|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
276-630 |
1.03e-102 |
|
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.
Pssm-ID: 462869 [Multi-domain] Cd Length: 303 Bit Score: 316.25 E-value: 1.03e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 276 LDEKSDKQYAENYT---------RPSSRNSASATTPLSGNSSRRGSGDTSSLIDPDTSLSELRDiydlkdqiqdvegrym 346
Cdd:pfam09738 30 VEENADRVFDMSSSsgadtasgsPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKH---------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 347 qglkelkeSLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKM 426
Cdd:pfam09738 94 --------ELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 427 EELKEGLRQRDELIeekqrmqqkidtmtkevfdlqetllwkdkkigalekqkeyiaclrnerdmlreeladlqetvktgE 506
Cdd:pfam09738 166 AELKEQLKQRDELI-----------------------------------------------------------------E 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 507 KHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQ-KCSRN 585
Cdd:pfam09738 181 KHGLVIVPDENTNGEEENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKSkRNSTR 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 578806710 586 DGTVGDLAGLQNGSDLqfIEMQRDANRQISEYKFKLSKAEQDITT 630
Cdd:pfam09738 261 SSQSPDGFGLENGSHV--IEVQREANKQISDYKFKLQKAEQEITT 303
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
303-681 |
1.73e-11 |
|
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: 67.79 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 303 LSGNSSRRGSGDTSSLIDPDTSLSELRDIYDLKDQ---IQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNN 379
Cdd:TIGR02169 655 MTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRElssLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 380 LIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQrdELIEEKQRMQQKIDtmtKEVFD 459
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLE---EEVSR 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 460 LQETLLWKDKKIGALEKQKEYiacLRNERDMLREELADLQETVKTGEKhglviipdgtpNGDVSHEPVAGAITVVSQEAA 539
Cdd:TIGR02169 810 IEARLREIEQKLNRLTLEKEY---LEKEIQELQEQRIDLKEQIKSIEK-----------EIENLNGKKEELEEELEELEA 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 540 QVLEsagegpLDVRLRKLAGEKEELLSQIRKLKL---QLEEERQKCSRNDGTVGDLAGLQNGsDLQFIEMQRDANRQISE 616
Cdd:TIGR02169 876 ALRD------LESRLGDLKKERDELEAQLRELERkieELEAQIEKKRKRLSELKAKLEALEE-ELSEIEDPKGEDEEIPE 948
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578806710 617 YKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEME 681
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
349-680 |
5.87e-10 |
|
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: 62.77 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 349 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEE 428
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 429 LKEglrQRDELIEEKQRMQQKIDTMTKEVFDLQETLlwkDKKIGALEKQKEYIACLRNERDMLREELADLQETVKTGEKh 508
Cdd:TIGR02168 759 LEA---EIEELEERLEEAEEELAEAEAEIEELEAQI---EQLKEELKALREALDELRAELTLLNEEAANLRERLESLER- 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 509 glviipdgtpngdvSHEPVAGAITVVSQEAAQVLEsagegpldvRLRKLAGEKEELLSQIRKLKLQLEE-ERQKCSRNDG 587
Cdd:TIGR02168 832 --------------RIAATERRLEDLEEQIEELSE---------DIESLAAEIEELEELIEELESELEAlLNERASLEEA 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 588 TVGDLAGLQN-GSDLQFIEMQR-DANRQISEYKFKLSKAEQDITTLEQSISRLEGQVL-RYKTAAENAEKVEDELKAEKR 664
Cdd:TIGR02168 889 LALLRSELEElSEELRELESKRsELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEE 968
|
330
....*....|....*.
gi 578806710 665 KLQRELRTALDKIEEM 680
Cdd:TIGR02168 969 EARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
310-680 |
7.60e-09 |
|
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: 59.30 E-value: 7.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 310 RGSGDTSSLIdpdtsLSELRDIYDLKDQIQDVEGRYMQGLKELKESLSEVEEkYKKAMVSNAQLDNEKNNLIYQVDTLKD 389
Cdd:TIGR02168 663 GGSAKTNSSI-----LERRREIEELEEKIEELEEKIAELEKALAELRKELEE-LEEELEQLRKELEELSRQISALRKDLA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 390 VIEEQEEQMAEFYRENEEKSKELERQKhmcSVLQHKMEELKEGLrqrDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDK 469
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEI---EELEERLEEAEEEL---AEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 470 KIGALE----KQKEYIACLRNERDMLREELADLQETVKTGEKHGLVI---IPDGTPNGDVSHEPVAGAITVV-SQEAAQV 541
Cdd:TIGR02168 811 ELTLLNeeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaaeIEELEELIEELESELEALLNERaSLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 542 LESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLagLQNGSDLQFIEMQrDANRQISEYKFKL 621
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL--QERLSEEYSLTLE-EAEALENKIEDDE 967
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 622 SKAEQDITTLEQSISRLeGQV-LRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEM 680
Cdd:TIGR02168 968 EEARRRLKRLENKIKEL-GPVnLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
349-681 |
3.11e-08 |
|
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: 57.37 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 349 LKELKESL------SEVEEKYKkamvsnaQLDNEKNNLiyQVDTLKDVIEEQEEQMAEF---YRENEEKSKELERQKHMc 419
Cdd:TIGR02168 195 LNELERQLkslerqAEKAERYK-------ELKAELREL--ELALLVLRLEELREELEELqeeLKEAEEELEELTAELQE- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 420 svLQHKMEELKEGLRQRDELIEEKQR----MQQKIDTMTKEVFDLQETLLWKDKKIGALEkqkEYIACLRNERDMLREEL 495
Cdd:TIGR02168 265 --LEEKLEELRLEVSELEEEIEELQKelyaLANEISRLEQQKQILRERLANLERQLEELE---AQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 496 ADLQETVKTGEKhglviipdgtpngdvSHEPVAGAITvVSQEAAQVLESAGEGpLDVRLRKLAGEKEELLSQIRKLKLQL 575
Cdd:TIGR02168 340 AELEEKLEELKE---------------ELESLEAELE-ELEAELEELESRLEE-LEEQLETLRSKVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 576 EEERQKCSRNDGTVGdlaglqngsdlQFIEMQRDANRQISEYKFKLSKAEqdITTLEQSISRLEGQVLRYKTAAENAEKV 655
Cdd:TIGR02168 403 ERLEARLERLEDRRE-----------RLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEALEELREE 469
|
330 340
....*....|....*....|....*.
gi 578806710 656 EDELKAEKRKLQRELRTALDKIEEME 681
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLE 495
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
403-652 |
7.40e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 7.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 403 RENEEKSKELERQkhmcsvLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQkeyIA 482
Cdd:COG4942 23 AEAEAELEQLQQE------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE---IA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 483 CLRNERDMLREELAD-LQETVKTGEKHGL-VIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEgpldvRLRKLAGE 560
Cdd:COG4942 94 ELRAELEAQKEELAElLRALYRLGRQPPLaLLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-----ELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 561 KEELLSQIRKLKLQLEEERQKcsrndgtvgdLAGLQNGSDlqfiEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEG 640
Cdd:COG4942 169 LEAERAELEALLAELEEERAA----------LEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
250
....*....|..
gi 578806710 641 QVLRYKTAAENA 652
Cdd:COG4942 235 EAAAAAERTPAA 246
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
332-507 |
4.47e-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: 50.06 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 332 YDLKDQIQDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKE 411
Cdd:TIGR02168 291 YALANEISRLEQQ----KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 412 LErqkhmcsVLQHKMEELKEGL-RQRDELIEEKQRMQQ---KIDTMTKEVFDLQETL---------LWKDKKIGALEKQK 478
Cdd:TIGR02168 367 LE-------ELESRLEELEEQLeTLRSKVAQLELQIASlnnEIERLEARLERLEDRRerlqqeieeLLKKLEEAELKELQ 439
|
170 180
....*....|....*....|....*....
