|
Name |
Accession |
Description |
Interval |
E-value |
| TBC |
smart00164 |
Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs; Widespread domain present in Gyp6 and ... |
160-368 |
1.50e-84 |
|
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: 267.25 E-value: 1.50e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 160 VRKGIPHHFRAIVWQLLCNAQSM---TIKDQYSELLKMTSPCEKL----IRRDIARTYPEHNFFKEKDSLGQEVLFNVMK 232
Cdd:smart00164 1 VRKGVPPSLRGVVWKLLLNAQPMdtsADKDLYSRLLKETAPDDKSivhqIEKDLRRTFPEHSFFQDKEGPGQESLRRVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 233 AYSLVDREVGYCQGSAFIVGLLLMQMP-EEEAFCVFVKLMQDYRLReLFKPSMAELGLCMYQFECMIQEYLPELFVHFQS 311
Cdd:smart00164 81 AYALYNPEVGYCQGMNFLAAPLLLVMEdEEDAFWCLVKLMERYGPN-FYLPDMSGLQLDLLQLDRLVKEYDPDLYKHLKD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568935311 312 QSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIVFRVGLALLQMNQAELM 368
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 ... |
200-368 |
4.86e-55 |
|
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: 187.08 E-value: 4.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 200 KLIRRDIARTYPEHNFFKEKDslGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLMQ-MPEEEAFCVFVKLMQDYRLRE 278
Cdd:pfam00566 10 EQIEKDVPRTFPHSFFFDNGP--GQNSLRRILKAYSIYNPDVGYCQGMNFIAAPLLLVyLDEEDAFWCFVSLLENYLLRD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 279 LFKPSMAELGLCMYQFECMIQEYLPELFVHFQSQSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIV-FRVGL 357
Cdd:pfam00566 88 FYTPDFPGLKRDLYVFEELLKKKLPKLYKHLKELGLDPDLFASQWFLTLFAREFPLSTVLRIWDYFFLEGEKFVlFRVAL 167
|
170
....*....|.
gi 568935311 358 ALLQMNQAELM 368
Cdd:pfam00566 168 AILKRFREELL 178
|
|
| COG5210 |
COG5210 |
GTPase-activating protein [General function prediction only]; |
85-414 |
2.37e-46 |
|
GTPase-activating protein [General function prediction only];
Pssm-ID: 227535 [Multi-domain] Cd Length: 496 Bit Score: 172.68 E-value: 2.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 85 LLAKLEEQNRLIETDSKSLRSVNGS-------RRNSGSSLVSSSSASSNLSHLEEDSWILWGRIVN-EWDDVRKKKEKQV 156
Cdd:COG5210 126 LKDSLPTHLPEASSTEKDFSSFKGSsslnsnpELNKEINELSLKEEPQKLRYYELAADKLWISYLDpNPLSFLPVQLSKL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 157 KELVRKGIPHHFRAIVWQLLCNAQSM--TIKDQYSELLKM-------TSPCEKLIRRDIARTYPEHNFFKEKDSLGQEVL 227
Cdd:COG5210 206 RELIRKGIPNELRGDVWEFLLGIGFDldKNPGLYERLLNLhreakipTQEIISQIEKDLSRTFPDNSLFQTEISIRAENL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 228 FNVMKAYSLVDREVGYCQGSAFIVGLLLMQMPEEE-AFCVFVKLMQDYRLRELFKPSMAELGLCMYQFECMIQEYLPELF 306
Cdd:COG5210 286 RRVLKAYSLYNPEVGYVQGMNFLAAPLLLVLESEEqAFWCLVKLLKNYGLPGYFLKNLSGLHRDLKVLDDLVEELDPELY 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 307 VHFQSQSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIVFRVGLALLQMNQAELMQLDMEGMLQhfqkVIPHQ 386
Cdd:COG5210 366 EHLLREGVVLLMFAFRWFLTLFVREFPLEYALRIWDCLFLEGSSMLFQLALAILKLLRDKLLKLDSDELLD----LLLKQ 441
|
330 340
....*....|....*....|....*...
gi 568935311 387 FDGGPEKLIQSayqvkYNSKKMKKLEKE 414
Cdd:COG5210 442 LFLHSGKEAWS-----SILKFRHGTDRD 464
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
406-674 |
4.33e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 406 KKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELATIKQQT 485
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 486 DAARAKLEQAESTIRELRHHRHwhkcsstynedfvlQLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFpdENNIA 565
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELA--------------EAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL--AAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 566 RLQEELIAVKLREAEAIMGLKELRQQVRTLEEhwqrhlartsgrwkdppkknAVNELQDELMSIRLREAETQAEIREMKQ 645
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEE--------------------EEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260
....*....|....*....|....*....
gi 568935311 646 RMMEMETQNQINSNQLRRAEQEVNSLQEK 674
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
428-763 |
2.34e-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: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 428 EIKRLRTENRLLKQRIETLEKESASLADRLIQGQvtraqeaEENYLIKRELATIKQQTDAARAKLEQAESTIRELRHHRh 507
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELE-------EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI- 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 508 whkcssTYNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKKnnsfpdennIARLQEELIAVKLREAEAIMGLKE 587
Cdd:TIGR02168 750 ------AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ---------IEQLKEELKALREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 588 LRQQVRTLEEHWQRHLARTSGrwkdppKKNAVNELQDELMSIRLREAETQAEIREMKQRMMEMETQNQINSNQLRRAEQE 667
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAA------TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 668 VNSLQEKVCSLSVKNKGLLAQLSEAkrRQAEIECKNKEEVMAVRLREADsiAAVAELQQHIAELEIQKEEGKLQGQLNRS 747
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSEL--RRELEELREKLAQLELRLEGLE--VRIDNLQERLSEEYSLTLEEAEALENKIE 964
|
330 340
....*....|....*....|
gi 568935311 748 DSNQYIRE----LKDQIAEL 763
Cdd:TIGR02168 965 DDEEEARRrlkrLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
439-762 |
8.34e-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: 65.85 E-value: 8.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 439 LKQRIETLEKEsASLADRLiqgqvtRAQEAEENYLikrELATIKQQTDAARAKLEQAESTIRELRHHRHwhkcsstyned 518
Cdd:TIGR02168 198 LERQLKSLERQ-AEKAERY------KELKAELREL---ELALLVLRLEELREELEELQEELKEAEEELE----------- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 519 fVLQLEKELVQARLSEAESqcALKEMQDKVLDIEKKNNSFpdENNIARLQEELIAVKLREAEAIMGLKELRQQVRTLEEH 598
Cdd:TIGR02168 257 -ELTAELQELEEKLEELRL--EVSELEEEIEELQKELYAL--ANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 599 WQRHLARTSGRwkdppkKNAVNELQDELMSIRLREAETQAEIREMKQRMMEMETQ------------NQINS--NQLRRA 664
Cdd:TIGR02168 332 LDELAEELAEL------EEKLEELKEELESLEAELEELEAELEELESRLEELEEQletlrskvaqleLQIASlnNEIERL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 665 EQEVNSLQEKVCSLSVKNKGLLAQLSEAKRRQAEIECKNKEEVMA-VRLREADSIAAVAELQQHIAELE--IQKEEGKLQ 741
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEeLQEELERLEEALEELREELEEAEqaLDAAERELA 485
|
330 340
....*....|....*....|.
