKEERQRMLLEKSFELKTQDYE 995
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRReleerlEELEEELAELEEELEELEEELeelEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 996 KQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKM 1075
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270
....*....|....*....|....*....|....
gi 767984698 1076 SEITKQLLESYDIEDVRSRLSVEDLEHLNEDGEL 1109
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
819-1317 |
7.10e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 7.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 819 RRRYRKMLEEHKAVILQKYARAWLARRRFQSIRRFVLNIQLtyRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKI 898
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELEL--ELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 899 QKLEAELEKAATHRRNYEEKgkryRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLtkqlfDDVQKEER 978
Cdd:COG1196 319 EELEEELAELEEELEELEEE----LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL-----EELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 979 QRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKI 1058
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1059 DVEKHVQSQKREMREKMSE------ITKQLLESYD--IEDVRSRLSVEDLEHLNEDGELW----FAYEGL---------- 1116
Cdd:COG1196 470 EEAALLEAALAELLEELAEaaarllLLLEAEADYEgfLEGVKAALLLAGLRGLAGAVAVLigveAAYEAAleaalaaalq 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1117 -------------------KKATRV----LESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEV 1173
Cdd:COG1196 550 nivveddevaaaaieylkaAKAGRAtflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1174 TRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEiHTKEKEKLIDK 1253
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE-ALLAEEEEERE 708
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767984698 1254 IQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDR----VIKKLQDQVKTLSKTI 1317
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELpeppDLEELERELERLEREI 776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
821-1157 |
1.36e-10 |
|
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: 66.63 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 821 RYRKMLEEhkaviLQKYaRAWLARRRFQSIRRfvlniqltyRVQRLQKKLEDQNKEnhglVEKLTslaalragdvEKIQK 900
Cdd:TIGR02169 212 RYQALLKE-----KREY-EGYELLKEKEALER---------QKEAIERQLASLEEE----LEKLT----------EEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 901 LEAELEKAathRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELkEKMDNLTKQLFddvqkEERQR 980
Cdd:TIGR02169 263 LEKRLEEI---EQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL-EDAEERLAKLE-----AEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 981 MLLEK-SFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKID 1059
Cdd:TIGR02169 334 LLAEIeELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1060 VEKHVQSQKREMREKMSEITKQLLEsydiedVRSRLSVEDLEhlnedgelwfayegLKKATRVLEShFQSQKDCYEKEIE 1139
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINE------LEEEKEDKALE--------------IKKQEWKLEQ-LAADLSKYEQELY 472
|
330
....*....|....*...
gi 767984698 1140 ALNFKVVHLSQEINHLQK 1157
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQR 490
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
938-1317 |
1.65e-10 |
|
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: 66.53 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 938 SELETQKEQIQLKLQEKTEELKEKMDNLTkqlfddvqKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEkmQLQH 1017
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLE--------ELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD--YLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1018 LVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLEsYDIEDVRSRLSV 1097
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE-LLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1098 EDLEHLNEDGELwfaYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQ--------EINHLQKLFREENDINESI 1169
Cdd:pfam02463 314 EKLKESEKEKKK---AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKlqekleqlEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1170 rhevtRLTSENMMIPDFKQQISELEKQ--KQDLEIRLNEQAEKMKGKLEELSnqlhrsqEEEGTQRKALEAQNEIHTKEK 1247
Cdd:pfam02463 391 -----KLKEEELELKSEEEKEAQLLLElaRQLEDLLKEEKKEELEILEEEEE-------SIELKQGKLTEEKEELEKQEL 458
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1248 EKLIDKIQEMQEASDHLKKQfETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTI 1317
Cdd:pfam02463 459 KLLKDELELKKSEDLLKETQ-LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISA 527
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
860-1225 |
1.93e-10 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 65.65 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 860 TYRVQRLQKKLEDqnkenhglVEKLTSLAAlraGDVEKIQK-LEAELEKAATHRRNYEEKGKRYR--------------- 923
Cdd:pfam06160 78 KYRFKKAKKALDE--------IEELLDDIE---EDIKQILEeLDELLESEEKNREEVEELKDKYRelrktllanrfsygp 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 924 --DAVEEKLAKLQKHNSELETQKEQ--------IQLKLQEKTEELKEKMDNLtKQLFDDVQKE---------ERQRMLLE 984
Cdd:pfam06160 147 aiDELEKQLAEIEEEFSQFEELTESgdyleareVLEKLEEETDALEELMEDI-PPLYEELKTElpdqleelkEGYREMEE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 985 KSFELKTQDYEKQIQSLKEEIKALkdekmqLQHLVEGEhvtSDGLKAEVARLSKQVKTISE-FEKEIEllqaQKIDVEKH 1063
Cdd:pfam06160 226 EGYALEHLNVDKEIQQLEEQLEEN------LALLENLE---LDEAEEALEEIEERIDQLYDlLEKEVD----AKKYVEKN 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1064 vQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHlnedgelwfayeglkkaTRVLESHFQSQKDCYEKEIEALNF 1143
Cdd:pfam06160 293 -LPEIEDYLEHAEEQNKELKEELERVQQSYTLNENELER-----------------VRGLEKQLEELEKRYDEIVERLEE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1144 KVVHLSQEINHLQKLFREENDINEsiRHEvtrltsenmmipDFKQQISELEKQkqdlEIRLNEQAEKMKGKLEELSNQLH 1223
Cdd:pfam06160 355 KEVAYSELQEELEEILEQLEEIEE--EQE------------EFKESLQSLRKD----ELEAREKLDEFKLELREIKRLVE 416
|
..
gi 767984698 1224 RS 1225
Cdd:pfam06160 417 KS 418
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
863-1237 |
3.65e-10 |
|
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: 65.38 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 863 VQRLQKKLEDQNKEnhgLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELET 942
Cdd:pfam02463 164 GSRLKRKKKEALKK---LIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 943 QKEQIQLKLQEKTEELKEKMDNlTKQLFDDVQKEERQrmlleksfelktqdyEKQIQSLKEEIKALKD-----EKMQLQH 1017
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEK-EEEKLAQVLKENKE---------------EEKEKKLQEEELKLLAkeeeeLKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1018 LVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSv 1097
Cdd:pfam02463 305 LERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1098 edlehlnedgelwfayeglkkatrvleSHFQSQKDCYEKEIEALNFKVvhlsQEINHLQKLFREENDINESIRHEVTRLT 1177
Cdd:pfam02463 384 ---------------------------ERLSSAAKLKEEELELKSEEE----KEAQLLLELARQLEDLLKEEKKEELEIL 432
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767984698 1178 SENMMIPDFKQQISELEKQKQDL----EIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALE 1237
Cdd:pfam02463 433 EEEEESIELKQGKLTEEKEELEKqelkLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
960-1319 |
3.74e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 960 EKMDNLTKQL--FDDVQKEERQRMLLEKSFELKTQDYEKQIQS---LKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVA 1034
Cdd:PRK03918 145 ESREKVVRQIlgLDDYENAYKNLGEVIKEIKRRIERLEKFIKRtenIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1035 RLSKQVKTISEFEKEIELLQAQKIDVEKHvqsqKREMREKMSEITKQLLES-YDIEDVRSRlsVEDLEHLNEDGELWFAY 1113
Cdd:PRK03918 225 KLEKEVKELEELKEEIEELEKELESLEGS----KRKLEEKIRELEERIEELkKEIEELEEK--VKELKELKEKAEEYIKL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1114 EGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREEndinESIRHEVTRLTSENMMIPDFKQQISEL 1193
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL----KELEKRLEELEERHELYEEAKAKKEEL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1194 EKQKQDLEirlNEQAEKMKGKLEELSNqlhrsqeeegtqrkaleAQNEIhTKEKEKLIDKIQEMQEASDHLKKQFE--TE 1271
Cdd:PRK03918 375 ERLKKRLT---GLTPEKLEKELEELEK-----------------AKEEI-EEEISKITARIGELKKEIKELKKAIEelKK 433
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 767984698 1272 SEVKC---------NFRQE-ASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGK 1319
Cdd:PRK03918 434 AKGKCpvcgrelteEHRKElLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
896-1317 |
4.75e-10 |
|
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: 64.81 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 896 EKIQKLEAEL--EKAATHRRNYEE-----KGKRyrdaVEEKLAKLQKHNSELETQKEQIQLKLQEKTEEL---KEKMDNL 965
Cdd:pfam01576 103 QHIQDLEEQLdeEEAARQKLQLEKvtteaKIKK----LEEDILLLEDQNSKLSKERKLLEERISEFTSNLaeeEEKAKSL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 966 TK----------QLFDDVQKEERQRMLLEKS---FELKTQDYEKQIQSLKEEIKALKdekMQLQHlvegehvTSDGLKAE 1032
Cdd:pfam01576 179 SKlknkheamisDLEERLKKEEKGRQELEKAkrkLEGESTDLQEQIAELQAQIAELR---AQLAK-------KEEELQAA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1033 VARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQkREMREKMSEITKQLLEsyDIEDVRSRLsvED-LEHLNEDGELWF 1111
Cdd:pfam01576 249 LARLEEETAQKNNALKKIRELEAQISELQEDLESE-RAARNKAEKQRRDLGE--ELEALKTEL--EDtLDTTAAQQELRS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1112 AYEG----LKKA----TRVLESHFQSQKDCYEKEIEALN--------FKVV------HLSQEINHLQKLFREENDINESI 1169
Cdd:pfam01576 324 KREQevteLKKAleeeTRSHEAQLQEMRQKHTQALEELTeqleqakrNKANlekakqALESENAELQAELRTLQQAKQDS 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1170 RHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNE---QAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEI---H 1243
Cdd:pfam01576 404 EHKRKKLEGQ---LQELQARLSESERQRAELAEKLSKlqsELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELlqeE 480
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767984698 1244 TKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTI 1317
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL 554
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
927-1266 |
8.66e-10 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 63.81 E-value: 8.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 927 EEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLfddvqkeeRQRML-LEKS---FELKTQDYEKQIQSLK 1002
Cdd:pfam15818 27 EEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAVFKKQL--------QMKMCaLEEEkgkYQLATEIKEKEIEGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1003 EEIKALKDEKMQLQhlvegehvtsdglkaevarlskqvKTISEFEKEIELLQAQKIDVEKhvqsQKREMREKMSEITKQL 1082
Cdd:pfam15818 99 ETLKALQVSKYSLQ------------------------KKVSEMEQKLQLHLLAKEDHHK----QLNEIEKYYATITGQF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1083 ---------LESYDIEDVR--SRLSVedlehLNE--DGELWFAYEGLKKATRVL-ESHFQSQkdcYEKEIEALNFKVVHl 1148
Cdd:pfam15818 151 glvkenhgkLEQNVQEAIQlnKRLSA-----LNKkqESEICSLKKELKKVTSDLiKSKVTCQ---YKMGEENINLTIKE- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1149 sQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELS--NQLHRSQ 1226
Cdd:pfam15818 222 -QKFQELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALKENNQTLErdNELQREK 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 767984698 1227 EEEgTQRKALEAQNEiHTK-------EKEKLIDKIQEMQEASDHLKK 1266
Cdd:pfam15818 301 VKE-NEEKFLNLQNE-HEKalgtwkkHVEELNGEINEIKNELSSLKE 345
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
900-1355 |
9.60e-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: 63.98 E-value: 9.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 900 KLEAELEkaaTHRRNYEEKGKRYRDAVEEKLA--------KLQKHNSELETQK---EQIQLKLQEKTEELKEKMDNLTkq 968
Cdd:pfam15921 56 KYEVELD---SPRKIIAYPGKEHIERVLEEYShqvkdlqrRLNESNELHEKQKfylRQSVIDLQTKLQEMQMERDAMA-- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 969 lfdDVQKEERQrmlleksfelKTQDYEKQIQSLKEEIKA---LKDE-------------KMQLQH---LVEGEHVTSDGL 1029
Cdd:pfam15921 131 ---DIRRRESQ----------SQEDLRNQLQNTVHELEAakcLKEDmledsntqieqlrKMMLSHegvLQEIRSILVDFE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1030 KAEVARLSKQ---------------VKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQ-------LLESYD 1087
Cdd:pfam15921 198 EASGKKIYEHdsmstmhfrslgsaiSKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQhqdrieqLISEHE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1088 IE----------------DVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVV----- 1146
Cdd:pfam15921 278 VEitgltekassarsqanSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVlanse 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1147 ---------HLSQEI----NHLQKLF-------------REEN------DINESIR--HEVTRLTSENMMIP-------- 1184
Cdd:pfam15921 358 ltearterdQFSQESgnldDQLQKLLadlhkrekelsleKEQNkrlwdrDTGNSITidHLRRELDDRNMEVQrleallka 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1185 -------DFKQQISELEKQKQDLE------IRLNEQAEKMKGKLEELSNQLHRSQEEEGT----------QRKALEAQNE 1241
Cdd:pfam15921 438 mksecqgQMERQMAAIQGKNESLEkvssltAQLESTKEMLRKVVEELTAKKMTLESSERTvsdltaslqeKERAIEATNA 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1242 IHTKEKEKLIDKIQEMQeasdHLKkqfeTESEVKCNFRQEASRLTLenrdleeELDMKDRVIKKLQDQVKTLSKTIGKan 1321
Cdd:pfam15921 518 EITKLRSRVDLKLQELQ----HLK----NEGDHLRNVQTECEALKL-------QMAEKDKVIEILRQQIENMTQLVGQ-- 580
|
570 580 590
....*....|....*....|....*....|....
gi 767984698 1322 dvHSSSGpkeylGMLQYKREDEAKLIQNLILDLK 1355
Cdd:pfam15921 581 --HGRTA-----GAMQVEKAQLEKEINDRRLELQ 607
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
984-1329 |
1.03e-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: 63.55 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 984 EKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQvktISEFEKEIELLQAQkidvekh 1063
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK---IGEIEKEIEQLEQE------- 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1064 vqsqkremREKMSEItkqllesydIEDVRSRLSVEDLEHLNEDGELwfayeglkkatrvleshfqsqkDCYEKEIEALNF 1143
Cdd:TIGR02169 732 --------EEKLKER---------LEELEEDLSSLEQEIENVKSEL----------------------KELEARIEELEE 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1144 KVVHLSQEINHLqklfreENDINESIRHEVTRLTSEnmmipdFKQQISELEKQKQDLEIRLNEQAEKmKGKLEELSNQLH 1223
Cdd:TIGR02169 773 DLHKLEEALNDL------EARLSHSRIPEIQAELSK------LEEEVSRIEARLREIEQKLNRLTLE-KEYLEKEIQELQ 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1224 RSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFEtesevkcNFRQEASRLTLENRDLEEELDMKDRVI 1303
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG-------DLKKERDELEAQLRELERKIEELEAQI 912
|
330 340
....*....|....*....|....*.
gi 767984698 1304 KKLQDQVKTLSKTIGKANDVHSSSGP 1329
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSEIED 938
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
883-1315 |
1.31e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 883 KLTSLAALRAGDVEKIQKLEAELEKAA--THRRNYEEkgkryRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKE 960
Cdd:COG4717 36 KSTLLAFIRAMLLERLEKEADELFKPQgrKPELNLKE-----LKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 961 KMDNLTKQLfDDVQKEERQRMLLEKSFELKTQ--DYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSK 1038
Cdd:COG4717 110 ELEELREEL-EKLEKLLQLLPLYQELEALEAElaELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1039 QV-KTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEI--TKQLLESYDIEDVRSRLSV----------------ED 1099
Cdd:COG4717 189 ATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELeqLENELEAAALEERLKEARLllliaaallallglggSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1100 LEHLNEDGELWFAYEGLkkaTRVLESHFQSQKDCYEKEIEALNfKVVHLSQEINHLQKLFREENDINESIrhEVTRLTSE 1179
Cdd:COG4717 269 LSLILTIAGVLFLVLGL---LALLFLLLAREKASLGKEAEELQ-ALPALEELEEEELEELLAALGLPPDL--SPEELLEL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1180 NMMIPDFKQQISELEKQKQDLEIRLNEQaekmkgKLEELSNQLHRSQEEEgtQRKALEAQNEIHtKEKEKLIDKIQEMQE 1259
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELEQ------EIAALLAEAGVEDEEE--LRAALEQAEEYQ-ELKEELEELEEQLEE 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 767984698 1260 ASDHLKKQFETESEVKCnfRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSK 1315
Cdd:COG4717 414 LLGELEELLEALDEEEL--EEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
925-1294 |
1.41e-09 |
|
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: 63.06 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 925 AVEEKLAKLQKHNSE------LETQKEQIQLkLQEKTEELKEKMDNLTK---------QLFDDVQKEERQRMLLEKSFEL 989
Cdd:TIGR00618 127 ETEEVIHDLLKLDYKtftrvvLLPQGEFAQF-LKAKSKEKKELLMNLFPldqytqlalMEFAKKKSLHGKAELLTLRSQL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 990 KTQDYEKQIQSLKEEIKALKDEKMQL----QHLVEGEHVTSDGLKAEVARLSKQvKTISEFEKEIELLQAQKIDVEKhvQ 1065
Cdd:TIGR00618 206 LTLCTPCMPDTYHERKQVLEKELKHLrealQQTQQSHAYLTQKREAQEEQLKKQ-QLLKQLRARIEELRAQEAVLEE--T 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1066 SQKREMREKMSEITkqllesydiedvrsrLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKV 1145
Cdd:TIGR00618 283 QERINRARKAAPLA---------------AHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1146 VHLSQEINHlqklFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQ----KQDLEIRLNEQAEKMKGKLEE--LS 1219
Cdd:TIGR00618 348 QTLHSQEIH----IRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKlqslCKELDILQREQATIDTRTSAFrdLQ 423
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767984698 1220 NQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEE 1294
Cdd:TIGR00618 424 GQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLE 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
938-1320 |
1.54e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 938 SELETQKEQIQLKLqEKTEElkekmdNLTKqlFDDVQKE--------ERQRMLLEKSFELKTQDYEKQIQSLKEEIKALK 1009
Cdd:COG1196 168 SKYKERKEEAERKL-EATEE------NLER--LEDILGElerqleplERQAEKAERYRELKEELKELEAELLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1010 DEKMQLQHLVEGEHVTSDGLKAEVARLskqvktisefEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQllesydie 1089
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAEL----------EAELEELRLELEELELELEEAQAEEYELLAELARL-------- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1090 dvrsrlsVEDLEHLNEDgelwfayeglkkatrvlESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINESI 1169
Cdd:COG1196 301 -------EQDIARLEER-----------------RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1170 RhevtrltsenmmipdfkQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEgTQRKALEAQNEIHTKEKEK 1249
Cdd:COG1196 357 E-----------------AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA-AQLEELEEAEEALLERLER 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767984698 1250 LIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKA 1320
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
845-1301 |
1.76e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 845 RRFQSIRRFVLNIQL-----TYRVQRLQKKLEDQNKENHGLVEKLTS--------LAAL--RAGDVEKIQKLEaELE--- 906
Cdd:COG4913 496 EHYAAALRWVNRLHLrgrlvYERVRTGLPDPERPRLDPDSLAGKLDFkphpfrawLEAElgRRFDYVCVDSPE-ELRrhp 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 907 KAAT------HRRNYEEKGKRYRDA--------VEEKLAKLQKhnsELETQKEQIQlKLQEKTEELKEKMDNLTKQLfdd 972
Cdd:COG4913 575 RAITragqvkGNGTRHEKDDRRRIRsryvlgfdNRAKLAALEA---ELAELEEELA-EAEERLEALEAELDALQERR--- 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 973 vqkeERQRMLLEKSF-ELKTQDYEKQIQSLKEEIKALKDEKMQLQHLvegehvtsdglkaevarlskqvktisefEKEIE 1051
Cdd:COG4913 648 ----EALQRLAEYSWdEIDVASAEREIAELEAELERLDASSDDLAAL----------------------------EEQLE 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1052 LLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQK 1131
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERI 775
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1132 DCYEKEIEALNFKVVHLSQEINHLQKLFREENDI----NESIRHEVTRLTSENmmIPDFKQQISELEKQ-----KQDLEI 1202
Cdd:COG4913 776 DALRARLNRAEEELERAMRAFNREWPAETADLDAdlesLPEYLALLDRLEEDG--LPEYEERFKELLNEnsiefVADLLS 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1203 RLNEQAEKMKGKLEELSNQLHRSQEEEGTqRKALEAQNEIHTKEKEKLidkiQEMQEASDHLKKQFETESEVKCNFRQEA 1282
Cdd:COG4913 854 KLRRAIREIKERIDPLNDSLKRIPFGPGR-YLRLEARPRPDPEVREFR----QELRAVTSGASLFDEELSEARFAALKRL 928
|
490 500
....*....|....*....|
gi 767984698 1283 -SRLtlenRDLEEELDMKDR 1301
Cdd:COG4913 929 iERL----RSEEEESDRRWR 944
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
864-1286 |
2.75e-09 |
|
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: 62.05 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 864 QRLQKKlEDQNK-------ENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKH 936
Cdd:pfam05483 370 QRLEKN-EDQLKiitmelqKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAR 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 937 NSE---LETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELkTQDYEKQIQSLKEEIKALKDEKM 1013
Cdd:pfam05483 449 EKEihdLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKEL-TQEASDMTLELKKHQEDIINCKK 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1014 QLQHLVegehvtsdglkaevarlskqvktisefeKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESydiEDVRS 1093
Cdd:pfam05483 528 QEERML----------------------------KQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKS---EENAR 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1094 RLSVEDLEHLNEDGELWFAYEGLKK----ATRVLESHFQSQK------DCYEKEIEALNFKVVHLSQEINHLQKLFREEN 1163
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKqienKNKNIEELHQENKalkkkgSAENKQLNAYEIKVNKLELELASAKQKFEEII 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1164 DiNESIRHEVTRLTSENMM--IPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNE 1241
Cdd:pfam05483 657 D-NYQKEIEDKKISEEKLLeeVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQ 735
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 767984698 1242 IHTKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLT 1286
Cdd:pfam05483 736 EQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
951-1309 |
5.47e-09 |
|
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: 60.68 E-value: 5.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 951 LQEKTEE-LKEKMDNLTKQLFDDVQKE-ERQRMLLEK-SFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSD 1027
Cdd:pfam07888 32 LQNRLEEcLQERAELLQAQEAANRQREkEKERYKRDReQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1028 GLKAEVARLSKQ----VKTISEFEKEIELLQAQKIDVEkhvqSQKREMREKMSEITKQLLESY-DIEDVRSRL--SVEDL 1100
Cdd:pfam07888 112 ELSEEKDALLAQraahEARIRELEEDIKTLTQRVLERE----TELERMKERAKKAGAQRKEEEaERKQLQAKLqqTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1101 EHLNEDgelwfaYEGLKKATRVLESHFQSQKDcyekeiealnfKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSEN 1180
Cdd:pfam07888 188 RSLSKE------FQELRNSLAQRDTQVLQLQD-----------TITTLTQKLTTAHRKEAENEALLEELRSLQERLNASE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1181 MMIPDFKQQISELEKQKQDLEIRLNE---QAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEM 1257
Cdd:pfam07888 251 RKVEGLGEELSSMAAQRDRTQAELHQarlQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRL 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 767984698 1258 QEA-----SDHLKKQFETESEVKCNFRQEAsrltlENRDLEEELDMKDRVIKKLQDQ 1309
Cdd:pfam07888 331 EERlqeerMEREKLEVELGREKDCNRVQLS-----ESRRELQELKASLRVAQKEKEQ 382
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
955-1360 |
6.44e-09 |
|
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: 61.01 E-value: 6.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 955 TEELKEKMDNLTKQLFDDVQKEERQrmllEKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHL-VEGEHVTSDGLKAEV 1033
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQAAA----EEQLVQANGELEKASREETFARTALKNARLDLRRLfDEKQSEKDKKNKALA 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1034 ARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSrlsvedlehlneDGELWFAY 1113
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALL------------KAAIAARR 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1114 EGLKKATRVLESHfqsqkdcYEKEIEALNF---KVVHLSQEINHL-QKLFREENDinesiRHEVTRLTsenmmipDFKQQ 1189
Cdd:pfam12128 743 SGAKAELKALETW-------YKRDLASLGVdpdVIAKLKREIRTLeRKIERIAVR-----RQEVLRYF-------DWYQE 803
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1190 ISELEKQkqdleiRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQneihTKEKEKLIDKIQEMQEASDHLKKQFE 1269
Cdd:pfam12128 804 TWLQRRP------RLATQLSNIERAISELQQQLARLIADTKLRRAKLEME----RKASEKQQVRLSENLRGLRCEMSKLA 873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1270 TESEvKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKandvHSSSGPKEYlgmLQYKREDEAKLIQN 1349
Cdd:pfam12128 874 TLKE-DANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIAD----HSGSGLAET---WESLREEDHYQNDK 945
|
410
....*....|.
