|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
135-467 |
3.49e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.17 E-value: 3.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 135 NEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDL 214
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 215 SD-------TQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSENIASL 287
Cdd:TIGR02168 757 TEleaeieeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 288 GESLAMKEKTISGMKNIIAEMEQASRQCTEALivceqdvSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQE 367
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELI-------EELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 368 NQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQL-RKANEDAENWENKARQSEADNNTLKLELI 446
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRLENKIKELGPVNL 989
|
330 340
....*....|....*....|.
gi 1034616921 447 TAEAEGNRLKEKVDSLNREVE 467
Cdd:TIGR02168 990 AAIEEYEELKERYDFLTAQKE 1010
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
50-681 |
2.34e-12 |
|
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: 70.53 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 50 IQGNVKVLKSE-RDKIFLLYEQAQEEITRLRREmmksckspksttaHAILRRVETERDVAftdlrrMTTERDSLRERLKI 128
Cdd:pfam15921 243 VEDQLEALKSEsQNKIELLLQQHQDRIEQLISE-------------HEVEITGLTEKASS------ARSQANSIQSQLEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 129 AQETAFNEKAHLEQRIEELECTVHNLDDErmeqmsnmtlMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYE 208
Cdd:pfam15921 304 IQEQARNQNSMYMRQLSDLESTVSQLRSE----------LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESG 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 209 NTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEK-------IDNFTRQNIAQREEISILGGTLNDLAKEKE---------- 271
Cdd:pfam15921 374 NLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQgqmerqmaai 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 272 -----------CLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDEL 340
Cdd:pfam15921 454 qgkneslekvsSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQEL 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 341 AQIARERDILAH---DNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKnilksEESENRQMMEQL 417
Cdd:pfam15921 534 QHLKNEGDHLRNvqtECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLE-----KEINDRRLELQE 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 418 RKANEDAEnwENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHK--SVVK------ 489
Cdd:pfam15921 609 FKILKDKK--DAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEdyEVLKrnfrnk 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 490 ---MEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANerismqn 566
Cdd:pfam15921 687 seeMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTN------- 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 567 leallvANRDKEYqsqiaLQEKESEIQLLKEHLCLAENKMA----IQSRDVAQFRNVVTQLEADLDITKRQLG-----TE 637
Cdd:pfam15921 760 ------ANKEKHF-----LKEEKNKLSQELSTVATEKNKMAgeleVLRSQERRLKEKVANMEVALDKASLQFAecqdiIQ 828
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1034616921 638 RFERERA---------VQELRRQNYSSNayhmsSTMKPN-TKCHSPERAHHRSP 681
Cdd:pfam15921 829 RQEQESVrlklqhtldVKELQGPGYTSN-----SSMKPRlLQPASFTRTHSNVP 877
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
255-568 |
5.22e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 255 EISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLd 334
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 335 etndelaQIARERDilahdnDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMM 414
Cdd:TIGR02168 305 -------QILRERL------ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 415 EQLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHlnaersyksqistlhksvvkmEEEL 494
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL---------------------LKKL 430
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034616921 495 QKVQFEKVSalADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLE 568
Cdd:TIGR02168 431 EEAELKELQ--AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
102-402 |
2.21e-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: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 102 ETERDVAFTDLRRMTTERDSLR---ERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKE 178
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 179 MKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISI 258
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 259 LGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKtisgmkniiaEMEQASRQCTEAlivcEQDVSRMRRQLDETND 338
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNERASLEEALALLRS----------ELEELSEELREL----ESKRSELRRELEELRE 922
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034616921 339 ELAQIARERDILAHDNDNLQEQFA-KAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNI 402
Cdd:TIGR02168 923 KLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPV 987
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
110-657 |
2.68e-11 |
|
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: 67.07 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 110 TDLRRMTTERDSL---RERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLArka 186
