|
Name |
Accession |
Description |
Interval |
E-value |
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
116-324 |
1.03e-81 |
|
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.
Pssm-ID: 214540 [Multi-domain] Cd Length: 216 Bit Score: 261.09 E-value: 1.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 116 VRKGIPHHFRAIVWQLLCDAQTMP---VKDQYSELLKMTSPCEKL----IRRDIARTYPEHNFFKEKDSLGQEVLFNVMK 188
Cdd:smart00164 1 VRKGVPPSLRGVVWKLLLNAQPMDtsaDKDLYSRLLKETAPDDKSivhqIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 189 AYSLVDREVGYCQGSAFIVGLLLLQMP-EEEAFCVFFKLMQDYRLReLFKPSMAELGLCMYQFECMIQEYLPELFVHFQS 267
Cdd:smart00164 81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958674929 268 QSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIVFRVGLALLQMNQAELM 324
Cdd:smart00164 160 LGITPSLYALRWFLTLFARELPLEIVLRIWDVLFAEGSDFLFRVALALLKLHRDVLL 216
|
|
| RabGAP-TBC |
pfam00566 |
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are ... |
156-324 |
4.70e-54 |
|
Rab-GTPase-TBC domain; Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.
Pssm-ID: 459855 Cd Length: 178 Bit Score: 184.77 E-value: 4.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 156 KLIRRDIARTYPEHNFFKEKDslGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLLQ-MPEEEAFCVFFKLMQDYRLRE 234
Cdd:pfam00566 10 EQIEKDVPRTFPHSFFFDNGP--GQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLVyLDEEDAFWCFVSLLENYLLRD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 235 LFKPSMAELGLCMYQFECMIQEYLPELFVHFQSQSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIV-FRVGL 313
Cdd:pfam00566 88 FYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVlFRVAL 167
|
170
....*....|.
gi 1958674929 314 ALLQMNQAELM 324
Cdd:pfam00566 168 AILKRFREELL 178
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
41-370 |
1.02e-43 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 165.75 E-value: 1.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 41 LLAKLEEQNRLIETDSKSLRSVNGS-------RRNSGSSLVSSSSASSNLSHLEEDSWILWGRIVN-EWDDVRKKKEKQV 112
Cdd:COG5210 126 LKDSLPTHLPEASSTEKDFSSFKGSsslnsnpELNKEINELSLKEEPQKLRYYELAADKLWISYLDpNPLSFLPVQLSKL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 113 KELVRKGIPHHFRAIVWQLLcdAQTMPVKDQ----YSELLKM-------TSPCEKLIRRDIARTYPEHNFFKEKDSLGQE 181
Cdd:COG5210 206 RELIRKGIPNELRGDVWEFL--LGIGFDLDKnpglYERLLNLhreakipTQEIISQIEKDLSRTFPDNSLFQTEISIRAE 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 182 VLFNVMKAYSLVDREVGYCQGSAFIVGLLLLQMPEEE-AFCVFFKLMQDYRLRELFKPSMAELGLCMYQFECMIQEYLPE 260
Cdd:COG5210 284 NLRRVLKAYSLYNPEVGYVQGMNFLAAPLLLVLESEEqAFWCLVKLLKNYGLPGYFLKNLSGLHRDLKVLDDLVEELDPE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 261 LFVHFQSQSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIVFRVGLALLQMNQAELMQLDMEGMLQhfqkVIP 340
Cdd:COG5210 364 LYEHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELLD----LLL 439
|
330 340 350
....*....|....*....|....*....|
gi 1958674929 341 HQFDGGPEKLIQSayqvkYNSKKMKKLEKE 370
Cdd:COG5210 440 KQLFLHSGKEAWS-----SILKFRHGTDRD 464
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
362-688 |
7.98e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 7.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 362 KKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELATIKQQT 441
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 442 DAARAKLEQAESTIRELQHHRHwhkcsstynedfvlQLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFpdENNIA 521
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELA--------------EAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL--AAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 522 RLQEELIAVKLREAEAIMGLKELRQQVRDLEEhwqrhvartsgrwKDPPKRNAVSELQGELMSIRLREAETQAEMREMKQ 601
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEE-------------EEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 602 RMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKEEVmAVRLREADSIAAVAELQ 681
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV-EAAYEAALEAALAAALQ 549
|
....*..
gi 1958674929 682 QHIAELE 688
Cdd:COG1196 550 NIVVEDD 556
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
395-718 |
2.39e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 395 LKQRIETLEKEsASLADRLiqgqvtRAQEAEENYLikrELATIKQQTDAARAKLEQAESTIRELQHHRHwhkcsstyned 474
Cdd:TIGR02168 198 LERQLKSLERQ-AEKAERY------KELKAELREL---ELALLVLRLEELREELEELQEELKEAEEELE----------- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 475 fVLQLEKELVQARLSEAESqcALKEMQDKVLDIEKKNNSFpdENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEH 554
Cdd:TIGR02168 257 -ELTAELQELEEKLEELRL--EVSELEEEIEELQKELYAL--ANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 555 WQRHVARTSgRWKDppkrnAVSELQGELMSIRLREAETQAEMREMKQRMMEMETQ------------NQINS--NQLRRA 620
Cdd:TIGR02168 332 LDELAEELA-ELEE-----KLEELKEELESLEAELEELEAELEELESRLEELEEQletlrskvaqleLQIASlnNEIERL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 621 EQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKEEVMA-VRLREADSIAAVAELQQHIAELE--IQKEEGKLQ 697
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEeLQEELERLEEALEELREELEEAEqaLDAAERELA 485
|
330 340
....*....|....*....|.
gi 1958674929 698 GQLNRSDSKQYIRELKDQIAE 718
Cdd:TIGR02168 486 QLQARLDSLERLQENLEGFSE 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
384-719 |
3.01e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 384 EIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELATIKQQTDAARAKLEQAESTIRELQHHRh 463
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL- 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 464 whkcsstynedfvLQLEKELVQARLSEAESQCALKEMQDKVLDIEKKnnsfpdennIARLQEELIAVKLREAEAIMGLKE 543
Cdd:TIGR02168 757 -------------TELEAEIEELEERLEEAEEELAEAEAEIEELEAQ---------IEQLKEELKALREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 544 LRQQVRDLEEHWQRHVARTSGrwkdppKRNAVSELQGELMSIRLREAETQAEMREMKQRMMEMETQNQINSNQLRRAEQE 623
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAA------TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 624 VTSLQEKVCSLSLKNKGLLAQLSEAkrRQAEIECKNKEEVMAVRLREADsiAAVAELQQHIAELEIQKEEGKLQGQLNRS 703
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSEL--RRELEELREKLAQLELRLEGLE--VRIDNLQERLSEEYSLTLEEAEALENKIE 964
|
330 340
....*....|....*....|
gi 1958674929 704 DSKQYIRE----LKDQIAEL 719
Cdd:TIGR02168 965 DDEEEARRrlkrLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
386-727 |
4.35e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 386 KRLRTENRLLKQRIETLEKESASLADRL--IQGQVTRAQEA-----EENYLIKRELATIKQQTDAARAKLEQAESTIREL 458
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELrrIENRLDELSQElsdasRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 459 QHHRhwhkcssTYNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLD--IEKKNNSFPDENNIARLQEEliavKLREAE 536
Cdd:TIGR02169 750 EQEI-------ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsrIPEIQAELSKLEEEVSRIEA----RLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 537 AIMGLKEL-RQQVRDLEEHWQRHVARTSGRWKDppKRNAVSELQGELMSIRLREAETQAEMREMKQRMMEMETQNQINSN 615
Cdd:TIGR02169 819 QKLNRLTLeKEYLEKEIQELQEQRIDLKEQIKS--IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 616 QLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKE--EVMAVRLREADSIAAVAELQQHIAELE----- 688
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeEIPEEELSLEDVQAELQRVEEEIRALEpvnml 976
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958674929 689 -IQKEEGKLQGQLNRSDSKQYIRELKDQIAELTHELRCLK 727
Cdd:TIGR02169 977 aIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
365-634 |
4.72e-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: 60.07 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 365 KKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRL--IQGQVTRAQEAEENYLIKRE-----LATI 437
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsrLEQQKQILRERLANLERQLEeleaqLEEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 438 KQQTDAARAKLEQAEstirelqhhrhwhkcsstyNEDFVLQLEKELVQARLSEAESQcaLKEMQDKVLDIEKKNNSFPDE 517
Cdd:TIGR02168 329 ESKLDELAEELAELE-------------------EKLEELKEELESLEAELEELEAE--LEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 518 NNIARLQEELIAVKLREAEAimglkelrqQVRDLEEHWQRHVARTSGRWKDpPKRNAVSELQGELMSIRLREAETQAEMR 597
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEA---------RLERLEDRRERLQQEIEELLKK-LEEAELKELQAELEELEEELEELQEELE 457
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958674929 598 EMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSL 634
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
386-724 |
3.07e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 386 KRLR-TENRL---------LKQRIETLEKEsaslADRLIQGQVTRAQEAE-ENYLIKRELATIKQQTDAARAKLEQAEST 454
Cdd:COG1196 179 RKLEaTEENLerledilgeLERQLEPLERQ----AEKAERYRELKEELKElEAELLLLKLRELEAELEELEAELEELEAE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 455 IRELQHHRHwhkcsstynedfvlQLEKELVQARLSEAESQCALKEMQDKVLDIEKKnnsfpdennIARLQEELIAVKLRE 534
Cdd:COG1196 255 LEELEAELA--------------ELEAELEELRLELEELELELEEAQAEEYELLAE---------LARLEQDIARLEERR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 535 AEAIMGLKELRQQVRDLEEHWQRHVARTSgrwkdppkrnavsELQGELMSIRLREAETQAEMREMKQRMMEMETQNQINS 614
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELE-------------ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 615 NQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIEcknkeevmavrlreadsIAAVAELQQHIAELEIQKEEG 694
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE-----------------EELEELEEALAELEEEEEEEE 441
|
330 340 350
....*....|....*....|....*....|..
