|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
378-734 |
4.66e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.17 E-value: 4.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 378 LASLTEKIQKMEENhhstAEELQATLQELSDQQqmvQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQE 457
Cdd:TIGR02168 679 IEELEEKIEELEEK----IAELEKALAELRKEL---EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 458 RvkNEEPTTQEGKIIELEQKctgiLEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHN 537
Cdd:TIGR02168 752 L--SKELTELEAEIEELEER----LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 538 NNMMAKTLEECRVTLEGLKMENGSLK--------SHLQGEKQKATEASAVEQ-TAESCEVQEMLKVARAEKDLLELSCNE 608
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSedieslaaEIEELEELIEELESELEAlLNERASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 609 LRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLS-RTSLKLQ---EKASESDAEIKDMKETIFELEDQVEQHR 684
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEeaeALENKIEDDEEEARRRLKRLENKIKELG 985
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1886308682 685 AVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWR-RFQA 734
Cdd:TIGR02168 986 PVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREAReRFKD 1036
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
375-779 |
1.41e-11 |
|
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: 68.12 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 375 ELSLASLTEKIQKMEEnhhstaeeLQATLQELSDQQQmvqELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNL 454
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKS--------LESQISELKKQNN---QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 455 LQErvKNEEPTTQEGKIIELEQKCTGI-LEQGRFEREKLLNIQQQLTCSLRKVEEENQGA-------LEMIKRLKEENEK 526
Cdd:TIGR04523 269 LSE--KQKELEQNNKKIKELEKQLNQLkSEISDLNNQKEQDWNKELKSELKNQEKKLEEIqnqisqnNKIISQLNEQISQ 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 527 LNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKAT--EASAVEQTAESCEVQEMLKVARAEKDLLEL 604
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINdlESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 605 SCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTS------------------------LKLQEKAS 660
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSrsinkikqnleqkqkelkskekelKKLNEEKK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 661 ESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSdlERQLKTLTKQMKEETEEWRRFQADLQTAV 740
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQ 584
|
410 420 430
....*....|....*....|....*....|....*....
gi 1886308682 741 VVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQ 779
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
470-775 |
1.61e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 470 KIIELEQKCTGI---LEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNNNMMAKTLE 546
Cdd:TIGR02168 678 EIEELEEKIEELeekIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 547 ECRVTLEGLKMENGSLKSHLQgekqkateasavEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSL 626
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELA------------EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 627 LAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEE 706
Cdd:TIGR02168 826 LESLERRIAATER----RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1886308682 707 QKSDLERQLKTLTKQMKEETEEWRRFQADLQtavvvandikcEAQQELRTVKRKLLEEEEKNARLQKEL 775
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLE-----------GLEVRIDNLQERLSEEYSLTLEEAEAL 959
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
517-775 |
1.42e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 517 IKRLKEENEKLNEFLELErhnnnmmaKTLEECRVTLEGLKMEngslksHLQGEKQKAtEASAVEQTAESCEVQEMLKVAR 596
Cdd:COG1196 202 LEPLERQAEKAERYRELK--------EELKELEAELLLLKLR------ELEAELEEL-EAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 597 AEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFEL 676
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE----RRRELEERLEELEEELAELEEELEELEEELEEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 677 EDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKcEAQQELRT 756
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL-ERLERLEE 421
|
250
....*....|....*....
gi 1886308682 757 VKRKLLEEEEKNARLQKEL 775
Cdd:COG1196 422 ELEELEEALAELEEEEEEE 440
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
378-646 |
3.43e-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: 60.46 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 378 LASLTEKIQKMEENHHSTAEELQATLQELSD-------QQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEK 450
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEElrlevseLEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 451 LMNLLQE-----RVKNEEPTTQEGKIIELEQKCTGILEQGrferEKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENE 525
Cdd:TIGR02168 321 LEAQLEElesklDELAEELAELEEKLEELKEELESLEAEL----EELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 526 KLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELS 605
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1886308682 606 CNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAE 646
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
503-785 |
4.17e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 503 LRKVEEENQGALeMIKRLKEENEKLNEFLELERHNNNMM---AKTLEECRVTLEGLKMENGSLKSHLQgEKQKATEASAV 579
Cdd:TIGR02168 218 LKAELRELELAL-LVLRLEELREELEELQEELKEAEEELeelTAELQELEEKLEELRLEVSELEEEIE-ELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 580 EQTaescEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQE-- 657
Cdd:TIGR02168 296 EIS----RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEle 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 658 -KASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQ--------MKEETEE 728
Cdd:TIGR02168 372 sRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKelqaeleeLEEELEE 451
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1886308682 729 WRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVV 785
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
375-635 |
4.92e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 375 ELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNL 454
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 455 LQERVKNEEptTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLtcsLRKVEEENQGALEMIKRLKEENEKLNEFLELE 534
Cdd:COG1196 332 LEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 535 RHNNNmMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELscNELRQELL 614
Cdd:COG1196 407 EAEEA-LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL--EAALAELL 483
|
250 260
....*....|....*....|.
gi 1886308682 615 KANGEIKHVSSLLAKVEKDYS 635
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYE 504
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
384-773 |
8.39e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 384 KIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETsFHQHRERAEQLSQENEKlmnlLQERVKNEE 463
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKKEELER----LKKRLTGLT 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 464 PTTQEGKIIELEQKCTGIleqgrfeREKLLNIQQQLTcSLRKVEEENQGALEMIKRLKEENEKLNEFLElERHNNNMMA- 542
Cdd:PRK03918 386 PEKLEKELEELEKAKEEI-------EEEISKITARIG-ELKKEIKELKKAIEELKKAKGKCPVCGRELT-EEHRKELLEe 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 543 ---------KTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELScnELRQEL 613
Cdd:PRK03918 457 ytaelkrieKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYE--KLKEKL 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 614 LKANGEIKHVSSLLAKV---EKDYSYLKEICDHQAEQLSRTSLKLQEKASESdaeIKDMKETIFELE----------DQV 680
Cdd:PRK03918 535 IKLKGEIKSLKKELEKLeelKKKLAELEKKLDELEEELAELLKELEELGFES---VEELEERLKELEpfyneylelkDAE 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 681 EQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLT-----------KQMKEETEEWRRFQADLQTAVVVANDIKCE 749
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEelekkyseeeyEELREEYLELSRELAGLRAELEELEKRREE 691
|
410 420
....*....|....*....|....