Cdd:pfam15921 117 TKLQEMQMERDAMadiRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 187 MDTESELGRQKAENNSLRLL-YENTEKDLSDTQRHLAKK---------KYELQL------TQEKIMCLDEKIDNFTRQNI 250
Cdd:pfam15921 194 VDFEEASGKKIYEHDSMSTMhFRSLGSAISKILRELDTEisylkgrifPVEDQLealkseSQNKIELLLQQHQDRIEQLI 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 251 AQRE-EISILGGTLNDLAKEKECLQACLDKKSENIASLGeslAMKEKTISGMKNIIAEMEQASRqctEALIVCEQDVSRM 329
Cdd:pfam15921 274 SEHEvEITGLTEKASSARSQANSIQSQLEIIQEQARNQN---SMYMRQLSDLESTVSQLRSELR---EAKRMYEDKIEEL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 330 RRQLDETNDELAQIARERDILAHDNDNLQEQFAK------AKQENQALSKKLN------DTHNEL--NDIKQKVQDTNLE 395
Cdd:pfam15921 348 EKQLVLANSELTEARTERDQFSQESGNLDDQLQKlladlhKREKELSLEKEQNkrlwdrDTGNSItiDHLRRELDDRNME 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 396 VNKLKNILKSEESENRQMMEQ----LRKANEDAENWENKARQSEADNNTLK--LELITAEAEGNRLKEK-VDSLNREVEQ 468
Cdd:pfam15921 428 VQRLEALLKAMKSECQGQMERqmaaIQGKNESLEKVSSLTAQLESTKEMLRkvVEELTAKKMTLESSERtVSDLTASLQE 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 469 HLNAERSYKSQISTLHKSVVKMEEELQKVQFEK---VSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDS 545
Cdd:pfam15921 508 KERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGA 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 546 AHSEIELLRSQMANERISMQNLEALlvanRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQ---------- 615
Cdd:pfam15921 588 MQVEKAQLEKEINDRRLELQEFKIL----KDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQerdqllnevk 663
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1034616921 616 -FRNVVTQLEADLDITKRQLGTERFERERAVQELRRQNYSSNA 657
Cdd:pfam15921 664 tSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQS 706
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
330-597 |
1.26e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 330 RRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQkvqdtnlEVNKLKNILKSEESE 409
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA-------ELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 410 NRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVK 489
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 490 MEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEA 569
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260
....*....|....*....|....*...
gi 1034616921 570 LLVANRDKEYQSQIALQEKESEIQLLKE 597
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
24-652 |
2.36e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 24 ELLKTTTRDREELKCMLEKYERHLAEIQGNVKVLKSERDKIFLLYEQAQEEITRLRREMMKSCKSPKSTT-----AHAIL 98
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLErqleeLEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 99 RRVETERDVAFTDLRRMTTERDSLR---ERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTV 175
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKeelESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 176 EKEMKSLAR-------------------KAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIM 236
Cdd:TIGR02168 406 EARLERLEDrrerlqqeieellkkleeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 237 CLDEKID-------------NFTRQNIAQREEISILGGTLNDLAKEKECLQACLDK-----------KSENIA------- 285
Cdd:TIGR02168 486 QLQARLDslerlqenlegfsEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAalggrlqavvvENLNAAkkaiafl 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 286 ---SLGESLAMKEKTISGMKNIIAEMEQASRQ--CTEALIVCEQDVSRMRR-------------QLDETNDELAQIARER 347
Cdd:TIGR02168 566 kqnELGRVTFLPLDSIKGTEIQGNDREILKNIegFLGVAKDLVKFDPKLRKalsyllggvlvvdDLDNALELAKKLRPGY 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 348 DILAHDNDNLQEQFAKAKQENQALSKKLNdTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAEnw 427
Cdd:TIGR02168 646 RIVTLDGDLVRPGGVITGGSAKTNSSILE-RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-- 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 428 enkarQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSALAD 507
Cdd:TIGR02168 723 -----ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 508 LSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVANRDKEYQSQIALQE 587
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034616921 588 KESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAVQELRRQN 652
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
280-607 |
3.19e-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: 60.46 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 280 KSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQE 359
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 360 QFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNN 439
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 440 TLKLELITAEAEGNRLKEKVDSLNREVEQhlnaersyksqistLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLD 519
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEE--------------LEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 520 SSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANerismqNLEALLVANRDkEYQSQIALQEK-ESEIQLLKEH 598
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN------LQERLSEEYSL-TLEEAEALENKiEDDEEEARRR 973
|
....*....
