|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
411-767 |
2.82e-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: 73.94 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 411 LASLTEKIQKMEENhhstAEELQATLQELSDQQqmvQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQE 490
Cdd:TIGR02168 679 IEELEEKIEELEEK----IAELEKALAELRKEL---EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 491 RvkNEEPTTQEGKIIELEQKctgiLEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHN 570
Cdd:TIGR02168 752 L--SKELTELEAEIEELEER----LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 571 NNMMAKTLEECRVTLEGLKMENGSLK--------SHLQGEKQKATEASAVEQ-TAESCEVQEMLKVARAEKDLLELSCNE 641
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSedieslaaEIEELEELIEELESELEAlLNERASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 642 LRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLS-RTSLKLQ---EKASESDAEIKDMKETIFELEDQVEQHR 717
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEeaeALENKIEDDEEEARRRLKRLENKIKELG 985
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2462558775 718 AVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWR-RFQA 767
Cdd:TIGR02168 986 PVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREAReRFKD 1036
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
408-812 |
1.41e-12 |
|
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: 71.59 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 408 ELSLASLTEKIQKMEEnhhstaeeLQATLQELSDQQQMVQE-LTAENEKLVDEKTILETSfhqhRERAEQLSQENEKLMN 486
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKS--------LESQISELKKQNNQLKDnIEKKQQEINEKTTEISNT----QTQLNQLKDEQNKIKK 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 487 LLQErvKNEEPTTQEGKIIELEQKCTGI-LEQGRFEREKLLNIQQQLTCSLRKVEEENQGA-------LEMIKRLKEENE 558
Cdd:TIGR04523 268 QLSE--KQKELEQNNKKIKELEKQLNQLkSEISDLNNQKEQDWNKELKSELKNQEKKLEEIqnqisqnNKIISQLNEQIS 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 559 KLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKAT--EASAVEQTAESCEVQEMLKVARAEKDLLE 636
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINdlESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 637 LSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTS------------------------LKLQEKA 692
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSrsinkikqnleqkqkelkskekelKKLNEEK 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 693 SESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSdlERQLKTLTKQMKEETEEWRRFQADLQTA 772
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKKK 583
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2462558775 773 VVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQ 812
Cdd:TIGR04523 584 QEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
503-808 |
1.24e-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: 65.46 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 503 KIIELEQKCTGI---LEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNNNMMAKTLE 579
Cdd:TIGR02168 678 EIEELEEKIEELeekIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 580 ECRVTLEGLKMENGSLKSHLQgekqkateasavEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSL 659
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELA------------EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 660 LAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEE 739
Cdd:TIGR02168 826 LESLERRIAATER----RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462558775 740 QKSDLERQLKTLTKQMKEETEEWRRFQADLQtavvvandikcEAQQELRTVKRKLLEEEEKNARLQKEL 808
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLE-----------GLEVRIDNLQERLSEEYSLTLEEAEAL 959
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
550-808 |
1.33e-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: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 550 IKRLKEENEKLNEFLELErhnnnmmaKTLEECRVTLEGLKMEngslksHLQGEKQKAtEASAVEQTAESCEVQEMLKVAR 629
Cdd:COG1196 202 LEPLERQAEKAERYRELK--------EELKELEAELLLLKLR------ELEAELEEL-EAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 630 AEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFEL 709
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE----RRRELEERLEELEEELAELEEELEELEEELEEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 710 EDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKcEAQQELRT 789
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL-ERLERLEE 421
|
250
....*....|....*....
