|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-595 |
1.44e-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: 75.09 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 263 NEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDL 342
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 343 SD-------TQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSENIASL 415
Cdd:TIGR02168 757 TEleaeieeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 416 GESLAMKEKTISGMKNIIAEMEQASRQCTEALivceqdvSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQE 495
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELI-------EELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 496 NQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQL-RKANEDAENWENKARQSEADNNTLKLELI 574
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRLENKIKELGPVNL 989
|
330 340
....*....|....*....|.
gi 767919985 575 TAEAEGNRLKEKVDSLNREVE 595
Cdd:TIGR02168 990 AAIEEYEELKERYDFLTAQKE 1010
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
178-809 |
1.80e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 74.77 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 178 IQGNVKVLKSE-RDKIFLLYEQAQEEITRLRREmmksckspksttaHAILRRVETERDVAftdlrrMTTERDSLRERLKI 256
Cdd:pfam15921 243 VEDQLEALKSEsQNKIELLLQQHQDRIEQLISE-------------HEVEITGLTEKASS------ARSQANSIQSQLEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 257 AQETAFNEKAHLEQRIEELECTVHNLDDErmeqmsnmtlMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYE 336
Cdd:pfam15921 304 IQEQARNQNSMYMRQLSDLESTVSQLRSE----------LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESG 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 337 NTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEK-------IDNFTRQNIAQREEISILGGTLNDLAKEKE---------- 399
Cdd:pfam15921 374 NLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQgqmerqmaai 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 400 -----------CLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDEL 468
Cdd:pfam15921 454 qgkneslekvsSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQEL 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 469 AQIARERDILAH---DNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKnilksEESENRQMMEQL 545
Cdd:pfam15921 534 QHLKNEGDHLRNvqtECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLE-----KEINDRRLELQE 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 546 RKANEDAEnwENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHK--SVVK------ 617
Cdd:pfam15921 609 FKILKDKK--DAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEdyEVLKrnfrnk 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 618 ---MEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANerismqn 694
Cdd:pfam15921 687 seeMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTN------- 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 695 leallvANRDKEYqsqiaLQEKESEIQLLKEHLCLAENKMA----IQSRDVAQFRNVVTQLEADLDITKRQLG-----TE 765
Cdd:pfam15921 760 ------ANKEKHF-----LKEEKNKLSQELSTVATEKNKMAgeleVLRSQERRLKEKVANMEVALDKASLQFAecqdiIQ 828
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 767919985 766 RFERERA---------VQELRRQNYSSNayhmsSTMKPN-TKCHSPERAHHRSP 809
Cdd:pfam15921 829 RQEQESVrlklqhtldVKELQGPGYTSN-----SSMKPRlLQPASFTRTHSNVP 877
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
383-696 |
1.93e-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: 71.24 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 383 EISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLd 462
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 463 etndelaQIARERDilahdnDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMM 542
Cdd:TIGR02168 305 -------QILRERL------ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 543 EQLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHlnaersyksqistlhksvvkmEEEL 622
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL---------------------LKKL 430
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767919985 623 QKVQFEKVSalADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLE 696
Cdd:TIGR02168 431 EEAELKELQ--AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
238-785 |
3.08e-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: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 238 TDLRRMTTERDSL---RERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLArka 314
Cdd:pfam15921 117 TKLQEMQMERDAMadiRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 315 MDTESELGRQKAENNSLRLL-YENTEKDLSDTQRHLAKK---------KYELQL------TQEKIMCLDEKIDNFTRQNI 378
Cdd:pfam15921 194 VDFEEASGKKIYEHDSMSTMhFRSLGSAISKILRELDTEisylkgrifPVEDQLealkseSQNKIELLLQQHQDRIEQLI 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 379 AQRE-EISILGGTLNDLAKEKECLQACLDKKSENIASLGeslAMKEKTISGMKNIIAEMEQASRqctEALIVCEQDVSRM 457
Cdd:pfam15921 274 SEHEvEITGLTEKASSARSQANSIQSQLEIIQEQARNQN---SMYMRQLSDLESTVSQLRSELR---EAKRMYEDKIEEL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 458 RRQLDETNDELAQIARERDILAHDNDNLQEQFAK------AKQENQALSKKLN------DTHNEL--NDIKQKVQDTNLE 523
Cdd:pfam15921 348 EKQLVLANSELTEARTERDQFSQESGNLDDQLQKlladlhKREKELSLEKEQNkrlwdrDTGNSItiDHLRRELDDRNME 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 524 VNKLKNILKSEESENRQMMEQ----LRKANEDAENWENKARQSEADNNTLK--LELITAEAEGNRLKEK-VDSLNREVEQ 596
Cdd:pfam15921 428 VQRLEALLKAMKSECQGQMERqmaaIQGKNESLEKVSSLTAQLESTKEMLRkvVEELTAKKMTLESSERtVSDLTASLQE 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 597 HLNAERSYKSQISTLHKSVVKMEEELQKVQFEK---VSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDS 673
Cdd:pfam15921 508 KERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGA 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 674 AHSEIELLRSQMANERISMQNLEALlvanRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQ---------- 743
Cdd:pfam15921 588 MQVEKAQLEKEINDRRLELQEFKIL----KDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQerdqllnevk 663
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 767919985 744 -FRNVVTQLEADLDITKRQLGTERFERERAVQELRRQNYSSNA 785
Cdd:pfam15921 664 tSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQS 706
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
230-530 |
9.47e-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: 68.93 E-value: 9.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 230 ETERDVAFTDLRRMTTERDSLR---ERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKE 306
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 307 MKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISI 386
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 387 LGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKtisgmkniiaEMEQASRQCTEAlivcEQDVSRMRRQLDETND 466
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNERASLEEALALLRS----------ELEELSEELREL----ESKRSELRRELEELRE 922
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767919985 467 ELAQIARERDILAHDNDNLQEQFA-KAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNI 530
Cdd:TIGR02168 923 KLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPV 987
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
152-780 |
6.22e-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: 66.23 E-value: 6.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 152 ELLKTTTRDREELKCMLEKYERHLAEIQGNVKVLKSERDKIFLLYEQAQEEITRLRREMMKSCKSPKSTT-----AHAIL 226
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLErqleeLEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 227 RRVETERDVAFTDLRRMTTERDSLR---ERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTV 303