gi 1958674929 695 KLQGQLNRSDSKQY--IRELKDQIAELTHELR 724
Cdd:COG1196 442 EALEEAAEEEAELEeeEEALLELLAELLEEAA 473
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
404-656 |
6.29e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.18 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 404 KESASLADRLIQGQVTRAQEAEENYLIKReLATIKQQTDAARAKLEQAEstiRELQHHRHWHKCSSTYNE-DFVLQ---- 478
Cdd:COG3206 148 ELAAAVANALAEAYLEQNLELRREEARKA-LEFLEEQLPELRKELEEAE---AALEEFRQKNGLVDLSEEaKLLLQqlse 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 479 LEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFPDENNIARLQEELIAVKLREAEAIMGL-------KELRQQVRDL 551
Cdd:COG3206 224 LESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 552 EEHWQRHVARtsgrwkdppkrnAVSELQGELMSIRLREAETQAEMREMKQRMMEMETQNQinsnQLRRAEQEVTSLQEkv 631
Cdd:COG3206 304 RAQLQQEAQR------------ILASLEAELEALQAREASLQAQLAQLEARLAELPELEA----ELRRLEREVEVARE-- 365
|
250 260
....*....|....*....|....*
gi 1958674929 632 cslslknkgLLAQLSeAKRRQAEIE 656
Cdd:COG3206 366 ---------LYESLL-QRLEEARLA 380
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
362-605 |
2.64e-07 |
|
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: 54.68 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 362 KKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELATIKQQT 441
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 442 DAARAKLEQAESTIRELqhHRHWHKCsstynEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFPDENNia 521
Cdd:TIGR02168 354 ESLEAELEELEAELEEL--ESRLEEL-----EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE-- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 522 rlQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVARTSgrwkdpPKRNAVSELQGELMSIRLREAETQAEMrEMKQ 601
Cdd:TIGR02168 425 --ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALE------ELREELEEAEQALDAAERELAQLQARL-DSLE 495
|
....
gi 1958674929 602 RMME 605
Cdd:TIGR02168 496 RLQE 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
517-731 |
3.87e-07 |
|
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: 53.91 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 517 ENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEhwQRHVARTSGRWKDPPKRNAVSELQGELMSIRLRE---AETQ 593
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEE--ELEQLRKELEELSRQISALRKDLARLEAEVEQLEeriAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 594 AEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIecknKEEVMAVRLREADS 673
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL----NEEAANLRERLESL 829
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958674929 674 IAAVAELQQHIAELEIQKEEGKLQGQ---LNRSDSKQYIRELKDQIAELTHELRCLKGQRD 731
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIEslaAEIEELEELIEELESELEALLNERASLEEALA 890
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
348-719 |
6.64e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 6.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 348 EKLIQSAYQVKYNSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEEN 427
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 428 YLIKRELATIKQQTD---AARAKLEQAESTIRELQHHRHWHKCSSTYNEdfVLQLEKELVQARLSEAESQCALKEMQD-- 502
Cdd:COG1196 480 AELLEELAEAAARLLlllEAEADYEGFLEGVKAALLLAGLRGLAGAVAV--LIGVEAAYEAALEAALAAALQNIVVEDde 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 503 ---KVLDIEKKNN----SFPDENNIARLqeELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVARTSGRWKDPPKRNAV 575
Cdd:COG1196 558 vaaAAIEYLKAAKagraTFLPLDKIRAR--AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 576 SELQGELmsiRLREAETQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEI 655
Cdd:COG1196 636 LRRAVTL---AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958674929 656 E---CKNKEEVMAVRLREADSIAAVAELQQHIAELEIQKEEGKLQGQLNRSDSKQYIRELKDQIAEL 719
Cdd:COG1196 713 EeerLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
356-719 |
7.34e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 7.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 356 QVKYNSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELA 435
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 436 TIKQQTDAARAKLEQAESTIRELQHHRHWHKCSSTYNEdfvlqLEKELVQARLSEAESQCA-----LKEMQDKVLDIEKK 510
Cdd:PRK02224 423 ELREREAELEATLRTARERVEEAEALLEAGKCPECGQP-----VEGSPHVETIEEDRERVEeleaeLEDLEEEVEEVEER 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 511 NNSFPD----ENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVARTSGrwkdppKRNAVSELQGELMSIR 586
Cdd:PRK02224 498 LERAEDlveaEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEE------KREAAAEAEEEAEEAR 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 587 LREAETQAEMREMKQRmmeMETQNQINSNQLRRAE--QEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECK-NKEEV 663
Cdd:PRK02224 572 EEVAELNSKLAELKER---IESLERIRTLLAAIADaeDEIERLREKREALAELNDERRERLAEKRERKRELEAEfDEARI 648
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958674929 664 MAVRLREADSIAAVAELQQHIAEL-----EIQKEEGKLQGQLNRsdskqyIRELKDQIAEL 719
Cdd:PRK02224 649 EEAREDKERAEEYLEQVEEKLDELreerdDLQAEIGAVENELEE------LEELRERREAL 703
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
519-730 |
1.17e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 519 NIARLQEELIavKLREAEAIMglKELRQQVRDLE---EHWQRHVArtsgrwkdppKRNAVSELQGELMSIRLREAET--- 592
Cdd:COG4913 226 AADALVEHFD--DLERAHEAL--EDAREQIELLEpirELAERYAA----------ARERLAELEYLRAALRLWFAQRrle 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 593 --QAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEiECKNKEEVMAVRLRE 670
Cdd:COG4913 292 llEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELE-ERERRRARLEALLAA 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958674929 671 A-----DSIAAVAELQQHIAELEIQKEEGKLQGQLNRSDSKQYIRELKDQIAELTHELRCLKGQR 730
Cdd:COG4913 371 LglplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
362-718 |
1.60e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 362 KKMKKLEKEYTTIKTKEMEEQGEIKRLRTEnrlLKQRIETLEKESASLADRliQGQVTRAQEAEENYLIKRELATIKQQT 441
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKADE---AKKKAEEDKKKADELKKA--AAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 442 DAARaKLEQAESTIRELQHHRHWHKCSSTYNEdfVLQLEKELVQARLSEaESQCALKEMQDKVLDIEKKNNSFPDENNIA 521
Cdd:PTZ00121 1441 EEAK-KADEAKKKAEEAKKAEEAKKKAEEAKK--ADEAKKKAEEAKKAD-EAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 522 RLQEELIAVKLREAEAIMGLKELR--QQVRDLEEHWQRHVARTSGRWKDPPKRNAVSELQGelMSIRLREAETQAEMREM 599