gi 1886308682 750 AQQELRTVKRKLLEEEEKNARLQK 773
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKELEK 715
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
375-780 |
8.83e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 8.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 375 ELSLASLTEKIQKMEENHH---STAEELQATLQELSDQQQMVQELTAENEKLVD-------EKTILETSFHQHRERAEQL 444
Cdd:PRK02224 212 ESELAELDEEIERYEEQREqarETRDEADEVLEEHEERREELETLEAEIEDLREtiaeterEREELAEEVRDLRERLEEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 445 SQENEKLmnLLQERVKNEEPTTQEGKIIELEQKCTGI---LEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLK 521
Cdd:PRK02224 292 EEERDDL--LAEAGLDDADAEAVEARREELEDRDEELrdrLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 522 EENEKLNEFLELERHNNNMMAKTLEECR-------VTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESC--EVQEML 592
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRerfgdapVDLGNAEDFLEELREERDELREREAELEATLRTARERveEAEALL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 593 KV---------------------ARAEKDLLELSCNELRQELLKANGEIKHVSSLlAKVEKDYSYLKE-------ICDHQ 644
Cdd:PRK02224 450 EAgkcpecgqpvegsphvetieeDRERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEErredleeLIAER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 645 AEQLSRTSLKLQEK---ASESDAEIKDMKETIFELEDQVEQHR-AVKLHNNQL---------ISELESSVIKLEEQKSDL 711
Cdd:PRK02224 529 RETIEEKRERAEELrerAAELEAEAEEKREAAAEAEEEAEEAReEVAELNSKLaelkeriesLERIRTLLAAIADAEDEI 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 712 ER------QLKTLTKQMKEETEEWRRFQADLQ-----TAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQG 780
Cdd:PRK02224 609 ERlrekreALAELNDERRERLAEKRERKRELEaefdeARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
364-728 |
1.25e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 364 STAGSSPNSVSEL-SLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAE 442
Cdd:TIGR02169 661 APRGGILFSRSEPaELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 443 QLSqenEKLMNLLQERVKNE-EPTTQEGKIIELEQKCTGI-LEQGRFEREKLLNIQQQLTCSLRKVEEENQgalEMIKRL 520
Cdd:TIGR02169 741 ELE---EDLSSLEQEIENVKsELKELEARIEELEEDLHKLeEALNDLEARLSHSRIPEIQAELSKLEEEVS---RIEARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 521 KEENEKLNEfLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKaTEASAVEQTAESCEVQEMLKVARAEKD 600
Cdd:TIGR02169 815 REIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE-LEEELEELEAALRDLESRLGDLKKERD 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 601 LLELSCNELRQELLKANGEI----KHVSSLLAKVEKDYSYLKEICDHQAEQLSrtslklqekASESDAEIKDMKETIFEL 676
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIekkrKRLSELKAKLEALEEELSEIEDPKGEDEE---------IPEEELSLEDVQAELQRV 963
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1886308682 677 EDQVEQHRAVklhNNQLISELESSVIKLEEQKSDLERqLKTLTKQMKEETEE 728
Cdd:TIGR02169 964 EEEIRALEPV---NMLAIQEYEEVLKRLDELKEKRAK-LEEERKAILERIEE 1011
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
372-774 |
3.06e-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: 54.26 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 372 SVSELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQL-SQENEK 450
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIkNKLLKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 451 LMNLLQERVKNEEPTTQEGKIIELEQKctgileqgrfeREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEF 530
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKSLESQISELKKQ-----------NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 531 L-----ELERHNNNMMAKT--LEECRVTLEGLKME-----NGSLKSHLQGEKQKATEA-SAVEQTAESC-EVQEMLKVAR 596
Cdd:TIGR04523 269 LsekqkELEQNNKKIKELEkqLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIqNQISQNNKIIsQLNEQISQLK 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 597 AEKDLLELSCNELRQELLKANGEIKHVssllaKVEKDySYLKEICD--HQAEQLSRTSLKLQEKASESDAEIKDMKETIF 674
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKL-----KKENQ-SYKQEIKNleSQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 675 ELEDQVEQHRAVKLHNNQLISELES-------SVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVvvandik 747
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNqdsvkelIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE------- 495
|
410 420
....*....|....*....|....*..
gi 1886308682 748 ceaqQELRTVKRKLLEEEEKNARLQKE 774
Cdd:TIGR04523 496 ----KELKKLNEEKKELEEKVKDLTKK 518
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
382-776 |
3.07e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 382 TEKIQKMEENHHstaEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhQHRERAEQLSQENEKL---MNLLQER 458
Cdd:PRK03918 188 TENIEELIKEKE---KELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLegsKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 459 VKN------------EEPTTQEGKIIELEQKCTGILEQGRFeREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEK 526
Cdd:PRK03918 261 IREleerieelkkeiEELEEKVKELKELKEKAEEYIKLSEF-YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 527 LNEFLELERHNNNMMAKtLEECRVTLEGLKMENGSLKSHLQGEKQKATEasaveqtaescEVQEMLKVARAEKDLLELSC 606
Cdd:PRK03918 340 LEELKKKLKELEKRLEE-LEERHELYEEAKAKKEELERLKKRLTGLTPE-----------KLEKELEELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 607 NELRQELLKANGEIKHVSSLLAKVEKdysyLKEICDHQAEQLSRTSLKlqEKASESDAEIKDMKETIFELEDQVEQHRAV 686
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKK----AKGKCPVCGRELTEEHRK--ELLEEYTAELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 687 KLHNNQLISElESSVIKLE---EQKSDLERQLKTLT-KQMKEETEEWRRFQADLQT----AVVVANDIK--CEAQQELRT 756
Cdd:PRK03918 482 LRELEKVLKK-ESELIKLKelaEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKlkgeIKSLKKELEklEELKKKLAE 560
|
410 420
....*....|....*....|
gi 1886308682 757 VKRKLLEEEEKNARLQKELG 776
Cdd:PRK03918 561 LEKKLDELEEELAELLKELE 580
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
514-766 |
8.27e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 8.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 514 LEMIKRLKEENEKLNEFL--ELERHNNNMMAKT--LEECRVTLEGLKMENGSLKSHLQGEKQKATEA----SAVEQTAEs 585
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLqsELRRIENRLDELSqeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELeedlSSLEQEIE- 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 586 cEVQEMLKVARAEKDLLELSCNELRQELLK-----ANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLK---LQE 657
Cdd:TIGR02169 755 -NVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEkeyLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 658 KASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQ 737
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913
|
250 260 270
....*....|....*....|....*....|..
gi 1886308682 738 TAVVVANDIKC---EAQQELRTVKRKLLEEEE 766
Cdd:TIGR02169 914 KKRKRLSELKAkleALEEELSEIEDPKGEDEE 945
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
378-772 |
1.15e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 378 LASLTEKIQKMEENH---HSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILET--SFHQHRERAEQLSQENEKLM 452
Cdd:COG4717 73 LKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 453 NLLQERVKNEEP-TTQEGKIIELEQKCTGILEQGRFEREKLLniqQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEfl 531
Cdd:COG4717 153 ERLEELRELEEElEELEAELAELQEELEELLEQLSLATEEEL---QDLAEELEELQQRLAELEEELEEAQEELEELEE-- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 532 ELERHNNNMMAKTLEEC-------------RVTLEGLKMENGSLKSHLQG----------------EKQKATEASAVEQT 582
Cdd:COG4717 228 ELEQLENELEAAALEERlkearlllliaaaLLALLGLGGSLLSLILTIAGvlflvlgllallflllAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 583 AESCEVQEMLKVARAE-KDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYS--YLKEICDHQAEQLSR---TSLKLQ 656
Cdd:COG4717 308 QALPALEELEEEELEElLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQLEELEQEIAALLAEagvEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 657 EKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEssvikLEEQKSDLERQLKTLTKQMKEETEEWRRFQADL 736
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELEEELEELEEELEELREELAELEAEL 462
|
410 420 430
....*....|....*....|....*....|....*.