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKeelESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 304 EKEMKSLAR-------------------KAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIM 364
Cdd:TIGR02168 406 EARLERLEDrrerlqqeieellkkleeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 365 CLDEKID-------------NFTRQNIAQREEISILGGTLNDLAKEKECLQACLDK-----------KSENIA------- 413
Cdd:TIGR02168 486 QLQARLDslerlqenlegfsEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAalggrlqavvvENLNAAkkaiafl 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 414 ---SLGESLAMKEKTISGMKNIIAEMEQASRQ--CTEALIVCEQDVSRMRR-------------QLDETNDELAQIARER 475
Cdd:TIGR02168 566 kqnELGRVTFLPLDSIKGTEIQGNDREILKNIegFLGVAKDLVKFDPKLRKalsyllggvlvvdDLDNALELAKKLRPGY 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 476 DILAHDNDNLQEQFAKAKQENQALSKKLNdTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAEnw 555
Cdd:TIGR02168 646 RIVTLDGDLVRPGGVITGGSAKTNSSILE-RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-- 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 556 enkarQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSALAD 635
Cdd:TIGR02168 723 -----ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 636 LSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVANRDKEYQSQIALQE 715
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767919985 716 KESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAVQELRRQN 780
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
458-725 |
6.58e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 6.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 458 RRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQkvqdtnlEVNKLKNILKSEESE 537
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA-------ELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 538 NRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVK 617
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 618 MEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEA 697
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260
....*....|....*....|....*...
gi 767919985 698 LLVANRDKEYQSQIALQEKESEIQLLKE 725
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
408-735 |
1.43e-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: 62.00 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 408 KSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQE 487
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 488 QFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNN 567
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 568 TLKLELITAEAEGNRLKEKVDSLNREVEQhlnaersyksqistLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLD 647
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEE--------------LEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 648 SSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANerismqNLEALLVANRDkEYQSQIALQEK-ESEIQLLKEH 726
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN------LQERLSEEYSL-TLEEAEALENKiEDDEEEARRR 973
|
....*....
gi 767919985 727 LCLAENKMA 735
Cdd:TIGR02168 974 LKRLENKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
458-777 |
3.25e-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: 60.84 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 458 RRQLDETNDELAQIArerDILAHDN---DNLQEQfAKAKQENQALSKKLNDTHNELndIKQKVQDTNLEVNKLKNILKSE 534
Cdd:TIGR02168 178 ERKLERTRENLDRLE---DILNELErqlKSLERQ-AEKAERYKELKAELRELELAL--LVLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 535 ESENRQMMEQLRKANEDAEnwENKARQSEADN--NTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLH 612
Cdd:TIGR02168 252 EEELEELTAELQELEEKLE--ELRLEVSELEEeiEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 613 KSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISM 692
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 693 QNLEallvANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRdVAQFRNVVTQLEAdLDITKRQLGTERFERERA 772
Cdd:TIGR02168 410 ERLE----DRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL-QEELERLEEALEE-LREELEEAEQALDAAERE 483
|
....*
gi 767919985 773 VQELR 777
Cdd:TIGR02168 484 LAQLQ 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
544-779 |
5.18e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 5.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 544 QLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQ 623
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 624 kvqfekvSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVANR 703
Cdd:COG1196 313 -------ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767919985 704 DKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAVQELRRQ 779
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
306-635 |
2.06e-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: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 306 EMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEIS 385
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 386 ILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMkektiSGMKNIIAEMEQAsrqctealivcEQDVSRMRRQLDETN 465
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSH-----SRIPEIQAELSKL-----------EEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 466 DELAQIARERDILAHDNDNLQEQfakakqenqalskkLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQL 545
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQ--------------RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 546 RKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSqISTLHKSVVKMEEELQKV 625
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE-IPEEELSLEDVQAELQRV 963
|
330
....*....|
gi 767919985 626 QfEKVSALAD 635
Cdd:TIGR02169 964 E-EEIRALEP 972
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
163-778 |
2.75e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 163 ELKCMLEKYERHLAEIQgnVKVLKSERDKIFLLYEQAQEEITRLRREMmksckspksttahailrrveTERDVAFTDLRR 242
Cdd:TIGR02168 217 ELKAELRELELALLVLR--LEELREELEELQEELKEAEEELEELTAEL--------------------QELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 243 MTTERDSLRERLKIAQETAFNEKAHLEQRIEELectvhnldDERMEQmsnmtlmketistVEKEMKSLARKAMDTESELG 322
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQIL--------RERLAN-------------LERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 323 RQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQ 402
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 403 ACLDKKSENIASLGESLAMKEK-----TISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDI 477
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAELkelqaELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 478 LAHDNDNLQEQFAKAKQENQALSkKLNDTHNELNDI------------------KQKVQDTNLE-VNKLKNILKSEESEN 538
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQS-GLSGILGVLSELisvdegyeaaieaalggrLQAVVVENLNaAKKAIAFLKQNELGR 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 539 RQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAE--------------------AEGNRLKEKVDSLNREV---- 594
Cdd:TIGR02168 573 VTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDpklrkalsyllggvlvvddlDNALELAKKLRPGYRIVtldg 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 595 -------------EQHLNAERSYKSQISTLHKSVVKMEEELQkvqfEKVSALADLSSTRELcikLDSSKELLNRQLVAKD 661
Cdd:TIGR02168 653 dlvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIA----ELEKALAELRKELEE---LEEELEQLRKELEELS 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 662 QEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDV 741
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL 805
|
650 660 670
....*....|....*....|....*....|....*..