gi 767984698 1350 LILDLKPRGVV 1360
Cdd:pfam12128 946 GIRLLDYRKLV 956
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
823-1258 |
6.69e-09 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 60.92 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 823 RKMLEEHKavilqkyarawlaRRRFQSIRRFVLNiQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVE------ 896
Cdd:pfam07111 131 RKNLEEGS-------------QRELEEIQRLHQE-QLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKqlaeaq 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 897 --------KIQKLEAELEKAAT-----------------HRRNYEEKGKRYRDAVEEklakLQKHNSELETQKEQIQLKL 951
Cdd:pfam07111 197 keaellrkQLSKTQEELEAQVTlveslrkyvgeqvppevHSQTWELERQELLDTMQH----LQEDRADLQATVELLQVRV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 952 QEKTEELKEKMDNLTK--QLFDDVQKE--ERQRMLL----EKSF----ELKTQDYEK---------QIQSLKEEIKALKD 1010
Cdd:pfam07111 273 QSLTHMLALQEEELTRkiQPSDSLEPEfpKKCRSLLnrwrEKVFalmvQLKAQDLEHrdsvkqlrgQVAELQEQVTSQSQ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1011 EKMQLQHL-------VEGEHVTSDGLKAEVARLS----KQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEI- 1078
Cdd:pfam07111 353 EQAILQRAlqdkaaeVEVERMSAKGLQMELSRAQearrRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIp 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1079 --TKQLleSYDIEDVRS------------RLSVE-----------------DLEHLNEDGELWFAYegLKKATRVLESHF 1127
Cdd:pfam07111 433 slSNRL--SYAVRKVHTikglmarkvalaQLRQEscpppppappvdadlslELEQLREERNRLDAE--LQLSAHLIQQEV 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1128 QSQKDCYEKEIEALNFKVVHLSQEINHLQKLF--------------REENDINESIRHEVTRltSENMMIPDFKQQISEL 1193
Cdd:pfam07111 509 GRAREQGEAERQQLSEVAQQLEQELQRAQESLasvgqqlevarqgqQESTEEAASLRQELTQ--QQEIYGQALQEKVAEV 586
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767984698 1194 E----KQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQ 1258
Cdd:pfam07111 587 EtrlrEQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKEEGQRLARRVQELE 655
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
989-1322 |
9.07e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 9.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 989 LKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQK 1068
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1069 rEMREKMSEITKQLlesydiedvrsrLSVE-DLEHLNED-GELWFAYEGLKKATRVLESHfqsqkdcyEKEIEALNFKVv 1146
Cdd:PRK03918 235 -ELKEEIEELEKEL------------ESLEgSKRKLEEKiRELEERIEELKKEIEELEEK--------VKELKELKEKA- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1147 hlsQEINHLQKLFREENDINESIRHEVTRLTsenmmipdfkQQISELEKQKQDLEiRLNEQAEKMKGKLEELSNQLHRSQ 1226
Cdd:PRK03918 293 ---EEYIKLSEFYEEYLDELREIEKRLSRLE----------EEINGIEERIKELE-EKEERLEELKKKLKELEKRLEELE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1227 EEEGTQRKALEAQNEIHT-------KEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLE----------- 1288
Cdd:PRK03918 359 ERHELYEEAKAKKEELERlkkrltgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAieelkkakgkc 438
|
330 340 350
....*....|....*....|....*....|....*..
gi 767984698 1289 ---NRDLEEEldMKDRVIKKLQDQVKTLSKTIGKAND 1322
Cdd:PRK03918 439 pvcGRELTEE--HRKELLEEYTAELKRIEKELKEIEE 473
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
851-1220 |
1.05e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.36 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 851 RRFVLNIQLTYRvQRLQKKLEDQNKENHGLVEKLTSLAALragdVEKIQKLEAELEKAATHR------RNYEEKGKRYRD 924
Cdd:PRK04863 281 RRVHLEEALELR-RELYTSRRQLAAEQYRLVEMARELAEL----NEAESDLEQDYQAASDHLnlvqtaLRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 925 AVEEKLAKLQKHNSELETQKEQiQLKLQEKTEELKEKMDNLTKQLFDDVQK-EERQRMLLEksfelktqdYEKQIQSLkE 1003
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEADEQ-QEENEARAEAAEEEVDELKSQLADYQQAlDVQQTRAIQ---------YQQAVQAL-E 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1004 EIKALKD---------EKMQLQHLVEGEHVTSDGLKAEvARLSKQVKTISEFEKEIELLQAQKIDVE------------- 1061
Cdd:PRK04863 425 RAKQLCGlpdltadnaEDWLEEFQAKEQEATEELLSLE-QKLSVAQAAHSQFEQAYQLVRKIAGEVSrseawdvarellr 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1062 -----KHVQSQKREMREKMSEITKQLLESYDIEDVRSRL---------SVEDLEHLNEDGElwfayeglkkatRVLESHF 1127
Cdd:PRK04863 504 rlreqRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFckrlgknldDEDELEQLQEELE------------ARLESLS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1128 QSQKDCYEKEIEaLNFKVVHLSQEINHLQKL---FREENDINESIRHEV--TRLTSENMMipDFKQQISELEKQKQDLEI 1202
Cdd:PRK04863 572 ESVSEARERRMA-LRQQLEQLQARIQRLAARapaWLAAQDALARLREQSgeEFEDSQDVT--EYMQQLLERERELTVERD 648
|
410
....*....|....*...
gi 767984698 1203 RLNEQAEKMKGKLEELSN 1220
Cdd:PRK04863 649 ELAARKQALDEEIERLSQ 666
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
893-1319 |
2.88e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.76 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 893 GDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLqekteelkekmdnltkqlfdd 972
Cdd:PRK01156 360 GYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKL--------------------- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 973 vqkeerqrmlleksfelktQDYEKQIQSLKEEIKALKDEKMQLQHLVE-----------GEHVTSDGLKAEVARLSKQVK 1041
Cdd:PRK01156 419 -------------------QDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcGTTLGEEKSNHIINHYNEKKS 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1042 TISEFEKEIElLQAQKIDvEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSvEDLEHLNEDGELWFAYEGLKKATR 1121
Cdd:PRK01156 480 RLEEKIREIE-IEVKDID-EKIVDLKKRKEYLESEEINKSINEYNKIESARADLE-DIKIKINELKDKHDKYEEIKNRYK 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1122 VLEshfqsQKDCYEKEIEALNFKVVHLSQEINHLQKLFreeNDINESIRHEVTRLTSENMMIPDFK----QQISELEKQK 1197
Cdd:PRK01156 557 SLK-----LEDLDSKRTSWLNALAVISLIDIETNRSRS---NEIKKQLNDLESRLQEIEIGFPDDKsyidKSIREIENEA 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1198 QDLEIRLNE------QAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHT--KEKEKLIDKIqemqeasdhLKKQFE 1269
Cdd:PRK01156 629 NNLNNKYNEiqenkiLIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDnlKKSRKALDDA---------KANRAR 699
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 767984698 1270 TESEVKCNfRQEASRLTLENRDLEEELDMKDRVIKKLQDqVKTLSKTIGK 1319
Cdd:PRK01156 700 LESTIEIL-RTRINELSDRINDINETLESMKKIKKAIGD-LKRLREAFDK 747
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
818-1345 |
5.46e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 818 ARR--RYRKMLEEHKAVILQKY--ARAWLARRRFQSIRRF--VLNIQLTYRVQRLQKKLEDQNKenhglvekltslaALR 891
Cdd:PTZ00121 1181 ARKaeEVRKAEELRKAEDARKAeaARKAEEERKAEEARKAedAKKAEAVKKAEEAKKDAEEAKK-------------AEE 1247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 892 AGDVEKIQKLEaELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFD 971
Cdd:PTZ00121 1248 ERNNEEIRKFE-EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 972 DVQKEERQRmllEKSFELKTQDYEKQIQSLKEEIKALKDEKmqlqhlvegehvtsdglKAEVARLSKqvktiSEFEKEIE 1051
Cdd:PTZ00121 1327 AKKKADAAK---KKAEEAKKAAEAAKAEAEAAADEAEAAEE-----------------KAEAAEKKK-----EEAKKKAD 1381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1052 LLQAQKIDVEKHVQSQKR--EMREKMSEITKQLLESYDIEDVRSRLSvedlehlnedgELWFAYEGLKKATRVLESHFQS 1129
Cdd:PTZ00121 1382 AAKKKAEEKKKADEAKKKaeEDKKKADELKKAAAAKKKADEAKKKAE-----------EKKKADEAKKKAEEAKKADEAK 1450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1130 QKDCYEKEIEALNfKVVHLSQEINHLQKLFREENDINESIR--HEVTRLTSENMMIPDFKQQISEL----EKQKQDlEIR 1203
Cdd:PTZ00121 1451 KKAEEAKKAEEAK-KKAEEAKKADEAKKKAEEAKKADEAKKkaEEAKKKADEAKKAAEAKKKADEAkkaeEAKKAD-EAK 1528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1204 LNEQAEKM--------KGKLEELSNQLHRSQEEEgtQRKALEAQNEihTKEKEKLIDKIQEMQEASDHLKKQFETESEVK 1275
Cdd:PTZ00121 1529 KAEEAKKAdeakkaeeKKKADELKKAEELKKAEE--KKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1276 CNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVHSSSGPKEYLGMLQYKREDEAK 1345
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
862-1331 |
5.78e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.99 E-value: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 862 RVQRLQKKLEDQNKENHGLVEKLTSLAALragdVEKIQKLEAELEKAATHRRNYEEKGKRYRDaVEEKLAKLQkhNSELE 941
Cdd:PRK01156 219 EIERLSIEYNNAMDDYNNLKSALNELSSL----EDMKNRYESEIKTAESDLSMELEKNNYYKE-LEERHMKII--NDPVY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 942 TQKEQIQ--LKLQEKTEELKEKMDNLTKQL--FDDVQKEERQrmlLEKSFElktqDYEKQiQSLKEEIKALKDEkmqlqh 1017
Cdd:PRK01156 292 KNRNYINdyFKYKNDIENKKQILSNIDAEInkYHAIIKKLSV---LQKDYN----DYIKK-KSRYDDLNNQILE------ 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1018 lVEGEHVTSDGLKAEVARLSKQvktISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLE-SYDIE--DVRSR 1094
Cdd:PRK01156 358 -LEGYEMDYNSYLKSIESLKKK---IEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDiSSKVSslNQRIR 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1095 LSVEDLEHLNEDGELWFAYE---------GLKKATRVLEsHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKL--FREEN 1163
Cdd:PRK01156 434 ALRENLDELSRNMEMLNGQSvcpvcgttlGEEKSNHIIN-HYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRkeYLESE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1164 DINESIrhevtrlTSENmmipdfkqQISELEKQKQDLEIRLNEQAEKmKGKLEELSNQlHRSQEEEGTQRKALEAQNEIH 1243
Cdd:PRK01156 513 EINKSI-------NEYN--------KIESARADLEDIKIKINELKDK-HDKYEEIKNR-YKSLKLEDLDSKRTSWLNALA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1244 TKEkekLIDkIQEMQEASDHLKKQF-ETES---EVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGK 1319
Cdd:PRK01156 576 VIS---LID-IETNRSRSNEIKKQLnDLESrlqEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGK 651
|
490
....*....|..
gi 767984698 1320 ANDVHSSSGPKE 1331
Cdd:PRK01156 652 IDNYKKQIAEID 663
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
858-1202 |
6.53e-08 |
|
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: 57.44 E-value: 6.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 858 QLTYRVQRLQKKLEDQNKENHGLVEKltslaalragdvEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHN 937
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQ------------ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 938 S-ELETQKEQIQLKLQEKTEELK-----------EKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQ--IQSLKE 1003
Cdd:pfam17380 341 RmAMERERELERIRQEERKRELErirqeeiameiSRMRELERLQMERQQKNERVRQELEAARKVKILEEERQrkIQQQKV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1004 EIKALKDEKmqlqhlvegehvtSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVekhVQSQKREMREKMSEITKQLL 1083
Cdd:pfam17380 421 EMEQIRAEQ-------------EEARQREVRRLEEERAREMERVRLEEQERQQQVER---LRQQEEERKRKKLELEKEKR 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1084 ESYDIEDVRSRLSVEDLEHLNEdgelwfAYEGLKKATRVLESHFQS-QKDCYEKEIEalnfkvvHLSQEINHLQKLFREE 1162
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQ------AMIEEERKRKLLEKEMEErQKAIYEEERR-------REAEEERRKQQEMEER 551
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 767984698 1163 NDINESIR---HEVTRLTS---ENMMIpdfkQQISELEKQKQDLEI 1202
Cdd:pfam17380 552 RRIQEQMRkatEERSRLEAmerEREMM----RQIVESEKARAEYEA 593
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
798-1210 |
6.62e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 798 LYQLIRMATITMQAYSRGFLARRRYRKMLEEHKAVILQkyarawlARRRFQSIRRFVLNIQLTYRVQRLQKKLEDQNKEN 877
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE-------LREELEKLEKLLQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 878 HGLVEKLTSLAALRagdvEKIQKLEAELEKAATHRRNYEEK-GKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTE 956
Cdd:COG4717 149 EELEERLEELRELE----EELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELE-EAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 957 ELKEKMDNLTKQLFDDVQKEERQRMLLEK-------SFELKTQDYEKQIQSLKEEIKA---------LKDEKMQLQHLVE 1020
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARLLLliaaallALLGLGGSLLSLILTIAGVLFLvlgllallfLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1021 GEHVTSDGLKAEVARLS-KQVKTISEFEKEIELLQAQK-IDVEKHVQSQKREMREKMSEITKQLLESyDIEDVRSRLSVE 1098
Cdd:COG4717 304 AEELQALPALEELEEEElEELLAALGLPPDLSPEELLElLDRIEELQELLREAEELEEELQLEELEQ-EIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1099 DLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKvvHLSQEINHLQ-KLFREENDINEsIRHEVTRLT 1177
Cdd:COG4717 383 DEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEeELEELEEELEE-LREELAELE 459
|
410 420 430
....*....|....*....|....*....|...
gi 767984698 1178 SENMMIPDfKQQISELEKQKQDLEIRLNEQAEK 1210
Cdd:COG4717 460 AELEQLEE-DGELAELLQELEELKAELRELAEE 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1043-1325 |
7.04e-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: 57.77 E-value: 7.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1043 ISEFEKEIELLQA------QKIDVEKHVQSQKREMREKMsEITKQLLESYDieDVRSRL-SVEDLEHLNEdgelwfayeg 1115
Cdd:TIGR02169 165 VAEFDRKKEKALEeleeveENIERLDLIIDEKRQQLERL-RREREKAERYQ--ALLKEKrEYEGYELLKE---------- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1116 lKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREEN-DINE-------SIRHEVTRLTSE----NMMI 1183
Cdd:TIGR02169 232 -KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNkKIKDlgeeeqlRVKEKIGELEAEiaslERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1184 PDFKQQISELEKQKQDLEIRLNEQAEKM----------KGKLEELSNQLHRSQEEEGTQRKALEAQNEIHT--------- 1244
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIeelereieeeRKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdelkdy 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1245 -KEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDV 1323
Cdd:TIGR02169 391 rEKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
..