gi 1886308682 737 QTAvvVANDIKCEAQQELRTVKRKLLEEEEKNARLQ 772
Cdd:COG4717 463 EQL--EEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
374-781 |
1.71e-06 |
|
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: 51.71 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 374 SELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKL-- 451
Cdd:pfam01576 24 AESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMqq 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 452 -MNLLQERVKNEEPTTQ---------EGKIIELEQKCTGILEQ-GRFEREKLLNIQQQLTCSLRKVEEENQGalEMIKRL 520
Cdd:pfam01576 104 hIQDLEEQLDEEEAARQklqlekvttEAKIKKLEEDILLLEDQnSKLSKERKLLEERISEFTSNLAEEEEKA--KSLSKL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 521 KEENEKLNEFLELERHNNNMMAKTLEECRVTLEG------------------LKMENGSLKSHLQGEKQKATEASAV--- 579
Cdd:pfam01576 182 KNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGestdlqeqiaelqaqiaeLRAQLAKKEEELQAALARLEEETAQknn 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 580 ------EQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKdysyLKEICDHQAEQLSRTsl 653
Cdd:pfam01576 262 alkkirELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE----LRSKREQEVTELKKA-- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 654 kLQEKASESDAEIKDMKE----TIFELEDQVEQHRAVKlhnnqliSELESSVIKLEEQKSDLERQLKTLTKQMKEETEEW 729
Cdd:pfam01576 336 -LEEETRSHEAQLQEMRQkhtqALEELTEQLEQAKRNK-------ANLEKAKQALESENAELQAELRTLQQAKQDSEHKR 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886308682 730 RRFQADLQTAVVVANDIK----------CEAQQELRTVKRKLLEEEEKNARLQKELGDVQGH 781
Cdd:pfam01576 408 KKLEGQLQELQARLSESErqraelaeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQ 469
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
439-797 |
1.82e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 439 ERAEQLSQENEKL---MNLLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTcSLRKVEEENQGALE 515
Cdd:COG1196 213 ERYRELKEELKELeaeLLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE-ELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 516 MIKRLKEENEKLNEFLELERHNNnmmaktleecRVTLEGLKMENGSLKSHLQGEKQKATEAsaveqtaescevQEMLKVA 595
Cdd:COG1196 292 ELLAELARLEQDIARLEERRREL----------EERLEELEEELAELEEELEELEEELEEL------------EEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 596 RAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFE 675
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR----AAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 676 LEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIK-CEAQQEL 754
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLeAEADYEG 505
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1886308682 755 RTVKRKLLEEEEKNARLQKELGDVQGHGRVVTsRAAPPSLGSV 797
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE-AALEAALAAA 547
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
587-788 |
1.96e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 587 EVQEMLKVARAEKDLLELSCnELRQELLKANGEIKHVSSLLAKV-----EKDYSYLKEICDHQAEQLSRtslkLQEKASE 661
Cdd:COG4913 239 RAHEALEDAREQIELLEPIR-ELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELAR----LEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 662 SDAEIKDMKETIFELEDQVEQHRAVKLHN-NQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAV 740
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1886308682 741 VVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVVTSR 788
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
378-775 |
6.64e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.97 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 378 LASLTEKIQKmeeNHHSTAEELQATLQELSD-QQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENE------K 450
Cdd:TIGR00618 181 LALMEFAKKK---SLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREaqeeqlK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 451 LMNLLQERVKNEEPTTQEGKIIELEQKCTGI-------------LEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMI 517
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAVLEETQERINRarkaaplaahikaVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 518 KRLKEENEKLNEFLELERHNnnmmAKTLEECRVTLEGLKMENgSLKSHLQGEKQKATEASAVEQTAesCEVQEMLKVARA 597
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHI----RDAHEVATSIREISCQQH-TLTQHIHTLQQQKTTLTQKLQSL--CKELDILQREQA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 598 EKDLLELSCNELRQELLKANGEI----KHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQ-----EKASESDAEIKD 668
Cdd:TIGR00618 411 TIDTRTSAFRDLQGQLAHAKKQQelqqRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQqlqtkEQIHLQETRKKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 669 MKETIfeLEDQVEQHRAVK---LHNNQ-------------LISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRF 732
Cdd:TIGR00618 491 VVLAR--LLELQEEPCPLCgscIHPNParqdidnpgpltrRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEI 568
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1886308682 733 QADLQTAVVVANDIKCEAQQeLRTVKRKLLEEEEKNARLQKEL 775
Cdd:TIGR00618 569 QQSFSILTQCDNRSKEDIPN-LQNITVRLQDLTEKLSEAEDML 610
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
375-659 |
7.50e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 375 ELSLASLTEKIQKMEEnhhsTAEELQATLQELSDQqqmVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNL 454
Cdd:COG1196 238 EAELEELEAELEELEA----ELEELEAELAELEAE---LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 455 LQERVKNEEptTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELE 534
Cdd:COG1196 311 RRELEERLE--ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 535 ---RHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELScNELRQ 611
Cdd:COG1196 389 leaLRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL-ELLAE 467
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1886308682 612 ELLKANGEIKHVSSLLAKVEKDYS--YLKEICDHQAEQLSRTSLKLQEKA 659
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAArlLLLLEAEADYEGFLEGVKAALLLA 517
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
515-775 |
1.71e-05 |
|
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: 48.58 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 515 EMIKRLKEENEKLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATE-ASAVEQTAESCEVQEMLK 593
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDlRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 594 varaeKDLLELS---CNELRQELLKANGEIKHVSSLLAKVEKDYSylKEIcdHQAEQLSRTSLK-----LQEKASESDAE 665
Cdd:pfam15921 162 -----EDMLEDSntqIEQLRKMMLSHEGVLQEIRSILVDFEEASG--KKI--YEHDSMSTMHFRslgsaISKILRELDTE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 666 IKDMKETIFELEDQVEQHRA---------VKLHNN---QLISELESSVIKLEE-------QKSDLERQLKTLTKQMKEET 726
Cdd:pfam15921 233 ISYLKGRIFPVEDQLEALKSesqnkiellLQQHQDrieQLISEHEVEITGLTEkassarsQANSIQSQLEIIQEQARNQN 312
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1886308682 727 EEWRRFQADLQTAVvvandikCEAQQELRTVKRKLleeEEKNARLQKEL 775
Cdd:pfam15921 313 SMYMRQLSDLESTV-------SQLRSELREAKRMY---EDKIEELEKQL 351
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
570-796 |
2.35e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 570 KQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLS 649
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 650 RTSlklqekASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEw 729
Cdd:COG3883 97 RSG------GSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA- 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1886308682 730 rrfQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVVTSRAAPPSLGS 796
Cdd:COG3883 170 ---KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
396-781 |
2.84e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 396 AEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhqhreRAEQLSQENEKLMNLLQErvkneEPTTQEGKIIELE 475
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHL--------QETRKKAVVLARLLELQE-----EPCPLCGSCIHPN 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 476 QKCTGILEQGRFER--EKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKL-NEFLELERHNN------NMMAKTLE 546
Cdd:TIGR00618 515 PARQDIDNPGPLTRrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIqQSFSILTQCDNrskediPNLQNITV 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 547 ECRVTLEGLKMENGSLKSHLQGEKQKATEASA---VEQTAESCEVQEMLKVARAEKDLLELSCNELRQELL--------- 614
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHALLRKLQPEQDlqdVRLHLQQCSQELALKLTALHALQLTLTQERVREHALsirvlpkel 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 615 ---------KANGEIKHVSSLLAKVEKDYSYLKEICDH------QAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQ 679
Cdd:TIGR00618 675 lasrqlalqKMQSEKEQLTYWKEMLAQCQTLLRELETHieeydrEFNEIENASSSLGSDLAAREDALNQSLKELMHQART 754
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 680 VEQHRAVKLHNNqliSELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKR 759
Cdd:TIGR00618 755 VLKARTEAHFNN---NEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEE 831
|
410 420
....*....|....*....|..