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKADEAKkaEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKN--MALRKAEEAKKAEEARI 1594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 600 KQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRlreADSIAAVAE 679
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK---AAEEAKKAE 1671
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958674929 680 LQQHIAElEIQKEE---GKLQGQLNR-SDSKQYIRELKDQIAE 718
Cdd:PTZ00121 1672 EDKKKAE-EAKKAEedeKKAAEALKKeAEEAKKAEELKKKEAE 1713
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
365-682 |
2.90e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.98 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 365 KKLE--KEYTTIKTKEMEEQGE-IKRLRTENRLLKQRIETLEkESASLADRLI-----QGQVTRAQEAEENYLIKRELAT 436
Cdd:pfam10174 401 KKIEnlQEQLRDKDKQLAGLKErVKSLQTDSSNTDTALTTLE-EALSEKERIIerlkeQREREDRERLEELESLKKENKD 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 437 IKQQTDAARAKLEQAESTIRELQHHRHWHKCSSTYNEDFVLQLEKELVQAR-------------LSEAESQCALKEMQDK 503
Cdd:pfam10174 480 LKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKeecsklenqlkkaHNAEEAVRTNPEINDR 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 504 VLDIEKKNNSFPDENNIARLQEELIAVKLREAEAIMGLKElrQQVRDLEEHWQRHVartsgrwKDPPKRNAVSELQGELM 583
Cdd:pfam10174 560 IRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKD--KKIAELESLTLRQM-------KEQNKKVANIKHGQQEM 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 584 siRLREAETQAEMREMKQRMMEMETQNQINS--NQLRRAEQEVTSLQEKVCS--LSLKNK-GLLAQLSEAKRRQAEIECK 658
Cdd:pfam10174 631 --KKKGAQLLEEARRREDNLADNSQQLQLEElmGALEKTRQELDATKARLSStqQSLAEKdGHLTNLRAERRKQLEEILE 708
|
330 340
....*....|....*....|....
gi 1958674929 659 NKEEVMAVRLREADSIAAVAELQQ 682
Cdd:pfam10174 709 MKQEALLAAISEKDANIALLELSS 732
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
385-731 |
3.46e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 385 IKRLR--TENRLLKQRIETLEKESASLADRLiqgQVTRAQEAEenylIKRELATIKQQTDAARAKLEQAESTIRELQHHR 462
Cdd:PRK02224 178 VERVLsdQRGSLDQLKAQIEEKEEKDLHERL---NGLESELAE----LDEEIERYEEQREQARETRDEADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 463 hwhkcsstyNEDFVLQLEKELVQARLSEAESQC-----ALKEMQDKVLDIEKKNNSFPDENNIARLQEELIAVKLREAEA 537
Cdd:PRK02224 251 ---------EELETLEAEIEDLRETIAETEREReelaeEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELED 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 538 imGLKELRQQVRDleehwqrhvartsgrwkdppKRNAVSELQGELMSIRLREAETQAEMREMKQRMMEMETQNQINSNQL 617
Cdd:PRK02224 322 --RDEELRDRLEE--------------------CRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 618 RRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIEcknkEEVMAVRLREADSIAAVAELQQHIAELEIQKEEGKLQ 697
Cdd:PRK02224 380 EDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR----EERDELREREAELEATLRTARERVEEAEALLEAGKCP 455
|
330 340 350
....*....|....*....|....*....|....*..
gi 1958674929 698 --GQ-LNRSDSKQYIRELKDQIAELTHELRCLKGQRD 731
Cdd:PRK02224 456 ecGQpVEGSPHVETIEEDRERVEELEAELEDLEEEVE 492
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
521-730 |
1.64e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.63 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 521 ARLQEEliavKLREAEAIMGLKELRQQVRDLEEHwqrhvartsgrwkdppkrnaVSELQGELMSIRLREAETQAEMREMK 600
Cdd:pfam01576 82 SRLEEE----EERSQQLQNEKKKMQQHIQDLEEQ--------------------LDEEEAARQKLQLEKVTTEAKIKKLE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 601 QRMMEMETQNQINSNQLRRAEQEVTSL-------QEKVCSLS-LKNK--GLLAQLS-----EAKRRQAEIECKNKEEVMA 665
Cdd:pfam01576 138 EDILLLEDQNSKLSKERKLLEERISEFtsnlaeeEEKAKSLSkLKNKheAMISDLEerlkkEEKGRQELEKAKRKLEGES 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958674929 666 VRLREAdsiaaVAELQQHIAELEIQ--KEEGKLQGQLNRSDSKQ--------YIRELKDQIAELTHELRCLKGQR 730
Cdd:pfam01576 218 TDLQEQ-----IAELQAQIAELRAQlaKKEEELQAALARLEEETaqknnalkKIRELEAQISELQEDLESERAAR 287
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
348-730 |
2.61e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 348 EKLIQSAYQVKynsKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKesasLADRLIQGQVTRAQEAEEN 427
Cdd:PRK03918 182 EKFIKRTENIE---ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 428 YLIKRELATIKQQTDAARAKLEQAESTIRELQHHRHWHKCSSTYNEdFVLQLEKEL--VQARLSEAESQcaLKEMQDKVL 505
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSE-FYEEYLDELreIEKRLSRLEEE--INGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 506 DIEKKnnsfpdENNIARLQEELIAVKlREAEAIMGLKELRQQVRDLEEHWQRHVARTSGRWKDppkrnavsELQGELMSI 585
Cdd:PRK03918 332 ELEEK------EERLEELKKKLKELE-KRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE--------KLEKELEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 586 RLREAETQAEMREMKQRMMEMETQnqinSNQLRRAEQEVTSLQEK--VC----------------SLSLKN-----KGLL 642
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKE----IKELKKAIEELKKAKGKcpVCgrelteehrkelleeyTAELKRiekelKEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 643 AQLSEAKRRQAEIECKNKEEVMAVRLRE-ADSIAAVAE---------LQQHIAELEIQKEE-GKLQGQLNR-SDSKQYIR 710
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESELIKLKElAEQLKELEEklkkynleeLEKKAEEYEKLKEKlIKLKGEIKSlKKELEKLE 552
|
410 420
....*....|....*....|
gi 1958674929 711 ELKDQIAELTHELRCLKGQR 730
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEEL 572
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
395-731 |
3.15e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 395 LKQRIETLEKESASLADRLIQgQVTRAQEAEENylIKRELATIKQQTDAARAKLEQAEstirelqhhrhwhkcsstyned 474
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEE-CRVAAQAHNEE--AESLREDADDLEERAEELREEAA---------------------- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 475 fvlQLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFPD-----ENNIARLQEELIAVKLREAEAIMGLKELRQQVR 549
Cdd:PRK02224 367 ---ELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVdlgnaEDFLEELREERDELREREAELEATLRTARERVE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 550 DLEEHWQRHVARTSGR-WKDPPKRNAVSELQGELMSIRLREAETQAEMREMKQRMMEMEtqnqinsnQLRRAEQEVTSLQ 628
Cdd:PRK02224 444 EAEALLEAGKCPECGQpVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE--------DLVEAEDRIERLE 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 629 EKVCSLSlknkGLLAQ---LSEAKRRQAEIECKNKEEVMAvRLREADSIAAVAELQQHIAELEIQKEEGKLQGQLNRSDS 705
Cdd:PRK02224 516 ERREDLE----ELIAErreTIEEKRERAEELRERAAELEA-EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES 590
|
330 340
....*....|....*....|....*.