gi 767919985 742 AQFRNVVTQLEADLDITKRQLGTERFERERAVQELRR 778
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
154-725 |
3.52e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 154 LKTTTRDREELKCMLEKYERHLAEIQGNVKVLKSERDKIFLLYEQAQEEITRLRREmmksckspksttahaiLRRVETER 233
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE----------------LARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 234 DVAFTDLRRMTTERDSLRERLKIAQEtafnEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARK 313
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEE----ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 314 AMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLND 393
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 394 LAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEA-LIVCEQDVSRMRRQLDETNDELAQIA 472
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAlLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 473 RERDILAHDNDNLQEQFAKAKQENQALSKKLNdthnelndikqkvQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDA 552
Cdd:COG1196 541 EAALAAALQNIVVEDDEVAAAAIEYLKAAKAG-------------RATFLPLDKIRARAALAAALARGAIGAAVDLVASD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 553 ENWENKARQSEADnnTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSA 632
Cdd:COG1196 608 LREADARYYVLGD--TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 633 LADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVANRDKEYQsqia 712
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD---- 761
|
570
....*....|...
gi 767919985 713 LQEKESEIQLLKE 725
Cdd:COG1196 762 LEELERELERLER 774
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
75-770 |
8.08e-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: 56.23 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 75 NNIIVLEDTIKRLKSIILDTEKAQNKSPSRLDSFVKTLEADKDHYKSEAQHLRKMMRSRSKSPRRPsptargancdvelL 154
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEK-------------I 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 155 KTTTRDREELKCMLEKYERHLAEIQGNVKVLKSERDKIFLLYEQAQEEITRLRREMMKsckspksttAHAILRRVETERD 234
Cdd:TIGR02169 297 GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK---------LTEEYAELKEELE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 235 VAFTDLRRMTTERDSLRERLKIAQEtafnEKAHLEQRIEELECTVHNLDDE------RMEQMSN-MTLMKETISTVEKEM 307
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDELKDYRE----KLEKLKREINELKRELDRLQEElqrlseELADLNAaIAGIEAKINELEEEK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 308 KSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISIL 387
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGV 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 388 GGTLNDLAKEKECLQACLD----KKSENIASLGESLA------MKEKTISGMK----NIIAEMEQASRQCTEA------- 446
Cdd:TIGR02169 524 HGTVAQLGSVGERYATAIEvaagNRLNNVVVEDDAVAkeaielLKRRKAGRATflplNKMRDERRDLSILSEDgvigfav 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 447 -LIVCEQD--------------VSRMrrqldETNDELAQIAR----ERDIL--------AHDNDNLQEQFAKA-KQENQA 498
Cdd:TIGR02169 604 dLVEFDPKyepafkyvfgdtlvVEDI-----EAARRLMGKYRmvtlEGELFeksgamtgGSRAPRGGILFSRSePAELQR 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 499 LSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAEA 578
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 579 EGNRLKEKVDSLNR---EVEQHLNA-ERSY-KSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELL 653
Cdd:TIGR02169 759 ELKELEARIEELEEdlhKLEEALNDlEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 654 NRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALL------VANRDKEY-QSQIALQEKESEIQLLKEH 726
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLgdlkkeRDELEAQLrELERKIEELEAQIEKKRKR 918
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 767919985 727 LCLAENKMAIQSRDVAQFRNVVTQL----EADLDITKRQLGTERFERE 770
Cdd:TIGR02169 919 LSELKAKLEALEEELSEIEDPKGEDeeipEEELSLEDVQAELQRVEEE 966
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
381-665 |
9.95e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 9.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 381 REEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISgmkniiaEMEQASRQCTEALIVCEQDVSRMRRQ 460
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE-------EAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 461 LDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDtnlEVNKLKNILKSEESENRQ 540
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE---AEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 541 MMEQLRKANEDaenwENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEE 620
Cdd:COG1196 388 LLEALRAAAEL----AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 767919985 621 ELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIE 665
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
66-625 |
7.47e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.72 E-value: 7.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 66 LQIDLICQQNNIIVLEDTIKRLKSII------LDTEKAQ----NKSPSRLDSFVKTLEADKDHYKSEAQHLRKMMRSRSK 135
Cdd:TIGR04523 59 LDKNLNKDEEKINNSNNKIKILEQQIkdlndkLKKNKDKinklNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 136 SPRRPSPTARGANCDVELL----KTTTRDREELKCMLEKYERHLAEIQGNVKVLKSERDKIFLLY---EQAQEEITRLRR 208
Cdd:TIGR04523 139 NIDKFLTEIKKKEKELEKLnnkyNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlKKKIQKNKSLES 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 209 EMMKSCKSPKSTTAHAILRRVE-----TERDVAFTDLRRMTTERDSLRERLKIAQ---ETAFNEKAHLEQRIEELECTVH 280
Cdd:TIGR04523 219 QISELKKQNNQLKDNIEKKQQEinektTEISNTQTQLNQLKDEQNKIKKQLSEKQkelEQNNKKIKELEKQLNQLKSEIS 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 281 NLDDERMEQMSN------------MTLMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRH 348
Cdd:TIGR04523 299 DLNNQKEQDWNKelkselknqekkLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 349 LAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISG 428
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 429 MKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHN 508
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 509 ELNDIKQKVQdtNLEVNKLKNILKSEESENRQMMEQLRKANEDAEN----WENKARQSEADNNTLKLELITAEAEGNRLK 584
Cdd:TIGR04523 539 KISDLEDELN--KDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKkqeeKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 767919985 585 EKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKV 625