gi 578806710 479 EYIACLRNERDMLREELADLQETVKTGEK 507
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELRE 468
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
335-598 |
5.92e-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: 49.67 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 335 KDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKN-------NLIYQVDTLKDVIEEQEEQMAEFYRENEE 407
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 408 KSKELERQKhmcSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQ----KEYIAC 483
Cdd:TIGR02168 321 LEAQLEELE---SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqlELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 484 LRNERDMLREELADLQETVktgEKHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEgpLDVRLRKLAGEKEE 563
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRR---ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELER--LEEALEELREELEE 472
|
250 260 270
....*....|....*....|....*....|....*
gi 578806710 564 LLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNG 598
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
383-696 |
6.22e-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: 49.68 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 383 QVDTLKDVIEEQEEQMAEFYRENEEKSKELErqkhmcsvLQHKMEELK--EGLRQRDELIEEKQRMQQKIDTMTKEVFDL 460
Cdd:TIGR02169 185 NIERLDLIIDEKRQQLERLRREREKAERYQA--------LLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 461 QETLLWKDKKIGALEKQKEYIAclRNERDMLREELADLQETVktGEKHGLViipdgtpngdvshEPVAGAITVVSQEAAQ 540
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKI--GELEAEI-------------ASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 541 vlesagegpLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNG--SDLQFIEMQRDANRQ-ISEY 617
Cdd:TIGR02169 320 ---------AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDlrAELEEVDKEFAETRDeLKDY 390
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806710 618 KFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 696
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
387-705 |
6.24e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 387 LKDVIEEQEEQM---------AEFYRENEEKSKELERQkhmcsVLQHKMEELKEGLRQRDELIEEKQRMQQKIDtmtkev 457
Cdd:COG1196 191 LEDILGELERQLeplerqaekAERYRELKEELKELEAE-----LLLLKLRELEAELEELEAELEELEAELEELE------ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 458 fdlqetllwkdKKIGALEKQKEYiacLRNERDMLREELADLQEtvktgekhglviipdgtpngdvshepvagAITVVSQE 537
Cdd:COG1196 260 -----------AELAELEAELEE---LRLELEELELELEEAQA-----------------------------EEYELLAE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 538 AAQvlESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQkcsrndgtvgdlaglqngsdlqfiemqrdanrQISEY 617
Cdd:COG1196 297 LAR--LEQDIARLEERRRELEERLEELEEELAELEEELEELEE--------------------------------ELEEL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 618 KFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKAN 697
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
....*...
gi 578806710 698 RTALLAQQ 705
Cdd:COG1196 423 LEELEEAL 430
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
333-696 |
9.26e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 9.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 333 DLKDQIQDVE--------GRYMQGLKELKESLSEVEEKYKKAMVSNAQLD---NEKNNLIYQVDTLKDVIEEQEEQMAEF 401
Cdd:PRK02224 191 QLKAQIEEKEekdlherlNGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 402 YRENEEKSKELERQKHMCSVLqhkmEELKEGLRQRDELIE-EKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEy 480
Cdd:PRK02224 271 EREREELAEEVRDLRERLEEL----EEERDDLLAEAGLDDaDAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAE- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 481 iaCLRNERDMLREELADLQETVKTGEKhglviipdGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGPldVRLRKLAGE 560
Cdd:PRK02224 346 --SLREDADDLEERAEELREEAAELES--------ELEEAREAVEDRREEIEELEEEIEELRERFGDAP--VDLGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 561 KEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDL----QFIEMQRDANRqISEYKFKLSKAEQDITTLEQSIS 636
Cdd:PRK02224 414 LEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpecgQPVEGSPHVET-IEEDRERVEELEAELEDLEEEVE 492
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578806710 637 RLEGQVLRYKTAAENAEKVEDelKAEKRKLQRELR-TALDKIEEMEMTNSHLAKRLEKMKA 696
Cdd:PRK02224 493 EVEERLERAEDLVEAEDRIER--LEERREDLEELIaERRETIEEKRERAEELRERAAELEA 551
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
333-696 |
1.03e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 333 DLKDQIQDVEGRYMQGLKELKESLSEVE---------EKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYR 403
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPelreeleklEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 404 ENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQEtllwkdkKIGALEKQKEYIAC 483
Cdd:PRK03918 270 ELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE-------RIKELEEKEERLEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 484 LRNERDMLREELADLQETVKTGEKhglviipdgtpngdvshepvAGAITVVSQEAAQVLESAGEGPLDVRLRKLAGEKEE 563
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEE--------------------AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 564 LLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQI-SEYKFKLSKAEQDITTLEQSISRL---- 638
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELlEEYTAELKRIEKELKEIEEKERKLrkel 482
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578806710 639 ---------EGQVLRYKTAAENAEKVEDELKA----EKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 696
Cdd:PRK03918 483 relekvlkkESELIKLKELAEQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
330-549 |
1.20e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 330 DIYDLKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLD---NEKNNLIYQVDTLKDVIEEQEEQMAEFYRENE 406
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEalqAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 407 EKSKE----------------LERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETllwKDKK 470
Cdd:COG3883 97 RSGGSvsyldvllgsesfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA---KAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806710 471 IGALEKQKEYIACLRNERDMLREELADLQETVKTGEKHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGP 549
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
329-704 |
1.26e-05 |
|
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: 48.90 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 329 RDIYDLKDQIQDVEgrymQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQM-------AEF 401
Cdd:TIGR02168 316 RQLEELEAQLEELE----SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLetlrskvAQL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 402 YRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQR--MQQKIDTMTKEVFDLQETLlwkDKKIGALEKQKE 479
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEEL---ERLEEALEELRE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 480 YIACLRNERDMLREELA-----------------DLQETVKTGEKHGLVIIPDGTPNGD-VSHEP------------VAG 529
Cdd:TIGR02168 469 ELEEAEQALDAAERELAqlqarldslerlqenleGFSEGVKALLKNQSGLSGILGVLSElISVDEgyeaaieaalggRLQ 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 530 AITVVSQEAA----QVLESAGEG-----PLD-VRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAG----- 594