gi 1886308682 760 KLLEEEEKNARLQKELGDVQGH 781
Cdd:TIGR00618 832 QFLSRLEEKSATLGEITHQLLK 853
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
359-774 |
5.70e-05 |
|
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: 46.64 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 359 KSSKCSTAGSSPNSVSELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTA----------ENEKLVDEKT 428
Cdd:pfam05483 339 ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKfknnkeveleELKKILAEDE 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 429 ILETSFHQHRERAEQLSQENEKLMNLLQERVKN-EEPTTQEGKIIELEQKCTGILEQGR--FEREKLLNIQQQLTCSLRK 505
Cdd:pfam05483 419 KLLDEKKQFEKIAEELKGKEQELIFLLQAREKEiHDLEIQLTAIKTSEEHYLKEVEDLKteLEKEKLKNIELTAHCDKLL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 506 VEEEN--QGALEMIKRLKEENEKLNEFLELERHnnnmMAKTLEECRVTLEGLKMENGSLKSHLqgeKQKATEASAVEQTA 583
Cdd:pfam05483 499 LENKEltQEASDMTLELKKHQEDIINCKKQEER----MLKQIENLEEKEMNLRDELESVREEF---IQKGDEVKCKLDKS 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 584 ESCEVQEMLKVARAEKDL--LELSCNELRQELLKANGEIKHVSSLLAKVEKDYSY------LKEICDHQAE-QLSRTSLK 654
Cdd:pfam05483 572 EENARSIEYEVLKKEKQMkiLENKCNNLKKQIENKNKNIEELHQENKALKKKGSAenkqlnAYEIKVNKLElELASAKQK 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 655 LQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVI-KLEEQKSDLERQLKTLTKQMKEETEEWRRFQ 733
Cdd:pfam05483 652 FEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhKIAEMVALMEKHKHQYDKIIEERDSELGLYK 731
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1886308682 734 ADLQTAVVVANDIKCE---AQQELRTVKRKLLEEEEKNARLQKE 774
Cdd:pfam05483 732 NKEQEQSSAKAALEIElsnIKAELLSLKKQLEIEKEEKEKLKME 775
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
517-775 |
9.35e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 9.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 517 IKRLKEENEKLNEFLELErhnnnmmaKTLEECRVTLEGLKMEngSLKSHLQgEKQKATEASAVEQTAESCEVQE------ 590
Cdd:TIGR02168 202 LKSLERQAEKAERYKELK--------AELRELELALLVLRLE--ELREELE-ELQEELKEAEEELEELTAELQEleekle 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 591 --MLKVARAEKDLLELS--CNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEI 666
Cdd:TIGR02168 271 elRLEVSELEEEIEELQkeLYALANEISRLEQQKQILRERLANLERQLEELEA----QLEELESKLDELAEELAELEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 667 KDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQ----------MKEETEEWRRFQADL 736
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEierlearlerLEDRRERLQQEIEEL 426
|
250 260 270
....*....|....*....|....*....|....*....
gi 1886308682 737 QTAVVVANdiKCEAQQELRTVKRKLLEEEEKNARLQKEL 775
Cdd:TIGR02168 427 LKKLEEAE--LKELQAELEELEEELEELQEELERLEEAL 463
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
404-762 |
1.04e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.60 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 404 QELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLM-NLLQERvkneeptTQEGKIIELeqkctgiL 482
Cdd:PRK04778 105 HEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRkSLLANR-------FSFGPALDE-------L 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 483 EqgrferEKLLNIQQQLTcslRKVEEENQG----ALEMIKRLKEENEKLNEFLE----LERHNNNMMAKTLEECRVTLEG 554
Cdd:PRK04778 171 E------KQLENLEEEFS---QFVELTESGdyveAREILDQLEEELAALEQIMEeipeLLKELQTELPDQLQELKAGYRE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 555 LKMENGSLKsHLQGEKqkateasaveqtaescEVQEML-KVARAEKDLLELSCNELRQELLKANGEIKHVSSLLakvEKD 633
Cdd:PRK04778 242 LVEEGYHLD-HLDIEK----------------EIQDLKeQIDENLALLEELDLDEAEEKNEEIQERIDQLYDIL---ERE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 634 YSYLKEIcDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQK---SD 710
Cdd:PRK04778 302 VKARKYV-EKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEiaySE 380
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1886308682 711 LERQLKTLTKQMKEETEEWRRFQADLQT---AVVVANDIKCEAQQELRTVKRKLL 762
Cdd:PRK04778 381 LQEELEEILKQLEEIEKEQEKLSEMLQGlrkDELEAREKLERYRNKLHEIKRYLE 435
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
396-774 |
1.23e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 396 AEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhqHRERAEQLSQENEKLMNLLQERVKNEEPTTQEgkiiELE 475
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE-----EKKKADEAKKKAEEAKKADEAKKKAEEAKKAE----EAK 1463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 476 QKCTgilEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNNNMMAKTLEECRVTLEGL 555
Cdd:PTZ00121 1464 KKAE---EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK 1540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 556 KMEngslkshlqgEKQKATEASAVEQTAESCEVQEMLKVARAEKD--LLELSCNELRQELLKANGEIKHVSSLLAKVEKD 633
Cdd:PTZ00121 1541 KAE----------EKKKADELKKAEELKKAEEKKKAEEAKKAEEDknMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 634 YSYLKEICDHQAEQLSrtslKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLE- 712
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELK----KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEd 1686
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1886308682 713 ---------------RQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKN--ARLQKE 774
Cdd:PTZ00121 1687 ekkaaealkkeaeeaKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKkiAHLKKE 1765
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
483-779 |
1.28e-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: 45.73 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 483 EQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNNNMMAKT----LEECRVTLEGLKME 558
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDylklNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 559 NGSLKSHLQGEKQKATEASAVEQTAESCEVQEMlKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKdysylk 638
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEK-KLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK------ 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 639 eicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQlKTL 718
Cdd:pfam02463 322 -----EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL-KEE 395
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886308682 719 TKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQ 779
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
397-723 |
1.32e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 397 EELQATLQELSDQQQMVQELTAENEKLVDEKTILETsfhQHRERAEQLSQENEKLMNLLQER-VKNEEPTTQEGKIIELE 475
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES---ENSEKQRELEEKQNEIEKLKKENqSYKQEIKNLESQINDLE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 476 QKctgileqgrFEREKLLNiqQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFL-ELERHNN------NMMAKTLEEC 548
Cdd:TIGR04523 398 SK---------IQNQEKLN--QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIkDLTNQDSvkeliiKNLDNTRESL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 549 RVTLEGLKMENGSLKSHLQGEKQ--KATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIkhvSSL 626
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKelKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI---SDL 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 627 LAKVEKDYSYLKEicdhqaEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEE 706
Cdd:TIGR04523 544 EDELNKDDFELKK------ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
|
330
....*....|....*..
gi 1886308682 707 QKSDLERQLKTLTKQMK 723
Cdd:TIGR04523 618 ELEKAKKENEKLSSIIK 634
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
608-790 |
1.45e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 608 ELRQELLKANGEIKHVSSLLAKVEKDYSYLKEIcdhqaeqlsRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAvk 687
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQER---------REALQRLAEYSWDEIDVASAEREIAELEAELERLDA-- 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 688 lhNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEK 767
Cdd:COG4913 683 --SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180
....*....|....*....|...