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEI 657
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
175-756 |
8.15e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 8.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 175 LAEIQGNVKVLKSERDKiFLLYEQAQEEITRLRREMM----KSCKSpKSTTAHAILRRVETERDVAFTDLRRMTTERDSL 250
Cdd:COG1196 195 LGELERQLEPLERQAEK-AERYRELKEELKELEAELLllklRELEA-ELEELEAELEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 251 RERLKIAQEtAFNEK----AHLEQRIEELEcTVHNLDDERMEQmsnmtlMKETISTVEKEMKSLARKAMDTESELGRQKA 326
Cdd:COG1196 273 RLELEELEL-ELEEAqaeeYELLAELARLE-QDIARLEERRRE------LEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 327 ENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLD 406
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 407 KKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDIL--AHDNDN 484
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLleAEADYE 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 485 LQEQFAKAKQENQALSKKLNDTHNELNDIK-QKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAEN--WENKARQ 561
Cdd:COG1196 505 GFLEGVKAALLLAGLRGLAGAVAVLIGVEAaYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflPLDKIRA 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 562 SEADNNTLKLELITAEAEG-NRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTR 640
Cdd:COG1196 585 RAALAAALARGAIGAAVDLvASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 641 ELCIKLDSSKELLNRQLV-AKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVANRDKEYQSQIALQEKESE 719
Cdd:COG1196 665 GSRRELLAALLEAEAELEeLAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
570 580 590
....*....|....*....|....*....|....*..
gi 767919985 720 IQLLKEHLCLAENKMAiqsrDVAQFRNVVTQLEADLD 756
Cdd:COG1196 745 EELLEEEALEELPEPP----DLEELERELERLEREIE 777
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
336-565 |
2.43e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 336 ENTEKDLSDTQRHLAKKKYELQLTQEKIMC-------LDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKK 408
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKAllkqlaaLERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 409 SENIASLgeslamkektisgmkniIAEMEQASRQCTEALIVCEQDVSRMRRQLdetnDELAQIARERDILAHDNDNLQEQ 488
Cdd:COG4942 103 KEELAEL-----------------LRALYRLGRQPPLALLLSPEDFLDAVRRL----QYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767919985 489 FAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEAD 565
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
383-684 |
2.97e-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: 51.22 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 383 EISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVceqdvsRMRRQLD 462
Cdd:TIGR02169 224 EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL------RVKEKIG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 463 ETNDELAQIARERDILAHDNDNLQEQFAKAKQEnqalskkLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESEnrqmM 542
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEERLAKLEAE-------IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE----L 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 543 EQLRkanedaenweNKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEEL 622
Cdd:TIGR02169 367 EDLR----------AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767919985 623 QKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQ 684
Cdd:TIGR02169 437 NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-547 |
4.39e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 197 EQAQEEITRLRREMmkSCKSPKSTTAHAILRRVETERDVAFTDLRRMTTERDSLRERLKIAQETAFN---EKAHLEQRIE 273
Cdd:TIGR02169 691 SSLQSELRRIENRL--DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENvksELKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 274 ELECTVHNLDD-----ERMEQMSNMTLMKETISTVEKEMKSLARKAMDTESELGRqkaennslrllyentekdlsdtqrh 348
Cdd:TIGR02169 769 ELEEDLHKLEEalndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR------------------------- 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 349 lakKKYELQLtqekimcLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISG 428
Cdd:TIGR02169 824 ---LTLEKEY-------LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 429 MKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARE--RDILAHDNDNLQEQFAKAKQENQALSKKLNDT 506
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPkgEDEEIPEEELSLEDVQAELQRVEEEIRALEPV 973
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 767919985 507 HNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRK 547
Cdd:TIGR02169 974 NMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
161-769 |
1.05e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 161 REELKCMLEKYERHLAEIQgnvkVLKSERDKIfllyeqaQEEITrlrremmksckspksttahailrRVETERDVAFTDL 240
Cdd:PRK02224 236 RDEADEVLEEHEERREELE----TLEAEIEDL-------RETIA-----------------------ETEREREELAEEV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 241 RRMTTERDSLRERLKIAQETAFNEKAH---LEQRIEELECTVHNLDDERMEQmsnmtlmKETISTVEKEMKSLARKAMDT 317
Cdd:PRK02224 282 RDLRERLEELEEERDDLLAEAGLDDADaeaVEARREELEDRDEELRDRLEEC-------RVAAQAHNEEAESLREDADDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 318 ESELGRQKAENNSLrllyentEKDLSDTQRHLAKKKYELQltqekimcldekidnftrqniAQREEISILGGTLNDLAKE 397
Cdd:PRK02224 355 EERAEELREEAAEL-------ESELEEAREAVEDRREEIE---------------------ELEEEIEELRERFGDAPVD 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 398 KECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQ--ASRQCTEalivCEQDV--SRMRRQLDETNDELAQIAR 473
Cdd:PRK02224 407 LGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAllEAGKCPE----CGQPVegSPHVETIEEDRERVEELEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 474 ERDILAHDNDNLQEQFAKAKQenqalskkLNDTHNELNDIKQKVQDtnleVNKLKNILKSEESENRQMMEQLRkanEDAE 553
Cdd:PRK02224 483 ELEDLEEEVEEVEERLERAED--------LVEAEDRIERLEERRED----LEELIAERRETIEEKRERAEELR---ERAA 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 554 NWENKARQSEADNNtlkleliTAEAEGNRLKEKVDSLNREVEQhLNAERSYKSQISTLHKSVVKMEEELQKVQfEKVSAL 633
Cdd:PRK02224 548 ELEAEAEEKREAAA-------EAEEEAEEAREEVAELNSKLAE-LKERIESLERIRTLLAAIADAEDEIERLR-EKREAL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 634 ADLSstrelciklDSSKELLnrqlvakdQEIEMRENELDSAHSE--IELLRSQMANERISMQNLEALLVANRDKEYQSQI 711
Cdd:PRK02224 619 AELN---------DERRERL--------AEKRERKRELEAEFDEarIEEAREDKERAEEYLEQVEEKLDELREERDDLQA 681