gi 568935311 742 GQLNRSDSNQYIRELKDQIAE 762
Cdd:TIGR02168 486 QLQARLDSLERLQENLEGFSE 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
475-762 |
8.75e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 8.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 475 KRELATIKQQTDAARAKLEQAESTIRELRHHRhwhkcsstynedfvLQLEKELVQARLSEAESQCALKEMQDKVLDIEKK 554
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKEL--------------EELEEELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 555 NNSFPDEN-----NIARLQEELIAVKLREAEAIMGLKELRQQVRTLEEHWQRHLAR-TSGRWKDPPKKNAVNELQDELMS 628
Cdd:TIGR02168 742 VEQLEERIaqlskELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEElKALREALDELRAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 629 IRLREAETQAEIREMKQRMMEMETQNQINSNQLRRAEQEVNSLQEKVCSLSVKNKGLLAQLSEAKRRQAEIecKNKEEVM 708
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL--RSELEEL 899
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 709 AVRLREADS-----IAAVAELQQHIAELEIQKEEGKLQG-QLNRSDSNQYIRELKDQIAE 762
Cdd:TIGR02168 900 SEELRELESkrselRRELEELREKLAQLELRLEGLEVRIdNLQERLSEEYSLTLEEAEAL 959
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
430-707 |
2.08e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 430 KRLRTENRLLKQRIETLEKESASLADRL--IQGQVTRAQEA-----EENYLIKRELATIKQQTDAARAKLEQAESTIREL 502
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELrrIENRLDELSQElsdasRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 503 RHHRhwhkcssTYNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLD--IEKKNNSFPDENNIARLQEEliavKLREAE 580
Cdd:TIGR02169 750 EQEI-------ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsrIPEIQAELSKLEEEVSRIEA----RLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 581 AIMGLKEL-RQQVRTLEEHWQRHLARTSGRWKDppKKNAVNELQDELMSIRLREAETQAEIREMKQRMMEMETQNQINSN 659
Cdd:TIGR02169 819 QKLNRLTLeKEYLEKEIQELQEQRIDLKEQIKS--IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 568935311 660 QLRRAEQEVNSLQEKVCSLSVKNKGLLAQLSEAKRRQAEIECKNKEEV 707
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
439-766 |
4.16e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 439 LKQRIETLEKESASLADRLIQGQVTRAQEaeenylikrELATIKQQTDAARAKLEQAESTIRELRHHRHwhkcsstyned 518
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEA---------ELEELEAELEELEAELAELEAELEELRLELE----------- 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 519 fVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNsfpdENNIARLQEELIAVKLREAEAIMGLKELRQQVRTLEEh 598
Cdd:COG1196 278 -ELELELEEAQAEEYELLAELARLEQDIARLEERRREL----EERLEELEEELAELEEELEELEEELEELEEELEEAEE- 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 599 wqrhlartsgrwkdppkknavnELQDELMSIRLREAETQAEIREMKQRMMEMETQNQINSNQLRRAEQEVNSLQEkvcsl 678
Cdd:COG1196 352 ----------------------ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE----- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 679 svknkgLLAQLSEAKRRQAEIEcknkeevmavrlreadsIAAVAELQQHIAELEIQKEEGKLQGQLNRSDSNQY--IREL 756
Cdd:COG1196 405 ------LEEAEEALLERLERLE-----------------EELEELEEALAELEEEEEEEEEALEEAAEEEAELEeeEEAL 461
|
330
....*....|
gi 568935311 757 KDQIAELTHE 766
Cdd:COG1196 462 LELLAELLEE 471
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
448-673 |
1.34e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 448 KESASLADRLIQGQVTRAQEAEENYLIKReLATIKQQTDAARAKLEQAESTIRELRhhrhwhkcsSTYN-------EDFV 520
Cdd:COG3206 148 ELAAAVANALAEAYLEQNLELRREEARKA-LEFLEEQLPELRKELEEAEAALEEFR---------QKNGlvdlseeAKLL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 521 LQ----LEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFPDENNIARLQEELIAVKLREAEAIMGL-------KELR 589
Cdd:COG3206 218 LQqlseLESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvIALR 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 590 QQVRTLEEHWQRHLARtsgrwkdppkknAVNELQDELMSIRLREAETQAEIREMKQRMMEMETQNQinsnQLRRAEQEVN 669
Cdd:COG3206 298 AQIAALRAQLQQEAQR------------ILASLEAELEALQAREASLQAQLAQLEARLAELPELEA----ELRRLEREVE 361
|
....
gi 568935311 670 SLQE 673
Cdd:COG3206 362 VARE 365
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
406-597 |
1.74e-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: 55.06 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 406 KKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELATIKQQT 485
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 486 DAARAKLEQAESTIRELRHHRH-WHKCSSTYNEDFV-LQLEKELVQARLSEAESQC-ALKEMQDKVLDIEKKNNSFPDEN 562
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEeLEEQLETLRSKVAqLELQIASLNNEIERLEARLeRLEDRRERLQQEIEELLKKLEEA 433
|
170 180 190
....*....|....*....|....*....|....*
gi 568935311 563 NIARLQEELIAVKLREAEAIMGLKELRQQVRTLEE 597
Cdd:TIGR02168 434 ELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
561-766 |
3.58e-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: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 561 ENNIARLQEELIAVKLREAEAIMGLKELRQQVRTLEEhwQRHLARTSGRWKDPPKKNAVNELQDELMSIRLRE---AETQ 637
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEE--ELEQLRKELEELSRQISALRKDLARLEAEVEQLEeriAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 638 AEIREMKQRMMEMETQNQINSNQLRRAEQEVNSLQEKVCSLSVKNKGLLAQLSEAKRRQAEIecknKEEVMAVRLREADS 717
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL----NEEAANLRERLESL 829
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568935311 718 IAAVAELQQHIAELEIQKEEGKLQGQ---LNRSDSNQYIRELKDQIAELTHE 766
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIEslaAEIEELEELIEELESELEALLNE 881
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
406-762 |
3.59e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 406 KKMKKLEKEYTTIKTKEMEEQGEIKRLRTEnrlLKQRIETLEKESASLADRliQGQVTRAQEAEENYLIKRELATIKQQT 485
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKADE---AKKKAEEDKKKADELKKA--AAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 486 DAARaKLEQAESTIRELRHHRHWHKCSSTYNEdfVLQLEKELVQARLSEaESQCALKEMQDKVLDIEKKNNSFPDENNIA 565