gi 1886308682 768 NARLQKELGDVQGHGRVVTSRAA 790
Cdd:COG4913 761 DAVERELRENLEERIDALRARLN 783
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
375-764 |
1.54e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.49 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 375 ELSLASLTEKIQKMEENHHSTAEeLQATLQELsdqQQMVQELTAENEKLVD-EKTILE-TSFHQHRERA-EQLSQENEKL 451
Cdd:pfam15921 447 ERQMAAIQGKNESLEKVSSLTAQ-LESTKEML---RKVVEELTAKKMTLESsERTVSDlTASLQEKERAiEATNAEITKL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 452 MNLLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNI-QQQLTCSLRKVEEENQGA----LEMIKRLKEENEK 526
Cdd:pfam15921 523 RSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEIlRQQIENMTQLVGQHGRTAgamqVEKAQLEKEINDR 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 527 LNEFLELERHNNNMMAKTLE-ECRVtleglkmengslkSHLQGEKQKATEASAveqtaescevqEMLKVARaekdllels 605
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRElEARV-------------SDLELEKVKLVNAGS-----------ERLRAVK--------- 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 606 cnELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRA 685
Cdd:pfam15921 650 --DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMK 727
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1886308682 686 VKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQeLRTVKRKLLEE 764
Cdd:pfam15921 728 VAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEV-LRSQERRLKEK 805
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
385-675 |
2.90e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 385 IQKMEENHHSTAEELQATLQELSDQQQMvQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQERVKNEEP 464
Cdd:TIGR00618 600 TEKLSEAEDMLACEQHALLRKLQPEQDL-QDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASR 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 465 TTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFL-ELERHNNNMMAK 543
Cdd:TIGR00618 679 QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLkELMHQARTVLKA 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 544 TLEECRVTLEGLKME--NGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIK 621
Cdd:TIGR00618 759 RTEAHFNNNEEVTAAlqTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLE 838
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1886308682 622 HVSSLLAKVEKDYSYLKEiCDHQAEQLSRTSLKLQEKasESDAEIKDMKETIFE 675
Cdd:TIGR00618 839 EKSATLGEITHQLLKYEE-CSKQLAQLTQEQAKIIQL--SDKLNGINQIKIQFD 889
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
397-784 |
3.04e-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: 44.67 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 397 EELQATLQELsdqqQMVQELTAENEKLVDEKtiletsfhqhRERAEQLSQENEKLMNL--LQERVKNEEPTTQEGKIIEL 474
Cdd:TIGR02169 170 RKKEKALEEL----EEVEENIERLDLIIDEK----------RQQLERLRREREKAERYqaLLKEKREYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 475 EQKctgiLEQGRFEREKLLNIQQQLTcslRKVEEENQGALEMIKRLKEENEKLNEFLELERhnnNMMAKTLEECRVTLEG 554
Cdd:TIGR02169 236 ERQ----KEAIERQLASLEEELEKLT---EEISELEKRLEEIEQLLEELNKKIKDLGEEEQ---LRVKEKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 555 LKMENGSLKSHLQ--GEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAK-VE 631
Cdd:TIGR02169 306 LERSIAEKERELEdaEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAEtRD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 632 KDYSYLKEICD--HQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKS 709
Cdd:TIGR02169 386 ELKDYREKLEKlkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886308682 710 DLERQLKTLTKQMKEETEEWRRFQADLQTAvvvandiKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRV 784
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQRELAEA-------EAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSV 533
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
448-779 |
4.50e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.91 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 448 NEKLMNLLQERVKNEEPTTQEGKiieLEQKCTGILEQGRFEREKL-LNIQQQLTCSLRKVEEENQgalEMIKRLKEENEK 526
Cdd:COG5022 775 QVIQHGFRLRRLVDYELKWRLFI---KLQPLLSLLGSRKEYRSYLaCIIKLQKTIKREKKLRETE---EVEFSLKAEVLI 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 527 LNEFLELERHNnnmMAKTLEECRVTLEGL-KMENgsLKSHLQGEKQKATEASAVEQTAEscevqemlkvaRAEKDLLELS 605
Cdd:COG5022 849 QKFGRSLKAKK---RFSLLKKETIYLQSAqRVEL--AERQLQELKIDVKSISSLKLVNL-----------ELESEIIELK 912
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 606 CNElrQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTsLKLQEkasesdaEIKDMKETIFELEDQVEQHRA 685
Cdd:COG5022 913 KSL--SSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPEL-NKLHE-------VESKLKETSEEYEDLLKKSTI 982
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 686 VKLHNNQLISELESSVIKLEEQKSDLERqLKTLTKQMKEEteewRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEE 765
Cdd:COG5022 983 LVREGNKANSELKNFKKELAELSKQYGA-LQESTKQLKEL----PVEVAELQSASKIISSESTELSILKPLQKLKGLLLL 1057
|
330
....*....|....
gi 1886308682 766 EKNaRLQKELGDVQ 779
Cdd:COG5022 1058 ENN-QLQARYKALK 1070
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
380-724 |
4.72e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 380 SLTEKIQKMEENH---HSTAEELQATLQ----ELSDQQQMVQELTAE----NEKLVDEKTILETSFHQHRERAEQLSQEN 448
Cdd:PRK02224 346 SLREDADDLEERAeelREEAAELESELEeareAVEDRREEIEELEEEieelRERFGDAPVDLGNAEDFLEELREERDELR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 449 EKLMNL------LQERVKNEEPTTQEGKIIELEQKCTG-----ILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEM- 516
Cdd:PRK02224 426 EREAELeatlrtARERVEEAEALLEAGKCPECGQPVEGsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLv 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 517 -----IKRLKEENEKLNEFLELERhnnnmmaKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEAsavEQTAEscEVQEM 591
Cdd:PRK02224 506 eaedrIERLEERREDLEELIAERR-------ETIEEKRERAEELRERAAELEAEAEEKREAAAEA---EEEAE--EAREE 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 592 LKvaraekdllelSCNELRQELLKANGEIKHVSSLLAKVEKdysylkeiCDHQAEQLSRTSLKLQEKASESDAEIKDMKE 671
Cdd:PRK02224 574 VA-----------ELNSKLAELKERIESLERIRTLLAAIAD--------AEDEIERLREKREALAELNDERRERLAEKRE 634
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1886308682 672 TIFELEDQVEQHRAVKLHNN-----QLISELESSVIKLEEQKSDLERQLKTLTKQMKE 724
Cdd:PRK02224 635 RKRELEAEFDEARIEEAREDkeraeEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
363-604 |
7.12e-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: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 363 CSTAGSSPNSVSELS--LASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRER 440
Cdd:COG4942 12 ALAAAAQADAAAEAEaeLEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 441 AEQLSQENEKLMNLLQERVKNeepttqegkiieleqkctgILEQGRFEREKLLNIQQQLTCSLRkveeenqgALEMIKRL 520
Cdd:COG4942 92 IAELRAELEAQKEELAELLRA-------------------LYRLGRQPPLALLLSPEDFLDAVR--------RLQYLKYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 521 KEENEKLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKD 600
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
....
gi 1886308682 601 LLEL 604
Cdd:COG4942 225 LEAL 228
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
573-796 |
7.12e-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: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 573 ATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRTS 652
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA----ELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 653 LKLQEKASESDAEIKDM------------------KETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQ 714
Cdd:COG4942 93 AELRAELEAQKEELAELlralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 715 LKTLTKQMKEETEEwrrfQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVVTSRAAPPSL 794
Cdd:COG4942 173 RAELEALLAELEEE----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
..