gi 767984698 1324 HS 1325
Cdd:TIGR02169 471 LY 472
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
880-1326 |
7.88e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 7.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 880 LVEKLTSLAALRAgDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEK-LAKLQKHNSELETQKEQIQlKLQEKTEEL 958
Cdd:COG4913 230 LVEHFDDLERAHE-ALEDAREQIELLEPIRELAERYAAARERLAELEYLRaALRLWFAQRRLELLEAELE-ELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 959 KEKMDNLTKQLfDDVQKEERQrmlLEKsfELKTQDYEkQIQSLKEEIKALKDEK-------MQLQHLVEGEHVTSDGLKA 1031
Cdd:COG4913 308 EAELERLEARL-DALREELDE---LEA--QIRGNGGD-RLEQLEREIERLERELeererrrARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1032 EVARLSKQVKTISEFEKEI-ELLQAQKIDVEKHVQSQKREMREKMSEItkQLLES------YDIEDVRSRLSvedlEHLN 1104
Cdd:COG4913 381 EFAALRAEAAALLEALEEElEALEEALAEAEAALRDLRRELRELEAEI--ASLERrksnipARLLALRDALA----EALG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1105 ED-GELWF----------------AYEGL---------------KKATRVLESHFQSQKDCYEKeIEALNFKVVHLSQEI 1152
Cdd:COG4913 455 LDeAELPFvgelievrpeeerwrgAIERVlggfaltllvppehyAAALRWVNRLHLRGRLVYER-VRTGLPDPERPRLDP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1153 NHL-QKLFREENDINESIRHEVTR-------------------LTSENMM--------------IP-------DFKQQIS 1191
Cdd:COG4913 534 DSLaGKLDFKPHPFRAWLEAELGRrfdyvcvdspeelrrhpraITRAGQVkgngtrhekddrrrIRsryvlgfDNRAKLA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1192 ELEKQKQDLEIRLNE---QAEKMKGKLEELSNQ---LHRSQEEEGTQRKALEAQNEIHTKEKEklidkIQEMQEASDHLK 1265
Cdd:COG4913 614 ALEAELAELEEELAEaeeRLEALEAELDALQERreaLQRLAEYSWDEIDVASAEREIAELEAE-----LERLDASSDDLA 688
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767984698 1266 KQfetesevkcnfRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVHSS 1326
Cdd:COG4913 689 AL-----------EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
862-1015 |
9.29e-08 |
|
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: 54.93 E-value: 9.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 862 RVQRLQKKLEDQNKEnhgLVEKLTSLAALRAgdveKIQKLEAELEKAATHRRNYEEKGKRYRDAVEekLAKLQKhnsELE 941
Cdd:COG1579 32 ELAELEDELAALEAR---LEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQLGNVRNNKE--YEALQK---EIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767984698 942 TQKEQIQlKLQEKTEELKEKMDNLTKQLfddvQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQL 1015
Cdd:COG1579 100 SLKRRIS-DLEDEILELMERIEELEEEL----AELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
862-1242 |
1.49e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 862 RVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAElEKAATHRRNYEEKGKRYRDAVEEKLaKLQKHNSELE 941
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE-EVMKLYEEEKKMKAEEAKKAEEAKI-KAEELKKAEE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 942 TQKEQIQLKLQE-----KTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEkmQLQ 1016
Cdd:PTZ00121 1631 EKKKVEQLKKKEaeekkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE--ELK 1708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1017 HLVEGEHVTSDGL-KAEVARLSKQVKTISEFEKEIELLQAQKIDVE--KHVQSQKREMREKMSEITKQ----LLESYDIE 1089
Cdd:PTZ00121 1709 KKEAEEKKKAEELkKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekKKIAHLKKEEEKKAEEIRKEkeavIEEELDEE 1788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1090 DVRSRLSVE-DLEHLNEDGELwfAYEGLKKATRVLeshfQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINES 1168
Cdd:PTZ00121 1789 DEKRRMEVDkKIKDIFDNFAN--IIEGGKEGNLVI----NDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGE 1862
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767984698 1169 IRHEVTRLTSENMMIPDFKQQISELEKQKQ----DLEIRLNEQaeKMKGKLEELSNQlhRSQEEEGTQRKALEAQNEI 1242
Cdd:PTZ00121 1863 DGNKEADFNKEKDLKEDDEEEIEEADEIEKidkdDIEREIPNN--NMAGKNNDIIDD--KLDKDEYIKRDAEETREEI 1936
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
938-1317 |
1.91e-07 |
|
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: 56.18 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 938 SELETQKEQIQLKLQEKTEELKekmdNLTKQLFDDVQKeerqrmllEKSFELKTQDYEKQIQSLKeeiKALKDEKMQLqh 1017
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELK----NLDKNLNKDEEK--------INNSNNKIKILEQQIKDLN---DKLKKNKDKI-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1018 lvegehvtsDGLKAEVARLSKQVKT----ISEFEKEIELLQAQKIDVEKHV----------QSQKREMREKMSEITKQLL 1083
Cdd:TIGR04523 99 ---------NKLNSDLSKINSEIKNdkeqKNKLEVELNKLEKQKKENKKNIdkflteikkkEKELEKLNNKYNDLKKQKE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1084 E--------SYDIEDVRSRLSVEDLEHLNEDGELwFAYEGLKKATRVLES---HFQSQKDCYEKEIEALNFKVVHLSQEI 1152
Cdd:TIGR04523 170 ElenelnllEKEKLNIQKNIDKIKNKLLKLELLL-SNLKKKIQKNKSLESqisELKKQNNQLKDNIEKKQQEINEKTTEI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1153 N----HLQKLFREENDINESIRHEVTRLTSENMMIPD-------FKQQISELEKQK-QDLEIRLNEQAEKMKGKLEELSN 1220
Cdd:TIGR04523 249 SntqtQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKElekqlnqLKSEISDLNNQKeQDWNKELKSELKNQEKKLEEIQN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1221 QLHRSQE---EEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELD 1297
Cdd:TIGR04523 329 QISQNNKiisQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ 408
|
410 420
....*....|....*....|
gi 767984698 1298 MKDRVIKKLQDQVKTLSKTI 1317
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEI 428
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
863-1314 |
2.00e-07 |
|
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: 56.34 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 863 VQRLQKKLEDQNKEnhgLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYR---DAVEEKLAKLQKHNSE 939
Cdd:pfam01576 403 SEHKRKKLEGQLQE---LQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSkdvSSLESQLQDTQELLQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 940 LETQK----------EQIQLKLQEKTEELKEKMDNLTK-------QLFDDVQKEERQRMLLEKSFELK---TQDYEKQIQ 999
Cdd:pfam01576 480 ETRQKlnlstrlrqlEDERNSLQEQLEEEEEAKRNVERqlstlqaQLSDMKKKLEEDAGTLEALEEGKkrlQRELEALTQ 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1000 SLKEEIKA---LKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMS 1076
Cdd:pfam01576 560 QLEEKAAAydkLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRAL 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1077 EITKQLLESYD----IEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQS---QKDCYEKEIEA-----LNFK 1144
Cdd:pfam01576 640 SLARALEEALEakeeLERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEmktQLEELEDELQAtedakLRLE 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1145 VVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNE-----------------Q 1207
Cdd:pfam01576 720 VNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKEleaqidaankgreeavkQ 799
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1208 AEKMKGKLEELSNQL---HRSQEEEGTQRKaleaQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETE-----SEVKCN-- 1277
Cdd:pfam01576 800 LKKLQAQMKDLQRELeeaRASRDEILAQSK----ESEKKLKNLEAELLQLQEDLAASERARRQAQQErdelaDEIASGas 875
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 767984698 1278 ----FRQEASRLTLENRDLEEELD--------MKDRViKKLQDQVKTLS 1314
Cdd:pfam01576 876 gksaLQDEKRRLEARIAQLEEELEeeqsntelLNDRL-RKSTLQVEQLT 923
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
867-1157 |
4.00e-07 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 54.05 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 867 QKKLEDQNKenHGLVEKLTSLAALRAGDVEK-IQKLEAELEK------AAThrrnyeekgkRYRDAVEEKLAKLQKHNSE 939
Cdd:pfam15905 66 QKNLKESKD--QKELEKEIRALVQERGEQDKrLQALEEELEKveaklnAAV----------REKTSLSASVASLEKQLLE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 940 LETQKEQIQLKLQEKTEelKEKMDNLTKQLF---DDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQ 1016
Cdd:pfam15905 134 LTRVNELLKAKFSEDGT--QKKMSSLSMELMklrNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1017 HLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQllesydIEDVRSRLS 1096
Cdd:pfam15905 212 KEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQ------IKDLNEKCK 285
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767984698 1097 VedLEHLNEDgelwfayeglkkatrvLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQK 1157
Cdd:pfam15905 286 L--LESEKEE----------------LLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
896-1296 |
4.29e-07 |
|
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: 55.18 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 896 EKIQKLEAELEKAathrrnyeekgKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKT------EELKEKMDNlTKQL 969
Cdd:pfam01576 5 EEMQAKEEELQKV-----------KERQQKAESELKELEKKHQQLCEEKNALQEQLQAETelcaeaEEMRARLAA-RKQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 970 FDDV---------QKEER-QRMLLEKsfelktQDYEKQIQSLKEEIKALKDEKMQLQHlvegEHVTSDGlkaevarlskq 1039
Cdd:pfam01576 73 LEEIlhelesrleEEEERsQQLQNEK------KKMQQHIQDLEEQLDEEEAARQKLQL----EKVTTEA----------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1040 vkTISEFEKEIELLQAQKIDVEKhvqsQKREMREKMSEITKQLLESYDIEDVRSRLS------VEDLE-HLNEDGELWFA 1112
Cdd:pfam01576 132 --KIKKLEEDILLLEDQNSKLSK----ERKLLEERISEFTSNLAEEEEKAKSLSKLKnkheamISDLEeRLKKEEKGRQE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1113 YEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREE----NDINESIRHEVTRLTSENMMIPDFKQ 1188
Cdd:pfam01576 206 LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEEtaqkNNALKKIRELEAQISELQEDLESERA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1189 QISELEKQKQDLEirlnEQAEKMKGKLEEL-----SNQLHRSQ-EEEGTQ-RKALEAQNEIHtkeKEKLIDKIQEMQEAS 1261
Cdd:pfam01576 286 ARNKAEKQRRDLG----EELEALKTELEDTldttaAQQELRSKrEQEVTElKKALEEETRSH---EAQLQEMRQKHTQAL 358
|
410 420 430
....*....|....*....|....*....|....*
gi 767984698 1262 DHLKKQFETESEVKCNFRQEASRLTLENRDLEEEL 1296
Cdd:pfam01576 359 EELTEQLEQAKRNKANLEKAKQALESENAELQAEL 393
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
866-1296 |
4.37e-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: 55.34 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 866 LQKKLEDQNKENHGLVEKLTSLAALRAGDVEkiqkLEAELEKAATHRR------NYEEKGKRYRDAVEEKLAKLQKHNSE 939
Cdd:COG3096 294 LFGARRQLAEEQYRLVEMARELEELSARESD----LEQDYQAASDHLNlvqtalRQQEKIERYQEDLEELTERLEEQEEV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 940 LETQKEQiQLKLQEKTEELKEKMDNLTKQLfDDVQK--EERQRMLLEksfelktqdYEKQIQSLKEEikalkdekmqlQH 1017
Cdd:COG3096 370 VEEAAEQ-LAEAEARLEAAEEEVDSLKSQL-ADYQQalDVQQTRAIQ---------YQQAVQALEKA-----------RA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1018 LVEGEHVTSDGLKAEVARLSKQVKTISEfekeiELLQA-QKIDVEkhvQSQKREMREKMseitkQLLESYDIEDVRSRls 1096
Cdd:COG3096 428 LCGLPDLTPENAEDYLAAFRAKEQQATE-----EVLELeQKLSVA---DAARRQFEKAY-----ELVCKIAGEVERSQ-- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1097 vedlehlnedgelwfAYEglkKATRVLESHfQSQKDCYEKEiEALNFKVVHLSQEINHLQKLFREENDINESIRHEVtrl 1176
Cdd:COG3096 493 ---------------AWQ---TARELLRRY-RSQQALAQRL-QQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQL--- 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1177 tSENMMIPDFKqqiSELEKQKQDLEIRLNEQAEKmkgkleelSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLiDKIQE 1256
Cdd:COG3096 550 -DAAEELEELL---AELEAQLEELEEQAAEAVEQ--------RSELRQQLEQLRARIKELAARAPAWLAAQDAL-ERLRE 616
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 767984698 1257 M--------QEASDHLKKQFETESEVKcnfrQEASRLTLENRDLEEEL 1296
Cdd:COG3096 617 QsgealadsQEVTAAMQQLLEREREAT----VERDELAARKQALESQI 660
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
927-1345 |
5.00e-07 |
|
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: 55.05 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 927 EEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNL------------TKQLFDDVQKEERQRMLLEKsfelKTQDY 994
Cdd:TIGR00606 590 RDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsqdeesdLERLKEEIEKSSKQRAMLAG----ATAVY 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 995 EKQIQSLKEEI--------------KALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEF----EKEIELLQAQ 1056
Cdd:TIGR00606 666 SQFITQLTDENqsccpvcqrvfqteAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLapgrQSIIDLKEKE 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1057 KIDVEKHVQSQKREMREKMSEITKQ--LLESYDIEDVRSRLSVED------LEHLNEDGELWFAYEGLKKATRVLESHFQ 1128
Cdd:TIGR00606 746 IPELRNKLQKVNRDIQRLKNDIEEQetLLGTIMPEEESAKVCLTDvtimerFQMELKDVERKIAQQAAKLQGSDLDRTVQ 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1129 SQKdcyeKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQA 1208
Cdd:TIGR00606 826 QVN----QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLI 901
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1209 EKMKGKLEELsnqlhrSQEEEGTQRKALEAQNEIHTKEKEKLI--DKIQEM------------------QEASDHLKKQF 1268
Cdd:TIGR00606 902 REIKDAKEQD------SPLETFLEKDQQEKEELISSKETSNKKaqDKVNDIkekvknihgymkdienkiQDGKDDYLKQK 975
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1269 ETE------SEVKCNFRQEasRLTLENRDLEEELDMKDRVIKKLQDQVkTLSKTIGKANDVHSSsgPKEYLGMLQYKRED 1342
Cdd:TIGR00606 976 ETElntvnaQLEECEKHQE--KINEDMRLMRQDIDTQKIQERWLQDNL-TLRKRENELKEVEEE--LKQHLKEMGQMQVL 1050
|
...
gi 767984698 1343 EAK 1345
Cdd:TIGR00606 1051 QMK 1053
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
895-1237 |
7.37e-07 |
|
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: 54.19 E-value: 7.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 895 VEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQ 974
Cdd:COG5185 235 LKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 975 KEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKdekmqlqhlvegehvtsDGLKAEVARLSKQVKTISEfEKEIELLQ 1054
Cdd:COG5185 315 EEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQ-----------------ESLTENLEAIKEEIENIVG-EVELSKSS 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1055 AQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDgelwfayegLKKATRVLEShFQSQKDCY 1134
Cdd:COG5185 377 EELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQ---------IEQATSSNEE-VSKLLNEL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1135 EKEIEalnfKVVHLSQEiNHLQKLFREENDINESIRHEVTRLTSENMMIpdfKQQISELEKQKQDLEIRLNEQAEKMKGK 1214
Cdd:COG5185 447 ISELN----KVMREADE-ESQSRLEEAYDEINRSVRSKKEDLNEELTQI---ESRVSTLKATLEKLRAKLERQLEGVRSK 518
|
330 340
....*....|....*....|...
gi 767984698 1215 LEELSNQLHRSQEEEGTQRKALE 1237
Cdd:COG5185 519 LDQVAESLKDFMRARGYAHILAL 541
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
945-1292 |
7.75e-07 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 53.99 E-value: 7.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 945 EQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERqrmlleKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHV 1024
Cdd:pfam09731 44 EEVVLYALGEDPPLAPKPKTFRPLQPSVVSAVTG------ESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1025 TSDglKAEVARLSKQVKTISEFEKEIELLQAQ--------KIDVEKHVQSQKREM------REKMSEITKQLLESYDIED 1090
Cdd:pfam09731 118 QLP--KSEQEKEKALEEVLKEAISKAESATAVakeakddaIQAVKAHTDSLKEASdtaeisREKATDSALQKAEALAEKL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1091 VRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINESIR 1170
Cdd:pfam09731 196 KEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1171 HEVTRLTSE-NMMIPDFKQQISELEKQKQDL----EIRLNEQAEKMKGKLEELSNQL------HRSQEEEGTQRKALEAQ 1239
Cdd:pfam09731 276 EDNLLSNDDlNSLIAHAHREIDQLSKKLAELkkreEKHIERALEKQKEELDKLAEELsarleeVRAADEAQLRLEFERER 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 767984698 1240 NEIHTKEKEKLIDKIQEMQEA-SDHLKKQFET-ESEVKCNFRQEASRLTLENRDL 1292
Cdd:pfam09731 356 EEIRESYEEKLRTELERQAEAhEEHLKDVLVEqEIELQREFLQDIKEKVEEERAG 410
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
884-1081 |
7.82e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 884 LTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKEKMD 963
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID-KLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 964 NLTKQL---FDDVQKEERQRMLLE-----KSFE--LKTQDYEKQI----QSLKEEIKALKDEKMQLQHLVEGEHVTSDGL 1029
Cdd:COG3883 83 ERREELgerARALYRSGGSVSYLDvllgsESFSdfLDRLSALSKIadadADLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767984698 1030 KAEVARLSKQV-KTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQ 1081
Cdd:COG3883 163 KAELEAAKAELeAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
858-1245 |
9.27e-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: 53.82 E-value: 9.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 858 QLTYRVQRLQKKLEDQNKEnhglvekLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEklakLQKHN 937
Cdd:TIGR00618 532 RGEQTYAQLETSEEDVYHQ-------LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVR----LQDLT 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 938 SELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLK--EEIKALKDEKMQ- 1014
Cdd:TIGR00618 601 EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALsiRVLPKELLASRQl 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1015 ----LQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQ----AQKIDVEKHVQSQKREMREKMSEITKQLLESY 1086
Cdd:TIGR00618 681 alqkMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIEnassSLGSDLAAREDALNQSLKELMHQARTVLKART 760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1087 DIEDVRSRLSVEDLEHLNE----DGELWF---AYEGLKKATRVLESHFQSQKDCYEkeiEALNFKVVHLSQEINHLQKLF 1159
Cdd:TIGR00618 761 EAHFNNNEEVTAALQTGAElshlAAEIQFfnrLREEDTHLLKTLEAEIGQEIPSDE---DILNLQCETLVQEEEQFLSRL 837
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1160 REendiNESIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLeIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQ 1239
Cdd:TIGR00618 838 EE----KSATLGEITHQLLK---YEECSKQLAQLTQEQAKI-IQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRLA 909
|
....*.
gi 767984698 1240 NEIHTK 1245
Cdd:TIGR00618 910 NQSEGR 915
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
868-1345 |
9.79e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 9.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 868 KKLEDQNKENHGLVEKLTSL--AALRAGDVEKIQKLE--AELEKAATHRRNYEEK----GKRYRDAVEEKLAKLQKHNSE 939
Cdd:PTZ00121 1098 GKAEEAKKTETGKAEEARKAeeAKKKAEDARKAEEARkaEDARKAEEARKAEDAKrveiARKAEDARKAEEARKAEDAKK 1177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 940 LETQKEQIQLKlqeKTEELKEKmdnltkqlfDDVQKEERQRMLLE--KSFELKTQDYEKQIQSLKEEIKALKDE----KM 1013
Cdd:PTZ00121 1178 AEAARKAEEVR---KAEELRKA---------EDARKAEAARKAEEerKAEEARKAEDAKKAEAVKKAEEAKKDAeeakKA 1245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1014 QLQHLVEGEHVTSDGLKAEVARLSKQVKTiSEFEKEIELLQAQkiDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRS 1093
Cdd:PTZ00121 1246 EEERNNEEIRKFEEARMAHFARRQAAIKA-EEARKADELKKAE--EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK 1322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1094 RLSvedlEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKeiealnfkvvhlSQEINHLQKLFREEndinESIRHEV 1173
Cdd:PTZ00121 1323 KAE----EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA------------AEEKAEAAEKKKEE----AKKKADA 1382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1174 TRLTSEnmmipdfkqqiselEKQKQDleiRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDK 1253
Cdd:PTZ00121 1383 AKKKAE--------------EKKKAD---EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1254 IQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVHSSSGPK--- 1330
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKkad 1525
|
490
....*....|....*
gi 767984698 1331 EYLGMLQYKREDEAK 1345
Cdd:PTZ00121 1526 EAKKAEEAKKADEAK 1540
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
915-1250 |
1.29e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.22 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 915 YEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKEKMDNLtkqlfddvqKEERQRMLleksfelktqdy 994
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRD-ELNAQVKELREEAQEL---------REKRDELN------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 995 eKQIQSLKEEIKALKDEKMQLQHLVegehvtsDGLKAEVARLSKQVKTISEFEKEIELLQaQKIDVEKHVQSQKREMREK 1074
Cdd:COG1340 71 -EKVKELKEERDELNEKLNELREEL-------DELRKELAELNKAGGSIDKLRKEIERLE-WRQQTEVLSPEEEKELVEK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1075 MSEITKQLlesydiedvrsrlsvEDLEHLNEdgelwfayegLKKATRVLESHFQSQKdcyeKEIEALNFKVVHLSQEINH 1154
Cdd:COG1340 142 IKELEKEL---------------EKAKKALE----------KNEKLKELRAELKELR----KEAEEIHKKIKELAEEAQE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1155 L----QKLFREENDINESIR--HEvtrltsenmMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNqLHRSQEE 1228
Cdd:COG1340 193 LheemIELYKEADELRKEADelHK---------EIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRA-LKREKEK 262
|
330 340
....*....|....*....|..