Cdd:PTZ00121 1441 EEAK-KADEAKKKAEEAKKAEEAKKKAEEAKK--ADEAKKKAEEAKKAD-EAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 566 RLQEELIAVKLREAEAIMGLKELR--QQVRTLEEHWQRHLARTSGRWKDPPKKNAVNElqDELMSIRLREAETQAEIREM 643
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKADEAKkaEEKKKADELKKAEELKKAEEKKKAEEAKKAEE--DKNMALRKAEEAKKAEEARI 1594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 644 KQRMMEMETQNQINSNQLRRAEQEVNSLQEKVCSLSVKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRlreADSIAAVAE 723
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK---AAEEAKKAE 1671
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 568935311 724 LQQHIAElEIQKEE---GKLQGQLNR-SDSNQYIRELKDQIAE 762
Cdd:PTZ00121 1672 EDKKKAE-EAKKAEedeKKAAEALKKeAEEAKKAEELKKKEAE 1713
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
400-763 |
7.87e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 400 QVKYNSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELA 479
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 480 TIKQQTDAARAKLEQAESTIRELRHHRHWHKCSSTYNEdfvlqLEKELVQARLSEAESQCA-----LKEMQDKVLDIEKK 554
Cdd:PRK02224 423 ELREREAELEATLRTARERVEEAEALLEAGKCPECGQP-----VEGSPHVETIEEDRERVEeleaeLEDLEEEVEEVEER 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 555 NNSFPD----ENNIARLQEELIAVKLREAEAIMGLKELRQQVRTLEEHWQRHLARTSGrwkdppKKNAVNELQDELMSIR 630
Cdd:PRK02224 498 LERAEDlveaEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEE------KREAAAEAEEEAEEAR 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 631 LREAETQAEIREMKQRmmeMETQNQINSNQLRRAE--QEVNSLQEKVCSLSVKNKGLLAQLSEAKRRQAEIECK-NKEEV 707
Cdd:PRK02224 572 EEVAELNSKLAELKER---IESLERIRTLLAAIADaeDEIERLREKREALAELNDERRERLAEKRERKRELEAEfDEARI 648
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568935311 708 MAVRLREADSIAAVAELQQHIAEL-----EIQKEEGKLQGQLNRsdsnqyIRELKDQIAEL 763
Cdd:PRK02224 649 EEAREDKERAEEYLEQVEEKLDELreerdDLQAEIGAVENELEE------LEELRERREAL 703
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
566-763 |
1.01e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 566 RLQEELIAVKLREAEAIMGLKELRQQVRTLEEHWQRHlartsgRWKDPPKKNAVNELQDELMSIRLREAETQAEIREMKQ 645
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEEL------RLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 646 RMMEMETQNQINSNQLRRAEQ-------EVNSLQEKVCSLSVKNKGLLAQLSEAKRRQAEIECKNK---EEVMAVRLREA 715
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESkldelaeELAELEEKLEELKEELESLEAELEELEAELEELESRLEeleEQLETLRSKVA 389
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568935311 716 DSIAAVAELQQHIAELEIQKEEgkLQGQLNRSDSNQYIRELKDQIAEL 763
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLER--LEDRRERLQQEIEELLKKLEEAEL 435
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
561-766 |
3.50e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 561 ENNIARLQEEliAVKLREAeaimglKELRQQVRTLE-EHWQRHLARTSGRWKDppKKNAVNELQDELMSIRLREAETQAE 639
Cdd:COG1196 199 ERQLEPLERQ--AEKAERY------RELKEELKELEaELLLLKLRELEAELEE--LEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 640 IREMKQRMMEMETQNQINSNQLRRAEQEVNSLQEKVCSLSVKNKGLLAQLSEAKRRQAEIEcKNKEEVMAVRLREADSIA 719
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE-EELEELEEELEELEEELE 347
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568935311 720 AVAELQQHIAELEIQKEEGKLQGQLNRSDSNQYIRELKDQIAELTHE 766
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
563-766 |
9.37e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 9.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 563 NIARLQEELIavKLREAEAIMglKELRQQVRTLE---EHWQRHLArtsgrwkdppKKNAVNELQDELMSIRLREAET--- 636
Cdd:COG4913 226 AADALVEHFD--DLERAHEAL--EDAREQIELLEpirELAERYAA----------ARERLAELEYLRAALRLWFAQRrle 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 637 --QAEIREMKQRMMEMETQNQINSNQLRRAEQEVNSLQEKVCSLSVKNKGLLAQLSEAKRRQAEiECKNKEEVMAVRLRE 714
Cdd:COG4913 292 llEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELE-ERERRRARLEALLAA 370
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568935311 715 A-----DSIAAVAELQQHIAELEIQKEEGKLQGQLNRSDSNQYIRELKDQIAELTHE 766
Cdd:COG4913 371 LglplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
424-646 |
1.15e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 424 EEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEaeenylikrELATIKQQTDAARAKLEQAESTIRELR 503
Cdd:COG4913 259 ELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRA---------ELARLEAELERLEARLDALREELDELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 504 HHRHwhkcSSTYNEdfVLQLEKELVQARLSEAESqcalkemqdkvldiekknnsfpdENNIARLQEELIAVKLREAEAIM 583
Cdd:COG4913 330 AQIR----GNGGDR--LEQLEREIERLERELEER-----------------------ERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568935311 584 GLKELRQQVRTLEEHWQRHLARTSgrwkdppkkNAVNELQDELMSIRLREAETQAEIREMKQR 646
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALE---------EALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
409-732 |
1.29e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 409 KKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELATIKQQTDAA 488
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 489 RAKLEQAEST--IRELRHHRHWHKCSSTYNEDFVLQLEKELVQARLSEAESQCA-LKEMQDKV---LDIEKKNNSFPDEN 562
Cdd:COG1196 511 KAALLLAGLRglAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEyLKAAKAGRatfLPLDKIRARAALAA 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 563 NIARLQEE----LIAVKLREAEAIMGLKELRQQVRTLE----EHWQRHLARTSGRWKD---------PPKKNAVNELQDE 625
Cdd:COG1196 591 ALARGAIGaavdLVASDLREADARYYVLGDTLLGRTLVaarlEAALRRAVTLAGRLREvtlegeggsAGGSLTGGSRREL 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 626 LMSIRLREAETQAEIREMKQRMMEMETQNQINSNQLRRAEQEVNSLQEkvcsLSVKNKGLLAQLSEAKRRQAEIECKNKE 705
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE----EELEEEALEEQLEAEREELLEELLEEEE 746
|
330 340
....*....|....*....|....*..