gi 1886308682 795 GS 796
Cdd:COG4942 249 AA 250
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
438-774 |
7.13e-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: 43.42 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 438 RERAEQLSQENEKLMNLLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMI 517
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 518 KRLKEENEKLNEFLELERHNNNMMAKTLEEcrvtlEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARA 597
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEK-----KLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 598 EKDLLELSCNELRQELLKANGEIKhvsSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELE 677
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIK---REAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 678 DQVEQHRAVKLHNNQLISELESSVI--KLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELR 755
Cdd:pfam02463 404 EKEAQLLLELARQLEDLLKEEKKEEleILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQ 483
|
330
....*....|....*....
gi 1886308682 756 TVKRKLLEEEEKNARLQKE 774
Cdd:pfam02463 484 EQLELLLSRQKLEERSQKE 502
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
542-774 |
9.11e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 9.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 542 AKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAEscevqEMLKVARAEKDLLELscNELRQELLKANGEIK 621
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-----DEIDVASAEREIAEL--EAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 622 HVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASE--------SDAEIKDMKETIFELEDQVEQHrAVKLHNNQL 693
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEldelqdrlEAAEDLARLELRALLEERFAAA-LGDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 694 ISELESSVIKLEEQKSDLERQLktlTKQMKEETEEWRRFQADLQTAVVVANDIkceaQQELRTVKRKLLEE-EEKNARLQ 772
Cdd:COG4913 768 RENLEERIDALRARLNRAEEEL---ERAMRAFNREWPAETADLDADLESLPEY----LALLDRLEEDGLPEyEERFKELL 840
|
..
gi 1886308682 773 KE 774
Cdd:COG4913 841 NE 842
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
378-780 |
9.33e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 9.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 378 LASLTEKIQKMEENHH---STAEELQATLQELSDQQQMVQEltaENEKLVDEKTILETSFHQHRERAEQLSQENEKL--- 451
Cdd:TIGR02169 352 RDKLTEEYAELKEELEdlrAELEEVDKEFAETRDELKDYRE---KLEKLKREINELKRELDRLQEELQRLSEELADLnaa 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 452 -------MNLLQERV--KNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCS-------------------- 502
Cdd:TIGR02169 429 iagieakINELEEEKedKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLqrelaeaeaqaraseervrg 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 503 ---------------------LRKVEEENQGALEM--------------------IKRLKEENEKLNEFLELER------ 535
Cdd:TIGR02169 509 graveevlkasiqgvhgtvaqLGSVGERYATAIEVaagnrlnnvvveddavakeaIELLKRRKAGRATFLPLNKmrderr 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 536 -------------------------------HNNNMMAKTLEECR--------VTLEGL------KMENGSLKSHLQGEK 570
Cdd:TIGR02169 589 dlsilsedgvigfavdlvefdpkyepafkyvFGDTLVVEDIEAARrlmgkyrmVTLEGElfeksgAMTGGSRAPRGGILF 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 571 QKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSR 650
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 651 TSLKLQEKASESD---AEIKDMKETIFELEDQVEQHRAVKLHnnQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETE 727
Cdd:TIGR02169 749 LEQEIENVKSELKeleARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTL 826
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1886308682 728 EWRRFQADLQTAVVVANDIK------CEAQQELRTVKRKLLEEEEKNA----RLQKELGDVQG 780
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKeqiksiEKEIENLNGKKEELEEELEELEaalrDLESRLGDLKK 889
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
542-747 |
9.40e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 9.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 542 AKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAES--CEVQEMLKVARAEKDLLELSCNELRQELLKANGE 619
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERriAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 620 IKHVSSLLAKV-------------------------EKDYSYLKEICDH---QAEQLSRTSLKLQEKASESDAEIKDMKE 671
Cdd:COG4942 99 LEAQKEELAELlralyrlgrqpplalllspedfldaVRRLQYLKYLAPArreQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886308682 672 TIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIK 747
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
488-778 |
9.42e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 9.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 488 EREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNnnmmAKTLEECRVTLEGLKMENGSLKSHLQ 567
Cdd:PRK03918 180 RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKE----VKELEELKEEIEELEKELESLEGSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 568 G--EKQKATEASAVEQTAESCEVQEmlKVARAEK-DLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDhQ 644
Cdd:PRK03918 256 KleEKIRELEERIEELKKEIEELEE--KVKELKElKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-E 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 645 AEQLSRTSLKLQEKASESDAEIKDMK------ETIFELEDQVEQHRAVKLHNNqlISELESSVIKLEEQKSDLERQLKTL 718
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEELEerhelyEEAKAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKI 410
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886308682 719 TkqmkEETEEWRRFQADLQTAVvvaNDIKcEAQQELRTVKRKLLEEEEKN--ARLQKELGDV 778
Cdd:PRK03918 411 T----ARIGELKKEIKELKKAI---EELK-KAKGKCPVCGRELTEEHRKEllEEYTAELKRI 464
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
379-738 |
9.94e-04 |
|
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: 42.73 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 379 ASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQER 458
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 459 VKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTC------------SLRKVEEENQGALEMIKRLKEENEK 526
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAklqgsdldrtvqQVNQEKQEKQHELDTVVSKIELNRK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 527 LNE-----FLELERHNNNM------MAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAES--CEVQEMLK 593
Cdd:TIGR00606 851 LIQdqqeqIQHLKSKTNELkseklqIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKdqQEKEELIS 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 594 VARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEI-----------CDHQAEQLSR---------TSL 653
Cdd:TIGR00606 931 SKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETelntvnaqleeCEKHQEKINEdmrlmrqdiDTQ 1010
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 654 KLQEKASESDAEIKDMKETIFELEDQVEQHraVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQ 733
Cdd:TIGR00606 1011 KIQERWLQDNLTLRKRENELKEVEEELKQH--LKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFK 1088
|
....*
gi 1886308682 734 ADLQT 738
Cdd:TIGR00606 1089 KELRE 1093
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
569-775 |
1.18e-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: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 569 EKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQL 648
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 649 SRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQ---LKTLTKQMKEE 725
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAEraeLEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1886308682 726 TEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKEL 775
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
559-725 |
1.46e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 559 NGSLKSHLQGEKQKATEASAVEQTAEScEVQEMLKVARAE-KDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYL 637
Cdd:PRK12705 18 LGVLVVLLKKRQRLAKEAERILQEAQK-EAEEKLEAALLEaKELLLRERNQQRQEARREREELQREEERLVQKEEQLDAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 638 KEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRavklhNNQLISELEssvikleeqkSDLERQLKT 717
Cdd:PRK12705 97 AEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQA-----RKLLLKLLD----------AELEEEKAQ 161
|
....*...
gi 1886308682 718 LTKQMKEE 725
Cdd:PRK12705 162 RVKKIEEE 169
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
389-780 |
2.33e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 389 EENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFH----------QHRERAEQLSQENEKLMNLLQER 458
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQaetelcaeaeEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 459 VKNEEPTTQ---------EGKIIELEQKctgiLEQGRFEREKLLNIQQQLTCSLRKVEEE------------------NQ 511
Cdd:pfam01576 84 LEEEEERSQqlqnekkkmQQHIQDLEEQ----LDEEEAARQKLQLEKVTTEAKIKKLEEDillledqnsklskerkllEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 512 GALEMIKRLKEENEKLNEFLELeRHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEkqkATEASavEQTAESCEVQEM 591
Cdd:pfam01576 160 RISEFTSNLAEEEEKAKSLSKL-KNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGE---STDLQ--EQIAELQAQIAE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 592 LKVARAEKDllelscNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEIC-DHQAEQLSRTSLKLQEK--ASESDAEIKD 668
Cdd:pfam01576 234 LRAQLAKKE------EELQAALARLEEETAQKNNALKKIRELEAQISELQeDLESERAARNKAEKQRRdlGEELEALKTE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 669 MKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKC 748
Cdd:pfam01576 308 LEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENA 387
|
410 420 430
....*....|....*....|....*....|..