gi 767984698 1229 EGTQRKALEAQNEIhtKEKEKL 1250
Cdd:COG1340 263 EELEEKAEEIFEKL--KKGEKL 282
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
864-1229 |
1.33e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 53.52 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 864 QRLQKKLEDQNKENHGLVEKLTSLAALRagDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVE--EKLAKLQKHNSELE 941
Cdd:TIGR01612 1325 KELQKNLLDAQKHNSDINLYLNEIANIY--NILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDksEKLIKKIKDDINLE 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 942 TQKEQIQLKLQE-------------KTEELKEKMDNLTkqLFDDVQKEERQRMLLEKSFEL---KTQ------------D 993
Cdd:TIGR01612 1403 ECKSKIESTLDDkdidecikkikelKNHILSEESNIDT--YFKNADENNENVLLLFKNIEMadnKSQhilkikkdnatnD 1480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 994 YEKQIQSLKEEI---KALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQV------KTISEFEKEIELLQAQKIDVEKHV 1064
Cdd:TIGR01612 1481 HDFNINELKEHIdksKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYsalaikNKFAKTKKDSEIIIKEIKDAHKKF 1560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1065 QSQKREMREKMSEITKqllESYDIEDvrsrlsveDLEHLNEDGElwfAYEGLKKATRVLESHF-------QSQKDCYeKE 1137
Cdd:TIGR01612 1561 ILEAEKSEQKIKEIKK---EKFRIED--------DAAKNDKSNK---AAIDIQLSLENFENKFlkisdikKKINDCL-KE 1625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1138 IEALNFKVVHLSqeINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEE 1217
Cdd:TIGR01612 1626 TESIEKKISSFS--IDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIE 1703
|
410
....*....|..
gi 767984698 1218 LSNQLHRSQEEE 1229
Cdd:TIGR01612 1704 KIKEIAIANKEE 1715
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
927-1274 |
1.41e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 53.15 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 927 EEKLAKLQKHNSELETQKEqiqlKLQEKTEELKE----------KMDNLTKQLfdDVQKEERQRmlLEKS---FELKTQD 993
Cdd:pfam05622 20 DQQVSLLQEEKNSLQQENK----KLQERLDQLESgddsgtpggkKYLLLQKQL--EQLQEENFR--LETArddYRIKCEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 994 YEKQI----------QSLKEEIKALKDEKMQLQHlvegehvTSDGLK---AEVARLSKQVKTISEFEKEIELLQ------ 1054
Cdd:pfam05622 92 LEKEVlelqhrneelTSLAEEAQALKDEMDILRE-------SSDKVKkleATVETYKKKLEDLGDLRRQVKLLEernaey 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1055 -AQKIDVEK----------HVQSQKREMRE---KMSEIT----------KQLLESYD-IEDVRSRLSVE--DLEHLNEDG 1107
Cdd:pfam05622 165 mQRTLQLEEelkkanalrgQLETYKRQVQElhgKLSEESkkadklefeyKKLEEKLEaLQKEKERLIIErdTLRETNEEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1108 ELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNF-----------KVVHLSQEINHLQKLFREENDINESIRhEVTRL 1176
Cdd:pfam05622 245 RCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIreklirlqhenKMLRLGQEGSYRERLTELQQLLEDANR-RKNEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1177 TSENMMIpdfKQQISELEKQKQDLEIRLNEQAEK------MKGKLEELSNQLHRSQEEEGTQRKALE-----AQNEIHTK 1245
Cdd:pfam05622 324 ETQNRLA---NQRILELQQQVEELQKALQEQGSKaedsslLKQKLEEHLEKLHEAQSELQKKKEQIEelepkQDSNLAQK 400
|
410 420 430
....*....|....*....|....*....|..
gi 767984698 1246 E---KEKLIDKIQEMQEASDHLKKQFETESEV 1274
Cdd:pfam05622 401 IdelQEALRKKDEDMKAMEERYKKYVEKAKSV 432
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
862-1105 |
1.50e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 862 RVQRLQKKLEDQNKENHGLVEKLTSL----AALRAGDVEKIQKLEAELEKAatHRRNYEEKGKRYRdaVEEKLAKLQKHN 937
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELAELlkelEELGFESVEELEERLKELEPF--YNEYLELKDAEKE--LEREEKELKKLE 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 938 SELETQKEQIQLKLQEkTEELKEKMDNLtKQLFDDVQKEERQRMLLEKSFELKtqdyekqiqSLKEEIKALKDEKmqlqh 1017
Cdd:PRK03918 626 EELDKAFEELAETEKR-LEELRKELEEL-EKKYSEEEYEELREEYLELSRELA---------GLRAELEELEKRR----- 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1018 lvegehvtsDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEkhvqsqkrEMREKMSEItKQLLESYDIEDVrSRLSV 1097
Cdd:PRK03918 690 ---------EEIKKTLEKLKEELEEREKAKKELEKLEKALERVE--------ELREKVKKY-KALLKERALSKV-GEIAS 750
|
....*...
gi 767984698 1098 EDLEHLNE 1105
Cdd:PRK03918 751 EIFEELTE 758
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
931-1141 |
1.68e-06 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 52.84 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 931 AKLQKHNSELETQKEQIQLKLQEKTEELKEKmdnltkqlFDDVQKEERQRMLLEKSFELKtqDYEKQIQSLKEEIKALKD 1010
Cdd:pfam09731 294 REIDQLSKKLAELKKREEKHIERALEKQKEE--------LDKLAEELSARLEEVRAADEA--QLRLEFEREREEIRESYE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1011 EKMQLQhLVEGEHVTSDGLKAEVArlskqvktisefEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLEsydIED 1090
Cdd:pfam09731 364 EKLRTE-LERQAEAHEEHLKDVLV------------EQEIELQREFLQDIKEKVEEERAGRLLKLNELLANLKG---LEK 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767984698 1091 VRSRLSVEDLEHLNEDgELWFAYEGLKKATRvlESHFQSQKDCYEKEIEAL 1141
Cdd:pfam09731 428 ATSSHSEVEDENRKAQ-QLWLAVEALRSTLE--DGSADSRPRPLVRELKAL 475
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
771-1008 |
2.03e-06 |
|
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: 52.75 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 771 LQRKKFLR-ERRAALIIQQYFRGQQTVSLYQLIRMATITMQAYSRGFLARRRyrKMLEEHKAVILQKYARAWLARRRFQS 849
Cdd:TIGR02168 730 ALRKDLARlEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE--AEIEELEAQIEQLKEELKALREALDE 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 850 IRRFV--LNI---QLTYRVQRLQKKLEDQNKENHGLV-------EKLTSLAALRAGDVEKIQKLEAELEKA--------- 908
Cdd:TIGR02168 808 LRAELtlLNEeaaNLRERLESLERRIAATERRLEDLEeqieelsEDIESLAAEIEELEELIEELESELEALlneraslee 887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 909 --ATHRRNYEEKGKRYRDaVEEKLAKLQKHNSELETQKEQIQLKLQekteELKEKMDNLTKQLFDDVQKEERQRMLLEKS 986
Cdd:TIGR02168 888 alALLRSELEELSEELRE-LESKRSELRRELEELREKLAQLELRLE----GLEVRIDNLQERLSEEYSLTLEEAEALENK 962
|
250 260
....*....|....*....|..
gi 767984698 987 FELKTQDYEKQIQSLKEEIKAL 1008
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKEL 984
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
862-1023 |
2.47e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 52.38 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 862 RVQRLQKKLEDQNKENHGLVEKLtSLAALRAGDVEkiQKLEaELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELE 941
Cdd:pfam05622 305 RLTELQQLLEDANRRKNELETQN-RLANQRILELQ--QQVE-ELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 942 TQKEQI-------QLKLQEKTEELKEkmdNLTKQLFDDVQKEERQRMLLEKSFE-LKTQDyEKQIQSLKEEIKALKD--- 1010
Cdd:pfam05622 381 KKKEQIeelepkqDSNLAQKIDELQE---ALRKKDEDMKAMEERYKKYVEKAKSvIKTLD-PKQNPASPPEIQALKNqll 456
|
170
....*....|...
gi 767984698 1011 EKMQLQHLVEGEH 1023
Cdd:pfam05622 457 EKDKKIEHLERDF 469
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
993-1261 |
2.48e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.45 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 993 DYEKQIQSLKEEIKALKDEKMQLQHLVEgehvtsdGLKAEVARLSKQVKTISEfekeiellQAQKIdvekhvQSQKREMR 1072
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELK-------ELAEKRDELNAQVKELRE--------EAQEL------REKRDELN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1073 EKMSEITKQLLESYD-IEDVRSRLSV--EDLEHLNEDGElwfAYEGLKKATRVLESHFQSQKDCYEKEIEALNfKVVHLS 1149
Cdd:COG1340 71 EKVKELKEERDELNEkLNELREELDElrKELAELNKAGG---SIDKLRKEIERLEWRQQTEVLSPEEEKELVE-KIKELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1150 QEINHLQKlfreENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQ---DLEIRLNEQAEKMKGKLEELSNQLHRSQ 1226
Cdd:COG1340 147 KELEKAKK----ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQelhEEMIELYKEADELRKEADELHKEIVEAQ 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 767984698 1227 EEEGTQRKAL-EAQNEIHtkEKEKLIDKIQEMQEAS 1261
Cdd:COG1340 223 EKADELHEEIiELQKELR--ELRKELKKLRKKQRAL 256
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
887-1082 |
4.60e-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: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 887 LAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQL------KLQEKTEELKE 960
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAleqelaALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 961 KMDNLTKQLfdDVQKEERQRMLLeKSFELKTQDYEKQIQSLKEEIKALKDEKMqLQHLVEGEHVTSDGLKAEVARLSKQV 1040
Cdd:COG4942 91 EIAELRAEL--EAQKEELAELLR-ALYRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767984698 1041 KTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQL 1082
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
862-1346 |
4.84e-06 |
|
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: 51.59 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 862 RVQRLQKKLEDQNKENHGLVEKLTSL------AALRAGDV-EKIQKLEAELEKAATH----------------------- 911
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQEKTELlveqgrLQLQADRHqEHIRARDSLIQSLATRleldgfergpfserqiknfhtlv 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 912 RRNYEEKGK---RYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFE 988
Cdd:TIGR00606 400 IERQEDEAKtaaQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 989 LKTQDYE-------KQIQSLKEEIKALKDEKMQLqhlvegehvtsDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVE 1061
Cdd:TIGR00606 480 LRKAERElskaeknSLTETLKKEVKSLQNEKADL-----------DRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKD 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1062 KHVQSQKREMREKMSEI------TKQLLESYDIEDVRSRLSVEDLEHLNEDGElwfAYEGLKKATRVLESHFQSQKDCYE 1135
Cdd:TIGR00606 549 EQIRKIKSRHSDELTSLlgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELA---SLEQNKNHINNELESKEEQLSSYE 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1136 KEI------EALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQAE 1209
Cdd:TIGR00606 626 DKLfdvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLR 705
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1210 KMKGKLEELSNQLHRSQEE-EGTQRKALEAQNEIHTKEKEklidkIQEMQEASDHLKKQFEtesEVKCNFRQEASRLTLE 1288
Cdd:TIGR00606 706 LAPDKLKSTESELKKKEKRrDEMLGLAPGRQSIIDLKEKE-----IPELRNKLQKVNRDIQ---RLKNDIEEQETLLGTI 777
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767984698 1289 NRDLE--EELDMKDRVIKKLQDQVKTLSKTIGK-ANDVHSSSGPKEYLGMLQYKREDEAKL 1346
Cdd:TIGR00606 778 MPEEEsaKVCLTDVTIMERFQMELKDVERKIAQqAAKLQGSDLDRTVQQVNQEKQEKQHEL 838
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1150-1317 |
4.92e-06 |
|
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: 49.54 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1150 QEINHLQKLFREENDINEsIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNE---QAEKMKGKLEELSNQLHRSQ 1226
Cdd:COG1579 4 EDLRALLDLQELDSELDR-LEHRLKELPAE---LAELEDELAALEARLEAAKTELEDlekEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1227 EEEGTQR-----KALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQF-ETESEVKcnfrQEASRLTLENRDLEEELDMKD 1300
Cdd:COG1579 80 EQLGNVRnnkeyEALQKEIESLKRRISDLEDEILELMERIEELEEELaELEAELA----ELEAELEEKKAELDEELAELE 155
|
170
....*....|....*..
gi 767984698 1301 RVIKKLQDQVKTLSKTI 1317
Cdd:COG1579 156 AELEELEAEREELAAKI 172
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1135-1269 |
5.19e-06 |
|
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: 49.54 E-value: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1135 EKEIEALNFKVVHLSQEINHLQKLFRE-ENDInESIRHEVTRLTSENMMIPDFKQ------QISELEKQKQDLE---IRL 1204
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRlELEI-EEVEARIKKYEEQLGNVRNNKEyealqkEIESLKRRISDLEdeiLEL 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767984698 1205 NEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEA-SDHLKKQFE 1269
Cdd:COG1579 116 MERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKiPPELLALYE 181
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
850-1169 |
5.66e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 850 IRRFVLNIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEK 929
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 930 LAKLQKHNSELETQKEQIQlKLQEKTEELKEKMDNLTKQLfddvQKEERQRMLLEKSFELKtqdyEKQIQSLKEEIKALK 1009
Cdd:COG4372 93 QAELAQAQEELESLQEEAE-ELQEELEELQKERQDLEQQR----KQLEAQIAELQSEIAER----EEELKELEEQLESLQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1010 DEKMQLQhlVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQaQKIDVEKHVQSQKREMREKMSEITKQLLESYDIE 1089
Cdd:COG4372 164 EELAALE--QELQALSEAEAEQALDELLKEANRNAEKEEELAEAE-KLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1090 DVRsrlSVEDLEHLNEDGELWFAYEGLKKATRVLESHfqsqkdcyEKEIEALNFKVVHLSQEINHLQKLFREENDINESI 1169
Cdd:COG4372 241 ALE---LEEDKEELLEEVILKEIEELELAILVEKDTE--------EEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
897-1307 |
7.31e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.98 E-value: 7.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 897 KIQKLEAELEKAATHR----------RNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLT 966
Cdd:pfam10174 290 KIDQLKQELSKKESELlalqtkletlTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 967 -------------KQLFDDVQKEERQRMLLEKSFE-LKTQ--DYEKQIQSLKEEIKALkdekmqlqhlvEGEHVTSDglk 1030
Cdd:pfam10174 370 dlteekstlageiRDLKDMLDVKERKINVLQKKIEnLQEQlrDKDKQLAGLKERVKSL-----------QTDSSNTD--- 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1031 aevARLSKQVKTISEFEKEIELLQAQKidvekhvqsqKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDGELW 1110
Cdd:pfam10174 436 ---TALTTLEEALSEKERIIERLKEQR----------EREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLK 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1111 -----FAYEGLKKatrvlESHFQSQKDCYEKEIEALNfKVVHLSQEINHLQKLFREENDINESIRH---EVTRLTSENMm 1182
Cdd:pfam10174 503 ehassLASSGLKK-----DSKLKSLEIAVEQKKEECS-KLENQLKKAHNAEEAVRTNPEINDRIRLleqEVARYKEESG- 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1183 ipdfKQQiSELEKQKQDLEIRLNEQAEKMK--GKLEELSNQLHRSQEEEGTQRKALeaQNEIHTKEKEKLID-KIQEMQE 1259
Cdd:pfam10174 576 ----KAQ-AEVERLLGILREVENEKNDKDKkiAELESLTLRQMKEQNKKVANIKHG--QQEMKKKGAQLLEEaRRREDNL 648
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 767984698 1260 ASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQ 1307
Cdd:pfam10174 649 ADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLR 696
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
860-1074 |
7.42e-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: 50.15 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 860 TYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSE 939
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 940 LETQKEQI--QLKLQEKTEELKEKMDNLTKQLFDDVQKeeRQRMLLEKSFELKTQDYE-----KQIQSLKEEIKALKDEK 1012
Cdd:COG4942 99 LEAQKEELaeLLRALYRLGRQPPLALLLSPEDFLDAVR--RLQYLKYLAPARREQAEElradlAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767984698 1013 MQLQHLVEGEHVTSDGLKAEVARLSKQV-KTISEFEKEIELLQAQKIDVEKHVQSQKREMREK 1074
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLeKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
862-1081 |
9.43e-06 |
|
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: 50.84 E-value: 9.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 862 RVQRLQKKLEDQNKENHGLVEKLTSLAAlragDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELE 941
Cdd:TIGR02169 792 RIPEIQAELSKLEEEVSRIEARLREIEQ----KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 942 TQKEQIQLK---LQEKTEELKEKMDNLTKQLfddVQKEERQRMLLEKSFELKTQDYE--KQIQSLKEEIKALKDEKMQLQ 1016
Cdd:TIGR02169 868 EELEELEAAlrdLESRLGDLKKERDELEAQL---RELERKIEELEAQIEKKRKRLSElkAKLEALEEELSEIEDPKGEDE 944
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767984698 1017 HLVEGEHVTSDgLKAEVARLSKQV--------KTISEFEkeiELLQAQKIDVEKH--VQSQKREMREKMSEITKQ 1081
Cdd:TIGR02169 945 EIPEEELSLED-VQAELQRVEEEIralepvnmLAIQEYE---EVLKRLDELKEKRakLEEERKAILERIEEYEKK 1015
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
990-1261 |
9.72e-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: 49.76 E-value: 9.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 990 KTQDYEKQIQSLKEEIKALKDEKMQLQhlvEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKR 1069
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALK---KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1070 EMREKMSEITKQLLESYDIEDvRSRLsvedlehlnedgELWFAYEGLKKATRVLEshfqsqkdcYEKEIEAlnfkvvHLS 1149
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGR-QPPL------------ALLLSPEDFLDAVRRLQ---------YLKYLAP------ARR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1150 QEINHLQKLFREENDINESIRHEVTRLtsenmmipdfKQQISELEKQKQDLEIRLNEQaekmkgklEELSNQLHRSQEEE 1229
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAEL----------EALLAELEEERAALEALKAER--------QKLLARLEKELAEL 211
|
250 260 270
....*....|....*....|....*....|..
gi 767984698 1230 GTQRKALEAQNEIHTKEKEKLIDKIQEMQEAS 1261
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
929-1119 |
1.01e-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: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 929 KLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKqLFDDVQKEERQRmlleKSFELKTQDYEKQIQSLKEEIKAL 1008
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEA-AKTELEDLEKEI----KRLELEIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1009 KDEK--MQLQHLVEgehvtsdGLKAEVARLSKQvktISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLEsy 1086
Cdd:COG1579 86 RNNKeyEALQKEIE-------SLKRRISDLEDE---ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE-- 153
|
170 180 190
....*....|....*....|....*....|....
gi 767984698 1087 dIEDVRSRLSVEDLEHLNE-DGELWFAYEGLKKA 1119
Cdd:COG1579 154 -LEAELEELEAEREELAAKiPPELLALYERIRKR 186
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
853-1016 |
1.09e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 49.42 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 853 FVLNIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYeEKGKRYRDAVEEKLAK 932
Cdd:pfam15905 176 MAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQV-EKYKLDIAQLEELLKE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 933 LQKHNSELetqkeqiQLKLQEKTEELKEKMDNLTKQLfdDVQKEERQRMLLEksFELKTQDYEKQIQSLKEEIKALKDEK 1012
Cdd:pfam15905 255 KNDEIESL-------KQSLEEKEQELSKQIKDLNEKC--KLLESEKEELLRE--YEEKEQTLNAELEELKEKLTLEEQEH 323
|
....
gi 767984698 1013 MQLQ 1016
Cdd:pfam15905 324 QKLQ 327
|
|
| Myo5p-like_CBD_Rasip1 |
cd15472 |
cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 ... |
1368-1647 |
1.23e-05 |
|
cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 (Rasip1 or RAIN) is an effector of the small G protein Rap1 and plays an important role in endothelial junction stabilization. Rasip1, like afadin, is a multi domain protein, that contains beside a myosin5-like CBD, a Ras-associated domain and a PDZ domain.