Cdd:TIGR02168 549 AVVVENLNAAkkaiAFLKQNELGrvtflPLDsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGgvlvv 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 595 --LQNGSDLQ--------FIEMQ--------------RDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAE 650
Cdd:TIGR02168 629 ddLDNALELAkklrpgyrIVTLDgdlvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELE 708
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 578806710 651 NAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 704
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
550-704 |
1.43e-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: 46.84 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 550 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAglqngSDLQFIEMQ-RDANRQISEYKFKLSKA---- 624
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE-----KEIKRLELEiEEVEARIKKYEEQLGNVrnnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 625 -----EQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEmtnSHLAKRLEKMKANRT 699
Cdd:COG1579 90 eyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL---AELEAELEELEAERE 166
|
....*
gi 578806710 700 ALLAQ 704
Cdd:COG1579 167 ELAAK 171
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
325-701 |
2.33e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 325 LSELRDIYDLKDQIQDVEGRYmqglKELKESLSEVEEKYKKAMVSNAQLDNEKNNLiyqvdtlkdvieEQEEQMAEFYRE 404
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKL------------EKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 405 NEEKSKELERqkhmcsvLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKigALEKQKEYIACL 484
Cdd:COG4717 134 LEALEAELAE-------LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE--ELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 485 RNERDMLREELADLQETVKTGEKH----------------------------GLVIIPDGTPNGDVSHEPVAGAITVV-- 534
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEEleqleneleaaaleerlkearlllliaaALLALLGLGGSLLSLILTIAGVLFLVlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 535 ---------SQEAAQVLESAGEGPLDVRLRKLAGEK-------------------EELLSQIRKLKL------QLEEERQ 580
Cdd:COG4717 285 llallflllAREKASLGKEAEELQALPALEELEEEEleellaalglppdlspeelLELLDRIEELQEllreaeELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 581 KCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQIsEYKFKLSKAEQDITTLEQSI---------SRLEGQVLRYKTAAEN 651
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELeellealdeEELEEELEELEEELEE 443
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 578806710 652 AEKVEDELKAEKRKLQRELRT---------ALDKIEEMEMTNSHLAKRLEKMKANRTAL 701
Cdd:COG4717 444 LEEELEELREELAELEAELEQleedgelaeLLQELEELKAELRELAEEWAALKLALELL 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
399-682 |
2.43e-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: 47.76 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 399 AEFYRENEEKSKELERQKHMCSVLQHKMEELKEglrQRDELIEEKQRmQQKIDTMTKEVFDLQETLLWKDKKigALEKQK 478
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREK-AERYQALLKEKREYEGYELLKEKE--ALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 479 EYIaclRNERDMLREELADLQETVKTGEKHglviipdgtpngdvshepVAGAITVVSQEAAQVLESAGEGPLDVR--LRK 556
Cdd:TIGR02169 240 EAI---ERQLASLEEELEKLTEEISELEKR------------------LEEIEQLLEELNKKIKDLGEEEQLRVKekIGE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 557 LAGEKEELLSQIRKLKLQLE----EERQKCSRNDGTVGDLAGLQngSDLQFIEMQRDA-NRQISEYKFKLSKAEQDITTL 631
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEdaeeRLAKLEAEIDKLLAEIEELE--REIEEERKRRDKlTEEYAELKEELEDLRAELEEV 376
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 578806710 632 EQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEM 682
Cdd:TIGR02169 377 DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
330-701 |
2.65e-05 |
|
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: 47.71 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 330 DIYDLKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEK---NNLIYQVDTLKDVIEEQEEQMAEFYRENE 406
Cdd:TIGR04523 69 KINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKeqkNKLEVELNKLEKQKKENKKNIDKFLTEIK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 407 EKSKELERQKHMCSVLQHKMEELKEglrQRDELIEEKQRMQQKIDTMTKEVFDLQETLL---WKDKKIGALEKQ----KE 479
Cdd:TIGR04523 149 KKEKELEKLNNKYNDLKKQKEELEN---ELNLLEKEKLNIQKNIDKIKNKLLKLELLLSnlkKKIQKNKSLESQiselKK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 480 YIACLRNERDMLREELADLQETVKTGEKHGLVIIPDGTPNGDVSHEP---VAGAITVVSQEAAQVLEsagegpLDVRLRK 556
Cdd:TIGR04523 226 QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKqkeLEQNNKKIKELEKQLNQ------LKSEISD 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 557 LAGEKE-----ELLSQIRKLKLQLEEERQKCSRNDGTVGDLaglqnGSDLQFIEMQRD--------ANRQISEYKFKLSK 623
Cdd:TIGR04523 300 LNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQL-----NEQISQLKKELTnsesenseKQRELEEKQNEIEK 374
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578806710 624 AEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTAL 701
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
327-698 |
2.74e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 327 ELRDIYDLKDQIQDVEGRymqgLKELKESLSEVEEK---YKKAMVSNAQLDNEKNNL-IYQVDTLKDVIEEQEEQMAEFY 402
Cdd:PRK03918 329 RIKELEEKEERLEELKKK----LKELEKRLEELEERhelYEEAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 403 RENEEKSKELERQKHMCSVLQHKMEELKEGLRQ----RDELIEEKQrmQQKIDTMTKEVFDLQETLLWKDKKIGALEKQK 478
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 479 EYI-ACLRNERDMLR-EELAD-LQETVKTGEKHGLVIIPDGTPNGDVSHEPVAGaitvVSQEAAQVLESAGEG-PLDVRL 554
Cdd:PRK03918 483 RELeKVLKKESELIKlKELAEqLKELEEKLKKYNLEELEKKAEEYEKLKEKLIK----LKGEIKSLKKELEKLeELKKKL 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 555 RKLAGEKEELLSQIRKLKLQLEEERQKCSRN-DGTVGDLAGLQNgsdlQFIEMqRDANRQISEYKFKLSKAEQDITTLEQ 633
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELGFESVEElEERLKELEPFYN----EYLEL-KDAEKELEREEKELKKLEEELDKAFE 633
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 634 SISRLEGQVLRYKTAAENAEKVEDE-----LKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANR 698
Cdd:PRK03918 634 ELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
483-705 |
3.22e-05 |
|
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: 47.36 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 483 CLRNERDMLREELADLQETVKTGEKhglviipdgtpngdvshepvagAITVVSQEAAQVLEsagegpldvRLRKLAGEKE 562
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEK----------------------ALAELRKELEELEE---------ELEQLRKELE 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 563 ELLSQIRKLKLQLEEERQKCSRndgtVGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQV 642
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQ----LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806710 643 LRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 705
Cdd:TIGR02168 799 KALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
333-507 |
3.76e-05 |
|
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: 46.81 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 333 DLKDQIQDVEgrymQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 412
Cdd:pfam07888 77 ELESRVAELK----EELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 413 ERQKhmcsvlqhkmEELKEGLRQRDELIEEKQRMQQKIDTMTKEV----FDLQETLLWKDKKIGALEKQKEYIACLRN-- 486
Cdd:pfam07888 153 ERMK----------ERAKKAGAQRKEEEAERKQLQAKLQQTEEELrslsKEFQELRNSLAQRDTQVLQLQDTITTLTQkl 222
|
170 180
....*....|....*....|....*....