gi 1958674929 706 KQYIRELKDQIAELTHELRCLKGQRD 731
Cdd:PRK02224 591 LERIRTLLAAIADAEDEIERLREKRE 616
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
352-721 |
6.51e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 352 QSAYQVKYNSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRL--------IQGQVTRAQE 423
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlvqtalrQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 424 AEENYLIKRE-----LATIKQQTDAARAKLEQAESTIRELQhhrhwhKCSSTYNEDFVLQLEKEL-----VQArLSEAES 493
Cdd:PRK04863 356 DLEELEERLEeqnevVEEADEQQEENEARAEAAEEEVDELK------SQLADYQQALDVQQTRAIqyqqaVQA-LERAKQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 494 QCAL-------------------KEMQDKVLDIEKKNNSFPDenniARLQEELIAVKLREAEAIMGLKELRQQVRDLEEH 554
Cdd:PRK04863 429 LCGLpdltadnaedwleefqakeQEATEELLSLEQKLSVAQA----AHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRR 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 555 W--QRHVARTSgrwkdPPKRNAVSELQGelmsiRLREAETQAEM-REMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKV 631
Cdd:PRK04863 505 LreQRHLAEQL-----QQLRMRLSELEQ-----RLRQQQRAERLlAEFCKRLGKNLDDEDELEQLQEELEARLESLSESV 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 632 CSLSLKNKGLLAQLSEAKRRQAEIECKNKEEVMA----VRLRE------ADSiAAVAELQQHIAELEIQKeegklqgQLN 701
Cdd:PRK04863 575 SEARERRMALRQQLEQLQARIQRLAARAPAWLAAqdalARLREqsgeefEDS-QDVTEYMQQLLEREREL-------TVE 646
|
410 420
....*....|....*....|
gi 1958674929 702 RSDSKQYIRELKDQIAELTH 721
Cdd:PRK04863 647 RDELAARKQALDEEIERLSQ 666
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
430-696 |
7.98e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 430 IKRELATIKQQTDAARAKLEQAESTIRELQHHrhwhkcsstynEDFVLQLEKELVQARLSEAESQcaLKEMQDKVLDIEK 509
Cdd:PRK04863 849 LERALADHESQEQQQRSQLEQAKEGLSALNRL-----------LPRLNLLADETLADRVEEIREQ--LDEAEEAKRFVQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 510 KNNSFPD-ENNIARLQ---EELIAVKLREAEAIMGLKELRQQVRDLEEHWQRhvaRTSGRWKDPPKR-NAVSELQgELMS 584
Cdd:PRK04863 916 HGNALAQlEPIVSVLQsdpEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQR---RAHFSYEDAAEMlAKNSDLN-EKLR 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 585 IRLREAEtqAEMREMKQRMmemeTQNQinsNQLRRAEQEVTSLQEkvcSLSLKNKgllaQLSEAKRR----------QAE 654
Cdd:PRK04863 992 QRLEQAE--QERTRAREQL----RQAQ---AQLAQYNQVLASLKS---SYDAKRQ----MLQELKQElqdlgvpadsGAE 1055
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958674929 655 IECKNKEEVMAVRLREADSIAAVAELQQHIAELEIQKEEGKL 696
Cdd:PRK04863 1056 ERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKL 1097
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
363-550 |
1.09e-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: 45.83 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 363 KMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRE---LATIKQ 439
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREldrLQEELQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 440 QTDAARAKLEQAESTIRELQhhrhwhkcsstyNEdfvLQLEKELVQARLSEAESQcaLKEMQDKVLDIEKKnnSFPDENN 519
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKI------------NE---LEEEKEDKALEIKKQEWK--LEQLAADLSKYEQE--LYDLKEE 477
|
170 180 190
....*....|....*....|....*....|.
gi 1958674929 520 IARLQEELIAVKLREAEAIMGLKELRQQVRD 550
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
478-693 |
1.16e-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: 45.14 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 478 QLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFpdENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQR 557
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--ERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 558 HVARTSGRWKDPPKRNAVSELQGELMSIRLREAETQAE-MREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSL 636
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958674929 637 KNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREADSIAAVAELQQHIAELEIQKEE 693
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
380-602 |
1.17e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 380 EEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEaeenylikrELATIKQQTDAARAKLEQAESTIRELQ 459
Cdd:COG4913 259 ELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRA---------ELARLEAELERLEARLDALREELDELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 460 HHRHwhkcSSTYNEdfVLQLEKELVQARLSEAESqcalkemqdkvldiekknnsfpdENNIARLQEELIAVKLREAEAIM 539
Cdd:COG4913 330 AQIR----GNGGDR--LEQLEREIERLERELEER-----------------------ERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958674929 540 GLKELRQQVRDLEEHWQRHVARTsgrwkdppkRNAVSELQGELMSIRLREAETQAEMREMKQR 602
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEAL---------EEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
362-733 |
1.28e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 362 KKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKEsASLADRLIQGQVTRAQEAEENYLIKRELATIKQQT 441
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL-LQLLPLYQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 442 DaARAKLEQAESTIRELQHH-RHWHKCSSTYNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFPDENNI 520
Cdd:COG4717 160 E-LEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 521 ARLQEEL--IAVKLREAEAIMGLKELRQQVRDLEEHWQ---------RHVARTSGRWKDPPKRNAVSELQGELMSIRLRE 589
Cdd:COG4717 239 AALEERLkeARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEE 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 590 AETQaemREMKQRMMEMETQNQINSNQLRRAEQEVTSLQE--------KVCSLSLKNKGLLAQLS-------EAKRRQAE 654
Cdd:COG4717 319 EELE---ELLAALGLPPDLSPEELLELLDRIEELQELLREaeeleeelQLEELEQEIAALLAEAGvedeeelRAALEQAE 395
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958674929 655 IECKNKEEVMAVRLREADSIAAVAELQQHIAELEIQKEEGKLQGQLNRSDSKqyIRELKDQIAELTHELRCLKGQRDFS 733
Cdd:COG4717 396 EYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEE--LEELREELAELEAELEQLEEDGELA 472
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
522-732 |
1.32e-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: 45.82 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 522 RLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHvartsgRWKDPPKRNAVSELQGELMSIRLREAETQAEMREMKQ 601
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEEL------RLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 602 RMMEMETQNQINSNQLRRAEQ-------EVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNK---EEVMAVRLREA 671
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESkldelaeELAELEEKLEELKEELESLEAELEELEAELEELESRLEeleEQLETLRSKVA 389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958674929 672 DSIAAVAELQQHIAELEIQKEEGKL--------QGQLNRSDSKQYIRELKDQIAELTHELRCLKGQRDF 732
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDrrerlqqeIEELLKKLEEAELKELQAELEELEEELEELQEELER 458
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
355-718 |
1.51e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.50 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 355 YQVKYNSKKMKklEKEYTTIKTKEMEEQGEIKRlrtenRLLKQRIETLEKEsasladRLIQGQVTRAQEAEEnylikrel 434
Cdd:pfam17380 256 YTVRYNGQTMT--ENEFLNQLLHIVQHQKAVSE-----RQQQEKFEKMEQE------RLRQEKEEKAREVER-------- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 435 atikqqtdaaRAKLEQAEsTIRELQHHRHwhkcSSTY--NEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKKNN 512
Cdd:pfam17380 315 ----------RRKLEEAE-KARQAEMDRQ----AAIYaeQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 513 sfpdennIARLQEEliavKLREAEAIMGLKELRQQVRDLEEHWQRHVArtsgrwKDPPKRNAVSELQGELMSIRLREAET 592
Cdd:pfam17380 380 -------LERLQME----RQQKNERVRQELEAARKVKILEEERQRKIQ------QQKVEMEQIRAEQEEARQREVRRLEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 593 QAEmREMKQ-RMMEMETQNQI-----NSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAkRRQAEIECKNKEEVMAV 666
Cdd:pfam17380 443 ERA-REMERvRLEEQERQQQVerlrqQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEE-RKQAMIEEERKRKLLEK 520
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958674929 667 RLREADSiAAVAELQQHIAELE------------IQKEEGKLQGQLNRSDSKQYIRELKDQIAE 718
Cdd:pfam17380 521 EMEERQK-AIYEEERRREAEEErrkqqemeerrrIQEQMRKATEERSRLEAMEREREMMRQIVE 583
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
361-683 |
2.20e-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: 44.81 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 361 SKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKE----SASLADRLIQGQVTRAQEAEENYLIKRELAT 436
Cdd:pfam10174 446 SEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPEltekESSLIDLKEHASSLASSGLKKDSKLKSLEIA 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 437 IKQQTDAArAKLEQAESTIRELQHhrhwhkcSSTYNEDFVLQ---LEKELVQARLSEAESQCALKEMQDKVLDIEKKNNS 513
Cdd:pfam10174 526 VEQKKEEC-SKLENQLKKAHNAEE-------AVRTNPEINDRirlLEQEVARYKEESGKAQAEVERLLGILREVENEKND 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 514 fpDENNIARLqEELIAVKLREAEAIMGLKELRQQV--RDLEEHWQRHVARTSGRwKDPPKRNAVSELQGELMSIRLREAE 591
Cdd:pfam10174 598 --KDKKIAEL-ESLTLRQMKEQNKKVANIKHGQQEmkKKGAQLLEEARRREDNL-ADNSQQLQLEELMGALEKTRQELDA 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 592 TQAEMREMKQRMMEMETqnQINSNQLRRAEQevtsLQEKvcsLSLKNKGLLAQLSEAKRRQAEIEC------KNKEEVMA 665
Cdd:pfam10174 674 TKARLSSTQQSLAEKDG--HLTNLRAERRKQ----LEEI---LEMKQEALLAAISEKDANIALLELssskkkKTQEEVMA 744
|
330
....*....|....*...