Pssm-ID: 271256 Cd Length: 366 Bit Score: 49.58 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1368 PAHILFMCVRYADS-----------LNDANMLKSLMNSTINGIKQVVKEHLE--------------DFEMLSFWLSNT-- 1420
Cdd:cd15472 25 PAFLLCLCIQHSAThfepghfgkllLKIAKRIQEIVWEKTKELAEKQPEHQDpaslsllsiaelapDLQPLLFWMSNSie 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1421 --CHFLNCLKQYSGE-EEFMKHNSPQQNKNCLNNfDLSEYRQILSDVAIRIYHQFIIIMEKNIQPIIvPGMLE------- 1490
Cdd:cd15472 105 llYFIQQKVPLYEQSmEEELDVGSKESLLSSTLT-ASEEAMTVLEEVIMYTFQQCVYYLTKTLYVAL-PALLDsnpftae 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1491 -YESLQGISGLkPTGFRKrsssiddtdgytMTSVLQ---QLsyfyTTMCQngLDPELVRQAVKQLFFLIGAVTLNSLFLR 1566
Cdd:cd15472 183 eRESWSGGSRL-PEGVRR------------VLEIYQatlDL----LRQYQ--VHPEIASQMFAYLFFFSNASLFNQLMEK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1567 KDMCSC---RKGMQIRCNISYLEEWLKDKNLqNSLAKETLEPLSQAAWLLQVKKTT--DSDAKEIYERCTSLSAVQIIKI 1641
Cdd:cd15472 244 GSGGGFfqwSRGVQIRANLDLLLDWLQGAGL-GDLAEEFFRKLSSTVNLLATPKEQllQMSWSSLRAEFPALNPAQLHHL 322
|
....*.
gi 767984698 1642 LNSYTP 1647
Cdd:cd15472 323 LRQYQL 328
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
543-652 |
1.46e-05 |
|
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: 47.34 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 543 NTSFVIQHFAD-------KVEYKCEGFLEKNRDTVYDMLVEILraskfhlcanffqenptppsPFGSMITVksAKQVIKP 615
Cdd:cd01363 68 TMKGVIPYLASvafnginKGETEGWVYLTEITVTLEDQILQAN--------------------PILEAFGN--AKTTRNE 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 767984698 616 NS----KHFRTTV---GS-KFRSSLYLLMETLNATTPHYVRCIKP 652
Cdd:cd01363 126 NSsrfgKFIEILLdiaGFeIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
888-1049 |
1.56e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.86 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 888 AALRAGDVEKIQKLEAELEKAATH-RRNYEEKGKRYRDaVEEKLAKLQKHNSELEtqkeqiqlklqEKTEELKEKMDNLT 966
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEHeERELTEEEEEIRR-LEEQVERLEAEVEELE-----------AELEEKDERIERLE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 967 KQLfDDVQKEERQRMLLEKsfELKTQDYE-----KQIQSLKEEIKALKDEKMQLQHLVEGEHvtSDGLKAevarlskqVK 1041
Cdd:COG2433 448 REL-SEARSEERREIRKDR--EISRLDREierleRELEEERERIEELKRKLERLKELWKLEH--SGELVP--------VK 514
|
....*...
gi 767984698 1042 TISEFEKE 1049
Cdd:COG2433 515 VVEKFTKE 522
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
827-1296 |
1.68e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 827 EEHKAVILQKYARAWLARRRFQSIRRFvlniqltYRVQRlQKKLEDQNKENHGLVEKLTSLAAlragDVEKIQKLEAELE 906
Cdd:PRK04863 753 EELEKAVVVKIADRQWRYSRFPEVPLF-------GRAAR-EKRIEQLRAEREELAERYATLSF----DVQKLQRLHQAFS 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 907 K-AATHRrnyeekgkryrdAV------EEKLAKLQKHNSELETQKEQiqlkLQEKTEELKEKMDNLtKQLFDDVQKEERQ 979
Cdd:PRK04863 821 RfIGSHL------------AVafeadpEAELRQLNRRRVELERALAD----HESQEQQQRSQLEQA-KEGLSALNRLLPR 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 980 RMLLEKsfelktQDYEKQIQSLKEEIKALKDEKMQL-QHlvegehvtsdglKAEVARLSKQVKTISEFEKEIELLQAQki 1058
Cdd:PRK04863 884 LNLLAD------ETLADRVEEIREQLDEAEEAKRFVqQH------------GNALAQLEPIVSVLQSDPEQFEQLKQD-- 943
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1059 dvekHVQSQKREMREKMseitkqllESYDIEDVRSRlsvedLEHlnedgelwFAYEglkkatrvleshfQSQKDCYEKei 1138
Cdd:PRK04863 944 ----YQQAQQTQRDAKQ--------QAFALTEVVQR-----RAH--------FSYE-------------DAAEMLAKN-- 983
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1139 EALNFKvvhLSQEINHLQklfREENDINESIRHEVTRLTSENMMIPDFK-------QQISELEKQKQDLEIRLNEQAE-K 1210
Cdd:PRK04863 984 SDLNEK---LRQRLEQAE---QERTRAREQLRQAQAQLAQYNQVLASLKssydakrQMLQELKQELQDLGVPADSGAEeR 1057
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1211 MKGKLEELSNQLHRSQeeegTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENR 1290
Cdd:PRK04863 1058 ARARRDELHARLSANR----SRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERR 1133
|
....*.
gi 767984698 1291 DLEEEL 1296
Cdd:PRK04863 1134 LHRREL 1139
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
973-1314 |
1.89e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.44 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 973 VQKEERQRMLLEKSFELKTQDYEKQ----IQSLKEEIKALKDekmqLQHLVEGEHVTSDGLKAE---VARLSKQ--VKTI 1043
Cdd:pfam10174 47 LRKEEAARISVLKEQYRVTQEENQHlqltIQALQDELRAQRD----LNQLLQQDFTTSPVDGEDkfsTPELTEEnfRRLQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1044 SEFE---KEIELLQAQKIDVEKHVQSQKREMrEKMSEITKQLLE----------SYDIEDVRSRLSVEDLEHLNE-DGEL 1109
Cdd:pfam10174 123 SEHErqaKELFLLRKTLEEMELRIETQKQTL-GARDESIKKLLEmlqskglpkkSGEEDWERTRRIAEAEMQLGHlEVLL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1110 WFAYEGLKKATRVLESHFQSQKD-----CYEKEIEALNFKVVHLSQEINHLQ---KLFREENDINESIRH------EVTR 1175
Cdd:pfam10174 202 DQKEKENIHLREELHRRNQLQPDpaktkALQTVIEMKDTKISSLERNIRDLEdevQMLKTNGLLHTEDREeeikqmEVYK 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1176 LTSENMmipdfKQQISELekqKQDLEiRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNE---IHTKEKEKLID 1252
Cdd:pfam10174 282 SHSKFM-----KNKIDQL---KQELS-KKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQraaILQTEVDALRL 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767984698 1253 KIQEMQEASDHLKKQFETESEvkcnfrqEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLS 1314
Cdd:pfam10174 353 RLEEKESFLNKKTKQLQDLTE-------EKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQ 407
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1026-1267 |
2.24e-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: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1026 SDGLKAEVARLSKQVKTISEFEKEIELLQAQKidveKHVQSQKREMREKMSEITKQL--LESyDIEDVRSRLSVedlehl 1103
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEE----KALLKQLAALERRIAALARRIraLEQ-ELAALEAELAE------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1104 nedgelwfayegLKKATRVLESHFQSQKDCYEKEIEALnfkvvHLSQEINHLQKLFREEnDINESIRhevtRLTSENMMI 1183
Cdd:COG4942 88 ------------LEKEIAELRAELEAQKEELAELLRAL-----YRLGRQPPLALLLSPE-DFLDAVR----RLQYLKYLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1184 PDFKQQISELEKQKQDLEiRLNEQAEKMKGKLEELsnqlhrsQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDH 1263
Cdd:COG4942 146 PARREQAEELRADLAELA-ALRAELEAERAELEAL-------LAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
....
gi 767984698 1264 LKKQ 1267
Cdd:COG4942 218 LQQE 221
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
850-1007 |
2.27e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.01 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 850 IRRFVLNIQLTYRVQRLQKKLEDQNKEnhglVEKLTSLAALRAGdvEKIQKLEAELEKAATHRRNY----EEKGKRYRDA 925
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRILEEAKKE----AEAIKKEALLEAK--EEIHKLRNEFEKELRERRNElqklEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 926 VEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKEKMDNLtkqlfddvQKEERQRmlLEKSFELkTQDYEKQI--QSLKE 1003
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELE-QKQQELEKKEEELEEL--------IEEQLQE--LERISGL-TAEEAKEIllEKVEE 165
|
....
gi 767984698 1004 EIKA 1007
Cdd:PRK12704 166 EARH 169
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
959-1228 |
2.30e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 48.38 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 959 KEKMDNLTKQL---FDDVQKEERQRMLLEKSFELKTQD-----------YEKQIQSLKEEIKALKDEKMQLQhlvegehV 1024
Cdd:pfam00038 3 KEQLQELNDRLasyIDKVRFLEQQNKLLETKISELRQKkgaepsrlyslYEKEIEDLRRQLDTLTVERARLQ-------L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1025 TSDGLKAEVARLSKQVKT-----------ISEFEKEIELLQAQKIDVEKHVQSQKREMR-------EKMSEITKQLLESY 1086
Cdd:pfam00038 76 ELDNLRLAAEDFRQKYEDelnlrtsaendLVGLRKDLDEATLARVDLEAKIESLKEELAflkknheEEVRELQAQVSDTQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1087 DIEDVRSRLSVEdlehlnedgelwfayegLKKATRVLESHFQSQKDCYEKEIEAL-NFKVVHLSQEIN-HLQKLFREEND 1164
Cdd:pfam00038 156 VNVEMDAARKLD-----------------LTSALAEIRAQYEEIAAKNREEAEEWyQSKLEELQQAAArNGDALRSAKEE 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767984698 1165 INESiRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEE 1228
Cdd:pfam00038 219 ITEL-RRTIQSLEIE---LQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQE 278
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
997-1313 |
2.51e-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: 49.45 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 997 QIQSLKEEIKALKDEKMQLQHLvegeHVtsdGLKAEVARLSKQVKTISEFEKEIELLQAQKIDvekhvqsqkrEMREKMS 1076
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHL----HF---GYKSDETLIASRQEERQETSAELNQLLRTLDD----------QWKEKRD 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1077 EITKQL-LESYDIEDVRSRLSVEDLEHLNedgelwFAYEGLKKATRVLES--HFQSQKDCYEKEIEALNFKVVHLSQEIN 1153
Cdd:pfam12128 305 ELNGELsAADAAVAKDRSELEALEDQHGA------FLDADIETAAADQEQlpSWQSELENLEERLKALTGKHQDVTAKYN 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1154 HLQKLFREEN-----DINE---SIRHEVTRLTSENMmiPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRS 1225
Cdd:pfam12128 379 RRRSKIKEQNnrdiaGIKDklaKIREARDRQLAVAE--DDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQA 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1226 Q--EEEGTQRKAleaqneihtkeKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEAS-RLTLENRDLEEELDMKDRV 1302
Cdd:pfam12128 457 TatPELLLQLEN-----------FDERIERAREEQEAANAEVERLQSELRQARKRRDQASeALRQASRRLEERQSALDEL 525
|
330
....*....|.
gi 767984698 1303 IKKLQDQVKTL 1313
Cdd:pfam12128 526 ELQLFPQAGTL 536
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1192-1311 |
2.51e-05 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 45.29 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1192 ELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEaqneihtkEKEKLIDKIQEMQEASDHLKKQFETE 1271
Cdd:pfam20492 3 EAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEE--------EAERLEQKRQEAEEEKERLEESAEME 74
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767984698 1272 SEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVK 1311
Cdd:pfam20492 75 AEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELE 114
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
932-1248 |
2.84e-05 |
|
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: 49.27 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 932 KLQKHNSELETQKEQIQLKLQE-KTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKD 1010
Cdd:TIGR00606 180 SATRYIKALETLRQVRQTQGQKvQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEH 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1011 EKMQLqHLVEGEHVTSDGLKAEVARLSKQVKTIseFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLlESYDIEd 1090
Cdd:TIGR00606 260 NLSKI-MKLDNEIKALKSRKKQMEKDNSELELK--MEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQREL-EKLNKE- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1091 vRSRLSVEDLEHLNEDGELWFAYE-----GLKKATRVLESHFQSQKDCYEKEIEAlnfkvvhlSQEINHLQKLFRE-END 1164
Cdd:TIGR00606 335 -RRLLNQEKTELLVEQGRLQLQADrhqehIRARDSLIQSLATRLELDGFERGPFS--------ERQIKNFHTLVIErQED 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1165 INESIRHEVTRLTSENMMIpdfKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHT 1244
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLK---QEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRK 482
|
....
gi 767984698 1245 KEKE 1248
Cdd:TIGR00606 483 AERE 486
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
932-1315 |
3.33e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 48.68 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 932 KLQKHNSELETQKEQI-------------QLKL----QEKTEELKEKMDNLTKQLFDDVQKE--------ERQRMLLEKS 986
Cdd:PRK04778 26 RNYKRIDELEERKQELenlpvndelekvkKLNLtgqsEEKFEEWRQKWDEIVTNSLPDIEEQlfeaeelnDKFRFRKAKH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 987 fELKT-----QDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVarLSKQVK---TISEFEKEIELLQAQ-- 1056
Cdd:PRK04778 106 -EINEiesllDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSL--LANRFSfgpALDELEKQLENLEEEfs 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1057 ----------KIDVEKHVQSQKREM---REKMSEItKQLLESY---------DIEDVRSRLSVE--DLEHLNEDGELwfa 1112
Cdd:PRK04778 183 qfveltesgdYVEAREILDQLEEELaalEQIMEEI-PELLKELqtelpdqlqELKAGYRELVEEgyHLDHLDIEKEI--- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1113 yEGLKKATRvleshfQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDinesIRHEVTRLtsenmmIPDFKQQISE 1192
Cdd:PRK04778 259 -QDLKEQID------ENLALLEELDLDEAEEKNEEIQERIDQLYDILEREVK----ARKYVEKN------SDTLPDFLEH 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1193 LEKQKQDLEI---------RLN----EQAEKMKGKLEELSNQLHRSQEEEGTQRKAL-EAQNEIhtKEKEKLIDKIQEMQ 1258
Cdd:PRK04778 322 AKEQNKELKEeidrvkqsyTLNeselESVRQLEKQLESLEKQYDEITERIAEQEIAYsELQEEL--EEILKQLEEIEKEQ 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767984698 1259 -EASDHLKKQFETESEVKCN---FRQEAS--RLTLENRDL----EEELDMKDRVIKKLQDQVKTLSK 1315
Cdd:PRK04778 400 eKLSEMLQGLRKDELEAREKlerYRNKLHeiKRYLEKSNLpglpEDYLEMFFEVSDEIEALAEELEE 466
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
858-1057 |
3.81e-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: 47.84 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 858 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKH- 936
Cdd:COG4942 38 ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 937 ---------NSELETQKEQIQLKLQEKTEELKEKMDNLTKQLfddvQKEERQRMLLEKsfelKTQDYEKQIQSLKEEIKA 1007
Cdd:COG4942 118 rqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADL----AELAALRAELEA----ERAELEALLAELEEERAA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767984698 1008 LKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQK 1057
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
817-1350 |
3.94e-05 |
|
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: 48.81 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 817 LARRRYRKMLEEHKAVILQKYARAWLARRRFQSIRRFVLNIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAalragdvE 896
Cdd:pfam02463 185 LAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESS-------K 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 897 KIQKLEAE-----------------------------LEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQI 947
Cdd:pfam02463 258 QEIEKEEEklaqvlkenkeeekekklqeeelkllakeEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 948 QLKLQEKTE--ELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQdYEKQIQSLKEEIKALKDEKMQ----LQHLVEG 1021
Cdd:pfam02463 338 EELEKELKEleIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE-RLSSAAKLKEEELELKSEEEKeaqlLLELARQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1022 EHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKmseITKQLLESYDIEDVRSRLSVEDLE 1101
Cdd:pfam02463 417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK---SEDLLKETQLVKLQEQLELLLSRQ 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1102 HLNEDGELWFAYEGLKKATRVLESHFQSQKDCYE------KEIEALNFKVVHLS----------QEINHLQKLFREENDI 1165
Cdd:pfam02463 494 KLEERSQKESKARSGLKVLLALIKDGVGGRIISAhgrlgdLGVAVENYKVAISTavivevsataDEVEERQKLVRALTEL 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1166 NESIRHEVTRLTSENM-----MIPDFKQQISELEKQKQDLEIRLNEQAEK---MKGKLEELSNQLHRSQEEEGTQRKALE 1237
Cdd:pfam02463 574 PLGARKLRLLIPKLKLplksiAVLEIDPILNLAQLDKATLEADEDDKRAKvveGILKDTELTKLKESAKAKESGLRKGVS 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1238 AQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTL---- 1313
Cdd:pfam02463 654 LEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEaqdk 733
|
570 580 590
....*....|....*....|....*....|....*..
gi 767984698 1314 SKTIGKANDVHSSSGPKEYLGMLQYKREDEAKLIQNL 1350
Cdd:pfam02463 734 INEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELS 770
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1167-1342 |
4.57e-05 |
|
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: 48.53 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1167 ESIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKE 1246
Cdd:TIGR02169 240 EAIERQLASLEEE---LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1247 KEKLIDKIQEMQEASDHLKKQFEtesevkcNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVHSS 1326
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIE-------ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
170
....*....|....*.
gi 767984698 1327 SgpKEYLGMLQYKRED 1342
Cdd:TIGR02169 390 Y--REKLEKLKREINE 403
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
856-1082 |
5.88e-05 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 46.27 E-value: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 856 NIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLaalragdvekiqKLEAELEKAATHRrnyeeKGKRYRDaVEEKLAKLQK 935
Cdd:pfam17078 19 NLQLTVQSQNLLSKLEIAQQKESKFLENLASL------------KHENDNLSSMLNR-----KERRLKD-LEDQLSELKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 936 HNSELETQKEQIQLKLQEKTE---ELKEKMDNLTKQLFDDVQKEERQRmlleksfelktQDYEKQIQSLKEEIKALK-DE 1011
Cdd:pfam17078 81 SYEELTESNKQLKKRLENSSAsetTLEAELERLQIQYDALVDSQNEYK-----------DHYQQEINTLQESLEDLKlEN 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767984698 1012 KMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKE--IELLQ-----AQKIDVEKHVQSQKrEMREKMSEITKQL 1082
Cdd:pfam17078 150 EKQLENYQQRISSNDKDIDTKLDSYNNKFKNLDNIYVNknNKLLTkldslAQLLDLPSWLNLYP-ESRNKILEYAEKM 226
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
895-1072 |
5.89e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.90 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 895 VEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKhnsELETQKEQIQLKLQEKTEELKEKMDNLTKQLfddvq 974
Cdd:PRK00409 522 IASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQE---EEDKLLEEAEKEAQQAIKEAKKEADEIIKEL----- 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 975 keerQRMLLEKSFELKTQDYEKQIQSLKEEIKAL---KDEKMQLQH-LVEGEHV--TSDGLKAEVARLSKQVKTISEF-- 1046
Cdd:PRK00409 594 ----RQLQKGGYASVKAHELIEARKRLNKANEKKekkKKKQKEKQEeLKVGDEVkyLSLGQKGEVLSIPDDKEAIVQAgi 669
|
170 180 190
....*....|....*....|....*....|..
gi 767984698 1047 ------EKEIELLQAQKIDVEKHVQSQKREMR 1072
Cdd:PRK00409 670 mkmkvpLSDLEKIQKPKKKKKKKPKTVKPKPR 701
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1064-1308 |
5.97e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1064 VQSQKREMREKMSEITKQL--LESYDIEDV----RSRLS--VEDLEHLNEDGElwFAYEGLKKATRVLESHFQSQK--DC 1133
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIeeKEEKDLHERlnglESELAelDEEIERYEEQRE--QARETRDEADEVLEEHEERREelET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1134 YEKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSE----NMMIPDFKQQISELEKQKQDLEIRL----- 1204
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEagldDADAEAVEARREELEDRDEELRDRLeecrv 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1205 -----NEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKL--IDK-IQEMQEASDHLKKQFETESEVKC 1276
Cdd:PRK02224 336 aaqahNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIeeLEEeIEELRERFGDAPVDLGNAEDFLE 415
|
250 260 270
....*....|....*....|....*....|..