gi 1034616921 599 LCLAENKMA 607
Cdd:TIGR02168 974 LKRLENKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
330-649 |
9.67e-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: 58.91 E-value: 9.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 330 RRQLDETNDELAQIArerDILAHDN---DNLQEQfAKAKQENQALSKKLNDTHNELndIKQKVQDTNLEVNKLKNILKSE 406
Cdd:TIGR02168 178 ERKLERTRENLDRLE---DILNELErqlKSLERQ-AEKAERYKELKAELRELELAL--LVLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 407 ESENRQMMEQLRKANEDAEnwENKARQSEADN--NTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLH 484
Cdd:TIGR02168 252 EEELEELTAELQELEEKLE--ELRLEVSELEEeiEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 485 KSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISM 564
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 565 QNLEallvANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRdVAQFRNVVTQLEAdLDITKRQLGTERFERERA 644
Cdd:TIGR02168 410 ERLE----DRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL-QEELERLEEALEE-LREELEEAEQALDAAERE 483
|
....*
gi 1034616921 645 VQELR 649
Cdd:TIGR02168 484 LAQLQ 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
416-651 |
1.03e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 416 QLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQ 495
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 496 kvqfekvSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVANR 575
Cdd:COG1196 313 -------ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034616921 576 DKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAVQELRRQ 651
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
178-507 |
4.88e-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: 56.61 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 178 EMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEIS 257
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 258 ILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMkektiSGMKNIIAEMEQAsrqctealivcEQDVSRMRRQLDETN 337
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSH-----SRIPEIQAELSKL-----------EEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 338 DELAQIARERDILAHDNDNLQEQfakakqenqalskkLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQL 417
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQ--------------RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 418 RKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSqISTLHKSVVKMEEELQKV 497
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE-IPEEELSLEDVQAELQRV 963
|
330
....*....|
gi 1034616921 498 QfEKVSALAD 507
Cdd:TIGR02169 964 E-EEIRALEP 972
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
26-597 |
1.01e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 26 LKTTTRDREELKCMLEKYERHLAEIQGNVKVLKSERDKIFLLYEQAQEEITRLRREmmksckspksttahaiLRRVETER 105
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE----------------LARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 106 DVAFTDLRRMTTERDSLRERLKIAQEtafnEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARK 185
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEE----ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 186 AMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLND 265
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 266 LAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEA-LIVCEQDVSRMRRQLDETNDELAQIA 344
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAlLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 345 RERDILAHDNDNLQEQFAKAKQENQALSKKLNdthnelndikqkvQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDA 424
Cdd:COG1196 541 EAALAAALQNIVVEDDEVAAAAIEYLKAAKAG-------------RATFLPLDKIRARAALAAALARGAIGAAVDLVASD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 425 ENWENKARQSEADnnTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSA 504
Cdd:COG1196 608 LREADARYYVLGD--TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 505 LADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVANRDKEYQsqia 584
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD---- 761
|
570
....*....|...
gi 1034616921 585 LQEKESEIQLLKE 597
Cdd:COG1196 762 LEELERELERLER 774
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
35-650 |
1.55e-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: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 35 ELKCMLEKYERHLAEIQgnVKVLKSERDKIFLLYEQAQEEITRLRREMmksckspksttahailrrveTERDVAFTDLRR 114
Cdd:TIGR02168 217 ELKAELRELELALLVLR--LEELREELEELQEELKEAEEELEELTAEL--------------------QELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 115 MTTERDSLRERLKIAQETAFNEKAHLEQRIEELectvhnldDERMEQmsnmtlmketistVEKEMKSLARKAMDTESELG 194
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQIL--------RERLAN-------------LERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 195 RQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQ 274
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 275 ACLDKKSENIASLGESLAMKEK-----TISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDI 349
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAELkelqaELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 350 LAHDNDNLQEQFAKAKQENQALSkKLNDTHNELNDI------------------KQKVQDTNLE-VNKLKNILKSEESEN 410
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQS-GLSGILGVLSELisvdegyeaaieaalggrLQAVVVENLNaAKKAIAFLKQNELGR 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 411 RQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAE--------------------AEGNRLKEKVDSLNREV---- 466
Cdd:TIGR02168 573 VTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDpklrkalsyllggvlvvddlDNALELAKKLRPGYRIVtldg 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 467 -------------EQHLNAERSYKSQISTLHKSVVKMEEELQkvqfEKVSALADLSSTRELcikLDSSKELLNRQLVAKD 533
Cdd:TIGR02168 653 dlvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIA----ELEKALAELRKELEE---LEEELEQLRKELEELS 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 534 QEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDV 613
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL 805
|
650 660 670
....*....|....*....|....*....|....*..