gi 568935311 706 EVMAVRLREADSIAAVAELQQHIAELE 732
Cdd:COG1196 747 LLEEEALEELPEPPDLEELERELERLE 773
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
419-726 |
2.08e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.89 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 419 KTKEMEEQGE-IKRLRTENRLLKQRIETLEkESASLADRLI-----QGQVTRAQEAEENYLIKRELATIKQQTDAARAKL 492
Cdd:pfam10174 413 KDKQLAGLKErVKSLQTDSSNTDTALTTLE-EALSEKERIIerlkeQREREDRERLEELESLKKENKDLKEKVSALQPEL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 493 EQAESTIRELRHHRHWHKCSSTYNEDFVLQLEKELVQAR-------------LSEAESQCALKEMQDKVLDIEKKNNSFP 559
Cdd:pfam10174 492 TEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKeecsklenqlkkaHNAEEAVRTNPEINDRIRLLEQEVARYK 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 560 DENNIARLQEELIAVKLREAEAIMGLKElrQQVRTLEEHWQRHLartsgrwKDPPKKNAVNELQDELMsiRLREAETQAE 639
Cdd:pfam10174 572 EESGKAQAEVERLLGILREVENEKNDKD--KKIAELESLTLRQM-------KEQNKKVANIKHGQQEM--KKKGAQLLEE 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 640 IREMKQRMMEMETQNQINS--NQLRRAEQEVNSLQEKVCS--LSVKNK-GLLAQLSEAKRRQAEIECKNKEEVMAVRLRE 714
Cdd:pfam10174 641 ARRREDNLADNSQQLQLEElmGALEKTRQELDATKARLSStqQSLAEKdGHLTNLRAERRKQLEEILEMKQEALLAAISE 720
|
330
....*....|..
gi 568935311 715 ADSIAAVAELQQ 726
Cdd:pfam10174 721 KDANIALLELSS 732
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
410-763 |
2.73e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 410 KLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELATIKQQTDAAR 489
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 490 AKLEQAESTIRELRHHRHWHKCSSTYNEDF---VLQLEKELVQARLSEAESQCALKEM-----QDKVLDIEKKNNSFPDE 561
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFlegVKAALLLAGLRGLAGAVAVLIGVEAayeaaLEAALAAALQNIVVEDD 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 562 NNIARLQEELIAVKLREAE-----AIMGLKELRQQVRTLEEHWQRHLARTSGRWKDPPKKNAVNELQDELM--------- 627
Cdd:COG1196 557 EVAAAAIEYLKAAKAGRATflpldKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLvaarleaal 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 628 ----SIRLREAETQAEIREMKQRMMEMETQNQINSNQLRRAEQEVNSLQEKVCSLSVKNKGLLAQLSEAKRRQAEIE--- 700
Cdd:COG1196 637 rravTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEeer 716
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568935311 701 CKNKEEVMAVRLREADSIAAVAELQQHIAELEIQKEEGKLQGQLNRSDSNQYIRELKDQIAEL 763
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
392-766 |
6.37e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 6.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 392 EKLIQSAYQVKynsKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKesasLADRLIQGQVTRAQEAEEN 471
Cdd:PRK03918 182 EKFIKRTENIE---ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 472 YLIKRELATIKQQTDAARAKLEQAESTIRELRHHRHWHKCSSTYNEdFVLQLEKEL--VQARLSEAESQcaLKEMQDKVL 549
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSE-FYEEYLDELreIEKRLSRLEEE--INGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 550 DIEKKnnsfpdENNIARLQEELIAVKlREAEAIMGLKELRQQVRTLEEHWQRHLARTSGRWKDPPKK------NAVNELQ 623
Cdd:PRK03918 332 ELEEK------EERLEELKKKLKELE-KRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKeleeleKAKEEIE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 624 DELMSIRLREAETQAEIREMKQRMMEMETQNQINSNQLRRAEQE-----VNSLQEKVCSLSVKNKGLLAQLSEAKRRQAE 698
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 699 IECKNKEEVMAVRLRE-ADSIAAVAE---------LQQHIAELEIQKEE-GKLQGQLNR-SDSNQYIRELKDQIAELTHE 766
Cdd:PRK03918 485 LEKVLKKESELIKLKElAEQLKELEEklkkynleeLEKKAEEYEKLKEKlIKLKGEIKSlKKELEKLEELKKKLAELEKK 564
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
404-646 |
7.41e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 404 NSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRL--IQGQVTRAQEAEENYLIKR----- 476
Cdd:TIGR02169 278 NKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIdkLLAEIEELEREIEEERKRRdklte 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 477 ELATIKQQTDAARAKLEQAESTIRELR--HHRHWHKCSSTYNEDFVLQLEKELVQARLSEAESQcaLKEMQDKVLDIEKK 554
Cdd:TIGR02169 358 EYAELKEELEDLRAELEEVDKEFAETRdeLKDYREKLEKLKREINELKRELDRLQEELQRLSEE--LADLNAAIAGIEAK 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 555 nnsfpdennIARLQEELIAVKLREAEAIMGLKELRQQVRTLEEHWQRhlartsgrwkdppKKNAVNELQDELMSIR--LR 632
Cdd:TIGR02169 436 ---------INELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD-------------LKEEYDRVEKELSKLQreLA 493
|
250
....*....|....
gi 568935311 633 EAETQAEIREMKQR 646
Cdd:TIGR02169 494 EAEAQARASEERVR 507
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
410-700 |
9.35e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 9.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 410 KLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQ--EAEENYLIKR---ELATIKQQ 484
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREltEEHRKELLEEytaELKRIEKE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 485 TDAARAKLEQAESTIRELRHHRHWHKCSSTYNE--DFVLQLEKELVQARLSEAESQCA-LKEMQDKVLDIEKKNNSFPDE 561
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEeYEKLKEKLIKLKGEIKSLKKE 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 562 -NNIARLQEELIAV--KLREAEAIMG-------------LKELRQQVRTLEEHWQRHLARTSGRWKDPPKKNAVNELQDE 625
Cdd:PRK03918 548 lEKLEELKKKLAELekKLDELEEELAellkeleelgfesVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEE 627
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568935311 626 LMSIRLREAETQAEIREMKQRMMEMETqnqinsnqlRRAEQEVNSLQEKVCSLSVKNKGLLAQLSEAKRRQAEIE 700
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEK---------KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIK 693
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
424-766 |
1.00e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 424 EEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELA-------TIKQQTDAARAKLEQAE 496
Cdd:PRK02224 248 ERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddadaeAVEARREELEDRDEELR 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 497 STIRELRHHRHWHKCSSTYNEDFVLQLE--------------KELVQARLSEAESQCALKEMQDKVLDIEKKNNSFPD-- 560