gi 767984698 1277 NFRQEASRLTLENRDLEEELDMKDRVIKKLQD 1308
Cdd:PRK02224 416 ELREERDELREREAELEATLRTARERVEEAEA 447
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
865-1301 |
6.22e-05 |
|
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: 47.86 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 865 RLQKKLEDqnkenhgLVEKLTSLAALrAGDVEKIQK----LEAElEKAAThRRNYEEKGKRYRDAvEEKLAKLQKHNSEL 940
Cdd:pfam01576 577 RLQQELDD-------LLVDLDHQRQL-VSNLEKKQKkfdqMLAE-EKAIS-ARYAEERDRAEAEA-REKETRALSLARAL 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 941 ETQKEQIQlKLQEKTEELKEKMDNLTKQLfDDVQKE----ERQRMLLEKSF-ELKTQdyekqIQSLKEEIKALKDEKMQL 1015
Cdd:pfam01576 646 EEALEAKE-ELERTNKQLRAEMEDLVSSK-DDVGKNvhelERSKRALEQQVeEMKTQ-----LEELEDELQATEDAKLRL 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1016 QhlvegehVTSDGLKAEvarlskqvktiseFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQL---------LESy 1086
Cdd:pfam01576 719 E-------VNMQALKAQ-------------FERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRaqavaakkkLEL- 777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1087 DIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCY------EKEIEALNFKVVHLSQEINHLQKLFR 1160
Cdd:pfam01576 778 DLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILaqskesEKKLKNLEAELLQLQEDLAASERARR 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1161 EENDINESIRHEVTRLTSENMMIPDFKQQIS--------ELEKQKQDLEIrLNEQAEKMKGKLEELSNQL----HRSQEE 1228
Cdd:pfam01576 858 QAQQERDELADEIASGASGKSALQDEKRRLEariaqleeELEEEQSNTEL-LNDRLRKSTLQVEQLTTELaaerSTSQKS 936
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767984698 1229 EGTqRKALEAQNeihtkeKEkLIDKIQEMqeasdhlkkqfetESEVKCNFRQEASRLTLENRDLEEELDMKDR 1301
Cdd:pfam01576 937 ESA-RQQLERQN------KE-LKAKLQEM-------------EGTVKSKFKSSIAALEAKIAQLEEQLEQESR 988
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
950-1324 |
9.46e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 950 KLQEKTEELKEKMDNLTKQLFD-DVQKEERQRMLLE--------KSFELKTQDYEKQIQSLKEEIKALKDEKmqlqhlve 1020
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNiDYLEEKLKSSNLElenikkqiADDEKSHSITLKEIERLSIEYNNAMDDY-------- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1021 gehvtsDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHV----QSQKREMR-------EKMSEITKQLLESYDIE 1089
Cdd:PRK01156 235 ------NNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNnyykELEERHMKiindpvyKNRNYINDYFKYKNDIE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1090 DVRSRLSvedlehlNEDGELWFAYEGLKKATrVLESHF------QSQKDCYEKEIEAL---NFKVVHLSQEINHLQKLFR 1160
Cdd:PRK01156 309 NKKQILS-------NIDAEINKYHAIIKKLS-VLQKDYndyikkKSRYDDLNNQILELegyEMDYNSYLKSIESLKKKIE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1161 EENDINESIRHEVTRLTSENMMIPD-FKQQISELEKQKQDLEIR---LNEQAEKMKGKLEELSnqlhRSQEEEGTQRKAL 1236
Cdd:PRK01156 381 EYSKNIERMSAFISEILKIQEIDPDaIKKELNEINVKLQDISSKvssLNQRIRALRENLDELS----RNMEMLNGQSVCP 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1237 EAQNEIHTKEKEKLIDKIQEmqEASDHLKKQFETESEVKC---NFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTL 1313
Cdd:PRK01156 457 VCGTTLGEEKSNHIINHYNE--KKSRLEEKIREIEIEVKDideKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDI 534
|
410
....*....|.
gi 767984698 1314 SKTIGKANDVH 1324
Cdd:PRK01156 535 KIKINELKDKH 545
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
904-1297 |
1.15e-04 |
|
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: 47.09 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 904 ELEKAathRRNYEEKGKRYRDAVEEKLAKLQ-----KHNSELETQ--KEQIQLKLQEKTEELKEKMDNLTKQLFD---DV 973
Cdd:pfam01576 682 ELERS---KRALEQQVEEMKTQLEELEDELQatedaKLRLEVNMQalKAQFERDLQARDEQGEEKRRQLVKQVREleaEL 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 974 QKEERQRMLL---EKSFELKTQDYEKQIQSL----KEEIKALKDEKMQLQHL---VEGEHVTSDGLKAEVARLSKQVKTI 1043
Cdd:pfam01576 759 EDERKQRAQAvaaKKKLELDLKELEAQIDAAnkgrEEAVKQLKKLQAQMKDLqreLEEARASRDEILAQSKESEKKLKNL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1044 sefekEIELLQAQKI-----DVEKHVQSQKREMREkmsEITKQLLESYDIEDVRSRLS--VEDLEHLNEDgelwfayegl 1116
Cdd:pfam01576 839 -----EAELLQLQEDlaaseRARRQAQQERDELAD---EIASGASGKSALQDEKRRLEarIAQLEEELEE---------- 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1117 kkatrvLESHFQSQKDCYEK---EIEALNfkvVHLSQEINHLQKlfreendiNESIRhevtrltsenmmipdfkqqiSEL 1193
Cdd:pfam01576 901 ------EQSNTELLNDRLRKstlQVEQLT---TELAAERSTSQK--------SESAR--------------------QQL 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1194 EKQKQDLEIRLNEQAEKMKGK-------LEELSNQLHRSQEEEGTQRKAleAQNEIHTKEK--EKLIDKIQEMQEASDHL 1264
Cdd:pfam01576 944 ERQNKELKAKLQEMEGTVKSKfkssiaaLEAKIAQLEEQLEQESRERQA--ANKLVRRTEKklKEVLLQVEDERRHADQY 1021
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 767984698 1265 KKQFE-TESEVKCNFRQ------EASRLTLENRDLEEELD 1297
Cdd:pfam01576 1022 KDQAEkGNSRMKQLKRQleeaeeEASRANAARRKLQRELD 1061
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
896-1087 |
1.32e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 896 EKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKEKMDNLTKQL----FD 971
Cdd:COG1340 29 EKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD-ELNEKLNELREELDELRKELaelnKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 972 DVQKEERQRML--LEKSFELKTQDYEK------QIQSLKEEIKALKDEKMQLQHLVEgehvtsdgLKAEVARLSKQVkti 1043
Cdd:COG1340 108 GGSIDKLRKEIerLEWRQQTEVLSPEEekelveKIKELEKELEKAKKALEKNEKLKE--------LRAELKELRKEA--- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767984698 1044 SEFEKEIELL--QAQKIDVEKHVQSQKR-EMREKMSEITKQLLESYD 1087
Cdd:COG1340 177 EEIHKKIKELaeEAQELHEEMIELYKEAdELRKEADELHKEIVEAQE 223
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
928-1057 |
1.49e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 928 EKLAK--LQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEK--------- 996
Cdd:PRK12704 37 EEEAKriLEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKreeelekke 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767984698 997 -QIQSLKEEIKALKDE--KMQLQHLVEGEHVTsdGLKAEVAR--LSKQVK---------TISEFEKEIElLQAQK 1057
Cdd:PRK12704 117 kELEQKQQELEKKEEEleELIEEQLQELERIS--GLTAEEAKeiLLEKVEeearheaavLIKEIEEEAK-EEADK 188
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
875-1084 |
1.59e-04 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 46.21 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 875 KENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAatHRRNYEEKGKRYRDAVEEKLAKLQKHNSELET--QKEQIQLKLQ 952
Cdd:pfam15742 107 KSQNSLQEKLAQEKSRVADAEEKILELQQKLEHA--HKVCLTDTCILEKKQLEERIKEASENEAKLKQqyQEEQQKRKLL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 953 EKT-EELKEKMDNL----------TKQLFDDVQKEERQRMLLEKsfELKTQD-YEKQIQSLKEEIKALKDEK----MQLQ 1016
Cdd:pfam15742 185 DQNvNELQQQVRSLqdkeaqlemtNSQQQLRIQQQEAQLKQLEN--EKRKSDeHLKSNQELSEKLSSLQQEKealqEELQ 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1017 HLVE--GEHVTS-----DGLKAEVAR----LSKQV----KTISEFEKEIELLQaQKIDVEKHVQSQKREMREKMSEITKQ 1081
Cdd:pfam15742 263 QVLKqlDVHVRKynekhHHHKAKLRRakdrLVHEVeqrdERIKQLENEIGILQ-QQSEKEKAFQKQVTAQNEILLLEKRK 341
|
...
gi 767984698 1082 LLE 1084
Cdd:pfam15742 342 LLE 344
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1183-1261 |
2.03e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1183 IPDFKQQISELEKQKQDLE---IRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQE 1259
Cdd:COG3883 18 IQAKQKELSELQAELEAAQaelDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
..
gi 767984698 1260 AS 1261
Cdd:COG3883 98 SG 99
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
817-1315 |
2.19e-04 |
|
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: 45.89 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 817 LARRRYRKMLEEHKAVILQKYARAWLARRRFQSIRRfvlNIQLTYRVQRLQKKLEDQNKENHGLVE----KLTSLAALRA 892
Cdd:pfam05557 14 LQNEKKQMELEHKRARIELEKKASALKRQLDRESDR---NQELQKRIRLLEKREAEAEEALREQAElnrlKKKYLEALNK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 893 GDVEKIQKLE----------------------AELEKAATH------RRNYEEKGKRYRDAvEEKLAKLQKHNSELETQK 944
Cdd:pfam05557 91 KLNEKESQLAdarevisclknelselrrqiqrAELELQSTNseleelQERLDLLKAKASEA-EQLRQNLEKQQSSLAEAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 945 EQIQ-----LKLQEK-TEELKE---------KMDNLTKQLFDDV---------------QKEERQRML------------ 982
Cdd:pfam05557 170 QRIKelefeIQSQEQdSEIVKNskselaripELEKELERLREHNkhlnenienklllkeEVEDLKRKLereekyreeaat 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 983 --LEKS-FELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVtsdgLKAEVARLSKQVK----TISEFEKEIELLQA 1055
Cdd:pfam05557 250 leLEKEkLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIV----LKEENSSLTSSARqlekARRELEQELAQYLK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1056 QKIDVE---KHVQSQKREMREKMSEITK------QLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVlesh 1126
Cdd:pfam05557 326 KIEDLNkklKRHKALVRRLQRRVLLLTKerdgyrAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEA---- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1127 fqsQKDCYEKEIEALNFKVVHLSQEInhlqKLFREENDINE--SIRHEVTRLTSENmmiPDFKQQISELEKQKQDLEIRL 1204
Cdd:pfam05557 402 ---QLSVAEEELGGYKQQAQTLEREL----QALRQQESLADpsYSKEEVDSLRRKL---ETLELERQRLREQKNELEMEL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1205 neqaekMKGKLEELSNQ-----LHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVkcNFR 1279
Cdd:pfam05557 472 ------ERRCLQGDYDPkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTM--NFK 543
|
570 580 590
....*....|....*....|....*....|....*.
gi 767984698 1280 qeasrltlENRDLEEELDMKDRVIKKLQDQVKTLSK 1315
Cdd:pfam05557 544 --------EVLDLRKELESAELKNQRLKEVFQAKIQ 571
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
899-1002 |
2.52e-04 |
|
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: 44.88 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 899 QKLEAELEKAATHRRnyEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEer 978
Cdd:cd16269 192 ALTEKEKEIEAERAK--AEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKE-- 267
|
90 100
....*....|....*....|....
gi 767984698 979 QRMLLEKSFELKTQDYEKQIQSLK 1002
Cdd:cd16269 268 QEALLEEGFKEQAELLQEEIRSLK 291
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
869-1090 |
2.83e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 44.71 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 869 KLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELE-TQKEQI 947
Cdd:pfam06008 41 QIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFaLPSSDL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 948 QLKLQEKTEELKE-KMDNLTKQLFDDVQKEERQRMLLEKSfelktqdyEKQIQSLKEEIKALKDekmQLQHLVeGEHvtS 1026
Cdd:pfam06008 121 SRMLAEAQRMLGEiRSRDFGTQLQNAEAELKAAQDLLSRI--------QTWFQSPQEENKALAN---ALRDSL-AEY--E 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767984698 1027 DGLKAEVARLSKQVKTISEFEkeiELLQAQKIDVEKHvQSQKREMREKMSEITKQLLESYDIED 1090
Cdd:pfam06008 187 AKLSDLRELLREAAAKTRDAN---RLNLANQANLREF-QRKKEEVSEQKNQLEETLKTARDSLD 246
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
858-1101 |
2.92e-04 |
|
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: 45.81 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 858 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEE------KLA 931
Cdd:TIGR00606 840 TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQdspletFLE 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 932 KLQKHNSELETQKEQIQLKLQEKTEELKEKMDNL---TKQLFDDVQ---------KE-------------ERQRMLLEKS 986
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgyMKDIENKIQdgkddylkqKEtelntvnaqleecEKHQEKINED 999
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 987 FELKTQDYEKQIQS------------LKEEIKALKDEKMQLQHLVEGEHVTSdgLKAEVARLSKQVKTIsefEKEIELLQ 1054
Cdd:TIGR00606 1000 MRLMRQDIDTQKIQerwlqdnltlrkRENELKEVEEELKQHLKEMGQMQVLQ--MKQEHQKLEENIDLI---KRNHVLAL 1074
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767984698 1055 AQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLE 1101
Cdd:TIGR00606 1075 GRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLD 1121
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1122-1319 |
3.63e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1122 VLESHFQSQKDCYEKEIEALNFKVvhlSQEINHLQKLFREENDINESIRHEVTRLTSEnmmipdfkqqISELEKQKQDLE 1201
Cdd:PHA02562 188 MKIDHIQQQIKTYNKNIEEQRKKN---GENIARKQNKYDELVEEAKTIKAEIEELTDE----------LLNLVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1202 I---RLNEQAEKMKGKLEELSNQLHR----------SQEEEGTQRKALEAQNEIH--TKEKEKLIDKIQEMQEASDHLKK 1266
Cdd:PHA02562 255 AalnKLNTAAAKIKSKIEQFQKVIKMyekggvcptcTQQISEGPDRITKIKDKLKelQHSLEKLDTAIDELEEIMDEFNE 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767984698 1267 QFETESEVKC---NFRQEASRLTLENRDLEEELD--MKDRV-----IKKLQDQVKTLSKTIGK 1319
Cdd:PHA02562 335 QSKKLLELKNkisTNKQSLITLVDKAKKVKAAIEelQAEFVdnaeeLAKLQDELDKIVKTKSE 397
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
859-1297 |
3.68e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 45.28 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 859 LTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRA--------GDVEKIQKLEAELEKAAT--HRRNYEEKGKRyRDAVEE 928
Cdd:pfam15964 236 LESQVKSLRKDLAESQKTCEDLKERLKHKESLVAastssrvgGLCLKCAQHEAVLAQTHTnvHMQTIERLTKE-RDDLMS 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 929 KLAKLQKHNSELETQK----EQIQLKLQEKTEELKEKMDNLTKqlFDDVQKE-ERQRMLLEKSFELKTQDYEKQIQSLKE 1003
Cdd:pfam15964 315 ALVSVRSSLAEAQQREssayEQVKQAVQMTEEANFEKTKALIQ--CEQLKSElERQKERLEKELASQQEKRAQEKEALRK 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1004 EIKALKDEKMQLQhLVEGEHVTSdgLKAEVARLSKQ-VKTISEFEKEIELLQAQKIDVEK----------HVQSQK---- 1068
Cdd:pfam15964 393 EMKKEREELGATM-LALSQNVAQ--LEAQVEKVTREkNSLVSQLEEAQKQLASQEMDVTKvcgemryqlnQTKMKKdeae 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1069 REMREKMSEITKQL-LESYDIEDVRSRL--SVEDLEHLNEDG-----ELWFAYEGLKKATRVLESHFQ---SQKDCYEKE 1137
Cdd:pfam15964 470 KEHREYRTKTGRQLeIKDQEIEKLGLELseSKQRLEQAQQDAarareECLKLTELLGESEHQLHLTRLekeSIQQSFSNE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1138 IEALNFKVVHLSQEINhlQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKqkqdleiRLNEQAEKMKGKLEE 1217
Cdd:pfam15964 550 AKAQALQAQQREQELT--QKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAK-------KLEEITQKSRSEVEQ 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1218 LSNQ---LHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEmqeasdhLKKQFETESEVKCNFRQEASRLTLENRDLEE 1294
Cdd:pfam15964 621 LSQEkeyLQDRLEKLQKRNEELEEQCVQHGRMHERMKQRLRQ-------LDKHCQATAQQLVQLLSKQNQLFKERQNLTE 693
|
...
gi 767984698 1295 ELD 1297
Cdd:pfam15964 694 EVQ 696
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1043-1260 |
4.27e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1043 ISEFEKEIELLQAQKidveKHVQSQKREMREKMSEITKQLLE-SYDIEDVRSRLSV--EDLEHLNEDgelwfayegLKKA 1119
Cdd:COG3883 18 IQAKQKELSELQAEL----EAAQAELDALQAELEELNEEYNElQAELEALQAEIDKlqAEIAEAEAE---------IEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1120 TRVLESHFQSQkdcYEKeiealnfkvvhlSQEINHLQKLFrEENDINESIR--HEVTRLTS-ENMMIPDFKQQISELEKQ 1196
Cdd:COG3883 85 REELGERARAL---YRS------------GGSVSYLDVLL-GSESFSDFLDrlSALSKIADaDADLLEELKADKAELEAK 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767984698 1197 KQDLEIRLNEqAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEA 1260
Cdd:COG3883 149 KAELEAKLAE-LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
862-1110 |
5.12e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 862 RVQRLQKKLEDQNKENHGLVEKLTSLAALRA------GDVEKIQKLEAELEKA---ATHRRNYEEKgkryrdaVEEKLAK 932
Cdd:COG1340 72 KVKELKEERDELNEKLNELREELDELRKELAelnkagGSIDKLRKEIERLEWRqqtEVLSPEEEKE-------LVEKIKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 933 LQKhnsELETQKEQIQLKlqEKTEELKEKMDNLTKQLfddvqKEERQRMlleksfelktQDYEKQIQSLKEEIKALKDEK 1012
Cdd:COG1340 145 LEK---ELEKAKKALEKN--EKLKELRAELKELRKEA-----EEIHKKI----------KELAEEAQELHEEMIELYKEA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1013 MQLQHLVEGEHVTSDGLKAEVARLSKQ----VKTISEFEKEIELLQAQKIDVEKhvQSQKREMREKMSEITKQLLESydi 1088
Cdd:COG1340 205 DELRKEADELHKEIVEAQEKADELHEEiielQKELRELRKELKKLRKKQRALKR--EKEKEELEEKAEEIFEKLKKG--- 279
|
250 260
....*....|....*....|..
gi 767984698 1089 edvrSRLSVEDLEHLNEDGELW 1110
Cdd:COG1340 280 ----EKLTTEELKLLQKSGLLE 297
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
876-1008 |
5.75e-04 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 42.89 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 876 ENHGLVEKLTSLAALRAgdvEKIQKLEAELEKaathRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKT 955
Cdd:pfam06785 66 EKSFLEEKEAKLTELDA---EGFKILEETLEE----LQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFR 138
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 767984698 956 EELKEKMDNLTKQLFDDVQKEERQRMLLEKSFElKTQDYEKQIQSLKEEIKAL 1008
Cdd:pfam06785 139 LESEEQLAEKQLLINEYQQTIEEQRSVLEKRQD-QIENLESKVRDLNYEIKTL 190
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
924-1109 |
5.76e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 924 DAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLfddvqkEERQRMLLEksFELKTQDYEKQIQSLKE 1003
Cdd:PHA02562 191 DHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEI------EELTDELLN--LVMDIEDPSAALNKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1004 EIKALKDEKMQLQ---HLVEGEHV---TSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHV------QSQKREM 1071
Cdd:PHA02562 263 AAAKIKSKIEQFQkviKMYEKGGVcptCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMdefneqSKKLLEL 342
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767984698 1072 REKMSEItKQLLESY-----DIEDVRSRLSVedlEHLNEDGEL 1109
Cdd:PHA02562 343 KNKISTN-KQSLITLvdkakKVKAAIEELQA---EFVDNAEEL 381
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
814-1008 |
6.58e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 814 RGFLARRRYRKMLEEHKAVILQKYARAWLARRRFQSIRRFVLNIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAG 893
Cdd:COG1196 583 RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSL 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 894 DVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQI--QLKLQEKTEELKEKMDNLTKQLFD 971
Cdd:COG1196 663 TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERleEELEEEALEEQLEAEREELLEELL 742
|
170 180 190
....*....|....*....|....*....|....*..