gi 1034616921 614 AQFRNVVTQLEADLDITKRQLGTERFERERAVQELRR 650
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
253-537 |
2.24e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 253 REEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISgmkniiaEMEQASRQCTEALIVCEQDVSRMRRQ 332
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE-------EAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 333 LDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDtnlEVNKLKNILKSEESENRQ 412
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE---AEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 413 MMEQLRKANEDaenwENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEE 492
Cdd:COG1196 388 LLEALRAAAEL----AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1034616921 493 ELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIE 537
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
26-642 |
6.58e-07 |
|
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: 52.76 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 26 LKTTTRDREELKCMLEKYERHLAEIQGNVKVLKSERDKIFLLYEQAQEEITRLRREMMKsckspksttAHAILRRVETER 105
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK---------LTEEYAELKEEL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 106 DVAFTDLRRMTTERDSLRERLKIAQEtafnEKAHLEQRIEELECTVHNLDDE------RMEQMSN-MTLMKETISTVEKE 178
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYRE----KLEKLKREINELKRELDRLQEElqrlseELADLNAaIAGIEAKINELEEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 179 MKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISI 258
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQG 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 259 LGGTLNDLAKEKECLQACLD----KKSENIASLGESLA------MKEKTISGMK----NIIAEMEQASRQCTEA------ 318
Cdd:TIGR02169 523 VHGTVAQLGSVGERYATAIEvaagNRLNNVVVEDDAVAkeaielLKRRKAGRATflplNKMRDERRDLSILSEDgvigfa 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 319 --LIVCEQD--------------VSRMrrqldETNDELAQIAR----ERDIL--------AHDNDNLQEQFAKA-KQENQ 369
Cdd:TIGR02169 603 vdLVEFDPKyepafkyvfgdtlvVEDI-----EAARRLMGKYRmvtlEGELFeksgamtgGSRAPRGGILFSRSePAELQ 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 370 ALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAE 449
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 450 AEGNRLKEKVDSLNR---EVEQHLNA-ERSY-KSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKEL 524
Cdd:TIGR02169 758 SELKELEARIEELEEdlhKLEEALNDlEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 525 LNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALL------VANRDKEY-QSQIALQEKESEIQLLKE 597
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLgdlkkeRDELEAQLrELERKIEELEAQIEKKRK 917
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1034616921 598 HLCLAENKMAIQSRDVAQFRNVVTQL----EADLDITKRQLGTERFERE 642
Cdd:TIGR02169 918 RLSELKAKLEALEEELSEIEDPKGEDeeipEEELSLEDVQAELQRVEEE 966
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
178-451 |
1.48e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 178 EMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEIS 257
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 258 ILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETN 337
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 338 DELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKlkniLKSEESENRQMMEQL 417
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE----LEEEEEALLELLAEL 468
|
250 260 270
....*....|....*....|....*....|....
gi 1034616921 418 RKANEDAENWENKARQSEADNNTLKLELITAEAE 451
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
47-628 |
2.88e-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: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 47 LAEIQGNVKVLKSERDKiFLLYEQAQEEITRLRREMM----KSCKSpKSTTAHAILRRVETERDVAFTDLRRMTTERDSL 122
Cdd:COG1196 195 LGELERQLEPLERQAEK-AERYRELKEELKELEAELLllklRELEA-ELEELEAELEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 123 RERLKIAQ---ETAFNEKAHLEQRIEELEcTVHNLDDERMEQmsnmtlMKETISTVEKEMKSLARKAMDTESELGRQKAE 199
Cdd:COG1196 273 RLELEELElelEEAQAEEYELLAELARLE-QDIARLEERRRE------LEERLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 200 NNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDK 279
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 280 KSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDIL--AHDNDNL 357
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLleAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 358 QEQFAKAKQENQALSKKLNDTHNELNDIK-QKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAEN--WENKARQS 434
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAaYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflPLDKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 435 EADNNTLKLELITAEAEG-NRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTRE 513
Cdd:COG1196 586 AALAAALARGAIGAAVDLvASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 514 LCIKLDSSKELLNRQLV-AKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVANRDKEYQSQIALQEKESEI 592
Cdd:COG1196 666 SRRELLAALLEAEAELEeLAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
570 580 590
....*....|....*....|....*....|....*.
gi 1034616921 593 QLLKEHLCLAENKMAiqsrDVAQFRNVVTQLEADLD 628
Cdd:COG1196 746 ELLEEEALEELPEPP----DLEELERELERLEREIE 777
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
208-437 |
3.48e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 208 ENTEKDLSDTQRHLAKKKYELQLTQEKIMC-------LDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKK 280
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKAllkqlaaLERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 281 SENIASLgeslamkektisgmkniIAEMEQASRQCTEALIVCEQDVSRMRRQLdetnDELAQIARERDILAHDNDNLQEQ 360
Cdd:COG4942 103 KEELAEL-----------------LRALYRLGRQPPLALLLSPEDFLDAVRRL----QYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034616921 361 FAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEAD 437
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
255-556 |
6.35e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 255 EISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVceqdvsRMRRQLD 334
Cdd:TIGR02169 224 EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL------RVKEKIG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 335 ETNDELAQIARERDILAHDNDNLQEQFAKAKQEnqalskkLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESEnrqmM 414
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEERLAKLEAE-------IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE----L 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 415 EQLRkanedaenweNKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEEL 494
Cdd:TIGR02169 367 EDLR----------AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034616921 495 QKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQ 556
Cdd:TIGR02169 437 NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
69-419 |
1.01e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 69 EQAQEEITRLRREMmkSCKSPKSTTAHAILRRVETERDVAFTDLRRMTTERDSLRERLKIAQETAFN---EKAHLEQRIE 145
Cdd:TIGR02169 691 SSLQSELRRIENRL--DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvksELKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 146 ELECTVHNLDD-----ERMEQMSNMTLMKETISTVEKEMKSLARKAMDTESELGRqkaennslrllyentekdlsdtqrh 220
Cdd:TIGR02169 769 ELEEDLHKLEEalndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR------------------------- 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 221 lakKKYELQLtqekimcLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISG 300
Cdd:TIGR02169 824 ---LTLEKEY-------LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 301 MKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARE--RDILAHDNDNLQEQFAKAKQENQALSKKLNDT 378
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPkgEDEEIPEEELSLEDVQAELQRVEEEIRALEPV 973
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1034616921 379 HNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRK 419
Cdd:TIGR02169 974 NMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
323-493 |
1.80e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 323 EQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNI 402
Cdd:COG3883 29 QAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 403 LKSEE---------------SENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEK----VDSLN 463
Cdd:COG3883 109 LGSESfsdfldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEqealLAQLS 188
|
170 180 190
....*....|....*....|....*....|
gi 1034616921 464 REVEQHLNAERSYKSQISTLHKSVVKMEEE 493
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
207-643 |
2.48e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 207 YENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQA---CLDKKSEN 283
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKevkELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 284 IASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSR-------------MRRQLDETNDELAQIARERDIL 350
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkelkekaeeyikLSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 351 AHDNDNLQEQFAKA---KQENQALSKKLNDTHNELNDIKQKVQDTNL------EVNKLKNILKSEESEN-RQMMEQLRKA 420
Cdd:PRK03918 320 EEEINGIEERIKELeekEERLEELKKKLKELEKRLEELEERHELYEEakakkeELERLKKRLTGLTPEKlEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 421 NEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAE--RSYKSQISTLHKSVVKMEEELQKVQ 498
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKEllEEYTAELKRIEKELKEIEEKERKLR 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 499 FEKVSALADLSSTRELCIKLDSSKELLN----------RQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLE 568
Cdd:PRK03918 480 KELRELEKVLKKESELIKLKELAEQLKEleeklkkynlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 569 ALLVANRDKE-------------------------------YQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFR 617
Cdd:PRK03918 560 ELEKKLDELEeelaellkeleelgfesveeleerlkelepfYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETE 639
|
490 500
....*....|....*....|....*.
gi 1034616921 618 NVVTQLEADLDITKRQLGTERFERER 643
Cdd:PRK03918 640 KRLEELRKELEELEKKYSEEEYEELR 665
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
142-564 |
3.90e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 142 QRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHL 221
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 222 AKKKYELQLTQEKIM---CLDEKIDNFTRQNI--------------AQREEISILGGTLNDLAKEKECLQACLDKKSENI 284
Cdd:TIGR04523 197 LKLELLLSNLKKKIQknkSLESQISELKKQNNqlkdniekkqqeinEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 285 ASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIvcEQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKA 364
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKEL--KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNS 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 365 KQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNNTLKLE 444
Cdd:TIGR04523 355 ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 445 LITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKEL 524
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD 514
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1034616921 525 LNRQLvakdQEIEMRENELDSAHSEIELLRSQMANERISM 564
Cdd:TIGR04523 515 LTKKI----SSLKEKIEKLESEKKEKESKISDLEDELNKD 550
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
98-432 |
4.04e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 98 LRRVETERDVAFTDLRRMTTERDSLRERLKIAQEtafnEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEK 177
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQINDLESKIQNQEK----LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 178 EMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEIS 257
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 258 ILGGTLNDLAKEKECLQACLDKKSENI--ASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLdE 335
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI-E 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 336 TNDELAqiarerdilahdnDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMME 415
Cdd:TIGR04523 607 EKEKKI-------------SSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKT 673
|
330
....*....|....*..