gi 578806710 487 --------ERDMLREELADLQETVKTGEK 507
Cdd:pfam07888 223 ttahrkeaENEALLEELRSLQERLNASER 251
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
334-705 |
4.42e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 334 LKDQIQDVEGRYMQGL-KELKESLSEVEEKYKkamvsnaQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 412
Cdd:TIGR04523 293 LKSEISDLNNQKEQDWnKELKSELKNQEKKLE-------EIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 413 ERqkhmcsvlqhKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEYiacLRNERDMLR 492
Cdd:TIGR04523 366 EE----------KQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL---LEKEIERLK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 493 EELADLQETVKTGEKhglviipdgtpngdvshepvagaitvvsQEAAqvlesagegpLDVRLRKLAGEKEELLSQIRKLK 572
Cdd:TIGR04523 433 ETIIKNNSEIKDLTN----------------------------QDSV----------KELIIKNLDNTRESLETQLKVLS 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 573 LQLEEERQKCSRNdgtvgdlaglqngsdlqfiemqrdanrqiseyKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENA 652
Cdd:TIGR04523 475 RSINKIKQNLEQK--------------------------------QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSL 522
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578806710 653 EKVEDELKAEKRKLQRELRTALDKIEEMEMTN---------SHLAKRLEKMKANRTALLAQQ 705
Cdd:TIGR04523 523 KEKIEKLESEKKEKESKISDLEDELNKDDFELkkenlekeiDEKNKEIEELKQTQKSLKKKQ 584
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
550-696 |
6.75e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 550 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCsrnDGTVGDLAGlQNGSDLQFIEMQ-RDANRQISEYKFKLSKAEQDI 628
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREEL---DELEAQIRG-NGGDRLEQLEREiERLERELEERERRRARLEALL 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806710 629 TTLEQSI-----------SRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 696
Cdd:COG4913 369 AALGLPLpasaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
333-681 |
7.08e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 7.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 333 DLKDQIQDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 412
Cdd:TIGR04523 311 ELKSELKNQEKK----LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 413 ERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDtmtKEVFDLQETLLWKDKKIGALEKQ----KEYIACLRNER 488
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE---KEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTR 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 489 DMLREELADLQETVKTgEKHGLviipdgtpngdvshEPVAGAITVVSQEAAQVLESAGEgpLDVRLRKLAGEKEELLSQI 568
Cdd:TIGR04523 464 ESLETQLKVLSRSINK-IKQNL--------------EQKQKELKSKEKELKKLNEEKKE--LEEKVKDLTKKISSLKEKI 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 569 RKLKLQLEEERQKCSRNDgtvGDLAGLQNGSDLQFIEMQRDA-NRQISEYKF-------KLSKAEQDITTLEQSISRLEG 640
Cdd:TIGR04523 527 EKLESEKKEKESKISDLE---DELNKDDFELKKENLEKEIDEkNKEIEELKQtqkslkkKQEEKQELIDQKEKEKKDLIK 603
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 578806710 641 QVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEME 681
Cdd:TIGR04523 604 EIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
347-688 |
7.57e-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: 45.97 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 347 QGLKELKESLSEVEEKykkamvsnaqldneKNNLIYQVDTLKDVIEEQEEQMAE----FYRENEEKSK---ELERQKHM- 418
Cdd:pfam10174 324 QHIEVLKESLTAKEQR--------------AAILQTEVDALRLRLEEKESFLNKktkqLQDLTEEKSTlagEIRDLKDMl 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 419 ------CSVLQHKMEELKEGLRQRDELIEEKQR----MQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEYI-ACLRNE 487
Cdd:pfam10174 390 dvkerkINVLQKKIENLQEQLRDKDKQLAGLKErvksLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREdRERLEE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 488 RDMLREELADLQETVKTGEKHGL----VIIPDGTPNGDVSHEPVAGAITVVSQEAAqvLESAGEGP--LDVRLRKL---- 557
Cdd:pfam10174 470 LESLKKENKDLKEKVSALQPELTekesSLIDLKEHASSLASSGLKKDSKLKSLEIA--VEQKKEECskLENQLKKAhnae 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 558 --AGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGL-------QNGSDLQFIEMQRDANRQISEykfkLSKAEQDI 628
Cdd:pfam10174 548 eaVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGIlreveneKNDKDKKIAELESLTLRQMKE----QNKKVANI 623
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578806710 629 TTLEQSISRLEGQVLryktaaENAEKVEDELKAEKRKLQ-RELRTALDKI-EEMEMTNSHLA 688
Cdd:pfam10174 624 KHGQQEMKKKGAQLL------EEARRREDNLADNSQQLQlEELMGALEKTrQELDATKARLS 679
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
391-701 |
7.87e-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: 46.21 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 391 IEEQEEQMAEFYRENEEKSKELER------QKHMCSVLQHKMEELK--EGLRQRDELIEEKQRMQQKIDTMTKEVFDLQE 462
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERlrrereKAERYQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELEKLTE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 463 TLLWKDKKIGALEKQKEYIAclRNERDMLREELADLQETVK--TGEKHGLV-IIPDGTPNGDVSHEPVAGAITVVSQEAA 539
Cdd:TIGR02169 259 EISELEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKIGelEAEIASLErSIAEKERELEDAEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 540 QVLESAGE-GPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKcsrNDGTVGDLAGLQNGSDlQFIEMQRDANRQISEYK 618
Cdd:TIGR02169 337 EIEELEREiEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE---FAETRDELKDYREKLE-KLKREINELKRELDRLQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 619 FKLSKAEQDITTLEQSISRLEGQVLRYKTAAENA----EKVEDELK---AEKRKLQRELRTALDKIEEMEMTNSHLAKRL 691
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKaleiKKQEWKLEqlaADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
330
....*....|
gi 578806710 692 EKMKANRTAL 701
Cdd:TIGR02169 493 AEAEAQARAS 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
538-705 |
8.58e-05 |
|
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: 46.20 E-value: 8.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 538 AAQVLESAGEG--PLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNgsdlQFIEMQRDANRQIS 615
Cdd:TIGR02168 230 LVLRLEELREEleELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY----ALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 616 EYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMK 695
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170
....*....|
gi 578806710 696 ANRTALLAQQ 705
Cdd:TIGR02168 386 SKVAQLELQI 395
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
330-679 |
1.26e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 330 DIYDLKDQIQDVEGRymqgLKELKESLSEVEE--KYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEE 407
Cdd:PRK03918 260 KIRELEERIEELKKE----IEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 408 KSKELERQKHMCSVLQHKMEELKEGLRQRDE---LIEEKQRMQQKIDTMTKEVFdlqetllwkDKKIGALEKQKEYIacl 484
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELYEEakaKKEELERLKKRLTGLTPEKL---------EKELEELEKAKEEI--- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 485 RNERDMLREELADLQETVKTGEKhglVIIPDGTPNGDVshePVAGAiTVVSQEAAQVLESAGEGPLDVR--LRKLAGEKE 562
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKK---AIEELKKAKGKC---PVCGR-ELTEEHRKELLEEYTAELKRIEkeLKEIEEKER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 563 ELLSQIRKLKLQLEEERqKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQV 642
Cdd:PRK03918 477 KLRKELRELEKVLKKES-ELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELK 555
|
330 340 350
....*....|....*....|....*....|....*..
gi 578806710 643 LRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEE 679
Cdd:PRK03918 556 KKLAELEKKLDELEEELAELLKELEELGFESVEELEE 592
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
474-701 |
1.57e-04 |
|
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: 45.05 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 474 LEKQKEYIACLRNERDMLREELADLQETVKTGEKHGLviipdgtpngDVSHEPVAGAITVVSQEAAQVLESAGEGPLDVR 553
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELE----------ELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 554 LRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQ----------ISEYKFKLSK 623
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeaanlrerLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 624 AEQDITTLEQSISRLEGQVLRY----KTAAENAEKVEDELKA---EKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 696
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLaaeiEELEELIEELESELEAllnERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
....*
gi 578806710 697 NRTAL 701
Cdd:TIGR02168 916 ELEEL 920
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
356-694 |
1.62e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 356 LSEVEEKYKKAMVSNAQLDNEKNNL---IYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEG 432
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLekfIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 433 LRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQ-----------KEYIAcLRNERDMLREELADLQET 501
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelkelkekaEEYIK-LSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 502 vktgekhglviipdgtpngdvshepvagaITVVSQEAAQVLESAGEGPLDV-RLRKLAGEKEELLSQIRKLK---LQLEE 577
Cdd:PRK03918 316 -----------------------------LSRLEEEINGIEERIKELEEKEeRLEELKKKLKELEKRLEELEerhELYEE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 578 ERQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQISEykfKLSKAEQDITTLEQSISRLEGQVLRYKTAAE-----NA 652
Cdd:PRK03918 367 AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEE---EISKITARIGELKKEIKELKKAIEELKKAKGkcpvcGR 443
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 578806710 653 EKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKM 694
Cdd:PRK03918 444 ELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
349-675 |
1.62e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 349 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQM----AEFYRENEEKSKELERQKHMCSVLQH 424
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 425 KMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLlwKDKKIGALEKQKEYIACLRNERDMLREELADLQEtvkt 504
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL--AEAEEALLEAEAELAEAEEELEELAEELLEALRA---- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 505 gekhglviipdgtpngdvshepvagaitvVSQEAAQVLEsagegpLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSR 584
Cdd:COG1196 395 -----------------------------AAELAAQLEE------LEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 585 NDGTVGDLAGLQNGSDLQfiemQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAE-KVEDELKAEK 663
Cdd:COG1196 440 EEEALEEAAEEEAELEEE----EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALL 515
|
330
....*....|..