gi 767984698 972 DVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKAL 1008
Cdd:COG1196 743 EEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
862-1101 |
6.59e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 44.29 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 862 RVQRLQKKLEDQNKENhglvEKLTSLAA-----------LRAGdVEKIQKLEAELEkaaTHRRNYEEKG--KRYRDAVEE 928
Cdd:pfam05622 88 KCEELEKEVLELQHRN----EELTSLAEeaqalkdemdiLRES-SDKVKKLEATVE---TYKKKLEDLGdlRRQVKLLEE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 929 KLA-----------KLQKHN---SELETQKEQIQ---LKLQE---KTEELKEKMDNLTKQLfDDVQKeERQRMLLEK--- 985
Cdd:pfam05622 160 RNAeymqrtlqleeELKKANalrGQLETYKRQVQelhGKLSEeskKADKLEFEYKKLEEKL-EALQK-EKERLIIERdtl 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 986 ----------------------------------SFELKTQDYEKQIQSLKEEIKALK--------DEKMQLQHLVEGEH 1023
Cdd:pfam05622 238 retneelrcaqlqqaelsqadallspssdpgdnlAAEIMPAEIREKLIRLQHENKMLRlgqegsyrERLTELQQLLEDAN 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1024 VTSDGLKAEvARLSKQvktisefekEIELLQAQKIDVEKHVQSQ--KRE----MREKMSEITKQLLESYDiEDVRSRLSV 1097
Cdd:pfam05622 318 RRKNELETQ-NRLANQ---------RILELQQQVEELQKALQEQgsKAEdsslLKQKLEEHLEKLHEAQS-ELQKKKEQI 386
|
....
gi 767984698 1098 EDLE 1101
Cdd:pfam05622 387 EELE 390
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
923-1235 |
6.85e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 43.92 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 923 RDAVEEKLAKLQKHNSELE-------TQKEQIQLKLQEKTEELKEKMDNL--TKQLFDDVQKEERQRML----------- 982
Cdd:pfam04108 37 RRGLSVQLANLEKVREGLEkvlnelkKDFKQLLKDLDAALERLEETLDKLrnTPVEPALPPGEEKQKTLldfidedsvei 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 983 LEKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEgehvTSDGLKAEVARLSKQVKTISEFEKEIELLqAQKI--DV 1060
Cdd:pfam04108 117 LRDALKELIDELQAAQESLDSDLKRFDDDLRDLQKELE----SLSSPSESISLIPTLLKELESLEEEMASL-LESLtnHY 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1061 EKHVQSQKREM--REKMSEITKQllESYDIEDVrsrlsVEDLEHLNEdgELWFAYEGLKKATRVLESHFQSQKDCYEKeI 1138
Cdd:pfam04108 192 DQCVTAVKLTEggRAEMLEVLEN--DARELDDV-----VPELQDRLD--EMENNYERLQKLLEQKNSLIDELLSALQL-I 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1139 EALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPD-FKQQISELEKQKqdleirlnEQAEKMKGKLEE 1217
Cdd:pfam04108 262 AEIQSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLREFYEGFPSaYGSLLLEVERRR--------EWAEKMKKILRK 333
|
330
....*....|....*...
gi 767984698 1218 LSNQLHRSQEEEGTQRKA 1235
Cdd:pfam04108 334 LAEELDRLQEEERKRREK 351
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
924-1034 |
7.30e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.30 E-value: 7.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 924 DAVEEKLAKLQKHNSELETQKEQI----QLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEK--Q 997
Cdd:COG0542 407 DSKPEELDELERRLEQLEIEKEALkkeqDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRygK 486
|
90 100 110
....*....|....*....|....*....|....*..
gi 767984698 998 IQSLKEEIKALKDEKMQLQHLVEgEHVTSDglkaEVA 1034
Cdd:COG0542 487 IPELEKELAELEEELAELAPLLR-EEVTEE----DIA 518
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
864-1013 |
7.31e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.47 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 864 QRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQ 943
Cdd:smart00787 147 EGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKK 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767984698 944 KEQIQLKLQEKTEELkEKMDNLTKQLFDDVQKEERQRmlleksfeLKTQDYE-KQIQSLKEEIKALKDEKM 1013
Cdd:smart00787 227 LEELEEELQELESKI-EDLTNKKSELNTEIAEAEKKL--------EQCRGFTfKEIEKLKEQLKLLQSLTG 288
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
857-1101 |
8.40e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.07 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 857 IQLTYRVQRLQKKLEDQNKENHGLVEKLTSlaalragdvEKIQKLEAELEKAATHRrnYEEKGkryrdaVEEKLAKLQKH 936
Cdd:PLN03229 432 RELEGEVEKLKEQILKAKESSSKPSELALN---------EMIEKLKKEIDLEYTEA--VIAMG------LQERLENLREE 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 937 NSELETQKEQIQLKLQEKTEELKEKMD-NLT--------KQLFDDVQKEERQRMLLE---KSFELKtQDYEKQIQS---- 1000
Cdd:PLN03229 495 FSKANSQDQLMHPVLMEKIEKLKDEFNkRLSrapnylslKYKLDMLNEFSRAKALSEkksKAEKLK-AEINKKFKEvmdr 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1001 --LKEEIKALKDEKMQLQHLVEGEhvTSDGLKAEVARLSKQV-----KTISEFEKEIELLQAQKIDVEKHVQSQkrEMRE 1073
Cdd:PLN03229 574 peIKEKMEALKAEVASSGASSGDE--LDDDLKEKVEKMKKEIelelaGVLKSMGLEVIGVTKKNKDTAEQTPPP--NLQE 649
|
250 260 270
....*....|....*....|....*....|..
gi 767984698 1074 KMS----EITKQLLESYDIEDVRSRLSVEDLE 1101
Cdd:PLN03229 650 KIEslneEINKKIERVIRSSDLKSKIELLKLE 681
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1187-1317 |
8.61e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.86 E-value: 8.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1187 KQQISELEKQKQDLEirlnEQAEKMKGKLEELSNQLHRSqEEEGTQRKALEAQNEIHTKEKEKLID----------KIQE 1256
Cdd:pfam05667 334 EEELEELQEQLEDLE----SSIQELEKEIKKLESSIKQV-EEELEELKEQNEELEKQYKVKKKTLDllpdaeeniaKLQA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1257 MQEASD----HLKKQFET----------ESEVKCNFRQEASRLTLEN--------RDLEEELDMKDRVIKKLQDQVKTLS 1314
Cdd:pfam05667 409 LVDASAqrlvELAGQWEKhrvplieeyrALKEAKSNKEDESQRKLEEikelrekiKEVAEEAKQKEELYKQLVAEYERLP 488
|
...
gi 767984698 1315 KTI 1317
Cdd:pfam05667 489 KDV 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
826-1280 |
8.70e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 826 LEEHKAVILQKYARAWLARRRFQSIRRFVLNIQLtyRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAEL 905
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLE--RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 906 EKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQE----KTEELKEKMDNLTKQLFDDVQKEERQRM 981
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFlegvKAALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 982 LLEKSFELKTQDY--------EKQIQSLKEE------------IKALKDEKMQLQHLVEGEHVtsDGLKAEVARLSKQVK 1041
Cdd:COG1196 539 ALEAALAAALQNIvveddevaAAAIEYLKAAkagratflpldkIRARAALAAALARGAIGAAV--DLVASDLREADARYY 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1042 TISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDGElwfAYEGLKKATR 1121
Cdd:COG1196 617 VLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE---LAERLAEEEL 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1122 VLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLE 1201
Cdd:COG1196 694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1202 IRL------NEQAekmkgkLEELsnqlhrsqEEEGTQRKALEAQNEIHTKEKEKLIDKIQEM-QEASDHLKKQFEtesEV 1274
Cdd:COG1196 774 REIealgpvNLLA------IEEY--------EELEERYDFLSEQREDLEEARETLEEAIEEIdRETRERFLETFD---AV 836
|
....*.
gi 767984698 1275 KCNFRQ 1280
Cdd:COG1196 837 NENFQE 842
|
|
| YkyA |
pfam10368 |
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ... |
867-1015 |
1.05e-03 |
|
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.
Pssm-ID: 431235 [Multi-domain] Cd Length: 185 Bit Score: 41.81 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 867 QKKLEDQNKENHGLVEKLTSLAAlraGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKeq 946
Cdd:pfam10368 24 QEPLVELEKKEQELYEEIIELGM---DEFDEIKKLSDEALENVEEREELLEKEKESIEEAKEEFKKIKEIIEEIEDEE-- 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767984698 947 iqlkLQEKTEELKEKMDNLTK---QLFDDVQK---EERQ--RMLLEKSFELKtqDYEKQIQSLKEEIKALKDEKMQL 1015
Cdd:pfam10368 99 ----LKKEAEELIDAMEERYEaydELYDAYKKaleLDKElyEMLKDEDLTLE--ELQEQIEKINESYEEVKEANEQF 169
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
932-1103 |
1.10e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.08 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 932 KLQKHNSELETQK----------EQIQLKLQEKTEELKEKMDNLTKQlfddvqkeerqrMLLEKSFELKTQDYEkqiQSL 1001
Cdd:smart00787 120 QLVKTFARLEAKKmwyewrmkllEGLKEGLDENLEGLKEDYKLLMKE------------LELLNSIKPKLRDRK---DAL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1002 KEEIKALKdekmqlQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQS---QKREMREKMSEI 1078
Cdd:smart00787 185 EEELRQLK------QLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDltnKKSELNTEIAEA 258
|
170 180
....*....|....*....|....*...
gi 767984698 1079 TKQLLES--YDIEDVRS-RLSVEDLEHL 1103
Cdd:smart00787 259 EKKLEQCrgFTFKEIEKlKEQLKLLQSL 286
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
862-996 |
1.34e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 40.75 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 862 RVQRLQKKLEDQNKENHGLVEKLTSLAAlragdveKIQKLEAELEKAathrrnyEEKGKRYRDAVEEKLAK------LQK 935
Cdd:pfam12718 15 RAEELEEKVKELEQENLEKEQEIKSLTH-------KNQQLEEEVEKL-------EEQLKEAKEKAEESEKLktnnenLTR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767984698 936 HNSELETQKEQIQLKLQEKTEELKEkMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEK 996
Cdd:pfam12718 81 KIQLLEEELEESDKRLKETTEKLRE-TDVKAEHLERKVQALEQERDEWEKKYEELEEKYKE 140
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1155-1313 |
1.42e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1155 LQKLFREENDINE---SIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLhRSQEEEGT 1231
Cdd:COG3883 25 LSELQAELEAAQAeldALQAELEELNEE---YNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA-RALYRSGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1232 QRKALE----------------AQNEIHTKEKEkLIDKIQEMQEASDHLKKQFETESEvkcNFRQEASRLTLENRDLEEE 1295
Cdd:COG3883 101 SVSYLDvllgsesfsdfldrlsALSKIADADAD-LLEELKADKAELEAKKAELEAKLA---ELEALKAELEAAKAELEAQ 176
|
170
....*....|....*...
gi 767984698 1296 LDMKDRVIKKLQDQVKTL 1313
Cdd:COG3883 177 QAEQEALLAQLSAEEAAA 194
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
995-1210 |
1.50e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 995 EKQIQSLKEEIKALKDEKMQLQHLVegehvtsDGLKAEVARLSKQVKTIsefEKEIELLQAQKIDVEKHVQSQKREMREK 1074
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAEL-------DALQAELEELNEEYNEL---QAELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1075 MSEITKQ----------------LLESYDIEDVRSRLSVedLEHLNE-DGELwfaYEGLKKATRVLEshfqSQKDCYEKE 1137
Cdd:COG3883 85 REELGERaralyrsggsvsyldvLLGSESFSDFLDRLSA--LSKIADaDADL---LEELKADKAELE----AKKAELEAK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767984698 1138 IEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLtsenmmipdfKQQISELEKQKQDLEIRLNEQAEK 1210
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA----------EAQLAELEAELAAAEAAAAAAAAA 218
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
858-1048 |
1.87e-03 |
|
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: 42.96 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 858 QLTYRVQRLQK----------KLEDQNKENHGLVEKLT----SLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYR 923
Cdd:pfam07888 77 ELESRVAELKEelrqsrekheELEEKYKELSASSEELSeekdALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 924 DAVEEKLAKLQkhnsELETQKEQIQLKLQEKTEELKEKMDNLtkQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKE 1003
Cdd:pfam07888 157 ERAKKAGAQRK----EEEAERKQLQAKLQQTEEELRSLSKEF--QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEA 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767984698 1004 EIKALKDEKMQLQHLVEGEHVTSDGLKAEVARL-SKQVKTISEFEK 1048
Cdd:pfam07888 231 ENEALLEELRSLQERLNASERKVEGLGEELSSMaAQRDRTQAELHQ 276
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
876-1106 |
1.89e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.90 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 876 ENHGLVEKL-TSLAALRAgDVEKIQKLEAELEK---------AATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKE 945
Cdd:PRK04778 195 EAREILDQLeEELAALEQ-IMEEIPELLKELQTelpdqlqelKAGYRELVEEGYHLDHLDIEKEIQDLKEQIDENLALLE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 946 QIQLK-LQEKTEELKEKMDNL-----------------TKQLFDDVQKEERQ-RMLLE------KSFELKTQDYEKQiQS 1000
Cdd:PRK04778 274 ELDLDeAEEKNEEIQERIDQLydilerevkarkyveknSDTLPDFLEHAKEQnKELKEeidrvkQSYTLNESELESV-RQ 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1001 LKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEI-ELLQAQKIDvEKHVQSQKREMREKMSEIt 1079
Cdd:PRK04778 353 LEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLsEMLQGLRKD-ELEAREKLERYRNKLHEI- 430
|
250 260 270
....*....|....*....|....*....|...
gi 767984698 1080 KQLLESYDI----EDVRSRL--SVEDLEHLNED 1106
Cdd:PRK04778 431 KRYLEKSNLpglpEDYLEMFfeVSDEIEALAEE 463
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
856-1346 |
2.06e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 856 NIQLTYRVQRLQKKLEDQNKENHGLVEKLTSlAALRAGDVEKIQKLEAE--LEKAATHRRNYEEKgKRYRDAVEEKLAKL 933
Cdd:pfam10174 69 NQHLQLTIQALQDELRAQRDLNQLLQQDFTT-SPVDGEDKFSTPELTEEnfRRLQSEHERQAKEL-FLLRKTLEEMELRI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 934 QKHNSELETQKEQIQlKLQEKTEelkekMDNLTKQLFDDVQkeERQRMLLEksFELKTQDYEKQIQSLKEEIKALKDE-- 1011
Cdd:pfam10174 147 ETQKQTLGARDESIK-KLLEMLQ-----SKGLPKKSGEEDW--ERTRRIAE--AEMQLGHLEVLLDQKEKENIHLREElh 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1012 -KMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQ-KIDVEKH---------VQSQKREMREKMSEItK 1080
Cdd:pfam10174 217 rRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNgLLHTEDReeeikqmevYKSHSKFMKNKIDQL-K 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1081 QLLESYDIEDVRSRLSVEDLEHLNEDGELWFayEGLKKATRVLE---SHFQSQKDCYEKEIEAlnfKVVHLSQEINHLQK 1157
Cdd:pfam10174 296 QELSKKESELLALQTKLETLTNQNSDCKQHI--EVLKESLTAKEqraAILQTEVDALRLRLEE---KESFLNKKTKQLQD 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1158 LFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNqlhrSQEEEGTQRKALe 1237
Cdd:pfam10174 371 LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSN----TDTALTTLEEAL- 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1238 aqneihtKEKEKLIDKIQEMQEASDHlkkqfetesevkcNFRQEASRLTLENRDLEEELDM-------KDRVIKKLQDQV 1310
Cdd:pfam10174 446 -------SEKERIIERLKEQREREDR-------------ERLEELESLKKENKDLKEKVSAlqpelteKESSLIDLKEHA 505
|
490 500 510
....*....|....*....|....*....|....*.
gi 767984698 1311 KTLSKTIGKANdvhssSGPKEYLGMLQYKREDEAKL 1346
Cdd:pfam10174 506 SSLASSGLKKD-----SKLKSLEIAVEQKKEECSKL 536
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
858-1126 |
2.08e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 858 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQkhn 937
Cdd:COG4372 77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK--- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 938 sELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKmqLQH 1017
Cdd:COG4372 154 -ELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSL--EAK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1018 LVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSV 1097
Cdd:COG4372 231 LGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310
|
250 260
....*....|....*....|....*....
gi 767984698 1098 EDLEHLNEDGELWFAYEGLKKATRVLESH 1126
Cdd:COG4372 311 GALEDALLAALLELAKKLELALAILLAEL 339
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1060-1293 |
2.10e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1060 VEKHVQSQKREMREKMSEITKQLlesydiEDVRSRLsvEDLEHlnedgelwfAYEGLKKATRVLEShfQSQKDCYEKEIE 1139
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQL------PELRKEL--EEAEA---------ALEEFRQKNGLVDL--SEEAKLLLQQLS 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1140 ALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLtSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELS 1219
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL-LQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA 301
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767984698 1220 NQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQfetesevkcnfRQEASRLtleNRDLE 1293
Cdd:COG3206 302 ALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL-----------EAELRRL---EREVE 361
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1174-1324 |
2.25e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1174 TRLTSENMMIPDFKQQISELEKQKQDLEIR---LNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKL 1250
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKrdeLNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767984698 1251 IDKIQEMQEASDHLKKQFEtESEVKCNFRQEASRLTLENRDLEEELDMKD---RVIKKLQDQVKTLSKTIGKANDVH 1324
Cdd:COG1340 81 DELNEKLNELREELDELRK-ELAELNKAGGSIDKLRKEIERLEWRQQTEVlspEEEKELVEKIKELEKELEKAKKAL 156
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
971-1272 |
2.26e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.55 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 971 DDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKalKDEKMQLQHLVEGEhvtsDGLKAEVARLSKQVKTISEFEKEI 1050
Cdd:pfam02029 34 ESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTA--KREERRQKRLQEAL----ERQKEFDPTIADEKESVAERKENN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1051 ELLQAQkiDVEKHVQSQKREMREKMSEITkqllesydiedVRSRlsvEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQ 1130
Cdd:pfam02029 108 EEEENS--SWEKEEKRDSRLGRYKEEETE-----------IREK---EYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1131 KDCYEKEIEALNFK---------VVHLSQEINHL-QKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDL 1200
Cdd:pfam02029 172 ENFAKEEVKDEKIKkekkvkyesKVFLDQKRGHPeVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1201 EIRL------NEQAEKMKGK-------LEEL---SNQLHRSQEEEGTQRKALEAQNEIHTKE-KEKLIDKIqEMQEASDH 1263
Cdd:pfam02029 252 ELRRrrqekeSEEFEKLRQKqqeaeleLEELkkkREERRKLLEEEEQRRKQEEAERKLREEEeKRRMKEEI-ERRRAEAA 330
|
....*....
gi 767984698 1264 LKKQFETES 1272
Cdd:pfam02029 331 EKRQKLPED 339
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1192-1319 |
2.28e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.11 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1192 ELEKQKQDLEIRLNE---QAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEK---EKLIDKIQEMQEASDHLK 1265
Cdd:pfam15905 160 ELMKLRNKLEAKMKEvmaKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKsetEKLLEYITELSCVSEQVE 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 767984698 1266 KQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGK 1319
Cdd:pfam15905 240 KYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEE 293
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
920-1317 |
2.36e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.12 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 920 KRYRDAVEEKLA--KLQKHNSELETQKEQIQLKLQeKTEELKEKMDNLtkQLFDDVQKEERQRMLLEKSFELKTQDYEKQ 997
Cdd:TIGR01612 466 KRFFEIFEEEWGsyDIKKDIDENSKQDNTVKLILM-RMKDFKDIIDFM--ELYKPDEVPSKNIIGFDIDQNIKAKLYKEI 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 998 IQSLKEEIKALKD-EKMQLQHLVEGEHVTSDGLKaevarLSKQVKTIseFEKEIELlqaqkIDVEKHVQSQKREMREKMS 1076
Cdd:TIGR01612 543 EAGLKESYELAKNwKKLIHEIKKELEEENEDSIH-----LEKEIKDL--FDKYLEI-----DDEIIYINKLKLELKEKIK 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1077 EITKQ---LLESYDIEDV--RSRLSVEDLEHLNEdgelWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQE 1151
Cdd:TIGR01612 611 NISDKneyIKKAIDLKKIieNNNAYIDELAKISP----YQVPEHLKNKDKIYSTIKSELSKIYEDDIDALYNELSSIVKE 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1152 --INHLQKLFREEnDINESIRHEVTRLtsENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGkleELSNQLHRSQEEe 1229
Cdd:TIGR01612 687 naIDNTEDKAKLD-DLKSKIDKEYDKI--QNMETATVELHLSNIENKKNELLDIIVEIKKHIHG---EINKDLNKILED- 759
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1230 gtqrkaleaqneIHTKEKEkLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQ 1309
Cdd:TIGR01612 760 ------------FKNKEKE-LSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIK 826
|
....*...