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767919985 712 ALQEKESEIQ----LLKEHLCLAENKMAIQS--RDVAQFRNVVTQLEADLditkRQLGTERFER 769
Cdd:PRK02224 682 EIGAVENELEeleeLRERREALENRVEALEAlyDEAEELESMYGDLRAEL----RQRNVETLER 741
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
270-692 |
1.55e-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: 48.48 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 270 QRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHL 349
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 350 AKKKYELQLTQEKImcldEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSENIASLGESlamKEKTISGM 429
Cdd:TIGR04523 197 LKLELLLSNLKKKI----QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE---QNKIKKQL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 430 KNIIAEMEQASRQCTEAlivcEQDVSRMRRQLDETN------------DELAQIARERDILAHDNDNLQEQFAKAKQENQ 497
Cdd:TIGR04523 270 SEKQKELEQNNKKIKEL----EKQLNQLKSEISDLNnqkeqdwnkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQIS 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 498 ALSKKLNDTHN-------ELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNNT-- 568
Cdd:TIGR04523 346 QLKKELTNSESensekqrELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELle 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 569 -----LKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELC 643
Cdd:TIGR04523 426 keierLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 767919985 644 IKLDSSKELLNRQLvakdQEIEMRENELDSAHSEIELLRSQMANERISM 692
Cdd:TIGR04523 506 KELEEKVKDLTKKI----SSLKEKIEKLESEKKEKESKISDLEDELNKD 550
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
226-560 |
1.69e-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: 48.48 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 226 LRRVETERDVAFTDLRRMTTERDSLRERLKIAQEtafnEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEK 305
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQINDLESKIQNQEK----LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 306 EMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEIS 385
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 386 ILGGTLNDLAKEKECLQACLDKKSENI--ASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLdE 463
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI-E 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 464 TNDELAqiarerdilahdnDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMME 543
Cdd:TIGR04523 607 EKEKKI-------------SSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKT 673
|
330
....*....|....*..
gi 767919985 544 QLRKANEDAENWENKAR 560
Cdd:TIGR04523 674 KIDDIIELMKDWLKELS 690
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
451-621 |
1.84e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 451 EQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNI 530
Cdd:COG3883 29 QAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 531 LKSEE---------------SENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEK----VDSLN 591
Cdd:COG3883 109 LGSESfsdfldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEqealLAQLS 188
|
170 180 190
....*....|....*....|....*....|
gi 767919985 592 REVEQHLNAERSYKSQISTLHKSVVKMEEE 621
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
379-579 |
6.77e-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: 45.91 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 379 AQREEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMR 458
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 459 RQLDETNDELA-------------------------QIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDI 513
Cdd:COG4942 97 AELEAQKEELAellralyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767919985 514 KQKVQdtnlEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAEAE 579
Cdd:COG4942 177 EALLA----ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
252-771 |
6.96e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 252 ERLKIAQETAFNEKAHLEQRIEELEctvhnlddERMEQMSNMtlmKETISTVEKEMKSLARKAMDTESELGRQKAENNSL 331
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLE--------KFIKRTENI---EELIKEKEKELEEVLREINEISSELPELREELEKL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 332 RLLYENTEKdlsdTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDL------AKEKECLQACL 405
Cdd:PRK03918 227 EKEVKELEE----LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELkelkekAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 406 DKKSENIASLGESLAMKEKTISGMKNIIAEMEQasrqctealivceqdvsrMRRQLDETNDELAQIARERDILAHDNDNL 485
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEE------------------KEERLEELKKKLKELEKRLEELEERHELY 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 486 QEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANE--------------- 550
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEelkkakgkcpvcgre 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 551 -DAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVdslnREVEQHLNAERSYKSQISTLhKSVVKMEEELQKVQFEK 629
Cdd:PRK03918 445 lTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKEL----RELEKVLKKESELIKLKELA-EQLKELEEKLKKYNLEE 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 630 VSALA-DLSSTRELCIKLDSSKELLNRQLvAKDQEIEMR----ENELDSAHSEIELLRSQMANERISMQNLEALLVANRD 704
Cdd:PRK03918 520 LEKKAeEYEKLKEKLIKLKGEIKSLKKEL-EKLEELKKKlaelEKKLDELEEELAELLKELEELGFESVEELEERLKELE 598
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767919985 705 KEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERER 771
Cdd:PRK03918 599 PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR 665
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
362-568 |
7.50e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 362 KIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISG----MKNIIAEME 437
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreeLGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 438 QASRQCTEALIVCEQD--------VSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNE 509
Cdd:COG3883 97 RSGGSVSYLDVLLGSEsfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767919985 510 LNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNNT 568
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
460-663 |
1.08e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 460 QLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKS------ 533
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 534 EESENRQMMEQLRKANEDAE---NWENKARQSEADNNTLKlELITAEAEGNRLKEKVDSLNREVEQHL----NAERSYKS 606