gi 1886308682 749 EAQQELRTVKRKLLEEEEKNARLQKELGDVQG 780
Cdd:pfam01576 388 ELQAELRTLQQAKQDSEHKRKKLEGQLQELQA 419
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
377-775 |
2.73e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 377 SLASLTEKIQKMEE-NHHSTAEELQATLQELSDQqqmVQELTAENEKLVDEKTILETSFHQHRERAEQLS---QENEKLM 452
Cdd:PRK02224 188 SLDQLKAQIEEKEEkDLHERLNGLESELAELDEE---IERYEEQREQARETRDEADEVLEEHEERREELEtleAEIEDLR 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 453 NLLQERVKN-----EEPTTQEGKIIELEQKCTGILEQGRFE----------REKLLNIQQQLTCSLRKVEEENQGALEMI 517
Cdd:PRK02224 265 ETIAETEREreelaEEVRDLRERLEELEEERDDLLAEAGLDdadaeavearREELEDRDEELRDRLEECRVAAQAHNEEA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 518 KRLKEENEKLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLkshlqgEKQKATEASAVEQTAESCE-VQEMLKVAR 596
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL------EEEIEELRERFGDAPVDLGnAEDFLEELR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 597 AEKDLLELSCNELRQELLKANGEIKHVSSLLAKVE--------KDYSYLKEICDHqaeqlsrtslklQEKASESDAEIKD 668
Cdd:PRK02224 419 EERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvEGSPHVETIEED------------RERVEELEAELED 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 669 MKETIFELEDQVEqhRAVKLhnnqliSELESSVIKLEEQKSDLERQL---KTLTKQMKEETEEWRRFQADLQTAVVVAND 745
Cdd:PRK02224 487 LEEEVEEVEERLE--RAEDL------VEAEDRIERLEERREDLEELIaerRETIEEKRERAEELRERAAELEAEAEEKRE 558
|
410 420 430
....*....|....*....|....*....|
gi 1886308682 746 IKCEAQQELRTVKRKLLEEEEKNARLQKEL 775
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAELNSKLAELKERI 588
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
374-657 |
2.93e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 374 SELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRER---AEQLSQENEK 450
Cdd:pfam15921 494 SERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKdkvIEILRQQIEN 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 451 LMNL-----------------LQERVKNEEPTTQEGKII---------ELEQKCTGIleqgRFEREKLLNIQQQLTCSLR 504
Cdd:pfam15921 574 MTQLvgqhgrtagamqvekaqLEKEINDRRLELQEFKILkdkkdakirELEARVSDL----ELEKVKLVNAGSERLRAVK 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 505 KVEEENQGALEMIKRLKEENEKLNEFLELERHNnnmMAKTLEECRVTLEGLKMENGSLKSHLQGEK-------------- 570
Cdd:pfam15921 650 DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN---FRNKSEEMETTTNKLKMQLKSAQSELEQTRntlksmegsdgham 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 571 ------QKATEASAVEQTAESCEVQ---EMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEIC 641
Cdd:pfam15921 727 kvamgmQKQITAKRGQIDALQSKIQfleEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKV 806
|
330
....*....|....*.
gi 1886308682 642 DHQAEQLSRTSLKLQE 657
Cdd:pfam15921 807 ANMEVALDKASLQFAE 822
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
432-770 |
3.30e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.04 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 432 TSFHQHRERAE-QLSQENEKLMNLLQERVKNEEPTT--QEGKIIEL---EQKCTGILEQGRFER----EKLLNIQQQLTC 501
Cdd:PLN02939 91 TSSDDDHNRASmQRDEAIAAIDNEQQTNSKDGEQLSdfQLEDLVGMiqnAEKNILLLNQARLQAledlEKILTEKEALQG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 502 SLRKVEEENQGALEMIKRLKEEN---EKLNEFLELERHNNNMMAKTLEECRVT----LEGLKMENGSLKSHLQGEKqkaT 574
Cdd:PLN02939 171 KINILEMRLSETDARIKLAAQEKihvEILEEQLEKLRNELLIRGATEGLCVHSlskeLDVLKEENMLLKDDIQFLK---A 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 575 EASAVEQTAESCEVQEmlkvarAEKDLLELSCNELRQELLKANGEIKHVSSL-----LAKVEKdysyLKEICDHQAEQLS 649
Cdd:PLN02939 248 ELIEVAETEERVFKLE------KERSLLDASLRELESKFIVAQEDVSKLSPLqydcwWEKVEN----LQDLLDRATNQVE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 650 RTSLKLQEKasesdaeiKDMKETIFELEDQVEqhravklhnnqliselESSVIKLEEQKSDLerqlktLTKQMKEETEEW 729
Cdd:PLN02939 318 KAALVLDQN--------QDLRDKVDKLEASLK----------------EANVSKFSSYKVEL------LQQKLKLLEERL 367
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1886308682 730 RRFQADLQTAVVVANDIKCEAQQELrtvkRKLLEEEEKNAR 770
Cdd:PLN02939 368 QASDHEIHSYIQLYQESIKEFQDTL----SKLKEESKKRSL 404
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
691-774 |
4.08e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 691 NQLISELESSVIKLEEQKSDLE---RQLKTLTKQMKEETEEWR-RFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEE 766
Cdd:PRK00409 519 NELIASLEELERELEQKAEEAEallKEAEKLKEELEEKKEKLQeEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQK 598
|
....*...
gi 1886308682 767 KNARLQKE 774
Cdd:PRK00409 599 GGYASVKA 606
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
375-728 |
4.22e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 375 ELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNL 454
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 455 LQERVKNEEPTTQEGKIIELEQKctgileqgrferEKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELE 534
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELAL------------KLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSE 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 535 RHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQgEKQKATEASAVEQTAESCEVQEMLKVARAEKDllelscnelrqELL 614
Cdd:TIGR00618 689 KEQLTYWKEMLAQCQTLLRELETHIEEYDREFN-EIENASSSLGSDLAAREDALNQSLKELMHQAR-----------TVL 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 615 KANGEIKHVSSLLAKVE----KDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDmKETIFELEDQVEQHRAVKLHN 690
Cdd:TIGR00618 757 KARTEAHFNNNEEVTAAlqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPS-DEDILNLQCETLVQEEEQFLS 835
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1886308682 691 nqLISELESSVIKLEEQKSDLE---RQLKTLTKQMKEETEE 728
Cdd:TIGR00618 836 --RLEEKSATLGEITHQLLKYEecsKQLAQLTQEQAKIIQL 874
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
378-776 |
4.42e-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: 40.80 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 378 LASLTEKIQKMEEN-HHSTAEELQATLQELSDQQQMVQELTAENEklvdektilETSFHQHRERAEQLSQENEKLMNLLQ 456
Cdd:TIGR00606 593 LAKLNKELASLEQNkNHINNELESKEEQLSSYEDKLFDVCGSQDE---------ESDLERLKEEIEKSSKQRAMLAGATA 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 457 ERVKNEEPTTQEgkiielEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERH 536
Cdd:TIGR00606 664 VYSQFITQLTDE------NQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQS 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 537 NNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESC--------EVQEMLK---------VARAEK 599
Cdd:TIGR00606 738 IIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCltdvtimeRFQMELKdverkiaqqAAKLQG 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 600 DLLELSCNELRQELLKANGEIKHVSS---LLAKVEKDY--------SYLKEICDHQAeQLSRTSLKLQEKASESDAEIKD 668
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQEKQHELDTVVSkieLNRKLIQDQqeqiqhlkSKTNELKSEKL-QIGTNLQRRQQFEEQLVELSTE 896
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 669 MKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAvvvANDIKC 748
Cdd:TIGR00606 897 VQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDG---KDDYLK 973
|
410 420
....*....|....*....|....*...