gi 578806710 664 RKLQRELRTALD 675
Cdd:COG1196 516 LAGLRGLAGAVA 527
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
477-704 |
2.14e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 477 QKEYIACLRNERDMLREELADLQETVKTGEKhglviipdgtpngdvSHEPVAGAITVVSQEAAQVLESAGEgpLDVRLRK 556
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKK---------------EEKALLKQLAALERRIAALARRIRA--LEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 557 LAGEKEELLSQIRKLKLQLEEERQKCSR------NDGTVGDLAGLQNGSDLQFIEMQRDANRQISEYKfklskaEQDITT 630
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAEllralyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR------REQAEE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578806710 631 LEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 704
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
337-692 |
2.61e-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: 44.40 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 337 QIQDVEGRYMQGLKELKESLsEVEEKYKKAMVSNAQ-LDNEKNNLIYQVDTLkdvieEQEEQmaefyrENEEKSKELERQ 415
Cdd:pfam01576 346 QLQEMRQKHTQALEELTEQL-EQAKRNKANLEKAKQaLESENAELQAELRTL-----QQAKQ------DSEHKRKKLEGQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 416 khmcsvLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKE---------------- 479
Cdd:pfam01576 414 ------LQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQdtqellqeetrqklnl 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 480 --YIACLRNERDMLREELADLQETVKTGEKHGLviipdgtpngdvSHEPVAGAITVVSQEAAQVLESAGEGpldvrlrkl 557
Cdd:pfam01576 488 stRLRQLEDERNSLQEQLEEEEEAKRNVERQLS------------TLQAQLSDMKKKLEEDAGTLEALEEG--------- 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 558 ageKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGlqngsDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISr 637
Cdd:pfam01576 547 ---KKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQ-----ELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAIS- 617
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 578806710 638 legqvLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLE 692
Cdd:pfam01576 618 -----ARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEME 667
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
333-504 |
3.08e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 333 DLKDQIQDVEGRY---MQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKS 409
Cdd:TIGR04523 465 SLETQLKVLSRSInkiKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 410 KELERQK------HMCSVLQHKMEELKEgLRQRDELIEEKQR-MQQKIDTMTKEVFDLQETLLWKDKKIGALEKQ----- 477
Cdd:TIGR04523 545 DELNKDDfelkkeNLEKEIDEKNKEIEE-LKQTQKSLKKKQEeKQELIDQKEKEKKDLIKEIEEKEKKISSLEKElekak 623
|
170 180 190
....*....|....*....|....*....|...
gi 578806710 478 KEY------IACLRNERDMLREELADLQETVKT 504
Cdd:TIGR04523 624 KENeklssiIKNIKSKKNKLKQEVKQIKETIKE 656
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
349-698 |
3.20e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 349 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVI------------EEQEEQMAEFYRENEEKSKELERQK 416
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteEHRKELLEEYTAELKRIEKELKEIE 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 417 HMCSVLQHKMEELKEGLRQRDELIEEKQRMQQ--------------KIDTMTKEVFDLQETLLWKDKKIGALEKQKEYIA 482
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESELIKLKELAEQlkeleeklkkynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 483 CLRNERDMLREELADLQETVKTGEKHGLVIipdgtpnGDVSHEPVAGAItvvsqeaaQVLESAGEGPLdvRLRKLAGEKE 562
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELEEL-------GFESVEELEERL--------KELEPFYNEYL--ELKDAEKELE 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 563 ELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNgsdlqfiemqrDANRQISEYKFKlsKAEQDITTLEQSISRLEGQV 642
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELE-----------ELEKKYSEEEYE--ELREEYLELSRELAGLRAEL 682
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 578806710 643 lryktaaENAEKVEDELKAEKRKLQRELRTALDKIEEMEMtnshLAKRLEKMKANR 698
Cdd:PRK03918 683 -------EELEKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
325-457 |
3.35e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 325 LSELRDIYD-LKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQ-----VDTLKDVIEEQEEQM 398
Cdd:COG1579 33 LAELEDELAaLEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEalqkeIESLKRRISDLEDEI 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 399 AEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQR-DELIEEKQRMQQKIDTMTKEV 457
Cdd:COG1579 113 LELMERIEELEEELAELEAELAELEAELEEKKAELDEElAELEAELEELEAEREELAAKI 172
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
400-695 |
5.25e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 400 EFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETllwkDKKIGALEKQKE 479
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL----KEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 480 YiacLRNERDMLREELADLQETVKTGEKHglviipdgtpngdvshepvagaITVVSQEAAQVLESAGEGPLDVRLRKLAG 559
Cdd:PRK03918 249 S---LEGSKRKLEEKIRELEERIEELKKE----------------------IEELEEKVKELKELKEKAEEYIKLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 560 EKEELLSQIRKLKLQLEEERQKCSRNdgtvgdlaglqngsdlqfIEMQRDANRQISEYKFKLSKAEQDITTLE------Q 633
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEER------------------IKELEEKEERLEELKKKLKELEKRLEELEerhelyE 365
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578806710 634 SISRLEGQVLRYKT--AAENAEKVEDELK-AEKRK--LQRELRTALDKIEEMEMTNSHLAKRLEKMK 695
Cdd:PRK03918 366 EAKAKKEELERLKKrlTGLTPEKLEKELEeLEKAKeeIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
349-701 |
5.42e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 349 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQH---K 425
Cdd:pfam15921 470 LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNvqtE 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 426 MEELKEGLRQRDELIEekqRMQQKIDTMTKEVFDLQETllwkdkkIGALEKQKEYIACLRNERDMLREELADLQET--VK 503
Cdd:pfam15921 550 CEALKLQMAEKDKVIE---ILRQQIENMTQLVGQHGRT-------AGAMQVEKAQLEKEINDRRLELQEFKILKDKkdAK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 504 TGEKHGLViipdgtpnGDVSHEPV----AG-----AITVVSQEAAQVLESAGEG---------PLDVRLRKLAGEKEELL 565
Cdd:pfam15921 620 IRELEARV--------SDLELEKVklvnAGserlrAVKDIKQERDQLLNEVKTSrnelnslseDYEVLKRNFRNKSEEME 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 566 SQIRKLKLQLEEERQKCSRNDGTVGDLaglqNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISrlegqvlry 645
Cdd:pfam15921 692 TTTNKLKMQLKSAQSELEQTRNTLKSM----EGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMT--------- 758
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 646 ktaaeNAEKVEDELKAEKRKLQRELRT-ALDKIE---EMEMTNSHLAKRLEKMKANRTAL 701
Cdd:pfam15921 759 -----NANKEKHFLKEEKNKLSQELSTvATEKNKmagELEVLRSQERRLKEKVANMEVAL 813
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
329-507 |
7.83e-04 |
|
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: 42.75 E-value: 7.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 329 RDIYDLKDQIQDVEGRYMQGLKELKESLSEVEE---KYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYREN 405
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEElerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 406 EEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEkqrMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEYIAclr 485
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELAD---LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA--- 461
|
170 180
....*....|....*....|..