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDfldRLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKaeleAAKAELEA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767919985 607 QISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQE 663
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
159-780 |
1.28e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 159 RDREELKCMLEKYERHLAEIQGNVKVLKSERDKIfLLYEQAQEEitrlRREMMKSCKSPKSTTAHAILRRVETERDVAFT 238
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKA-ERYQALLKE----KREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 239 DLRRMTTERDSLRERLkiaqetafnekAHLEQRIEELECTVHNLDDERMEQM--------SNMTLMKETISTVEKEMKSL 310
Cdd:TIGR02169 252 ELEKLTEEISELEKRL-----------EEIEQLLEELNKKIKDLGEEEQLRVkekigeleAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 311 ARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGT 390
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 391 LNDLAKEKECLQACLDKKSENIASLGESLAMKE----KTISGMKNIIAEMEQASR---QCTEALIVCEQDVSRMRRQLDE 463
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEakinELEEEKEDKALEIKKQEWkleQLAADLSKYEQELYDLKEEYDR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 464 TNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHN---ELNDIKQKVQdTNLEV---NKLKNILKSEESE 537
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGtvaQLGSVGERYA-TAIEVaagNRLNNVVVEDDAV 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 538 NRQMMEQLRKANEDAENW--ENKARQSEADNNTLK--------LELITAE--------------------AEGNRLKEKV 587
Cdd:TIGR02169 560 AKEAIELLKRRKAGRATFlpLNKMRDERRDLSILSedgvigfaVDLVEFDpkyepafkyvfgdtlvvediEAARRLMGKY 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 588 DSLNREVEQH---------LNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLV 658
Cdd:TIGR02169 640 RMVTLEGELFeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 659 AKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHlcLAENKMAIQS 738
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--LSHSRIPEIQ 797
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 767919985 739 RDVAQFRNVVTQLEADLDITKRQLGTERFER---ERAVQELRRQN 780
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKeylEKEIQELQEQR 842
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
584-712 |
2.00e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.57 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 584 KEKV-DSLNREVEQ---HLNAERSYKSQistlhksvvkMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVA 659
Cdd:PRK09039 51 KDSAlDRLNSQIAEladLLSLERQGNQD----------LQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGE 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 767919985 660 KDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVA--NRDKEYQSQIA 712
Cdd:PRK09039 121 LAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDAseKRDRESQAKIA 175
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
536-771 |
3.57e-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: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 536 SENRQMMEQLRKANEDAENWENKARQSEADnntLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSV 615
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKA---LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 616 VKMEEELQKVqfekVSALADLSSTRELCIKLDS-SKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQN 694
Cdd:COG4942 100 EAQKEELAEL----LRALYRLGRQPPLALLLSPeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767919985 695 LEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERER 771
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
459-687 |
4.35e-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: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 459 RQLDETNDELAQIARERDILAHDNDnLQEQFAKAKQEnqalskklndtHNELNDIKQKVQdtnLEVNKLKNILKSEESEN 538
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRE-LAERYAAARER-----------LAELEYLRAALR---LWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 539 RQmmEQLRKANEDAEnwENKARQSEADNNTLKLELITAEAEGNR---LKEKVDSLNREVEQHLNAERSYKSQISTLHKSV 615
Cdd:COG4913 300 LR--AELARLEAELE--RLEARLDALREELDELEAQIRGNGGDRleqLEREIERLERELEERERRRARLEALLAALGLPL 375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767919985 616 VKMEEELQKVQFEKVSALADLSSTRElcikldsskELLNRQLVAKDQEIEMREnELDSAHSEIELLRSQMAN 687
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELE---------ALEEALAEAEAALRDLRR-ELRELEAEIASLERRKSN 437
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
252-777 |
5.06e-04 |
|
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: 43.56 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 252 ERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSlarkAMDTESELGRQKAENnsl 331
Cdd:pfam05483 299 EDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEA----TTCSLEELLRTEQQR--- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 332 rllYENTEKDLSDTQRHLAKKKYELqltqekimcldEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSEN 411
Cdd:pfam05483 372 ---LEKNEDQLKIITMELQKKSSEL-----------EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 412 IASLGESLAMKEKTISGMKNIIAEMEQASRQCTealivceQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAK 491
Cdd:pfam05483 438 EQELIFLLQAREKEIHDLEIQLTAIKTSEEHYL-------KEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASD 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 492 AKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLR-KANEDAENwenkARQSEADNNTLK 570
Cdd:pfam05483 511 MTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKcKLDKSEEN----ARSIEYEVLKKE 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 571 LELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSK 650
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDK 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 651 ELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQnleallvanRDKEYQSQIALQEKESEIQLLKehlcla 730
Cdd:pfam05483 667 KISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALM---------EKHKHQYDKIIEERDSELGLYK------ 731
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 767919985 731 eNKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAVQELR 777
Cdd:pfam05483 732 -NKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
497-699 |
6.08e-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: 42.83 E-value: 6.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 497 QALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITA 576