gi 1958674929 666 VRlREADSIaaVAELQQH 683
Cdd:pfam10174 745 LK-REKDRL--VHQLKQQ 759
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
360-653 |
2.32e-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: 45.06 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 360 NSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESAsladrliQGQVTRAQEAEENYLIKRELATIKQ 439
Cdd:TIGR02169 278 NKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA-------KLEAEIDKLLAEIEELEREIEEERK 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 440 QTDAARAKLEQAESTIRELQHhrhwhkcsstynedfvlQLEKELVQARLSEAEsqcaLKEMQDKVLDIEKKNNSFpdENN 519
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLRA-----------------ELEEVDKEFAETRDE----LKDYREKLEKLKREINEL--KRE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 520 IARLQEELIAVKLREAEAIMGLKELRQQVRDLEEhwqrhvartsgRWKDppKRNAVSELQGELMSIRLREAETQAEMREM 599
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIAGIEAKINELEE-----------EKED--KALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958674929 600 KQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLS----LKNK------GLLAQLSEAKRRQA 653
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRaveeVLKAsiqgvhGTVAQLGSVGERYA 538
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
366-656 |
2.37e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 366 KLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQ--EAEENYLIKR---ELATIKQQ 440
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREltEEHRKELLEEytaELKRIEKE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 441 TDAARAKLEQAESTIRELQHHRHWHKCSSTYNE--DFVLQLEKELVQARLSEAESQCA-LKEMQDKVLDIEKKNNSFPDE 517
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEeYEKLKEKLIKLKGEIKSLKKE 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 518 -NNIARLQEELIAV--KLREAEAimGLKELRQQVRDLEEHWQRHVARTSGRWKDPPKR-----NAVSELQGELMSIRLRE 589
Cdd:PRK03918 548 lEKLEELKKKLAELekKLDELEE--ELAELLKELEELGFESVEELEERLKELEPFYNEylelkDAEKELEREEKELKKLE 625
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 590 AE---TQAEMREMKQRMMEMEtqNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIE 656
Cdd:PRK03918 626 EEldkAFEELAETEKRLEELR--KELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIK 693
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
396-602 |
2.59e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 396 KQRIETLEKESASLADRL--IQGQVTRAQEAEENYLIKRELATIKQQTDAARAKLEQAESTIRELQHHRhwHKCSSTYNE 473
Cdd:COG4913 609 RAKLAALEAELAELEEELaeAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAEL--ERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 474 dfVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKKnnsfpdennIARLQEELIAVKLREAEAIMGLKELRQQvrDLEE 553
Cdd:COG4913 687 --LAALEEQLEELEAELEELEEELDELKGEIGRLEKE---------LEQAEEELDELQDRLEAAEDLARLELRA--LLEE 753
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958674929 554 HWQRHVARTSGrwkdppkRNAVSELQGELMSI--RLREAETQAE--MREMKQR 602
Cdd:COG4913 754 RFAAALGDAVE-------RELRENLEERIDALraRLNRAEEELEraMRAFNRE 799
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
360-724 |
2.62e-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: 44.72 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 360 NSKKMKKLEKEYTTIKTKEMEeqgeikrLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELatikQ 439
Cdd:pfam15921 312 NSMYMRQLSDLESTVSQLRSE-------LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL----Q 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 440 QTDAARAKLEQAESTIRElQHHRHWHKcsSTYNEDFVLQLEKEL---------VQARLSEAESQCAlKEMQDKVLDIEKK 510
Cdd:pfam15921 381 KLLADLHKREKELSLEKE-QNKRLWDR--DTGNSITIDHLRRELddrnmevqrLEALLKAMKSECQ-GQMERQMAAIQGK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 511 NNSFpdeNNIARLQEELIAVK--LREAeaimgLKELRQQVRDLEEHwQRHVARTSGRWKDppKRNAVSELQGELMSIRLR 588
Cdd:pfam15921 457 NESL---EKVSSLTAQLESTKemLRKV-----VEELTAKKMTLESS-ERTVSDLTASLQE--KERAIEATNAEITKLRSR 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 589 EAETQAEMREMKQRMMEME-TQNQINSNQLRRAEQE--VTSLQEKVCSLS--LKNKGLLAQLSEAKRRQAEIECKNKE-E 662
Cdd:pfam15921 526 VDLKLQELQHLKNEGDHLRnVQTECEALKLQMAEKDkvIEILRQQIENMTqlVGQHGRTAGAMQVEKAQLEKEINDRRlE 605
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958674929 663 VMAVRLREADSIAAVAELQQHIAELEIQKEEGKLQGqlnrSDSKQYIRELKDQIAELTHELR 724
Cdd:pfam15921 606 LQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAG----SERLRAVKDIKQERDQLLNEVK 663
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
520-720 |
3.04e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 520 IARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVARTSGRWKD---PPKRNAVSELQGELMSIRL--------- 587
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAELERLDAssddlaale 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 588 -REAETQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIEckNKEEVMAV 666
Cdd:COG4913 692 eQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD--AVERELRE 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958674929 667 RLREadsiaavaelQQHIAELEIQKEEGKLQGQLNrsdskQYIRELKDQIAELT 720
Cdd:COG4913 770 NLEE----------RIDALRARLNRAEEELERAMR-----AFNREWPAETADLD 808
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
377-553 |
3.09e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 377 KEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRL--IQGQVTRAQEAEENylIKRELATIK-QQTDAARAKLEQAES 453
Cdd:COG4913 275 EYLRAALRLWFAQRRLELLEAELEELRAELARLEAELerLEARLDALREELDE--LEAQIRGNGgDRLEQLEREIERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 454 TIRELQHHRhwhkcsstynedfvLQLEKELVQARLSEAESQCALKEMQDKVLDIekknnsfpdennIARLQEELIAVKLR 533
Cdd:COG4913 353 ELEERERRR--------------ARLEALLAALGLPLPASAEEFAALRAEAAAL------------LEALEEELEALEEA 406
|
170 180
....*....|....*....|
gi 1958674929 534 EAEAIMGLKELRQQVRDLEE 553
Cdd:COG4913 407 LAEAEAALRDLRRELRELEA 426
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
368-459 |
4.50e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 368 EKEYTTIKTKEMEEQ-----GEIKRLRTENRLLKQRIETLEKESASLADRLiqgqVTRAQEAEENYLIKRELATIKQQTD 442
Cdd:COG2433 400 EKEHEERELTEEEEEirrleEQVERLEAEVEELEAELEEKDERIERLEREL----SEARSEERREIRKDREISRLDREIE 475
|
90
....*....|....*..