gi 2462558775 790 VKRKLLEEEEKNARLQKEL 808
Cdd:COG1196 422 ELEELEEALAELEEEEEEE 440
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
411-679 |
2.76e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 411 LASLTEKIQKMEENHHSTAEELQATLQELSD-------QQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEK 483
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEElrlevseLEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 484 LMNLLQE-----RVKNEEPTTQEGKIIELEQKCTGILEQGrferEKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENE 558
Cdd:TIGR02168 321 LEAQLEElesklDELAEELAELEEKLEELKEELESLEAEL----EELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 559 KLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELS 638
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2462558775 639 CNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAE 679
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
536-818 |
2.86e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 536 LRKVEEENQGALeMIKRLKEENEKLNEFLELERHNNNMMAKT---LEECRVTLEGLKMENGSLKSHLQgEKQKATEASAV 612
Cdd:TIGR02168 218 LKAELRELELAL-LVLRLEELREELEELQEELKEAEEELEELtaeLQELEEKLEELRLEVSELEEEIE-ELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 613 EQTaescEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQE-- 690
Cdd:TIGR02168 296 EIS----RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEle 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 691 -KASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQ--------MKEETEE 761
Cdd:TIGR02168 372 sRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKelqaeleeLEEELEE 451
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462558775 762 WRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVV 818
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
405-807 |
2.94e-08 |
|
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: 57.34 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 405 SVSELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQL-SQENEK 483
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIkNKLLKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 484 LMNLLQERVKNEEPTTQEGKIIELEQKctgileqgrfeREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEF 563
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKSLESQISELKKQ-----------NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 564 L-----ELERHNNNMMAKT--LEECRVTLEGLKME-----NGSLKSHLQGEKQKATEA-SAVEQTAESC-EVQEMLKVAR 629
Cdd:TIGR04523 269 LsekqkELEQNNKKIKELEkqLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIqNQISQNNKIIsQLNEQISQLK 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 630 AEKDLLELSCNELRQELLKANGEIKHVssllaKVEKDySYLKEICD--HQAEQLSRTSLKLQEKASESDAEIKDMKETIF 707
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKL-----KKENQ-SYKQEIKNleSQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 708 ELEDQVEQHRAVKLHNNQLISELES-------SVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVvvandik 780
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNqdsvkelIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE------- 495
|
410 420
....*....|....*....|....*..
gi 2462558775 781 ceaqQELRTVKRKLLEEEEKNARLQKE 807
Cdd:TIGR04523 496 ----KELKKLNEEKKELEEKVKDLTKK 518
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
417-806 |
4.22e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 417 KIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETsFHQHRERAEQLSQENEKlmnlLQERVKNEE 496
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKKEELER----LKKRLTGLT 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 497 PTTQEGKIIELEQKCTGIleqgrfeREKLLNIQQQLTcSLRKVEEENQGALEMIKRLKEENEKLNEFLElERHNNNMMA- 575
Cdd:PRK03918 386 PEKLEKELEELEKAKEEI-------EEEISKITARIG-ELKKEIKELKKAIEELKKAKGKCPVCGRELT-EEHRKELLEe 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 576 ---------KTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELScnELRQEL 646
Cdd:PRK03918 457 ytaelkrieKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYE--KLKEKL 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 647 LKANGEIKHVSSLLAKV---EKDYSYLKEICDHQAEQLSRTSLKLQEKASESdaeIKDMKETIFELE----------DQV 713
Cdd:PRK03918 535 IKLKGEIKSLKKELEKLeelKKKLAELEKKLDELEEELAELLKELEELGFES---VEELEERLKELEpfyneylelkDAE 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 714 EQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLT-----------KQMKEETEEWRRFQADLQTAVVVANDIKCE 782
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEelekkyseeeyEELREEYLELSRELAGLRAELEELEKRREE 691
|
410 420
....*....|....*....|....
gi 2462558775 783 AQQELRTVKRKLLEEEEKNARLQK 806
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKELEK 715
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
408-668 |
4.39e-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: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 408 ELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNL 487
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 488 LQERVKNEEptTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLtcsLRKVEEENQGALEMIKRLKEENEKLNEFLELE 567
Cdd:COG1196 332 LEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 568 RHNNNmMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELscNELRQELL 647
Cdd:COG1196 407 EAEEA-LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL--EAALAELL 483
|
250 260
....*....|....*....|.