gi 767984698 1310 VKTLSKTI 1317
Cdd:TIGR01612 827 EDEIFKII 834
|
|
| TBCA |
pfam02970 |
Tubulin binding cofactor A; |
1116-1220 |
2.84e-03 |
|
Tubulin binding cofactor A;
Pssm-ID: 460769 [Multi-domain] Cd Length: 99 Bit Score: 38.64 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1116 LKKATRVLEsHFQSQKDCYEKEIEalnfkvvhlsQEINHLQKLFREENDINEsIRHEVTRLTSENMMIPDFKQQIselEK 1195
Cdd:pfam02970 6 LKIKTGVVK-RLVKEEASYEKELE----------EQEARLEKLKADGADEYD-LKKQEEVLEETKAMIPDLKKRL---EE 70
|
90 100
....*....|....*....|....*
gi 767984698 1196 QKQDLEIRLNEQAEKMKGkLEELSN 1220
Cdd:pfam02970 71 AVEDLEEFLEEEEDLGAD-TEELTA 94
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1024-1307 |
2.87e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.72 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1024 VTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDvrsrlSVEDLEHL 1103
Cdd:pfam15905 56 VKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSA-----SVASLEKQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1104 NEDgelwfayegLKKATRVLESHFQSqkDCYEKEIEALNFKVVHLSQEINHLQK-LFREENDINESIRHEVTRLTSENMM 1182
Cdd:pfam15905 131 LLE---------LTRVNELLKAKFSE--DGTQKKMSSLSMELMKLRNKLEAKMKeVMAKQEGMEGKLQVTQKNLEHSKGK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1183 IPDFKQQISELEKQKQDLEirlnEQAEKMKGKLEELSN---QLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQE 1259
Cdd:pfam15905 200 VAQLEEKLVSTEKEKIEEK----SETEKLLEYITELSCvseQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSK 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 767984698 1260 ASDHLK---KQFETESEVKCN-FRQEASRLTLENRDLEEELDMKDRVIKKLQ 1307
Cdd:pfam15905 276 QIKDLNekcKLLESEKEELLReYEEKEQTLNAELEELKEKLTLEEQEHQKLQ 327
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
867-1273 |
2.87e-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: 42.73 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 867 QKKLEDQNKENHGLVEKLTSLAALRagdvEKIQKLEAELEKAATH---------RRNYEEKGKRYRDAvEEKLAKLQKhn 937
Cdd:TIGR00606 254 LKEIEHNLSKIMKLDNEIKALKSRK----KQMEKDNSELELKMEKvfqgtdeqlNDLYHNHQRTVREK-ERELVDCQR-- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 938 sELETQKEQIQLKLQEKTEELKEKMdnlTKQLFDDVQKEErqrmlleksfelkTQDYEKQIQSLkeeikALKDEKMQLQH 1017
Cdd:TIGR00606 327 -ELEKLNKERRLLNQEKTELLVEQG---RLQLQADRHQEH-------------IRARDSLIQSL-----ATRLELDGFER 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1018 LVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIEllqaqkiDVEKHVQSQKREMREKMSEITKQLlesyDIEDVRSRLSV 1097
Cdd:TIGR00606 385 GPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQ-------SKERLKQEQADEIRDEKKGLGRTI----ELKKEILEKKQ 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1098 EDLEHLNEDGELwfAYEGLKKATRVLESHFQSQKDCYEKE----IEALNFKVVHLSQEINHLQKLFREENDINESIRHEV 1173
Cdd:TIGR00606 454 EELKFVIKELQQ--LEGSSDRILELDQELRKAERELSKAEknslTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHT 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1174 TRLTSENMMIP---DFKQQISELEKQKQDLEI-----------------RLNEQAEKMKGKLEELSNQLHRSQEEEGTQR 1233
Cdd:TIGR00606 532 TTRTQMEMLTKdkmDKDEQIRKIKSRHSDELTsllgyfpnkkqledwlhSKSKEINQTRDRLAKLNKELASLEQNKNHIN 611
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 767984698 1234 KALEAQNEIHTKEKEKLIDKIQEMQEASD--HLKKQFETESE 1273
Cdd:TIGR00606 612 NELESKEEQLSSYEDKLFDVCGSQDEESDleRLKEEIEKSSK 653
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
1185-1348 |
2.90e-03 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 40.91 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1185 DFKQQISELEKQKQDLEIRLNEQaekmkgkLEELSNQLHRSQEEEGTQRKALEAQNEIhTKEKEKLIDKIQEMQEASDHL 1264
Cdd:pfam14988 26 QYVQECEEIERRRQELASRYTQQ-------TAELQTQLLQKEKEQASLKKELQALRPF-AKLKESQEREIQDLEEEKEKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1265 KKQF-ETESEVKCNFRQEASRLTLENRDLeEELDMKDRVIKKLQDQVKTLSKTIGKANDVHSSSGPKEYlgmlQYKREDE 1343
Cdd:pfam14988 98 RAETaEKDREAHLQFLKEKALLEKQLQEL-RILELGERATRELKRKAQALKLAAKQALSEFCRSIKREN----RQLQKEL 172
|
....*
gi 767984698 1344 AKLIQ 1348
Cdd:pfam14988 173 LQLIQ 177
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1187-1313 |
3.30e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1187 KQQISELEKQKQDLEIRL---NEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEihtkEKEKLIDKIQEMQEASDH 1263
Cdd:COG4372 51 REELEQAREELEQLEEELeqaRSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE----EAEELQEELEELQKERQD 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767984698 1264 LKkqfetesevkcnfrQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTL 1313
Cdd:COG4372 127 LE--------------QQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
|
| DUF6262 |
pfam19776 |
Family of unknown function (DUF6262); This family of proteins, functionally uncharacterized, ... |
914-1015 |
3.64e-03 |
|
Family of unknown function (DUF6262); This family of proteins, functionally uncharacterized, is found in bacteria. Proteins in this family are typically between 124 and 143 amino acids in length. Some members included in this family are hypothetical transposases, associated with transposon Tn554. There is a conserved sequence GV/LSR/K and a highly conserved tyrosine residue.
Pssm-ID: 466180 [Multi-domain] Cd Length: 110 Bit Score: 38.75 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 914 NYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQL-KLQEKT----------EELKEKMDNLTKQlfddvQKE--ERQR 980
Cdd:pfam19776 1 KYDKMVELNRKESEEKIELAKKAIQEMLEEGEKITVpELVKRTglsrgffyknPEVRRELDEAIEQ-----QGGmvNPKR 75
|
90 100 110
....*....|....*....|....*....|....*
gi 767984698 981 MLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQL 1015
Cdd:pfam19776 76 EILDMALEKRIELLKKEIKELKRENEELKKENEKL 110
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
958-1226 |
3.76e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 958 LKEKMDNLTKQL-------FDDVQKEErQRMLLEKSFELKTQDYEK--QIQSLKEEIKALKDEKMQLQHLVegehvTSDG 1028
Cdd:PRK05771 14 LKSYKDEVLEALhelgvvhIEDLKEEL-SNERLRKLRSLLTKLSEAldKLRSYLPKLNPLREEKKKVSVKS-----LEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1029 LKAEVARLSKQVKTISEFEKEIELLQaqkidvekhvqSQKREMREKMSEITKqlLESYDIedvrsrlsveDLEHLNeDGE 1108
Cdd:PRK05771 88 IKDVEEELEKIEKEIKELEEEISELE-----------NEIKELEQEIERLEP--WGNFDL----------DLSLLL-GFK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1109 LWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFRE-------ENDINESIrhEVTRLtsenm 1181
Cdd:PRK05771 144 YVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEElkklgfeRLELEEEG--TPSEL----- 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 767984698 1182 mIPDFKQQISELEKQKQDLEIRLNEQAEK----MKGKLEELSNQLHRSQ 1226
Cdd:PRK05771 217 -IREIKEELEEIEKERESLLEELKELAKKyleeLLALYEYLEIELERAE 264
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
858-1082 |
3.90e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 858 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYR--DAVEEKLAKLQK 935
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQleELEQEIAALLAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 936 HNSELETQKEQIQLKLQEKtEELKEKMDNLTKQLfDDVQKEERQRMLLEKSFELKT--QDYEKQIQSLKEEIKALKDEKM 1013
Cdd:COG4717 379 AGVEDEEELRAALEQAEEY-QELKEELEELEEQL-EELLGELEELLEALDEEELEEelEELEEELEELEEELEELREELA 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767984698 1014 QLQHLVE--GEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKR-EMREKMSEITKQL 1082
Cdd:COG4717 457 ELEAELEqlEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLpPVLERASEYFSRL 528
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
926-1140 |
4.20e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.94 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 926 VEEKLAKLQKH---NSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEER-----QRMLLEKSFELktQDYEKQ 997
Cdd:pfam05701 231 AEEELQRLNQQllsAKDLKSKLETASALLLDLKAELAAYMESKLKEEADGEGNEKKtstsiQAALASAKKEL--EEVKAN 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 998 IQSLKEEIKALKDEKMQLQHLVEGEhvtsdglKAEVARLSKQ----VKTISEFEKEIELLQaQKIDVekhVQSQKREMRE 1073
Cdd:pfam05701 309 IEKAKDEVNCLRVAAASLRSELEKE-------KAELASLRQRegmaSIAVSSLEAELNRTK-SEIAL---VQAKEKEARE 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1074 KMSEITKQLLE-SYDIEDVRS--RLSVEDLEHLNEDGELwfayegLKKATRVLESHFQSQKdcyeKEIEA 1140
Cdd:pfam05701 378 KMVELPKQLQQaAQEAEEAKSlaQAAREELRKAKEEAEQ------AKAAASTVESRLEAVL----KEIEA 437
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
997-1258 |
4.23e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 997 QIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKA---EVARLSKQV----KTISEFEKEIELLQAQKIDVEKHVQSQKR 1069
Cdd:PRK01156 160 EINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSsnlELENIKKQIaddeKSHSITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1070 EMREKMS-EITKQLLESyDIEDVRSRLSVEdLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHL 1148
Cdd:PRK01156 240 ALNELSSlEDMKNRYES-EIKTAESDLSME-LEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNI 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1149 SQEINHLQKLFREENDInESIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNEqAEKMKGKLEELSNQLHRSQEE 1228
Cdd:PRK01156 318 DAEINKYHAIIKKLSVL-QKDYNDYIKKKSR---YDDLNNQILELEGYEMDYNSYLKS-IESLKKKIEEYSKNIERMSAF 392
|
250 260 270
....*....|....*....|....*....|
gi 767984698 1229 EGTQRKALEAQNEIHTKEKEKLIDKIQEMQ 1258
Cdd:PRK01156 393 ISEILKIQEIDPDAIKKELNEINVKLQDIS 422
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
898-1263 |
4.33e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.96 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 898 IQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQK---------HNSELETQKEQIQLKLQEKteelKEKMDNLTKq 968
Cdd:TIGR01612 1120 IKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDvadkaisndDPEEIEKKIENIVTKIDKK----KNIYDEIKK- 1194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 969 LFDDVQKEERQRMLLEKSFELKTQdYEKQIQSLKEEikALKDEKMQLQHLV---EGEHVTSDGLKAEVARLSKQVKTISE 1045
Cdd:TIGR01612 1195 LLNEIAEIEKDKTSLEEVKGINLS-YGKNLGKLFLE--KIDEEKKKSEHMIkamEAYIEDLDEIKEKSPEIENEMGIEMD 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1046 FEKEIELLQAQKIDVEKH-VQSQKR-----EMREKMSEITKQLLESYDIEDVRSRLSvedlehlnedgelwfayeglkka 1119
Cdd:TIGR01612 1272 IKAEMETFNISHDDDKDHhIISKKHdenisDIREKSLKIIEDFSEESDINDIKKELQ----------------------- 1328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1120 TRVLESH-FQSQKDCYEKEIEALnFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISeLEKQKQ 1198
Cdd:TIGR01612 1329 KNLLDAQkHNSDINLYLNEIANI-YNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDIN-LEECKS 1406
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767984698 1199 DLEIRL-----NEQAEKMKGK-----LEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDH 1263
Cdd:TIGR01612 1407 KIESTLddkdiDECIKKIKELknhilSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDH 1481
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
896-1111 |
4.63e-03 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 40.97 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 896 EKIQKLEAELEKAAthrRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQK 975
Cdd:pfam09755 85 KKIQALKKEKETLA---MNYEQEEEFLTNDLSRKLTQLRQEKVELEQTLEQEQEYQVNKLMRKIEKLEAETLNKQTNLEQ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 976 EERQRMLLEKSFElktQDYEKQIQSLKEEIKALKDEKMQLQHLVE-------------GEHVTSDGLKAEVARLSKQVkt 1042
Cdd:pfam09755 162 LRREKVELENTLE---QEQEALVNRLWKRMDKLEAEKRLLQEKLDqpvsappsprdstSEGDTAQNLTAHIQYLRKEV-- 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767984698 1043 iSEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDGELWF 1111
Cdd:pfam09755 237 -ERLRRQLATAQQEHTEKMAQYAQEERHIREENLRLQRKLQLEMERREALCRHLSESESSLEMDEERYF 304
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
895-1041 |
4.74e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 41.12 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 895 VEKIQKLEAELEKAATHRRNYEEKGKRY---RDAVEEKLAKLQKHNSELETQKEqiqlKLQEKTEELKEKmdnltKQLFD 971
Cdd:pfam02841 154 LEERDKLEAKYNQVPRKGVKAEEVLQEFlqsKEAVEEAILQTDQALTAKEKAIE----AERAKAEAAEAE-----QELLR 224
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767984698 972 DVQKEERQRMlleksfELKTQDYEKQIQSLKEEIKALKD------EKMQLQHLVEGEHVTSDGLKAEVARLSKQVK 1041
Cdd:pfam02841 225 EKQKEEEQMM------EAQERSYQEHVKQLIEKMEAEREqllaeqERMLEHKLQEQEELLKEGFKTEAESLQKEIQ 294
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
931-1014 |
5.20e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.10 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 931 AKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQlfddvQKEERqrmllEKSFELKTQDYEKQIQSLKEEIKALKD 1010
Cdd:smart00935 21 KQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEA-----AREKK-----EKELQKKVQEFQRKQQKLQQDLQKRQQ 90
|
....
gi 767984698 1011 EKMQ 1014
Cdd:smart00935 91 EELQ 94
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1114-1321 |
5.51e-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: 41.48 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1114 EGLKKATRVLESHFQSQKDCYEKEIEALNfKVVHLSQEINHLQKLFREENDI-NESIRHEVTRLTSENMMIPDFKQQISE 1192
Cdd:COG5185 186 LGLLKGISELKKAEPSGTVNSIKESETGN-LGSESTLLEKAKEIINIEEALKgFQDPESELEDLAQTSDKLEKLVEQNTD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1193 LEK----QKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEK-LIDKIQEMQEASDHLKKQ 1267
Cdd:COG5185 265 LRLeklgENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQeLEESKRETETGIQNLTAE 344
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767984698 1268 FETESEvKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKAN 1321
Cdd:COG5185 345 IEQGQE-SLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIP 397
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
924-1005 |
5.65e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 39.43 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 924 DAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQ--LFDDVQKEERQRML--LEKSFELKTQDYEKQIQ 999
Cdd:COG2825 32 QRILQESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEaaTLSEEERQKKERELqkKQQELQRKQQEAQQDLQ 111
|
....*.
gi 767984698 1000 SLKEEI 1005
Cdd:COG2825 112 KRQQEL 117
|
|
| IQ |
pfam00612 |
IQ calmodulin-binding motif; Calmodulin-binding motif. |
803-823 |
6.28e-03 |
|
IQ calmodulin-binding motif; Calmodulin-binding motif.
Pssm-ID: 459869 Cd Length: 21 Bit Score: 35.76 E-value: 6.28e-03
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
862-988 |
7.73e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 38.87 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 862 RVQRLQKKLEDQNKENHGLVEKLtSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRY-RDAVEEKLAKLQKHNSEL 940
Cdd:pfam05672 21 RQAREQREREEQERLEKEEEERL-RKEELRRRAEEERARREEEARRLEEERRREEEERQRKaEEEAEEREQREQEEQERL 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 767984698 941 ETQKEQIQLKLQEKTEELKEKMDNLTkqlfddvQKEERQRMLLEKSFE 988
Cdd:pfam05672 100 QKQKEEAEAKAREEAERQRQEREKIM-------QQEEQERLERKKRIE 140
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
857-993 |
8.02e-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: 41.19 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 857 IQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKR---YRDAVEEKLAKL 933
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRrqqFEEQLVELSTEV 897
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767984698 934 QKHNSELETQKEQI------QLKLQEKTEEL---KEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQD 993
Cdd:TIGR00606 898 QSLIREIKDAKEQDspletfLEKDQQEKEELissKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQD 966
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
905-1002 |
8.10e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 40.35 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 905 LEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDV-----QKEERQ 979
Cdd:pfam02841 195 TDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEKMEAEREQLLAEQermleHKLQEQ 274
|
90 100
....*....|....*....|...
gi 767984698 980 RMLLEKSFELKTQDYEKQIQSLK 1002
Cdd:pfam02841 275 EELLKEGFKTEAESLQKEIQDLK 297
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1150-1333 |
8.31e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1150 QEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLN-----EQAEKMKGKLEELSNQLHR 1224
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1225 SQEEEgTQRKALEaqneihtKEKEKLIDKIQEMQEASDHLKKQFETESevkcnfRQEASRLTLENRDLEEELDMKDRVIK 1304
Cdd:COG4717 151 LEERL-EELRELE-------EELEELEAELAELQEELEELLEQLSLAT------EEELQDLAEELEELQQRLAELEEELE 216
|
170 180
....*....|....*....|....*....
gi 767984698 1305 KLQDQVKTLSKTIGKANDVHSSSGPKEYL 1333
Cdd:COG4717 217 EAQEELEELEEELEQLENELEAAALEERL 245
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
951-1157 |
8.55e-03 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 39.37 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 951 LQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQiqsLKEEIKALKDEKMQLQHLvegehvtsdglk 1030
Cdd:pfam14988 9 LAKKTEEKQKKIEKLWNQYVQECEEIERRRQELASRYTQQTAELQTQ---LLQKEKEQASLKKELQAL------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1031 AEVARLSKQVktisefEKEIELLQAQKIDVEKHVQSQKREMREKMSEiTKQLLESyDIEDVRSRLSVEDLEHlnedgELW 1110
Cdd:pfam14988 74 RPFAKLKESQ------EREIQDLEEEKEKVRAETAEKDREAHLQFLK-EKALLEK-QLQELRILELGERATR-----ELK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767984698 1111 FAYEGLK-KATRVLESHFQSQKdcyeKEIEALNFKVVHLSQEINHLQK 1157
Cdd:pfam14988 141 RKAQALKlAAKQALSEFCRSIK----RENRQLQKELLQLIQETQALEA 184
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1160-1269 |
9.07e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 9.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767984698 1160 REENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEirlnEQAEKMKGKLEELSNQLHRSQEEEgtqRKALEAQ 1239
Cdd:COG2433 392 EEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE----AELEEKDERIERLERELSEARSEE---RREIRKD 464
|
90 100 110
....*....|....*....|....*....|..
gi 767984698 1240 NEIHTKEKE--KLIDKIQEMQEASDHLKKQFE 1269
Cdd:COG2433 465 REISRLDREieRLERELEEERERIEELKRKLE 496
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
755-776 |
9.97e-03 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 34.99 E-value: 9.97e-03
|
| |