gi 578806710 486 NERDMLREELADLQETVKTGEK 507
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEK 483
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
322-694 |
8.43e-04 |
|
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: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 322 DTSLSEL-RDIYDLKDQIQDVEGRYMQGLKELKESLSEVE--EKYKKAMVSNA-QLDNEKNNLIYQVDTLKDVIEEQEEQ 397
Cdd:pfam10174 239 DTKISSLeRNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEvyKSHSKFMKNKIdQLKQELSKKESELLALQTKLETLTNQ 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 398 MAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEK----QRMQQKIDTMTKEVFDLQETLLWKDKKIGA 473
Cdd:pfam10174 319 NSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKtkqlQDLTEEKSTLAGEIRDLKDMLDVKERKINV 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 474 LEKQKEyiaclrNERDMLRE---ELADLQETVKTGEKHglviipdgTPNGDVSHEPVAGAITvvsqEAAQVLEsagegpl 550
Cdd:pfam10174 399 LQKKIE------NLQEQLRDkdkQLAGLKERVKSLQTD--------SSNTDTALTTLEEALS----EKERIIE------- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 551 dvRLRK-LAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDlaglQNGSdlqFIEMQRDANRQISEYKFKLSKAEQDIT 629
Cdd:pfam10174 454 --RLKEqREREDRERLEELESLKKENKDLKEKVSALQPELTE----KESS---LIDLKEHASSLASSGLKKDSKLKSLEI 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 630 TLEQSI---SRLEGQVLRYKTAAENAEKVED-------------ELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEK 693
Cdd:pfam10174 525 AVEQKKeecSKLENQLKKAHNAEEAVRTNPEindrirlleqevaRYKEESGKAQAEVERLLGILREVENEKNDKDKKIAE 604
|
.
gi 578806710 694 M 694
Cdd:pfam10174 605 L 605
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
381-575 |
8.91e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 381 IYQVDTLK--DVI---EEQEEQMAEFYRENEEKSKELERQKhmcSVLQHKMEELKEglrQRDELIEE-KQRMQQKIDTMT 454
Cdd:PRK00409 510 LIGEDKEKlnELIaslEELERELEQKAEEAEALLKEAEKLK---EELEEKKEKLQE---EEDKLLEEaEKEAQQAIKEAK 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 455 KEVFDLQETLLWKDKKIGALEKQKEYIACLR--NERDMLREELADL----QETVKTGEKhglVIIPDGTPNGDVshepva 528
Cdd:PRK00409 584 KEADEIIKELRQLQKGGYASVKAHELIEARKrlNKANEKKEKKKKKqkekQEELKVGDE---VKYLSLGQKGEV------ 654
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578806710 529 gaITVVSQEAAQVLesagEGPLDVR-----LRKLAGEKEELLSQIRKLKLQL 575
Cdd:PRK00409 655 --LSIPDDKEAIVQ----AGIMKMKvplsdLEKIQKPKKKKKKKPKTVKPKP 700
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
605-696 |
1.00e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 605 EMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKtaAENA-------------EKVEDELKAEKRKLQRELR 671
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE--AEVEeleaeleekderiERLERELSEARSEERREIR 462
|
90 100 110
....*....|....*....|....*....|....*...
gi 578806710 672 -----TALD--------KIEEMEMTNSHLAKRLEKMKA 696
Cdd:COG2433 463 kdreiSRLDreierlerELEEERERIEELKRKLERLKE 500
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
372-695 |
1.04e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 372 QLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSvlqhkmEELKEGLRQRDELIEEKQRMQqkiD 451
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAN------SELTEARTERDQFSQESGNLD---D 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 452 TMTKEVFDLQetllwKDKKIGALEKQKEYIACLRNER-----DMLREELADLQETVKTGEkhGLVIIPDGTPNGDVSHEP 526
Cdd:pfam15921 378 QLQKLLADLH-----KREKELSLEKEQNKRLWDRDTGnsitiDHLRRELDDRNMEVQRLE--ALLKAMKSECQGQMERQM 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 527 VA-----GAITVVSQEAAQvLESAGEGPLDVrLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDL 601
Cdd:pfam15921 451 AAiqgknESLEKVSSLTAQ-LESTKEMLRKV-VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDL 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 602 QFIEMQ---------RDANRQISEYKFKLSKAEQDITTLEQSI---SRLEGQVLRyKTAAENAEKVEDELKAEKRKLQ-R 668
Cdd:pfam15921 529 KLQELQhlknegdhlRNVQTECEALKLQMAEKDKVIEILRQQIenmTQLVGQHGR-TAGAMQVEKAQLEKEINDRRLElQ 607
|
330 340 350
....*....|....*....|....*....|.
gi 578806710 669 ELRTALD----KIEEMEMTNSHLakRLEKMK 695
Cdd:pfam15921 608 EFKILKDkkdaKIRELEARVSDL--ELEKVK 636
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
322-668 |
1.06e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 322 DTSLSELRDIYDLKDQIQDVEGRY---MQGLKELKESLSEVEEKYKKAmvsNAQLDNEKNNLIYQvdtlkdvieEQEEQm 398
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDYQAA---SDHLNLVQTALRQQ---------EKIER- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 399 aefYREN-EEKSKELERQkhmcsvlqhkMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIG----- 472
Cdd:PRK04863 353 ---YQADlEELEERLEEQ----------NEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIqyqqa 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 473 --ALEKQK--------------EYIACLRNERDMLREELADLQETVKtgekhglviipdgtpngdvshepvagaitvVSQ 536
Cdd:PRK04863 420 vqALERAKqlcglpdltadnaeDWLEEFQAKEQEATEELLSLEQKLS------------------------------VAQ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 537 EAAQVLESAGEgpldvRLRKLAGE--KEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQngsdlQFIEMQRDANRQI 614
Cdd:PRK04863 470 AAHSQFEQAYQ-----LVRKIAGEvsRSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELE-----QRLRQQQRAERLL 539
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 578806710 615 SEYKFKLSKAEQDITTLEQSISRLEGQVLRYK----TAAENAEKVEDELKAEKRKLQR 668
Cdd:PRK04863 540 AEFCKRLGKNLDDEDELEQLQEELEARLESLSesvsEARERRMALRQQLEQLQARIQR 597
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
333-500 |
1.78e-03 |
|
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: 41.29 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 333 DLKDQIQDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 412
Cdd:COG4942 24 EAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 413 ERQKHMCSVL------QHKMEELKEGLRQRD--ELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEYIACL 484
Cdd:COG4942 100 EAQKEELAELlralyrLGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170
....*....|....*.
gi 578806710 485 RNERDMLREELADLQE 500
Cdd:COG4942 180 LAELEEERAALEALKA 195
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
391-696 |
1.89e-03 |
|
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: 41.63 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 391 IEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKK 470
Cdd:pfam05483 372 LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 471 IGALEKQkeyIACLRNERDMLREELADLQETVKtgekhglviipdgtpNGDVSHEPVAGAITVVSQEAAQVLESAGEGPL 550
Cdd:pfam05483 452 IHDLEIQ---LTAIKTSEEHYLKEVEDLKTELE---------------KEKLKNIELTAHCDKLLLENKELTQEASDMTL 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 551 DVR-----LRKLAGEKEELLSQIRKLK---LQLEEERQKCSRNDGTVGDLAGL------QNGSDLQFIEMQRDANRQISE 616
Cdd:pfam05483 514 ELKkhqedIINCKKQEERMLKQIENLEekeMNLRDELESVREEFIQKGDEVKCkldkseENARSIEYEVLKKEKQMKILE 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 617 YkfKLSKAEQDITTLEQSISRL--EGQVLRYKTAAENAE---------KVEDELKAEKRKLQRELRTALDKIEEMEMTNS 685
Cdd:pfam05483 594 N--KCNNLKKQIENKNKNIEELhqENKALKKKGSAENKQlnayeikvnKLELELASAKQKFEEIIDNYQKEIEDKKISEE 671
|
330
....*....|.