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEeraeelreeaaeleSELEEAREAVEDRREEIEELEEEIEELRERFGDAPVdl 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 561 ---ENNIARLQEELIAVKLREAEAIMGLKELRQQVRTLEEHWQRHLARTSGR-WKDPPKKNAVNELQDELMSIRLREAET 636
Cdd:PRK02224 408 gnaEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQpVEGSPHVETIEEDRERVEELEAELEDL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 637 QAEIREMKQRMMEMEtqnqinsnQLRRAEQEVNSLQEKVcSLSVKNKGLLAQLSEAKRRQAEIECKNKEEVMAvRLREAD 716
Cdd:PRK02224 488 EEEVEEVEERLERAE--------DLVEAEDRIERLEERR-EDLEELIAERRETIEEKRERAEELRERAAELEA-EAEEKR 557
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 568935311 717 SIAAVAELQQHIAELEIQKEEGKLQGQLNRSDSNQYIRELKDQIAELTHE 766
Cdd:PRK02224 558 EAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDE 607
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
564-764 |
1.20e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 564 IARLQEELIAVKLREAEAIMGLKELRQQVRTLEEHWQRHLARTSGRWKD---PPKKNAVNELQDELMSIRL--------- 631
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAELERLDAssddlaale 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 632 -REAETQAEIREMKQRMMEMETQNQINSNQLRRAEQEVNSLQEKVCSLSVKNKGLLAQLSEAKRRQAEIEckNKEEVMAV 710
Cdd:COG4913 692 eQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD--AVERELRE 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568935311 711 RLREadsiaavaelQQHIAELEIQKEEGKLQGQLnrsdsNQYIRELKDQIAELT 764
Cdd:COG4913 770 NLEE----------RIDALRARLNRAEEELERAM-----RAFNREWPAETADLD 808
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
440-642 |
1.57e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 440 KQRIETLEKESASLADRL--IQGQVTRAQEAEENYLIKRELATIKQQTDAARAKLEQAESTIRELRHHRhwHKCSSTYNE 517
Cdd:COG4913 609 RAKLAALEAELAELEEELaeAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAEL--ERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 518 dfVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKKnnsfpdennIARLQEELIAVKLREAEAIMGLKELRQQvrTLEE 597
Cdd:COG4913 687 --LAALEEQLEELEAELEELEEELDELKGEIGRLEKE---------LEQAEEELDELQDRLEAAEDLARLELRA--LLEE 753
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568935311 598 HWQRHLARTSGRwkdppkkNAVNELQDELMSIRLREAETQAEIRE 642
Cdd:COG4913 754 RFAAALGDAVER-------ELRENLEERIDALRARLNRAEEELER 791
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
399-762 |
1.75e-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: 45.11 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 399 YQVKYNSKKMKklEKEYTTIKTKEMEEQGEIKRlrtenRLLKQRIETLEKEsasladRLIQGQVTRAQEAEEnyliKREL 478
Cdd:pfam17380 256 YTVRYNGQTMT--ENEFLNQLLHIVQHQKAVSE-----RQQQEKFEKMEQE------RLRQEKEEKAREVER----RRKL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 479 AtikQQTDAARAKLEQAESTIRElrhhrhwhkcsstyNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNsf 558
Cdd:pfam17380 319 E---EAEKARQAEMDRQAAIYAE--------------QERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRE-- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 559 pdennIARLQEEliavKLREAEAIMGLKELRQQVRTLEEHWQRHLArtsgrwKDPPKKNAVNELQDELMSIRLREAETQA 638
Cdd:pfam17380 380 -----LERLQME----RQQKNERVRQELEAARKVKILEEERQRKIQ------QQKVEMEQIRAEQEEARQREVRRLEEER 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 639 EiREMKQ-RMMEMETQNQI-----NSNQLRRAEQEVNSLQEKVCSLSVKNKGLLAQLSEAkRRQAEIECKNKEEVMAVRL 712
Cdd:pfam17380 445 A-REMERvRLEEQERQQQVerlrqQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEE-RKQAMIEEERKRKLLEKEM 522
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568935311 713 READSiAAVAELQQHIAELE------------IQKEEGKLQGQLNRSDSNQYIRELKDQIAE 762
Cdd:pfam17380 523 EERQK-AIYEEERRREAEEErrkqqemeerrrIQEQMRKATEERSRLEAMEREREMMRQIVE 583
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
400-653 |
2.52e-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: 44.66 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 400 QVKYNSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRL--IQGQVTRAQEAEENYLIKRE 477
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIesLAAEIEELEELIEELESELE 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 478 LAT-----IKQQTDAARAKLEQAESTIRELRHHRHwhkcsstynedfvlQLEKELVQARLSEAESQCALKEMqdkvldie 552
Cdd:TIGR02168 877 ALLnerasLEEALALLRSELEELSEELRELESKRS--------------ELRRELEELREKLAQLELRLEGL-------- 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 553 kknnsfpdENNIARLQEELIAVKLREAEAIMGLKELRQqvrTLEEHWQRHLARTsgrwkdppkKNAVNELQD-ELMSIrl 631
Cdd:TIGR02168 935 --------EVRIDNLQERLSEEYSLTLEEAEALENKIE---DDEEEARRRLKRL---------ENKIKELGPvNLAAI-- 992
|
250 260
....*....|....*....|..
gi 568935311 632 reaetqAEIREMKQRMMEMETQ 653
Cdd:TIGR02168 993 ------EEYEELKERYDFLTAQ 1008
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
474-740 |
2.68e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 474 IKRELATIKQQTDAARAKLEQAESTIRELRHHrhwhkcsstynEDFVLQLEKELVQARLSEAESQcaLKEMQDKVLDIEK 553
Cdd:PRK04863 849 LERALADHESQEQQQRSQLEQAKEGLSALNRL-----------LPRLNLLADETLADRVEEIREQ--LDEAEEAKRFVQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 554 KNNSFPD-ENNIARLQ---EELIAVKLREAEAIMGLKELRQQVRTLEEHWQR--HLArtsgrWKDPPKKNAVNELQDELM 627
Cdd:PRK04863 916 HGNALAQlEPIVSVLQsdpEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRraHFS-----YEDAAEMLAKNSDLNEKL 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 628 SIRLREAETQAeiREMKQRMmemeTQNQinsNQLRRAEQEVNSLQEkvcSLSVKNKgllaQLSEAKRR----------QA 697
Cdd:PRK04863 991 RQRLEQAEQER--TRAREQL----RQAQ---AQLAQYNQVLASLKS---SYDAKRQ----MLQELKQElqdlgvpadsGA 1054
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568935311 698 EIECKNKEEVMAVRLREADSIAAVAELQQHIAELEIQKEEGKL 740
Cdd:PRK04863 1055 EERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKL 1097
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
412-503 |
3.17e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 412 EKEYTTIKTKEMEEQ-----GEIKRLRTENRLLKQRIETLEKESASLADRLiqgqVTRAQEAEENYLIKRELATIKQQTD 486
Cdd:COG2433 400 EKEHEERELTEEEEEirrleEQVERLEAEVEELEAELEEKDERIERLEREL----SEARSEERREIRKDREISRLDREIE 475
|
90
....*....|....*..