gi 1034616921 416 QLRKANEDAENWENKAR 432
Cdd:TIGR04523 674 KIDDIIELMKDWLKELS 690
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
234-440 |
6.96e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 234 KIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISG----MKNIIAEME 309
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreeLGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 310 QASRQCTEALIVCEQD--------VSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNE 381
Cdd:COG3883 97 RSGGSVSYLDVLLGSEsfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034616921 382 LNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNNT 440
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
251-451 |
8.54e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 251 AQREEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMR 330
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 331 RQLDETNDELA-------------------------QIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDI 385
Cdd:COG4942 97 AELEAQKEELAellralyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034616921 386 KQKVQdtnlEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAEAE 451
Cdd:COG4942 177 EALLA----ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
332-535 |
1.07e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 332 QLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKS------ 405
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 406 EESENRQMMEQLRKANEDAE---NWENKARQSEADNNTLKlELITAEAEGNRLKEKVDSLNREVEQHL----NAERSYKS 478
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDfldRLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKaeleAAKAELEA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034616921 479 QISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQE 535
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
33-641 |
1.39e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 33 REELKCMLEKYERHLAEIQgnvkVLKSERDKIfllyeqaQEEITrlrremmksckspksttahailrRVETERDVAFTDL 112
Cdd:PRK02224 236 RDEADEVLEEHEERREELE----TLEAEIEDL-------RETIA-----------------------ETEREREELAEEV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 113 RRMTTERDSLRERLKIAQETAFNEKAH---LEQRIEELECTVHNLDDERMEQmsnmtlmKETISTVEKEMKSLARKAMDT 189
Cdd:PRK02224 282 RDLRERLEELEEERDDLLAEAGLDDADaeaVEARREELEDRDEELRDRLEEC-------RVAAQAHNEEAESLREDADDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 190 ESELGRQKAENNSLrllyentEKDLSDTQRHLAKKKYELQltqekimcldekidnftrqniAQREEISILGGTLNDLAKE 269
Cdd:PRK02224 355 EERAEELREEAAEL-------ESELEEAREAVEDRREEIE---------------------ELEEEIEELRERFGDAPVD 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 270 KECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQ--ASRQCTEalivCEQDV--SRMRRQLDETNDELAQIAR 345
Cdd:PRK02224 407 LGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAllEAGKCPE----CGQPVegSPHVETIEEDRERVEELEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 346 ERDILAHDNDNLQEQFAKAKQenqalskkLNDTHNELNDIKQKVQDtnleVNKLKNILKSEESENRQMMEQLRkanEDAE 425
Cdd:PRK02224 483 ELEDLEEEVEEVEERLERAED--------LVEAEDRIERLEERRED----LEELIAERRETIEEKRERAEELR---ERAA 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 426 NWENKARQSEADNNtlkleliTAEAEGNRLKEKVDSLNREVEQhLNAERSYKSQISTLHKSVVKMEEELQKVQfEKVSAL 505
Cdd:PRK02224 548 ELEAEAEEKREAAA-------EAEEEAEEAREEVAELNSKLAE-LKERIESLERIRTLLAAIADAEDEIERLR-EKREAL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 506 ADLSstrelciklDSSKELLnrqlvakdQEIEMRENELDSAHSE--IELLRSQMANERISMQNLEALLVANRDKEYQSQI 583
Cdd:PRK02224 619 AELN---------DERRERL--------AEKRERKRELEAEFDEarIEEAREDKERAEEYLEQVEEKLDELREERDDLQA 681
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034616921 584 ALQEKESEIQ----LLKEHLCLAENKMAIQS--RDVAQFRNVVTQLEADLditkRQLGTERFER 641
Cdd:PRK02224 682 EIGAVENELEeleeLRERREALENRVEALEAlyDEAEELESMYGDLRAEL----RQRNVETLER 741
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
172-501 |
2.00e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 172 ISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIA 251
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 252 QREEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRR 331
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 332 QLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQdtNLEVNKLKNILKSEESENR 411
Cdd:TIGR04523 490 ELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN--KDDFELKKENLEKEIDEKN 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 412 QMMEQLRKANEdaenwENKARQSEADNNTLKLElitaeaegnrlKEKVDslnreveqhlnaersYKSQISTLHKSVVKME 491
Cdd:TIGR04523 568 KEIEELKQTQK-----SLKKKQEEKQELIDQKE-----------KEKKD---------------LIKEIEEKEKKISSLE 616
|
330
....*....|
gi 1034616921 492 EELQKVQFEK 501
Cdd:TIGR04523 617 KELEKAKKEN 626
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
456-584 |
2.16e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.19 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 456 KEKV-DSLNREVEQ---HLNAERSYKSQistlhksvvkMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVA 531
Cdd:PRK09039 51 KDSAlDRLNSQIAEladLLSLERQGNQD----------LQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGE 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1034616921 532 KDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVA--NRDKEYQSQIA 584
Cdd:PRK09039 121 LAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDAseKRDRESQAKIA 175
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
408-643 |
4.44e-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: 43.21 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 408 SENRQMMEQLRKANEDAENWENKARQSEADnntLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSV 487
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKA---LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 488 VKMEEELQKVqfekVSALADLSSTRELCIKLDS-SKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQN 566
Cdd:COG4942 100 EAQKEELAEL----LRALYRLGRQPPLALLLSPeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034616921 567 LEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERER 643