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 577 EAEGNRLKEKVDSLNREVEQH---------LNAERSYKSQ-----ISTLHKSVVKMEEELQKVQFEKVSALADLSSTREl 642
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLgrqpplallLSPEDFLDAVrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERA- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767919985 643 ciKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALL 699
Cdd:COG4942 175 --ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
296-598 |
6.31e-04 |
|
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: 43.67 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 296 MKETISTVEKEMKSLARKAMDTESELG-------RQKAENNSLRLLYENTEKDL---SDTQRHLAKK-----KYELQLTQ 360
Cdd:pfam12128 602 LRERLDKAEEALQSAREKQAAAEEQLVqangeleKASREETFARTALKNARLDLrrlFDEKQSEKDKknkalAERKDSAN 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 361 EKIMCLDEKIDNFTRQNIAQREEISilgGTLNDLAKEK-ECLQACLDKKSENIASLGESLAMKEktiSGMKNIIAEMEQA 439
Cdd:pfam12128 682 ERLNSLEAQLKQLDKKHQAWLEEQK---EQKREARTEKqAYWQVVEGALDAQLALLKAAIAARR---SGAKAELKALETW 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 440 SRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAkakQENQALSKKLNDTHNELNDIKQ---- 515
Cdd:pfam12128 756 YKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWL---QRRPRLATQLSNIERAISELQQqlar 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 516 KVQDTNLEVNKLKNILKSEESENRQMMEQLRKAnedaenwenKARQS-------EADNNTLKLELITAEAEGNRLKEKVD 588
Cdd:pfam12128 833 LIADTKLRRAKLEMERKASEKQQVRLSENLRGL---------RCEMSklatlkeDANSEQAQGSIGERLAQLEDLKLKRD 903
|
330
....*....|
gi 767919985 589 SLNREVEQHL 598
Cdd:pfam12128 904 YLSESVKKYV 913
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
240-502 |
6.82e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.88 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 240 LRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEE---LECTVHNLDDERMEQMSNMTLMKETIS--TVEKEMKSLARKA 314
Cdd:pfam15905 82 IRALVQERGEQDKRLQALEEELEKVEAKLNAAVREktsLSASVASLEKQLLELTRVNELLKAKFSedGTQKKMSSLSMEL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 315 MDTESELgrqKAENNSLRLLYENTEKDLSDTQRHlakkkyeLQLTQEKIMCLDEKIDNFTRQNIAQREEIsilgGTLNDL 394
Cdd:pfam15905 162 MKLRNKL---EAKMKEVMAKQEGMEGKLQVTQKN-------LEHSKGKVAQLEEKLVSTEKEKIEEKSET----EKLLEY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 395 AKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEalivceqDVSRMRRQLDETNDELAQIARE 474
Cdd:pfam15905 228 ITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIK-------DLNEKCKLLESEKEELLREYEE 300
|
250 260
....*....|....*....|....*....
gi 767919985 475 RDI-LAHDNDNLQEQFAKAKQENQALSKK 502
Cdd:pfam15905 301 KEQtLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
240-595 |
9.94e-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: 43.04 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 240 LRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQmsnmtlmketISTVEKEMKSLARKAMDTES 319
Cdd:pfam02463 175 LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE----------YLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 320 ELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKE 399
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 400 CLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILA 479
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 480 HDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKA 559
Cdd:pfam02463 405 KEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE 484
|
330 340 350
....*....|....*....|....*....|....*.
gi 767919985 560 RQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVE 595
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGV 520
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
263-474 |
1.19e-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: 42.06 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 263 NEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDL 342
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 343 SDTQRHLAKKKYELQ-----------LTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSEN 411
Cdd:COG4942 100 EAQKEELAELLRALYrlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767919985 412 IASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARE 474
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
605-779 |
1.95e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 605 KSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQ 684
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 685 MAN-----ERISMQNLEALLV-------ANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRdvaqfRNVVTQLE 752
Cdd:COG4942 106 LAEllralYRLGRQPPLALLLspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE-----RAELEALL 180
|
170 180
....*....|....*....|....*..
gi 767919985 753 ADLDITKRQLGTERFERERAVQELRRQ 779
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKE 207
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
460-720 |
3.27e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 460 QLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENR 539
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 540 QMMEQLRKANEdaenWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKME 619
Cdd:PRK01156 243 ELSSLEDMKNR----YESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNID 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 620 EELQKVQfEKVSALADLSSTRELCIKLDSSKELLNRQLvakdQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALL 699
Cdd:PRK01156 319 AEINKYH-AIIKKLSVLQKDYNDYIKKKSRYDDLNNQI----LELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFI 393
|
250 260
....*....|....*....|.
gi 767919985 700 VANRDKEYQSQIALQEKESEI 720
Cdd:PRK01156 394 SEILKIQEIDPDAIKKELNEI 414
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
454-777 |
3.67e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 454 VSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKS 533
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 534 EESENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQisTLHK 613
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA--EAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 614 SVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQ 693
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 694 NLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAV 773
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLL 343
|
....