gi 568935311 487 AARAKLEQAESTIRELR 503
Cdd:COG2433 476 RLERELEEERERIEELK 492
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
483-737 |
3.26e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 483 QQTDAARAKLEQAESTIRelrhhrhwhkcsstynedfvlQLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFpdEN 562
Cdd:COG4942 20 DAAAEAEAELEQLQQEIA---------------------ELEKELAALKKEEKALLKQLAALERRIAALARRIRAL--EQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 563 NIARLQEELIAVKLREAEAIMGLKELRQQVRTLEEHWQRHLARtsGRWKDPPKKNAVNELQDELMSIRLREAETQAEIRE 642
Cdd:COG4942 77 ELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQ--PPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 643 MKQRMMEMETQNQINSNQLRRAEQEVNSLQEKvcslsvknkglLAQLSEAKRRQAEIECKNKEEVMAVRLREADSIAAVA 722
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEE-----------RAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250
....*....|....*
gi 568935311 723 ELQQHIAELEIQKEE 737
Cdd:COG4942 224 ELEALIARLEAEAAA 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
421-597 |
4.02e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 421 KEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRL--IQGQVTRAQEAEENylIKRELATIK-QQTDAARAKLEQAES 497
Cdd:COG4913 275 EYLRAALRLWFAQRRLELLEAELEELRAELARLEAELerLEARLDALREELDE--LEAQIRGNGgDRLEQLEREIERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 498 TIRELRHHRhwhkcsstynedfvLQLEKELVQARLSEAESQCALKEMQDKVLDIekknnsfpdennIARLQEELIAVKLR 577
Cdd:COG4913 353 ELEERERRR--------------ARLEALLAALGLPLPASAEEFAALRAEAAAL------------LEALEEELEALEEA 406
|
170 180
....*....|....*....|
gi 568935311 578 EAEAIMGLKELRQQVRTLEE 597
Cdd:COG4913 407 LAEAEAALRDLRRELRELEA 426
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
405-727 |
6.33e-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: 43.27 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 405 SKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKE----SASLADRLIQGQVTRAQEAEENYLIKRELAT 480
Cdd:pfam10174 446 SEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPEltekESSLIDLKEHASSLASSGLKKDSKLKSLEIA 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 481 IKQQTDAArAKLEQAESTIRELrhhrhwhKCSSTYNEDFVLQ---LEKELVQARLSEAESQCALKEMQDKVLDIEKKNNS 557
Cdd:pfam10174 526 VEQKKEEC-SKLENQLKKAHNA-------EEAVRTNPEINDRirlLEQEVARYKEESGKAQAEVERLLGILREVENEKND 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 558 fpDENNIARLqEELIAVKLREAEAIMGLKELRQQVRTLEEHWQRHLARtsgRWKDPPKKNAVNELQDELMSIRLReaeTQ 637
Cdd:pfam10174 598 --KDKKIAEL-ESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEAR---RREDNLADNSQQLQLEELMGALEK---TR 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 638 AEIREMKQRMMEMETQNQINSNQLRRAEQEVNSLQEKVcsLSVKNKGLLAQLSEAKRRQAEIEC------KNKEEVMAVR 711
Cdd:pfam10174 669 QELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEI--LEMKQEALLAAISEKDANIALLELssskkkKTQEEVMALK 746
|
330
....*....|....*.
gi 568935311 712 lREADSIaaVAELQQH 727
Cdd:pfam10174 747 -REKDRL--VHQLKQQ 759
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
396-765 |
8.43e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 396 QSAYQVKYNSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRL--------IQGQVTRAQE 467
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlvqtalrQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 468 AEENYLIKRE-----LATIKQQTDAARAKLEQAESTIRELRhhrhwhKCSSTYNEDFVLQLEKEL-----VQArLSEAES 537
Cdd:PRK04863 356 DLEELEERLEeqnevVEEADEQQEENEARAEAAEEEVDELK------SQLADYQQALDVQQTRAIqyqqaVQA-LERAKQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 538 QCAL-------------------KEMQDKVLDIEKKNNSFPDenniARLQEELIAVKLREAEAIMGLKELRQQVRTLEEH 598
Cdd:PRK04863 429 LCGLpdltadnaedwleefqakeQEATEELLSLEQKLSVAQA----AHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRR 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 599 W--QRHLARTSgrwkdPPKKNAVNELQDELMSirlrEAETQAEIREMKQRMMEMETQNQINSNQLRRAEQEVNSLQEKVC 676
Cdd:PRK04863 505 LreQRHLAEQL-----QQLRMRLSELEQRLRQ----QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 677 SLSVKNKGLLAQLSEAKRRQAEIECKNKEEVMA----VRLRE------ADSiAAVAELQQHIAELEIQKeegklqgQLNR 746
Cdd:PRK04863 576 EARERRMALRQQLEQLQARIQRLAARAPAWLAAqdalARLREqsgeefEDS-QDVTEYMQQLLEREREL-------TVER 647
|
410
....*....|....*....
gi 568935311 747 SDSNQYIRELKDQIAELTH 765
Cdd:PRK04863 648 DELAARKQALDEEIERLSQ 666
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
421-759 |
9.36e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.65 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 421 KEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIK-----------RELATIKQQTDAAR 489
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYlklneeridllQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 490 AKLEQAESTIRELRhhrhwHKCSSTYNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFPDENN------ 563
Cdd:pfam02463 257 KQEIEKEEEKLAQV-----LKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKaekelk 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 564 -----IARLQEELIAVKLREAEAIMGLKELRQQVRTLEEHWQRHLARTSGRWKDPPKKNAVNELQDELMSIRLREAETQA 638
Cdd:pfam02463 332 kekeeIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 639 EIREMKQ--RMMEMETQNQINSNQLRRAEQEVNSLQEKVCSLSVKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREAD 716
Cdd:pfam02463 412 ELARQLEdlLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLS 491
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 568935311 717 SIAAVAELQQHIAELEIQKEEGKLQGQLNRSDSNQYIRELKDQ 759
Cdd:pfam02463 492 RQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDL 534
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
404-650 |
1.04e-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: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 404 NSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRL----IQGQVTRAQEAEENY------- 472
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLeaaeDLARLELRALLEERFaaalgda 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 473 LIKRELATIKQQTDAARAKLEQAESTIREL--RHHRHWHKCSST------YNEDFVLQLEKeLVQARLSEAESQcaLKEM 544
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAEEELERAmrAFNREWPAETADldadleSLPEYLALLDR-LEEDGLPEYEER--FKEL 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 545 qdkvldieKKNNSfpdENNIARLQEELiavkLREAEAIMG-LKELRQQVRTLEEHWQRHLARTSGRWKDPpkknAVNELQ 623
Cdd:COG4913 840 --------LNENS---IEFVADLLSKL----RRAIREIKErIDPLNDSLKRIPFGPGRYLRLEARPRPDP----EVREFR 900
|
250 260 270
....*....|....*....|....*....|.
gi 568935311 624 DELMSIRLREAETQAEIREMK----QRMMEM 650
Cdd:COG4913 901 QELRAVTSGASLFDEELSEARfaalKRLIER 931
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
404-735 |
1.07e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 404 NSKKMKKLEKEYTTIKTKEMEeqgeikrLRTENRLLKQRIETLEKESASLADRLIQGQVTRAQEAEENYLIKRELatikQ 483
Cdd:pfam15921 312 NSMYMRQLSDLESTVSQLRSE-------LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL----Q 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 484 QTDAARAKLEQAESTIRElRHHRHWHKcsSTYNEDFVLQLEKEL---------VQARLSEAESQCAlKEMQDKVLDIEKK 554
Cdd:pfam15921 381 KLLADLHKREKELSLEKE-QNKRLWDR--DTGNSITIDHLRRELddrnmevqrLEALLKAMKSECQ-GQMERQMAAIQGK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 555 NNSFpdeNNIARLQEELIAVK--LREAeaimgLKELRQQVRTLEEHwQRHLARTSGRWKDppKKNAVNELQDELMSIRLR 632
Cdd:pfam15921 457 NESL---EKVSSLTAQLESTKemLRKV-----VEELTAKKMTLESS-ERTVSDLTASLQE--KERAIEATNAEITKLRSR 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 633 EAETQAEIREMKQRMMEME-TQNQINSNQLRRAEQE--VNSLQEKVCSLS--VKNKGLLAQLSEAKRRQAEIECKNKE-E 706
Cdd:pfam15921 526 VDLKLQELQHLKNEGDHLRnVQTECEALKLQMAEKDkvIEILRQQIENMTqlVGQHGRTAGAMQVEKAQLEKEINDRRlE 605
|
330 340
....*....|....*....|....*....