gi 1958674929 443 AARAKLEQAESTIRELQ 459
Cdd:COG2433 476 RLERELEEERERIEELK 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
520-731 |
5.24e-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: 43.90 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 520 IARLQEELIAVKLREAEAIMGLKELRQQVRDLEEhwqrhvartsgrwkdppKRNAVSELQGelMSIRLREAETQAEMREM 599
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRR-----------------EREKAERYQA--LLKEKREYEGYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 600 KqrmmEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRqaeIECKNKEEVMAVRLREADSIAAVAE 679
Cdd:TIGR02169 233 E----ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKK---IKDLGEEEQLRVKEKIGELEAEIAS 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958674929 680 LQQHIAELEIQKEEgkLQGQLNRSDSKqyIRELKDQIAELTHELRCLKGQRD 731
Cdd:TIGR02169 306 LERSIAEKERELED--AEERLAKLEAE--IDKLLAEIEELEREIEEERKRRD 353
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
356-609 |
5.24e-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: 43.89 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 356 QVKYNSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRL--IQGQVTRAQEAEENYLIKRE 433
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIesLAAEIEELEELIEELESELE 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 434 LAT-----IKQQTDAARAKLEQAESTIRELQHHRHwhkcsstynedfvlQLEKELVQARLSEAESQCALKEMqdkvldie 508
Cdd:TIGR02168 877 ALLnerasLEEALALLRSELEELSEELRELESKRS--------------ELRRELEELREKLAQLELRLEGL-------- 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 509 kknnsfpdENNIARLQEELIAVKLREAEAIMGLKELRQqvrDLEEHWQRHVARTsgrwkdppkRNAVSELqGE--LMSIr 586
Cdd:TIGR02168 935 --------EVRIDNLQERLSEEYSLTLEEAEALENKIE---DDEEEARRRLKRL---------ENKIKEL-GPvnLAAI- 992
|
250 260
....*....|....*....|...
gi 1958674929 587 lreaetqAEMREMKQRMMEMETQ 609
Cdd:TIGR02168 993 -------EEYEELKERYDFLTAQ 1008
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
478-715 |
5.45e-04 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 43.31 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 478 QLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSfpdeNNIARLQEE--------LIAVKLREAEAIMGLKELRQQVR 549
Cdd:pfam08017 25 QSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQG----NVLERRQRDaenrsqgnVLERRQRDAENRSQGNVLERRQR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 550 DLEEHWQRHVA---------RTSGRWKDPPKRNAVSELQGELMSIRLREAETQAEMREMKQRMMEMETQNQINSNQLRRA 620
Cdd:pfam08017 101 DAENRSQGNVLerrqrdaenKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 621 EQEVTSlQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREAD--SIAAVAELQQHIAE-------LEIQK 691
Cdd:pfam08017 181 DAENKS-QGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAEnrSQGNVLERRQRDAEnksqgnvLERRQ 259
|
250 260
....*....|....*....|....
gi 1958674929 692 EEGKLQGQLNRSDSKQYIRELKDQ 715
Cdd:pfam08017 260 RDAENRSQGNVLERRQRDAENRSQ 283
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
522-699 |
6.54e-04 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 42.93 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 522 RLQEELIAVKLREAEAIMGLKELRQQVRDLEEhwqrhvaRTSGRWKDPPKRNAVSELQGELMSIRLREAETQAEMREMKQ 601
Cdd:pfam08017 137 RSQGNVLERRQRDAENRSQGNVLERRQRDAEN-------RSQGNVLERRQRDAENKSQGNVLERRQRDAENRSQGNVLER 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 602 RMMEMETQNQINSNQLRRAEQEVTSlQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREADSIAAVAELQ 681
Cdd:pfam08017 210 RQRDAENRSQGNVLERRQRDAENRS-QGNVLERRQRDAENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLE 288
|
170
....*....|....*...
gi 1958674929 682 QHIAELEIQKEEGKLQGQ 699
Cdd:pfam08017 289 RRQRDAENKSQVGQLIGK 306
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
362-718 |
8.55e-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: 43.09 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 362 KKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELATIKQQT 441
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEI 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 442 DAARAKLEQAESTIRELQhhrhwhkcsstyNEDFVLQLE-KELVQARLSEaesqcalkEMQDKVLDIEKKNNsfpdENNI 520
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLT------------NQDSVKELIiKNLDNTRESL--------ETQLKVLSRSINKI----KQNL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 521 ARLQEELiavKLREAEaimgLKELRQQVRDLEEhwqrhvartsgRWKDPPKRNAVSELQGELMSIRLREAETqaEMREMK 600
Cdd:TIGR04523 485 EQKQKEL---KSKEKE----LKKLNEEKKELEE-----------KVKDLTKKISSLKEKIEKLESEKKEKES--KISDLE 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 601 QRMMEMETQNqiNSNQLrraEQEVTSLQEKVCSLSLKNKGLlaqlsEAKRRQAEIECKNKE-EVMAVRLREADSIAAVAE 679
Cdd:TIGR04523 545 DELNKDDFEL--KKENL---EKEIDEKNKEIEELKQTQKSL-----KKKQEEKQELIDQKEkEKKDLIKEIEEKEKKISS 614
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958674929 680 LQQHIAelEIQKEEGKLQGQLNRSDSK-----QYIRELKDQIAE 718
Cdd:TIGR04523 615 LEKELE--KAKKENEKLSSIIKNIKSKknklkQEVKQIKETIKE 656
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
348-722 |
8.68e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 348 EKLIQSAYQVKYNSKKMKKLEKEYTtiKTKEMEEQGEIKRLRTEnrlLKQRIETLEK--------ESASLADRLIQG--Q 417
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKK--KADEAKKKAEEKKKADE---AKKKAEEAKKadeakkkaEEAKKAEEAKKKaeE 1468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 418 VTRAQEAEENYLIKRELATIKQQTDAARAKLEQAESTIRELQHHRHWHKCSSTYNEDFVLQLEKELVQARLSEAESQCAL 497
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA 1548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 498 KEMQ--------DKVLDIEKKNNSFPDENNIARLQEELIAVKLREAEAIMGLKELR-----QQVRDLEEhwqrhvartsG 564
Cdd:PTZ00121 1549 DELKkaeelkkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEkkmkaEEAKKAEE----------A 1618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 565 RWKDPPKRNAvSELQGELMSIRLREAETQAEMREMKQRmmemETQNQINSNQL-RRAEQEVTSLQEkvcslslknkglLA 643
Cdd:PTZ00121 1619 KIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKKA----EEENKIKAAEEaKKAEEDKKKAEE------------AK 1681
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 644 QLSEAKRRQAEIECKNKEE---VMAVRLREADSIAAVAELQQHIAELEIQKEEGKLQGQLNRSDSKQYIRE--LKDQIAE 718
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEakkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDeeEKKKIAH 1761
|
....