gi 767919985 774 QELR 777
Cdd:COG4372 344 QLLL 347
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
481-554 |
4.42e-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: 4.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767919985 481 DNDNLQEQFAKAKQENQALSKKLNDTHNELNDIK-QKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAEN 554
Cdd:TIGR04320 276 ALNTAQAALTSAQTAYAAAQAALATAQKELANAQaQALQTAQNNLATAQAALANAEARLAKAKEALANLNADLAK 350
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
239-658 |
5.61e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 239 DLRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARKAMD-T 317
Cdd:TIGR00606 713 STESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDvT 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 318 ESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKE 397
Cdd:TIGR00606 793 IMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 398 KECLqacldkkSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDI 477
Cdd:TIGR00606 873 KLQI-------GTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVND 945
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 478 LAHDNDNLQ------EQFAKAKQENQALSKK--LNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKAN 549
Cdd:TIGR00606 946 IKEKVKNIHgymkdiENKIQDGKDDYLKQKEteLNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRK 1025
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 550 EDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVvkMEEELQKVQFEK 629
Cdd:TIGR00606 1026 RENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL--REPQFRDAEEKY 1103
|
410 420
....*....|....*....|....*....
gi 767919985 630 VSALADLSSTRELCIKLDSSKELLNRQLV 658
Cdd:TIGR00606 1104 REMMIVMRTTELVNKDLDIYYKTLDQAIM 1132
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
563-780 |
6.82e-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: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 563 EADNNTLKLELITAEaegnrLKEKVDSLNREVEQhlnAER--SYKSQISTLHKSVVKME-----EELQKVQFEKVSALAD 635
Cdd:TIGR02168 183 RTRENLDRLEDILNE-----LERQLKSLERQAEK---AERykELKAELRELELALLVLRleelrEELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 636 LSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVANRDKEYQSQIALQE 715
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767919985 716 KESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAVQELRRQN 780
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
268-626 |
8.13e-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: 39.77 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 268 LEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVE-------KEMKSLARKAMDTESELGRQKAENNSLRLLYENTEK 340
Cdd:pfam01576 108 LEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEdqnsklsKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 341 DLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLndlAKEKECLQACLDKKSENIASLGESLa 420
Cdd:pfam01576 188 MISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQL---AKKEEELQAALARLEEETAQKNNAL- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 421 mkeKTISGMKNIIAEME-----------QASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQEQF 489
Cdd:pfam01576 264 ---KKIRELEAQISELQedleseraarnKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEET 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 490 AKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILkseESENRQMMEQLRKANEDAENWENKARQSEADNNTL 569
Cdd:pfam01576 341 RSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQAL---ESENAELQAELRTLQQAKQDSEHKRKKLEGQLQEL 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 767919985 570 KLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQ 626
Cdd:pfam01576 418 QARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ 474
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
76-641 |
8.35e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 76 NIIVLEDTIKRLKSIILDTEKAQNKSPSRLDsfvktleaDKDHYKSEAQHLRKMMRSRSKSPRRPSPTARGANCDVELLK 155
Cdd:PRK01156 167 NYDKLKDVIDMLRAEISNIDYLEEKLKSSNL--------ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLK 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 156 TTTRDREELKCMLEKYERHLAEIQGNVKVLKSERDKIFLLYEQAQEEITRL--------------------RREMMKSCK 215
Cdd:PRK01156 239 SALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPvyknrnyindyfkykndienKKQILSNID 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 216 SP--KSTTAHAILRRVETERDVAFTDLRRM---TTERDSLRERlKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQM 290
Cdd:PRK01156 319 AEinKYHAIIKKLSVLQKDYNDYIKKKSRYddlNNQILELEGY-EMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEIL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 291 SNMTLMKETIStveKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQ---------RHLAKKKYE--LQLT 359
Cdd:PRK01156 398 KIQEIDPDAIK---KELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNgqsvcpvcgTTLGEEKSNhiINHY 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 360 QEKIMCLDEKIDNFTRqniaqreEISILGGTLNDLAKEKECLQACLDKKSENIASLGESlamKEKTISGMKNIIAEMEQA 439
Cdd:PRK01156 475 NEKKSRLEEKIREIEI-------EVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIES---ARADLEDIKIKINELKDK 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 440 SRQCTEALivcEQDVSRMRRQLDETNDELAQIARERDILahDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIK----Q 515
Cdd:PRK01156 545 HDKYEEIK---NRYKSLKLEDLDSKRTSWLNALAVISLI--DIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKsyidK 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 516 KVQDTNLEVNKLKNiLKSEESENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVE 595
Cdd:PRK01156 620 SIREIENEANNLNN-KYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRA 698
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 767919985 596 QHLNAERSYKSQISTLHKSVVKMEEELQKVQfEKVSALADLSSTRE 641
Cdd:PRK01156 699 RLESTIEILRTRINELSDRINDINETLESMK-KIKKAIGDLKRLRE 743
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
152-380 |
9.75e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 9.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 152 ELLKTTTRDREELKCMLEKYERHlAEIQGNVKVLKSERDKI-----FLLYEQAQEEITRLRREmmksckspksttahaiL 226
Cdd:COG4913 242 EALEDAREQIELLEPIRELAERY-AAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAE----------------L 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919985 227 RRVETERDVAFTDLRRMTTERDSLRERLkiaQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKE 306
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQI---RGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767919985 307 MKSLARKAMDTESELGRQKAEnnsLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFtRQNIAQ 380
Cdd:COG4913 382 FAALRAEAAALLEALEEELEA---LEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL-RDALAE 451
|
|
| |