gi 568935311 707 VMAVRLREADSIAAVAELQQHIAELEIQK 735
Cdd:pfam15921 606 LQEFKILKDKKDAKIRELEARVSDLELEK 634
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
514-763 |
1.34e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 514 TYNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFPD----ENNIARLQEEL---IAVKLREAEAIMGLK 586
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEqlqaETELCAEAEEMrarLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 587 ELRqqvrtLEEHWQRHLARTSGRWKDPPKKNAVNELQDELMSIR----LREAETQAEIREMKQRMMEMETQNQINSNQLR 662
Cdd:pfam01576 81 ESR-----LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARqklqLEKVTTEAKIKKLEEDILLLEDQNSKLSKERK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 663 RAEQEVNSL-------QEKVCSLS---VKNKGLLAQLS-----EAKRRQAEIECKNKEEVMAVRLREadsiaAVAELQQH 727
Cdd:pfam01576 156 LLEERISEFtsnlaeeEEKAKSLSklkNKHEAMISDLEerlkkEEKGRQELEKAKRKLEGESTDLQE-----QIAELQAQ 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 568935311 728 IAELEIQ--KEEGKLQGQLNRSDSNQ--------YIRELKDQIAEL 763
Cdd:pfam01576 231 IAELRAQlaKKEEELQAALARLEEETaqknnalkKIRELEAQISEL 276
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
585-763 |
1.38e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 585 LKELRQQVRTLEEhwqrhlartsgrwkdppKKNAVNELQDELMSIRLREAETQAEIREMKQRMMEMETQNQINS--NQLR 662
Cdd:COG4717 73 LKELEEELKEAEE-----------------KEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 663 RAEQEVNSLQEKVCSLSVKNKGLLAQLSEAKRRQAEIECKNKEevmAVRLREADSIAAVAELQQHIAELE-IQKEEGKLQ 741
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEE---LEELLEQLSLATEEELQDLAEELEeLQQRLAELE 212
|
170 180
....*....|....*....|..
gi 568935311 742 GQLNRSDsnQYIRELKDQIAEL 763
Cdd:COG4717 213 EELEEAQ--EELEELEEELEQL 232
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
522-761 |
1.93e-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: 41.75 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 522 QLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFpdENNIARLQ---------EELIAVKLREAEAimGLKELRQQV 592
Cdd:pfam12128 217 RLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTL--ESAELRLShlhfgyksdETLIASRQEERQE--TSAELNQLL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 593 RTLEEHWQRHLARTSGRWKDPPKKNAVNELQDELMSIRLR-----EAETQAEIREM-KQRMMEMETQNQINSNQL---RR 663
Cdd:pfam12128 293 RTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGafldaDIETAAADQEQlPSWQSELENLEERLKALTgkhQD 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 664 AEQEVNSLQEKVCS-----LSVKNKGLLAQlSEAKRRQAEiECKNKEEVMAVRLREadsiaavaELQQHIAELEIQKEEG 738
Cdd:pfam12128 373 VTAKYNRRRSKIKEqnnrdIAGIKDKLAKI-REARDRQLA-VAEDDLQALESELRE--------QLEAGKLEFNEEEYRL 442
|
250 260
....*....|....*....|....*
gi 568935311 739 KLQ-GQLN-RSDSNQYIRELKDQIA 761
Cdd:pfam12128 443 KSRlGELKlRLNQATATPELLLQLE 467
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
587-758 |
1.96e-03 |
|
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: 41.39 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 587 ELRQQVRTLEEHWQRHLARTSGRWKDPPKKNAVNELQDELMSIRLREAETQAEIREMKQRMMEMETQNQINSNQLRRAEQ 666
Cdd:pfam08017 55 ENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQGNVLERRQRDA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 667 EvNSLQEKVCSLSVKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREAD--SIAAVAELQQHIAELEIQKE--EGKLQG 742
Cdd:pfam08017 135 E-NRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAEnkSQGNVLERRQRDAENRSQGNvlERRQRD 213
|
170
....*....|....*.
gi 568935311 743 QLNRSDSNQYIRELKD 758
Cdd:pfam08017 214 AENRSQGNVLERRQRD 229
|
|
| DUF1129 |
pfam06570 |
Protein of unknown function (DUF1129); This family consists of several hypothetical bacterial ... |
516-554 |
3.27e-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: 39.57 E-value: 3.27e-03
10 20 30
....*....|....*....|....*....|....*....
gi 568935311 516 NEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKK 554
Cdd:pfam06570 6 NQDYIFRLTKQLIKDGKSDEEIKEILDEMLPEILEGQKK 44
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
392-705 |
4.26e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 392 EKLIQSAYQVKYNSKKMKKLEKEYTTIKTKemeeqgeikrlrtenrllkqrIETLEKEsasladrliqgqvtraQEAEEN 471
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSE---------------------ISDLNNQ----------------KEQDWN 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 472 YLIKRELATIKQQTDAARAKLEQAESTIRELrhhrhwhkcsstynEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDI 551
Cdd:TIGR04523 310 KELKSELKNQEKKLEEIQNQISQNNKIISQL--------------NEQISQLKKELTNSESENSEKQRELEEKQNEIEKL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 552 EKKNNSFPDE-----NNIARLQEELIAVKLREAEAIMGLKELRQQVRTLEEHWQRHLARTS---GRWKDPPKKNAVNELQ 623
Cdd:TIGR04523 376 KKENQSYKQEiknleSQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIknnSEIKDLTNQDSVKELI 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 624 DELMSIRLREAETQaeIREMKQRMMEMETQNQINSNQLRRAEQEVNSLQEKVCSLSVKNKGLLAQLSEAKRRQAEIECKN 703
Cdd:TIGR04523 456 IKNLDNTRESLETQ--LKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEK 533
|
..