gi 1958674929 719 LTHE 722
Cdd:PTZ00121 1762 LKKE 1765
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
522-719 |
9.75e-04 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 42.54 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 522 RLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVA---------RTSGRWKDPPKRNAVSELQGELMSIRLREAET 592
Cdd:pfam08017 105 RSQGNVLERRQRDAENKSQGNVLERRQRDAENRSQGNVLerrqrdaenRSQGNVLERRQRDAENRSQGNVLERRQRDAEN 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 593 QAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSlQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREAD 672
Cdd:pfam08017 185 KSQGNVLERRQRDAENRSQGNVLERRQRDAENRS-QGNVLERRQRDAENRSQGNVLERRQRDAENKSQGNVLERRQRDAE 263
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958674929 673 SIAavaelQQHIAELEIQKEEGKLQGqlNRSDSKQYIRELKDQIAEL 719
Cdd:pfam08017 264 NRS-----QGNVLERRQRDAENRSQG--NVLERRQRDAENKSQVGQL 303
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
541-724 |
1.07e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 541 LKELRQQVRDLEEHWQRHVArtsgrwkdppKRNAVSELQGELMSIRLREAETQAEMREMKQrmmemETQNQINSNQLRRA 620
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAE----------LQEELEELEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 621 EQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKEevmAVRLREADSIAAVAELQQHIAELE-IQKEEGKLQGQ 699
Cdd:COG4717 138 EAELAELPERLEELEERLEELRELEEELEELEAELAELQEE---LEELLEQLSLATEEELQDLAEELEeLQQRLAELEEE 214
|
170 180
....*....|....*....|....*
gi 1958674929 700 LNRsdSKQYIRELKDQIAELTHELR 724
Cdd:COG4717 215 LEE--AQEELEELEEELEQLENELE 237
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
382-731 |
1.13e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 382 QGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQ---EAEENylIKRELATIKQQTDAARAKLEQAESTIREL 458
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggDRLEQ--LEREIERLERELEERERRRARLEALLAAL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 459 QH------------HRHWHKCSSTYNEDFVlQLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFPDE--NNIARLQ 524
Cdd:COG4913 372 GLplpasaeefaalRAEAAALLEALEEELE-ALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARllALRDALA 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 525 E-------------ELIAVKLREAE---AIMGLkeLRQQVRDL---EEHWQ---RHVARTSGR----------------- 565
Cdd:COG4913 451 EalgldeaelpfvgELIEVRPEEERwrgAIERV--LGGFALTLlvpPEHYAaalRWVNRLHLRgrlvyervrtglpdper 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 566 -------------WKDPPKRNAVSELQGELMSI----------RLREAETQAEMREMKQRMMEMETQNQINSN------- 615
Cdd:COG4913 529 prldpdslagkldFKPHPFRAWLEAELGRRFDYvcvdspeelrRHPRAITRAGQVKGNGTRHEKDDRRRIRSRyvlgfdn 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 616 --QLRRAEQEVTSLQEKVcslslknKGLLAQLSEAKRRQAEIEckNKEEVMAVRLREADSIAAVAELQQHIAELEIQKEe 693
Cdd:COG4913 609 raKLAALEAELAELEEEL-------AEAEERLEALEAELDALQ--ERREALQRLAEYSWDEIDVASAEREIAELEAELE- 678
|
410 420 430
....*....|....*....|....*....|....*...
gi 1958674929 694 gklqgQLNRSDSKqyIRELKDQIAELTHELRCLKGQRD 731
Cdd:COG4913 679 -----RLDASSDD--LAALEEQLEELEAELEELEEELD 709
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
360-731 |
1.45e-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: 42.31 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 360 NSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQvtraqeaEENYLIKRELATIKQ 439
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLE-------KEKLNIQKNIDKIKN 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 440 QtdaaRAKLEQAESTIREL-QHHR-------HWHKCSSTYNEDFV-LQLEKELVQARLSEAESQC---------ALKEMQ 501
Cdd:TIGR04523 195 K----LLKLELLLSNLKKKiQKNKslesqisELKKQNNQLKDNIEkKQQEINEKTTEISNTQTQLnqlkdeqnkIKKQLS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 502 DKVLDIEKKNNSFPD-ENNIARLQEELIAVKLREAEAIMglKELRQQVRDleehwqrhvartsgrwkdppKRNAVSELQG 580
Cdd:TIGR04523 271 EKQKELEQNNKKIKElEKQLNQLKSEISDLNNQKEQDWN--KELKSELKN--------------------QEKKLEEIQN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 581 ELMSIRLREAETQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNK 660
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ 408
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958674929 661 eevmavrlreadsiaavaELQQHIAELEIQKEEGKLQGQL---NRSDSKQYIRELKDQIAELTHELRCLKGQRD 731
Cdd:TIGR04523 409 ------------------QKDEQIKKLQQEKELLEKEIERlkeTIIKNNSEIKDLTNQDSVKELIIKNLDNTRE 464
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
377-715 |
1.54e-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: 42.27 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 377 KEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKREL--ATIKQQTDAARAKLEQAEST 454
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLneERIDLLQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 455 IRELQHH----RHWHKCSSTYNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFPDENN----------- 519
Cdd:pfam02463 257 KQEIEKEeeklAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKaekelkkekee 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 520 IARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVARTSGRWKDPPKRNAVSELQGELMSIRLREAETQAEMREM 599
Cdd:pfam02463 337 IEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 600 KQ--RMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREADSIAAV 677
Cdd:pfam02463 417 LEdlLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958674929 678 AELQQHIAELEIQKEEGKLQGQLNRSDSKQYIRELKDQ 715
Cdd:pfam02463 497 ERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDL 534
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
360-494 |
2.17e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 360 NSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRL----IQGQVTRAQEAEENY------- 428
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLeaaeDLARLELRALLEERFaaalgda 762
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958674929 429 LIKRELATIKQQTDAARAKLEQAESTIREL--QHHRHWHKCSST------YNEDFVLQLEKeLVQARLSEAESQ 494
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAEEELERAmrAFNREWPAETADldadleSLPEYLALLDR-LEEDGLPEYEER 835
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
347-582 |
2.38e-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: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 347 PEKLIQSAYQVKYNSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRL----IQGQVTRAQ 422
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 423 EAEENYLIKRELATIKQQTDAARAKLEQAESTIRELQHHRHWHKCSSTYNEDFVLQLEKELVQARLSEAESQCALKEMQD 502
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 503 KVLDIEKKNNSFpdENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVARTSGRWKDPPKRNaVSELQGEL 582
Cdd:COG4942 179 LLAELEEERAAL--EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG-FAALKGKL 255
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
367-706 |
2.93e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.26 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 367 LEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELATIKQQTD---- 442
Cdd:pfam05557 109 LKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQdsei 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 443 --AARAKLEQAESTIRELQHHRHWHKCSSTYNED-FVLQLEKELVQARLSEAEsqcalkEMQDKVLDIEKKNNSFPDE-- 517
Cdd:pfam05557 189 vkNSKSELARIPELEKELERLREHNKHLNENIENkLLLKEEVEDLKRKLEREE------KYREEAATLELEKEKLEQElq 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 518 --------------------NNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVAR-TSGRWKDPPKRNAVS 576
Cdd:pfam05557 263 swvklaqdtglnlrspedlsRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKiEDLNKKLKRHKALVR 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 577 ELQGELMSI----------------RLREAETQAE----MREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSL 636
Cdd:pfam05557 343 RLQRRVLLLtkerdgyrailesydkELTMSNYSPQllerIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLER 422
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 637 KNKGLLAQLSEAKRRQAeiecknKEEVMAVRLREADSIAAVAELQQHIAELEIQKEEGKLQGQLNRSDSK 706
Cdd:pfam05557 423 ELQALRQQESLADPSYS------KEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTK 486
|
|
| DUF1129 |
pfam06570 |
Protein of unknown function (DUF1129); This family consists of several hypothetical bacterial ... |
472-510 |
2.94e-03 |
|
Protein of unknown function (DUF1129); This family consists of several hypothetical bacterial proteins of unknown function.