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
31-652 |
5.60e-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: 43.52 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 31 RDREELKCMLEKYERHLAEIQGNVKVLKSERDKIfLLYEQAQEEitrlRREMMKSCKSPKSTTAHAILRRVETERDVAFT 110
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKA-ERYQALLKE----KREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 111 DLRRMTTERDSLRERLkiaqetafnekAHLEQRIEELECTVHNLDDERMEQM--------SNMTLMKETISTVEKEMKSL 182
Cdd:TIGR02169 252 ELEKLTEEISELEKRL-----------EEIEQLLEELNKKIKDLGEEEQLRVkekigeleAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 183 ARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGT 262
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 263 LNDLAKEKECLQACLDKKSENIASLGESLAMKE----KTISGMKNIIAEMEQASR---QCTEALIVCEQDVSRMRRQLDE 335
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEakinELEEEKEDKALEIKKQEWkleQLAADLSKYEQELYDLKEEYDR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 336 TNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHN---ELNDIKQKVQdTNLEV---NKLKNILKSEESE 409
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGtvaQLGSVGERYA-TAIEVaagNRLNNVVVEDDAV 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 410 NRQMMEQLRKANEDAENW--ENKARQSEADNNTLK--------LELITAE--------------------AEGNRLKEKV 459
Cdd:TIGR02169 560 AKEAIELLKRRKAGRATFlpLNKMRDERRDLSILSedgvigfaVDLVEFDpkyepafkyvfgdtlvvediEAARRLMGKY 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 460 DSLNREVEQH---------LNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLV 530
Cdd:TIGR02169 640 RMVTLEGELFeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 531 AKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHlcLAENKMAIQS 610
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--LSHSRIPEIQ 797
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1034616921 611 RDVAQFRNVVTQLEADLDITKRQLGTERFER---ERAVQELRRQN 652
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKeylEKEIQELQEQR 842
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
331-559 |
7.17e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 331 RQLDETNDELAQIARERDILAHDNDnLQEQFAKAKQEnqalskklndtHNELNDIKQKVQdtnLEVNKLKNILKSEESEN 410
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRE-LAERYAAARER-----------LAELEYLRAALR---LWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 411 RQmmEQLRKANEDAEnwENKARQSEADNNTLKLELITAEAEGNR---LKEKVDSLNREVEQHLNAERSYKSQISTLHKSV 487
Cdd:COG4913 300 LR--AELARLEAELE--RLEARLDALREELDELEAQIRGNGGDRleqLEREIERLERELEERERRRARLEALLAALGLPL 375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034616921 488 VKMEEELQKVQFEKVSALADLSSTRElcikldsskELLNRQLVAKDQEIEMREnELDSAHSEIELLRSQMAN 559
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELE---------ALEEALAEAEAALRDLRR-ELRELEAEIASLERRKSN 437
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
369-571 |
7.68e-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: 42.44 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 369 QALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITA 448
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 449 EAEGNRLKEKVDSLNREVEQH---------LNAERSYKSQ-----ISTLHKSVVKMEEELQKVQFEKVSALADLSSTREl 514
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLgrqpplallLSPEDFLDAVrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERA- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034616921 515 ciKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALL 571
Cdd:COG4942 175 --ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
135-346 |
1.26e-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: 41.67 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 135 NEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDL 214
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 215 SDTQRHLAKKKYELQ-----------LTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSEN 283
Cdd:COG4942 100 EAQKEELAELLRALYrlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034616921 284 IASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARE 346
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
168-470 |
1.35e-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: 42.13 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 168 MKETISTVEKEMKSLARKAMDTESEL-------GRQKAENNSLRLLYENTEKDL---SDTQRHLAKK-----KYELQLTQ 232
Cdd:pfam12128 602 LRERLDKAEEALQSAREKQAAAEEQLvqangelEKASREETFARTALKNARLDLrrlFDEKQSEKDKknkalAERKDSAN 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 233 EKIMCLDEKIDNFTRQNIAQREEISilgGTLNDLAKEK-ECLQACLDKKSENIASLGESLAMKEktiSGMKNIIAEMEQA 311
Cdd:pfam12128 682 ERLNSLEAQLKQLDKKHQAWLEEQK---EQKREARTEKqAYWQVVEGALDAQLALLKAAIAARR---SGAKAELKALETW 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 312 SRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAkakQENQALSKKLNDTHNELNDIKQ---- 387
Cdd:pfam12128 756 YKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWL---QRRPRLATQLSNIERAISELQQqlar 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 388 KVQDTNLEVNKLKNILKSEESENRQMMEQLRKAneDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVE 467
Cdd:pfam12128 833 LIADTKLRRAKLEMERKASEKQQVRLSENLRGL--RCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVK 910
|
...
gi 1034616921 468 QHL 470
Cdd:pfam12128 911 KYV 913
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
33-271 |
1.86e-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: 41.58 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 33 REELKCMLEKYERHLAEIQGNVKVLKSERDKIFLLYEQAQEEITRLRREMmkscKSPKSTTAHAILRRVETERDVAftDL 112
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL----TLLNEEAANLRERLESLERRIA--AT 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 113 RRMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARKAMDTESE 192
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 193 LGRQKAENNSLRLLYENTEKDLSDTQ---------------RHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEIS 257
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQerlseeysltleeaeALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYE 996
|
250
....*....|....