gi 578806710 686 HLAKRLEKMKA 696
Cdd:pfam05483 672 KLLEEVEKAKA 682
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
349-682 |
2.01e-03 |
|
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: 41.63 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 349 LKELKESLSEVEEKYKKamvsnaqldnEKNNLIYQVDTLKDVIEEQEEQMAEF---YRENEEKSKELERQKHMCSvlqhk 425
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKK----------EINDKEKQVSLLLIQITEKENKMKDLtflLEESRDKANQLEEKTKLQD----- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 426 mEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEyiaclrnerdmlreelADLQETVKTG 505
Cdd:pfam05483 282 -ENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKE----------------AQMEELNKAK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 506 EKHGLVIipdgtpngdVSHEPVAGAITVVSQEAAQVLESAGE--GPLDVRLRKLAGEKEELLSQIRKLKLQLEE------ 577
Cdd:pfam05483 345 AAHSFVV---------TEFEATTCSLEELLRTEQQRLEKNEDqlKIITMELQKKSSELEEMTKFKNNKEVELEElkkila 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 578 ERQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKaeqdITTLEQSISRlegQVLRYKTAAENAEKVED 657
Cdd:pfam05483 416 EDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTA----IKTSEEHYLK---EVEDLKTELEKEKLKNI 488
|
330 340
....*....|....*....|....*
gi 578806710 658 ELKAEKRKLQRELRTALDKIEEMEM 682
Cdd:pfam05483 489 ELTAHCDKLLLENKELTQEASDMTL 513
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
550-705 |
2.42e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 550 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCS-------RNDGTVGDLAGLQNGSDLQ-FIE-------MQRDANRQI 614
Cdd:COG3883 56 LQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralyRSGGSVSYLDVLLGSESFSdFLDrlsalskIADADADLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 615 SEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKM 694
Cdd:COG3883 136 EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
170
....*....|.
gi 578806710 695 KANRTALLAQQ 705
Cdd:COG3883 216 AAAAAAAAAAA 226
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
329-661 |
2.53e-03 |
|
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: 41.21 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 329 RDIYDLKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVsnaQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFyrENEEK 408
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL---RVKEKIGELEAEIASLERSIAEKERELEDA--EERLA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 409 SKELERQKhmcsvLQHKMEELKEGL----RQRDELIEEKQRMQQKIDTMTKEVFDLQETL-LWKDKkigaLEKQKEYIAC 483
Cdd:TIGR02169 326 KLEAEIDK-----LLAEIEELEREIeeerKRRDKLTEEYAELKEELEDLRAELEEVDKEFaETRDE----LKDYREKLEK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 484 LRNERDMLREELADLQETVKTGEKHGLVIipdgtpngdvshepvagaitvvsQEAAQVLESagegpldvRLRKLAGEKEE 563
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADL-----------------------NAAIAGIEA--------KINELEEEKED 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 564 LLSQIRKLKLQLEeerqkcsrndgtvgdlaglqngsdlQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVL 643
Cdd:TIGR02169 446 KALEIKKQEWKLE-------------------------QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
330
....*....|....*...
gi 578806710 644 RYKTAAENAEKVEDELKA 661
Cdd:TIGR02169 501 ASEERVRGGRAVEEVLKA 518
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
381-687 |
2.65e-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: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 381 IYQVDTLKDVIEEQEEQMAE------FYRENEEKSKELERQkhmCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMT 454
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEhqmelkYLKQYKEKACEIRDQ---ITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 455 KEVFDLQETllwkdkkIGALEKQKEyiaclrnERDMLREELADLQETVKTGEKHGLviipdgtpnGDVSHEPVAgaiTVV 534
Cdd:TIGR00606 262 SKIMKLDNE-------IKALKSRKK-------QMEKDNSELELKMEKVFQGTDEQL---------NDLYHNHQR---TVR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 535 SQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDlagLQNGSDLQFIEMQRDANRQI 614
Cdd:TIGR00606 316 EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS---LATRLELDGFERGPFSERQI 392
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578806710 615 SEY-KFKLSKAEQDITTLEQSISRLEGQVlryKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHL 687
Cdd:TIGR00606 393 KNFhTLVIERQEDEAKTAAQLCADLQSKE---RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL 463
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
553-698 |
2.74e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 553 RLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVG------DLAGLQngSDLQFIEMQR-DANRQISEYKFKLSKAE 625
Cdd:COG1579 46 RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnkEYEALQ--KEIESLKRRIsDLEDEILELMERIEELE 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806710 626 QDITTLEQSISRLEGQVLRYKTAAENAEKvedELKAEKRKLQRELRTALDKIEEmemtnsHLAKRLEKMKANR 698
Cdd:COG1579 124 EELAELEAELAELEAELEEKKAELDEELA---ELEAELEELEAEREELAAKIPP------ELLALYERIRKRK 187
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
349-675 |
2.76e-03 |
|
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: 41.31 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 349 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLiyqvdtlkdviEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKME- 427
Cdd:pfam01576 14 LQKVKERQQKAESELKELEKKHQQLCEEKNAL-----------QEQLQAETELCAEAEEMRARLAARKQELEEILHELEs 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 428 ELKEGLRQRDELIEEKQRMQQKIDTMTKEVFD-------LQETLLWKDKKIGALEKQ----KEYIACLRNERDMLREELA 496
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEeeaarqkLQLEKVTTEAKIKKLEEDilllEDQNSKLSKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 497 DLQETVKTGEKHGLVIIPDGTpngdvSHEPVagaitVVSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLE 576
Cdd:pfam01576 163 EFTSNLAEEEEKAKSLSKLKN-----KHEAM-----ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 577 EERQKCSRNDgtvgdlaglqngsdlqfiEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVE 656
Cdd:pfam01576 233 ELRAQLAKKE------------------EELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQR 294
|
330
....*....|....*....
gi 578806710 657 DELKAEKRKLQRELRTALD 675
Cdd:pfam01576 295 RDLGEELEALKTELEDTLD 313
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
327-701 |
2.89e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 327 ELRDIYDLKDQIQDVEGRyMQGLKELKESLSEVEEKYKKAMvSNAQLDNEKNNLIY----QVDTLKDVIEEQEEqmaefy 402
Cdd:TIGR00606 452 KQEELKFVIKELQQLEGS-SDRILELDQELRKAERELSKAE-KNSLTETLKKEVKSlqneKADLDRKLRKLDQE------ 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 403 reNEEKSKELERQKHMCSVLQHKMEE----LKEGLRQRDELIEE------KQRMQQKIDTMTKEVFDLQETLLWKDKKIG 472
Cdd:TIGR00606 524 --MEQLNHHTTTRTQMEMLTKDKMDKdeqiRKIKSRHSDELTSLlgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELA 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 473 ALEKQKEYIaclRNERDMLREELADLQETV-----KTGEKHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVL-ESAG 546
Cdd:TIGR00606 602 SLEQNKNHI---NNELESKEEQLSSYEDKLfdvcgSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTdENQS 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 547 EGPLDVRLRKLAGEKEELLSQIR--------KLKLQLEEERQKCSRNDGTVGDLAGLQNGSDLQFIEMQ------RDANR 612
Cdd:TIGR00606 679 CCPVCQRVFQTEAELQEFISDLQsklrlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPelrnklQKVNR 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 613 QISEYKFKLSKAEQ-----------------DITTLEQSISRLEGQVLRYKTAAENAEKVE-----DELKAEKRKLQREL 670
Cdd:TIGR00606 759 DIQRLKNDIEEQETllgtimpeeesakvcltDVTIMERFQMELKDVERKIAQQAAKLQGSDldrtvQQVNQEKQEKQHEL 838
|
410 420 430
....*....|....*....|....*....|.
gi 578806710 671 RTALDKIEEMEMTNSHLAKRLEKMKANRTAL 701
Cdd:TIGR00606 839 DTVVSKIELNRKLIQDQQEQIQHLKSKTNEL 869
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
326-507 |
2.92e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 326 SELRDIYDLKDQIQDVEGRYM----------QGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQ-------VDTLK 388
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQnqeklnqqkdEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkeliIKNLD 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 389 DVIEEQEEQMAEFYRE-------NEEKSKELERQKHMCSVLQHKMEELKEGL----RQRDELIE-------EKQRMQQKI 450
Cdd:TIGR04523 461 NTRESLETQLKVLSRSinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVkdltKKISSLKEkieklesEKKEKESKI 540
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 578806710 451 DTMTKEVFDLQETLLWKDKKIGALEKQKEyIACLRNERDMLREELADLQETVKTGEK 507
Cdd:TIGR04523 541 SDLEDELNKDDFELKKENLEKEIDEKNKE-IEELKQTQKSLKKKQEEKQELIDQKEK 596
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
387-464 |
4.44e-03 |
|
Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.
Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 38.79 E-value: 4.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578806710 387 LKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKeglRQRDELIEEKQRMQQKIDTMTKEVFDLQETL 464
Cdd:pfam05266 100 LKDRQTKLLEELKKLEKKIAEEESEKRKLEEEIDELEKKILELE---RQLALAKEKKEAADKEIARLKSEAEKLEQEI 174
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
346-431 |
5.43e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 39.33 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 346 MQGLKELKESLSEVEEKYKkamvsnaQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHK 425
Cdd:COG4026 127 IPEYNELREELLELKEKID-------EIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSR 199
|
....*.
gi 578806710 426 MEELKE 431
Cdd:COG4026 200 FEELLK 205
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
322-581 |
6.14e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 322 DTSLSELRD-----IYDLKDQIQDVEGR----YMQGLKELKESLSEVEEKYKKAmvsnaqldnEKNNLIYQVDTLKDVIE 392
Cdd:PRK05771 19 DEVLEALHElgvvhIEDLKEELSNERLRklrsLLTKLSEALDKLRSYLPKLNPL---------REEKKKVSVKSLEELIK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 393 EQEEQMAEFYRENEEKSKELErqkhmcsvlqhkmeelkeglrqrdELIEEKQRMQQKIDTMTK-EVFDLQETLLWKDKKI 471
Cdd:PRK05771 90 DVEEELEKIEKEIKELEEEIS------------------------ELENEIKELEQEIERLEPwGNFDLDLSLLLGFKYV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 472 ----GALEKQKEyiaclrnERDMLREELADLQETVKTGEKHGLVIIPDgtpngdvshepvAGAITVVSQEAAQV----LE 543
Cdd:PRK05771 146 svfvGTVPEDKL-------EELKLESDVENVEYISTDKGYVYVVVVVL------------KELSDEVEEELKKLgferLE 206
|
250 260 270
....*....|....*....|....*....|....*...
gi 578806710 544 SAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQK 581
Cdd:PRK05771 207 LEEEGTPSELIREIKEELEEIEKERESLLEELKELAKK 244
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
327-668 |
6.34e-03 |
|
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: 39.95 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 327 ELRDIYDLKDQIQDVEGRYMQGLKELKES------LSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDV-----IEEQE 395
Cdd:TIGR00618 227 ELKHLREALQQTQQSHAYLTQKREAQEEQlkkqqlLKQLRARIEELRAQEAVLEETQERINRARKAAPLAahikaVTQIE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 396 EQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKID--TMTKEVFDLQETLLwkdKKIGA 473
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEvaTSIREISCQQHTLT---QHIHT 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 474 LEKQKEYIACLRNERDMLREELADLQETVKTgekhglviiPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEG----- 548
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQREQATIDT---------RTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCtaqce 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 549 ----PLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKcsrndgtvgdlaglqngsDLQFIEMQRDANRQISEYKFKLSKA 624
Cdd:TIGR00618 455 klekIHLQESAQSLKEREQQLQTKEQIHLQETRKKAV------------------VLARLLELQEEPCPLCGSCIHPNPA 516
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 578806710 625 EQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQR 668
Cdd:TIGR00618 517 RQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRAS 560
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
345-698 |
7.18e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.95 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 345 YMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQH 424
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 425 KMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETllWKDKKIGALEKQKEYIACLRNERDMLREELADLQETVKT 504
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE--ELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 505 GEKHglviipdgtpngdvshepvagaitvVSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQ--KC 582
Cdd:pfam02463 326 AEKE-------------------------LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLakKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 583 SRNDGTVGDLAGL-QNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKA 661
Cdd:pfam02463 381 LESERLSSAAKLKeEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350
....*....|....*....|....*....|....*..
gi 578806710 662 EKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANR 698
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEE 497
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
386-508 |
7.65e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.46 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 386 TLKDVIEEQEEqmaefyrenEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQrmqqkidtmtKEVFDLQETLL 465
Cdd:COG2433 377 SIEEALEELIE---------KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELE 437
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 578806710 466 WKDKKIGALE------KQKEY--------IACLRNERDMLREELADLQETVKTGEKH 508
Cdd:COG2433 438 EKDERIERLErelseaRSEERreirkdreISRLDREIERLERELEEERERIEELKRK 494
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
403-700 |
8.64e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 38.74 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 403 RENEEKSKELERQKhmcSVLQHKMEELKEglrQRDELIEEKQRMQQKIDTMTKEVFDLQEtllwkdkKIGALEKQK---- 478
Cdd:COG1340 4 DELSSSLEELEEKI---EELREEIEELKE---KRDELNEELKELAEKRDELNAQVKELRE-------EAQELREKRdeln 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 479 EYIACLRNERDMLREELADLQETVKTGEKHGLVIIPDGTPngdvshepvagaITVVSQEAAQVLESAGEGPLDVrlrkla 558
Cdd:COG1340 71 EKVKELKEERDELNEKLNELREELDELRKELAELNKAGGS------------IDKLRKEIERLEWRQQTEVLSP------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 559 gEKE-ELLSQIRKLKLQLEEERQKCSRNDgtvgDLAGLQNGSDLQFIEMqRDANRQISEYKFKLSKAEQDITTLEQSISR 637
Cdd:COG1340 133 -EEEkELVEKIKELEKELEKAKKALEKNE----KLKELRAELKELRKEA-EEIHKKIKELAEEAQELHEEMIELYKEADE 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806710 638 LEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTA 700
Cdd:COG1340 207 LRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKA 269
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
329-504 |
8.83e-03 |
|
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: 39.07 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 329 RDIYDLKDQIQDVEGRY---MQGLKELKESLSEVEEKYKKAMVSNAQLDNE--KNNLIY--QVDTLKDVIEEQEEQMAEF 401
Cdd:pfam06160 86 KALDEIEELLDDIEEDIkqiLEELDELLESEEKNREEVEELKDKYRELRKTllANRFSYgpAIDELEKQLAEIEEEFSQF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 402 YRENE-----EKSKELERQKHMCSVLQHKMEELKEGLRQ-RDELIEEKQRMQQKIDTMTKEVFDLQETLLwkDKKIGALE 475
Cdd:pfam06160 166 EELTEsgdylEAREVLEKLEEETDALEELMEDIPPLYEElKTELPDQLEELKEGYREMEEEGYALEHLNV--DKEIQQLE 243
|
170 180 190
....*....|....*....|....*....|.
gi 578806710 476 KQ-KEYIACLRN-ERDMLREELADLQETVKT 504
Cdd:pfam06160 244 EQlEENLALLENlELDEAEEALEEIEERIDQ 274
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
349-509 |
9.49e-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: 39.26 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 349 LKELKESLSEVEEKYKKAMvsnAQLDNEKNNLIYQvdTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEE 428
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQA---AKLQGSDLDRTVQ--QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNE 868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806710 429 LKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALE--------KQKEYIACLRNERDMLREELADLQE 500
Cdd:TIGR00606 869 LKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLEtflekdqqEKEELISSKETSNKKAQDKVNDIKE 948
|
....*....
gi 578806710 501 TVKtgEKHG 509
Cdd:TIGR00606 949 KVK--NIHG 955
|
|
| |