gi 568935311 704 KE 705
Cdd:TIGR04523 534 KE 535
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
429-766 |
4.91e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 429 IKRLR--TENRLLKQRIETLEKESASLADRLiqgQVTRAQEAEenylIKRELATIKQQTDAARAKLEQAESTIRELRHHR 506
Cdd:PRK02224 178 VERVLsdQRGSLDQLKAQIEEKEEKDLHERL---NGLESELAE----LDEEIERYEEQREQARETRDEADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 507 hwhkcsstynedfvlqlekelvqARLSEAESqcALKEMQDKVLDIEKKNNSFPDENNIARLQEELIAVKLREAEAIMGLK 586
Cdd:PRK02224 251 -----------------------EELETLEA--EIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 587 ELRQQvrTLEEHWQRHLARTSgrwkdppkknavnELQDELMSIR------------LREAETQAEIR--EMKQRMMEMET 652
Cdd:PRK02224 306 DADAE--AVEARREELEDRDE-------------ELRDRLEECRvaaqahneeaesLREDADDLEERaeELREEAAELES 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 653 QNQINSNQLRRAEQEVNSLQEKVCSLSVKNKGLLAQLSEAKRRQAEIEcknkEEVMAVRLREADSIAAVAELQQHIAELE 732
Cdd:PRK02224 371 ELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR----EERDELREREAELEATLRTARERVEEAE 446
|
330 340 350
....*....|....*....|....*....|....*..
gi 568935311 733 IQKEEGKLQ--GQ-LNRSDSNQYIRELKDQIAELTHE 766
Cdd:PRK02224 447 ALLEAGKCPecGQpVEGSPHVETIEEDRERVEELEAE 483
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
564-763 |
5.06e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 564 IARLQEELIAVKLREAEAIMGLKELRQQVRTLEehwqrhlartsgrwKDPPKKNAVNELQDElmsirLREAETQAEIREM 643
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLR--------------REREKAERYQALLKE-----KREYEGYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 644 KqrmmEMETQNQINSNQLRRAEQEVNSLQEKvcsLSVKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREADSIAAVAE 723
Cdd:TIGR02169 233 E----ALERQKEAIERQLASLEEELEKLTEE---ISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAS 305
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568935311 724 LQQHIAELE-----IQKEEGKLQGQLNRSDSNqyIRELKDQIAEL 763
Cdd:TIGR02169 306 LERSIAEKEreledAEERLAKLEAEIDKLLAE--IEELEREIEEE 348
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
587-743 |
5.09e-03 |
|
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: 39.85 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 587 ELRQQVRTLEEHWQRHLARTSGRWKDPPKKNAVNELQDELMSIRLREAETQAEIREMKQRMMEMETQNQINSNQLRRAEQ 666
Cdd:pfam08017 151 ENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDA 230
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568935311 667 EvNSLQEKVCSLSVKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREADSIAAVAELQQHIAELEIQKEEGKLQGQ 743
Cdd:pfam08017 231 E-NRSQGNVLERRQRDAENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQVGQLIGK 306
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
406-763 |
5.16e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 406 KKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKEsASLADRLIQGQVTRAQEAEENYLIKRELATIKQQT 485
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL-LQLLPLYQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 486 DaARAKLEQAESTIRELRHH-RHWHKCSSTYNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFPDENNI 564
Cdd:COG4717 160 E-LEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 565 ARLQEEL--IAVKLREAEAIMGLKELRQQVRTLEEHWQ---------RHLARTSGRWKDPPKKNAVNELQDELMSIRLRE 633
Cdd:COG4717 239 AALEERLkeARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEE 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 634 AETQA---------------------EIREMKQRMMEMETQNQinSNQLRRAEQEVNSLQEKVcslSVKNKGLLAQLSEA 692
Cdd:COG4717 319 EELEEllaalglppdlspeellelldRIEELQELLREAEELEE--ELQLEELEQEIAALLAEA---GVEDEEELRAALEQ 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 693 KRRQAEIECKNKE------------EVMAVRLREADSIAAVAELQQHIAELE-----IQKEEGKLQGQLNRSDSNQYIRE 755
Cdd:COG4717 394 AEEYQELKEELEEleeqleellgelEELLEALDEEELEEELEELEEELEELEeeleeLREELAELEAELEQLEEDGELAE 473
|
....*...
gi 568935311 756 LKDQIAEL 763
Cdd:COG4717 474 LLQELEEL 481
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
561-763 |
5.64e-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: 39.75 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 561 ENNIARLQEELIAVKLREAEAIMGLKELRQQVRTLEehwqRHLARTSGRwkdppkknaVNELQDELMSIRLREAETQAEI 640
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALA----RRIRALEQE---------LAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 641 REMKQRMMEMETQNQINSNQlrraEQEVNSLQEKVCSLSVKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREADSIA- 719
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQ----PPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAe 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568935311 720 ---AVAELQQHIAELEIQKEE-GKLQGQLNR--SDSNQYIRELKDQIAEL 763
Cdd:COG4942 176 leaLLAELEEERAALEALKAErQKLLARLEKelAELAAELAELQQEAEEL 225
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
635-764 |
6.43e-03 |
|
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: 40.04 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 635 ETQAEIREMKQRMMEMETQNQINSNQLRRAEQEVNSLQEKVCSLSVKNKGLLAQLSEAKR--RQAEIECKNKEEVMAVRL 712
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 568935311 713 RE-ADSIAAVAELQQHIAELEIQKEEGKLQGQLNRSDSNQYIRELKDQIAELT 764
Cdd:TIGR02168 754 KElTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
490-667 |
6.78e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 490 AKLEQAESTIRELRHHRHwhkcssTYNEdfvLQLEKELVQARLSEAESQcaLKEMQDKVLDIEKKNNSFPDENNIARLQE 569
Cdd:COG4717 71 KELKELEEELKEAEEKEE------EYAE---LQEELEELEEELEELEAE--LEELREELEKLEKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 570 ELIAVKLREAEAIMGLKELRQQVRTLE------EHWQRHLARTSGRWkDPPKKNAVNELQDELMSIRLREAETQAEIREM 643
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEeleaelAELQEELEELLEQL-SLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180
....*....|....*....|....
gi 568935311 644 KQRMMEMETQNQINSNQLRRAEQE 667
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALE 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
405-597 |
6.83e-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: 39.36 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 405 SKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRLiqgqvtRAQEAEENyLIKRELATIKQQ 484
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI------RALEQELA-ALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 485 TDAARAKLEQAESTIREL--------RHHRHWHKCSSTYNEDFV--LQLEKELVQARLSEAESQCA-LKEMQDKVLDIEK 553
Cdd:COG4942 92 IAELRAELEAQKEELAELlralyrlgRQPPLALLLSPEDFLDAVrrLQYLKYLAPARREQAEELRAdLAELAALRAELEA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568935311 554 KNNSFpdENNIARLQEELIAVKLREAEAIMGLKELRQQVRTLEE 597
Cdd:COG4942 172 ERAEL--EALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
391-617 |
9.75e-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: 38.98 E-value: 9.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 391 PEKLIQSAYQVKYNSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKESASLADRL----IQGQVTRAQ 466
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568935311 467 EAEENYLIKRELATIKQQTDAARAKLEQAESTIRELRHHRHWHKCSSTYNEDFVLQLEKELVQARLSEAESQCALKEMQD 546
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568935311 547 KVLDIEKKNNSFpdENNIARLQEELIAVKLREAEAIMGLKELRQQVRTLEEHWQRHLARTSGRWKDPPKKN 617
Cdd:COG4942 179 LLAELEEERAAL--EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| |