gi 1034616921 258 ILGGTLNDLAKEKE 271
Cdd:TIGR02168 997 ELKERYDFLTAQKE 1010
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
112-374 |
2.01e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.95 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 112 LRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEE---LECTVHNLDDERMEQMSNMTLMKETIS--TVEKEMKSLARKA 186
Cdd:pfam15905 82 IRALVQERGEQDKRLQALEEELEKVEAKLNAAVREktsLSASVASLEKQLLELTRVNELLKAKFSedGTQKKMSSLSMEL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 187 MDTESELgrqKAENNSLRLLYENTEKDLSDTQRHlakkkyeLQLTQEKIMCLDEKIDNFTRQNIAQREEIsilgGTLNDL 266
Cdd:pfam15905 162 MKLRNKL---EAKMKEVMAKQEGMEGKLQVTQKN-------LEHSKGKVAQLEEKLVSTEKEKIEEKSET----EKLLEY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 267 AKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEalivceqDVSRMRRQLDETNDELAQIARE 346
Cdd:pfam15905 228 ITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIK-------DLNEKCKLLESEKEELLREYEE 300
|
250 260
....*....|....*....|....*....
gi 1034616921 347 RDI-LAHDNDNLQEQFAKAKQENQALSKK 374
Cdd:pfam15905 301 KEQtLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
477-651 |
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: 40.90 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 477 KSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQ 556
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 557 MAN-----ERISMQNLEALLV-------ANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRdvaqfRNVVTQLE 624
Cdd:COG4942 106 LAEllralYRLGRQPPLALLLspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE-----RAELEALL 180
|
170 180
....*....|....*....|....*..
gi 1034616921 625 ADLDITKRQLGTERFERERAVQELRRQ 651
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKE 207
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
112-467 |
2.39e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 112 LRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQmsnmtlmketISTVEKEMKSLARKAMDTES 191
Cdd:pfam02463 175 LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE----------YLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 192 ELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKE 271
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 272 CLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILA 351
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 352 HDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKA 431
Cdd:pfam02463 405 KEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE 484
|
330 340 350
....*....|....*....|....*....|....*.
gi 1034616921 432 RQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVE 467
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGV 520
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
124-649 |
2.61e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 124 ERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSlarkAMDTESELGRQKAENnsl 203
Cdd:pfam05483 299 EDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEA----TTCSLEELLRTEQQR--- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 204 rllYENTEKDLSDTQRHLAKKKYELqltqekimcldEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSEN 283
Cdd:pfam05483 372 ---LEKNEDQLKIITMELQKKSSEL-----------EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 284 IASLGESLAMKEKTISGMKNIIAEMEQASRQCTealivceQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAK 363
Cdd:pfam05483 438 EQELIFLLQAREKEIHDLEIQLTAIKTSEEHYL-------KEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASD 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 364 AKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLR-KANEDAENwenkARQSEADNNTLK 442
Cdd:pfam05483 511 MTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKcKLDKSEEN----ARSIEYEVLKKE 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 443 LELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSK 522
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDK 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 523 ELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQnleallvanRDKEYQSQIALQEKESEIQLLKehlcla 602
Cdd:pfam05483 667 KISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALM---------EKHKHQYDKIIEERDSELGLYK------ 731
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1034616921 603 eNKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAVQELR 649
Cdd:pfam05483 732 -NKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
326-649 |
2.98e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 326 VSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKS 405
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 406 EESENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQisTLHK 485
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA--EAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 486 SVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQ 565
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 566 NLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAV 645
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLL 343
|
....
gi 1034616921 646 QELR 649
Cdd:COG4372 344 QLLL 347
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
353-426 |
3.83e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 40.10 E-value: 3.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034616921 353 DNDNLQEQFAKAKQENQALSKKLNDTHNELNDIK-QKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAEN 426
Cdd:TIGR04320 276 ALNTAQAALTSAQTAYAAAQAALATAQKELANAQaQALQTAQNNLATAQAALANAEARLAKAKEALANLNADLAK 350
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
332-592 |
4.24e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 332 QLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENR 411
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 412 QMMEQLRKANEdaenWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKME 491
Cdd:PRK01156 243 ELSSLEDMKNR----YESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNID 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616921 492 EELQKVQfEKVSALADLSSTRELCIKLDSSKELLNRQLvakdQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALL 571
Cdd:PRK01156 319 AEINKYH-AIIKKLSVLQKDYNDYIKKKSRYDDLNNQI----LELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFI 393
|
250 260
....*....|....*....|.
gi 1034616921 572 VANRDKEYQSQIALQEKESEI 592
Cdd:PRK01156 394 SEILKIQEIDPDAIKKELNEI 414
|
|
| |