Pssm-ID: 429008 Cd Length: 200 Bit Score: 39.95 E-value: 2.94e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1958674929 472 NEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKK 510
Cdd:pfam06570 6 NQDYIFRLTKQLIKDGKSDEEIKEILDEMLPEILEGQKK 44
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
517-726 |
4.55e-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: 40.13 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 517 ENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHvartsgrwkdppkRNAVSELQGELMSIRLREAETQAEM 596
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL-------------EQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 597 REMKQRMMEMETQNQINSNQlrraEQEVTSLQEKVCSLSLKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREADSIA- 675
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQ----PPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAe 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958674929 676 ---AVAELQQHIAELEIQKEE-GKLQGQLNR--SDSKQYIRELKDQIAELTHELRCL 726
Cdd:COG4942 176 leaLLAELEEERAALEALKAErQKLLARLEKelAELAAELAELQQEAEELEALIARL 232
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
348-724 |
5.32e-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: 40.42 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 348 EKLIQSAYQVKYNSKKMKKLEKEYTTIKTKEmeeQGEIKRLRTENRLLKQR-IETLEKESASLADRLIQGQVTRAQEAEE 426
Cdd:TIGR00606 447 EILEKKQEELKFVIKELQQLEGSSDRILELD---QELRKAERELSKAEKNSlTETLKKEVKSLQNEKADLDRKLRKLDQE 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 427 NYLIKRELATIKQQTDAARAKLEQAESTIRELQHHRH------------------WHKCSSTYN--EDFVLQLEKELVQA 486
Cdd:TIGR00606 524 MEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDeltsllgyfpnkkqledwLHSKSKEINqtRDRLAKLNKELASL 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 487 RLSEAESQCALKEMQDKVLDIEKK----NNSFPDENNIARLQEELIAVKLREAEAIMGLKELRQQVRDLEEHWQRHVART 562
Cdd:TIGR00606 604 EQNKNHINNELESKEEQLSSYEDKlfdvCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVC 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 563 SGRWKDPPKRNAV-SELQGELMSIRLREAETQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGL 641
Cdd:TIGR00606 684 QRVFQTEAELQEFiSDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRL 763
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 642 LAQLSEakrRQAEIECKNKEEVMAvrlreADSIAAVAELQQHIAEL-EIQKEEGKLQGQLNRSDSKQYIRELKDQIAELT 720
Cdd:TIGR00606 764 KNDIEE---QETLLGTIMPEEESA-----KVCLTDVTIMERFQMELkDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ 835
|
....
gi 1958674929 721 HELR 724
Cdd:TIGR00606 836 HELD 839
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
478-735 |
6.28e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.21 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 478 QLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFpdENNIARLQ---------EELIAVKLREAEAimGLKELRQQV 548
Cdd:pfam12128 217 RLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTL--ESAELRLShlhfgyksdETLIASRQEERQE--TSAELNQLL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 549 RDLEEHWQRHVARTSGRWKdpPKRNAVSELQGELMsiRLREAETQAEMREMKQRMMEMETQNQInSNQLRRAEQEVTSLQ 628
Cdd:pfam12128 293 RTLDDQWKEKRDELNGELS--AADAAVAKDRSELE--ALEDQHGAFLDADIETAAADQEQLPSW-QSELENLEERLKALT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 629 EKVCSLSLKNKGLLAQLSEakRRQAEIEcKNKEEVMAVRlREADSIAAVAE--LQQHIAELEIQKEEGKLQGQLNRSDSK 706
Cdd:pfam12128 368 GKHQDVTAKYNRRRSKIKE--QNNRDIA-GIKDKLAKIR-EARDRQLAVAEddLQALESELREQLEAGKLEFNEEEYRLK 443
|
250 260
....*....|....*....|....*....
gi 1958674929 707 QYIRELKDQIAELTHELRCLKGQRDFSSR 735
Cdd:pfam12128 444 SRLGELKLRLNQATATPELLLQLENFDER 472
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
343-630 |
7.26e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 343 FDGGPEKLIQSAYQvkynskKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQ---RIETLEKESasLADRL--IQGQ 417
Cdd:PRK04863 831 FEADPEAELRQLNR------RRVELERALADHESQEQQQRSQLEQAKEGLSALNRllpRLNLLADET--LADRVeeIREQ 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 418 VTRAQEAEeNYL---------IKRELATIK---QQTDAARAKLEQAESTIRELQhhrhwhkcsstyNEDFVLqleKELVQ 485
Cdd:PRK04863 903 LDEAEEAK-RFVqqhgnalaqLEPIVSVLQsdpEQFEQLKQDYQQAQQTQRDAK------------QQAFAL---TEVVQ 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 486 AR--LSEAESQCALKEMQDkvldiekknnsfpdenniarLQEELIAvKLREAEAiMGLK---ELRQQVRDLEEHWQRHVA 560
Cdd:PRK04863 967 RRahFSYEDAAEMLAKNSD--------------------LNEKLRQ-RLEQAEQ-ERTRareQLRQAQAQLAQYNQVLAS 1024
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 561 RTSGRwkdPPKRNAVSELQGELMSI------------RLREAETQAEMREMKQRMMEMETQNQINSNQLRRAEQEVTSLQ 628
Cdd:PRK04863 1025 LKSSY---DAKRQMLQELKQELQDLgvpadsgaeeraRARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLE 1101
|
..
gi 1958674929 629 EK 630
Cdd:PRK04863 1102 RD 1103
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
384-561 |
7.68e-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: 38.75 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 384 EIKRLRTENRLLKQRIETLEKESASLADRLiqgqVTRAQEAEEnylIKRELATIKQQTDAARAKLEQAE------STIRE 457
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARL----EAAKTELED---LEKEIKRLELEIEEVEARIKKYEeqlgnvRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 458 LQHhrhwhkcsstynedfvLQLEKELVQARLSEAESQcaLKEMQDKVLDIEKKNNSFpdENNIARLQEELIAVKlREAEA 537
Cdd:COG1579 91 YEA----------------LQKEIESLKRRISDLEDE--ILELMERIEELEEELAEL--EAELAELEAELEEKK-AELDE 149
|
170 180
....*....|....*....|....
gi 1958674929 538 ImgLKELRQQVRDLEEHWQRHVAR 561
Cdd:COG1579 150 E--LAELEAELEELEAEREELAAK 171
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
572-729 |
7.75e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 572 RNAVSELQGELMSIRLREAETQAEMREMKQR--MMEMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNKGLLAQLSEAK 649
Cdd:COG3206 174 RKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 650 RRQAEIecKNKEEVMAVRLREADSIAAVAELQQH-------IAEL--EIQKEEGKLQGQLNR--SDSKQYIRELKDQIAE 718
Cdd:COG3206 254 DALPEL--LQSPVIQQLRAQLAELEAELAELSARytpnhpdVIALraQIAALRAQLQQEAQRilASLEAELEALQAREAS 331
|
170
....*....|.
gi 1958674929 719 LTHELRCLKGQ 729
Cdd:COG3206 332 LQAQLAQLEAR 342
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
446-639 |
8.16e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 446 AKLEQAESTIRELQ-HHRHWHKcsstynedfvLQLEKELVQARLSEAESQcaLKEMQDKVLDIEKKNNSFPDENNIARLQ 524
Cdd:COG4717 71 KELKELEEELKEAEeKEEEYAE----------LQEELEELEEELEELEAE--LEELREELEKLEKLLQLLPLYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958674929 525 EELIAVKLREAEAIMGLKELRQQVRDLEEhWQRHVARTsgrwkdppKRNAVSELQGELMSIRLREAETQAEMREMKQRMM 604
Cdd:COG4717 139 AELAELPERLEELEERLEELRELEEELEE-LEAELAEL--------QEELEELLEQLSLATEEELQDLAEELEELQQRLA 209
|
170 180 190
....*....|....*....|....*....|....*
gi 1958674929 605 EMETQNQINSNQLRRAEQEVTSLQEKVCSLSLKNK 639
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| |