gi 1886308682 749 EAQQELRTVKRKLLEEEEKNARLQKELG 776
Cdd:TIGR00606 974 QKETELNTVNAQLEECEKHQEKINEDMR 1001
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
398-733 |
4.49e-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: 40.54 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 398 ELQATLQELSDQ-QQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQERVKNEEPTTQEGKIIE-LE 475
Cdd:pfam01576 226 ELQAQIAELRAQlAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEaLK 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 476 QKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEE----NQGALEMIKRLKEENEKLNEFLELERHNNNMMAKTLEecrvt 551
Cdd:pfam01576 306 TELEDTLDTTAAQQELRSKREQEVTELKKALEEEtrshEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQ----- 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 552 leGLKMENGSLKSHLQGEKQKATEASAVEQTAEScEVQE-MLKVARAEKDLlelscNELRQELLKANGEIKHVSSLLAKV 630
Cdd:pfam01576 381 --ALESENAELQAELRTLQQAKQDSEHKRKKLEG-QLQElQARLSESERQR-----AELAEKLSKLQSELESVSSLLNEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 631 EKDYSYLKEICDHQAEQLSRTSLKLQEKASES---DAEIKDMKETIFELEDQVEQH--------RAVKLHNNQL------ 693
Cdd:pfam01576 453 EGKNIKLSKDVSSLESQLQDTQELLQEETRQKlnlSTRLRQLEDERNSLQEQLEEEeeakrnveRQLSTLQAQLsdmkkk 532
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1886308682 694 ISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQ 733
Cdd:pfam01576 533 LEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLE 572
|
|
| PRK10884 |
PRK10884 |
SH3 domain-containing protein; Provisional |
655-779 |
4.65e-03 |
|
SH3 domain-containing protein; Provisional
Pssm-ID: 182809 [Multi-domain] Cd Length: 206 Bit Score: 39.25 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 655 LQEKASESDAEIKDMKEtifeledqveqhRAVKLHNNQLiseleSSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQA 734
Cdd:PRK10884 59 LQVNANTNYAQIRDSKG------------RTAWIPLKQL-----STTPSLRTRVPDLENQVKTLTDKLNNIDNTWNQRTA 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1886308682 735 DLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQ 779
Cdd:PRK10884 122 EMQQKVAQSDSVINGLKEENQKLKNQLIVAQKKVDAANLQLDDKQ 166
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
371-776 |
5.64e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 371 NSVSELSlASLTEKIQKMEENHHS----TAEELQATLQElsDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLsQ 446
Cdd:PRK04863 796 EELAERY-ATLSFDVQKLQRLHQAfsrfIGSHLAVAFEA--DPEAELRQLNRRRVELERALADHESQEQQQRSQLEQA-K 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 447 ENEKLMNLLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFERE--KLLNIQQQLTCSLRKVEEEnqgaLEMIKRLKEEN 524
Cdd:PRK04863 872 EGLSALNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFVQQhgNALAQLEPIVSVLQSDPEQ----FEQLKQDYQQA 947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 525 EKlneflelERHNNNMMAKTLEECRVTLEGLKMENgslkshlqgekqkateasAVEQTAESCEVQEMLkvaRAEKDLLEL 604
Cdd:PRK04863 948 QQ-------TQRDAKQQAFALTEVVQRRAHFSYED------------------AAEMLAKNSDLNEKL---RQRLEQAEQ 999
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 605 SCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDmketifELEDQVEQHR 684
Cdd:PRK04863 1000 ERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARARRD------ELHARLSANR 1073
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 685 AVKlhnNQLiselessviklEEQKSDLERQLKTLTKQMKEETEEWRrfqaDLQTAVVVANDIKCEAQQELRT--VKRKLL 762
Cdd:PRK04863 1074 SRR---NQL-----------EKQLTFCEAEMDNLTKKLRKLERDYH----EMREQVVNAKAGWCAVLRLVKDngVERRLH 1135
|
410 420
....*....|....*....|.
gi 1886308682 763 EEE-------EKNARLQKELG 776
Cdd:PRK04863 1136 RRElaylsadELRSMSDKALG 1156
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
482-735 |
6.26e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 39.41 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 482 LEQGRFEREKLLniqQQLTCSLRKVEEENQGALEMIKRLKEENEKLN-EFLELERHNNNMMAKTLEE-CRVTLEGLKMEN 559
Cdd:pfam15905 85 LVQERGEQDKRL---QALEEELEKVEAKLNAAVREKTSLSASVASLEkQLLELTRVNELLKAKFSEDgTQKKMSSLSMEL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 560 GSLKSHLQGeKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQE----------LLKANGEIKHVSSLLAK 629
Cdd:pfam15905 162 MKLRNKLEA-KMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEkieeksetekLLEYITELSCVSEQVEK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 630 VEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEdqveqhravklhnnqliSELESSVIKLEEQKS 709
Cdd:pfam15905 241 YKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLE-----------------SEKEELLREYEEKEQ 303
|
250 260
....*....|....*....|....*.
gi 1886308682 710 DLERQLKTLTKQMKEETEEWRRFQAD 735
Cdd:pfam15905 304 TLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
381-548 |
6.34e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 381 LTEKIQKMEENHHSTAEELQATLQeLSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQERVK 460
Cdd:PRK12705 31 LAKEAERILQEAQKEAEEKLEAAL-LEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 461 NEEP-TTQEGKIIELEQKCTGILEQ-GRFEREKllniQQQLTCSLRKVEEENQGALEmIKRLKEENEklnefLELERHNN 538
Cdd:PRK12705 110 REKAlSARELELEELEKQLDNELYRvAGLTPEQ----ARKLLLKLLDAELEEEKAQR-VKKIEEEAD-----LEAERKAQ 179
|
170
....*....|
gi 1886308682 539 NMMAKTLEEC 548
Cdd:PRK12705 180 NILAQAMQRI 189
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
443-775 |
8.88e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 39.70 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 443 QLSQENEKLMNL---LQERVKNEEPTTQEG-KIIELEQKCtgiLEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIK 518
Cdd:pfam05483 82 KLYKEAEKIKKWkvsIEAELKQKENKLQENrKIIEAQRKA---IQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 519 RLKE----ENEKLNEFlELERH---------NNNM--MAKTLEECRVTLEGLKMENgSLKSHLQGEKQKATEASAVEQTA 583
Cdd:pfam05483 159 LLKEtcarSAEKTKKY-EYEREetrqvymdlNNNIekMILAFEELRVQAENARLEM-HFKLKEDHEKIQHLEEEYKKEIN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 584 ESCEVQEMLKVARAEKdllELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESD 663
Cdd:pfam05483 237 DKEKQVSLLLIQITEK---ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886308682 664 AEIKDMK---ETIFEL----EDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADL 736
Cdd:pfam05483 314 ALEEDLQiatKTICQLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL 393
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1886308682 737 QTAVVVANDIKCEAqQELRTV---KRKLLEEEEKNARLQKEL 775
Cdd:pfam05483 394 EEMTKFKNNKEVEL-EELKKIlaeDEKLLDEKKQFEKIAEEL 434
|
|
| |