gi 2462558775 648 KANGEIKHVSSLLAKVEKDYS 668
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYE 504
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
408-813 |
6.19e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 408 ELSLASLTEKIQKMEENHH---STAEELQATLQELSDQQQMVQELTAENEKLVD-------EKTILETSFHQHRERAEQL 477
Cdd:PRK02224 212 ESELAELDEEIERYEEQREqarETRDEADEVLEEHEERREELETLEAEIEDLREtiaeterEREELAEEVRDLRERLEEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 478 SQENEKLmnLLQERVKNEEPTTQEGKIIELEQKCTGI---LEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLK 554
Cdd:PRK02224 292 EEERDDL--LAEAGLDDADAEAVEARREELEDRDEELrdrLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 555 EENEKLNEFLELERHNNNMMAKTLEECR-------VTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESC--EVQEML 625
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRerfgdapVDLGNAEDFLEELREERDELREREAELEATLRTARERveEAEALL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 626 KV---------------------ARAEKDLLELSCNELRQELLKANGEIKHVSSLlAKVEKDYSYLKE-------ICDHQ 677
Cdd:PRK02224 450 EAgkcpecgqpvegsphvetieeDRERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEErredleeLIAER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 678 AEQLSRTSLKLQEK---ASESDAEIKDMKETIFELEDQVEQHR-AVKLHNNQL---------ISELESSVIKLEEQKSDL 744
Cdd:PRK02224 529 RETIEEKRERAEELrerAAELEAEAEEKREAAAEAEEEAEEAReEVAELNSKLaelkeriesLERIRTLLAAIADAEDEI 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 745 ER------QLKTLTKQMKEETEEWRRFQADLQ-----TAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQG 813
Cdd:PRK02224 609 ERlrekreALAELNDERRERLAEKRERKRELEaefdeARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
400-761 |
8.71e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 8.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 400 GSSPNSVSEL-SLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLS 478
Cdd:TIGR02169 664 GGILFSRSEPaELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 479 qenEKLMNLLQERVKNE-EPTTQEGKIIELEQKCTGI-LEQGRFEREKLLNIQQQLTCSLRKVEEENQgalEMIKRLKEE 556
Cdd:TIGR02169 744 ---EDLSSLEQEIENVKsELKELEARIEELEEDLHKLeEALNDLEARLSHSRIPEIQAELSKLEEEVS---RIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 557 NEKLNEfLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKaTEASAVEQTAESCEVQEMLKVARAEKDLLE 636
Cdd:TIGR02169 818 EQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE-LEEELEELEAALRDLESRLGDLKKERDELE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 637 LSCNELRQELLKANGEI----KHVSSLLAKVEKDYSYLKEICDHQAEQLSrtslklqekASESDAEIKDMKETIFELEDQ 712
Cdd:TIGR02169 896 AQLRELERKIEELEAQIekkrKRLSELKAKLEALEEELSEIEDPKGEDEE---------IPEEELSLEDVQAELQRVEEE 966
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2462558775 713 VEQHRAVklhNNQLISELESSVIKLEEQKSDLERqLKTLTKQMKEETEE 761
Cdd:TIGR02169 967 IRALEPV---NMLAIQEYEEVLKRLDELKEKRAK-LEEERKAILERIEE 1011
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
415-809 |
1.42e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 415 TEKIQKMEENHHstaEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhQHRERAEQLSQENEKL---MNLLQER 491
Cdd:PRK03918 188 TENIEELIKEKE---KELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLegsKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 492 VKN------------EEPTTQEGKIIELEQKCTGILEQGRFeREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEK 559
Cdd:PRK03918 261 IREleerieelkkeiEELEEKVKELKELKEKAEEYIKLSEF-YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 560 LNEFLELERHNNNMMAKtLEECRVTLEGLKMENGSLKSHLQGEKQKATEasaveqtaescEVQEMLKVARAEKDLLELSC 639
Cdd:PRK03918 340 LEELKKKLKELEKRLEE-LEERHELYEEAKAKKEELERLKKRLTGLTPE-----------KLEKELEELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 640 NELRQELLKANGEIKHVSSLLAKVEKdysyLKEICDHQAEQLSRTSLKlqEKASESDAEIKDMKETIFELEDQVEQHRAV 719
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKK----AKGKCPVCGRELTEEHRK--ELLEEYTAELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 720 KLHNNQLISElESSVIKLE---EQKSDLERQLKTLT-KQMKEETEEWRRFQADLQT----AVVVANDIK--CEAQQELRT 789
Cdd:PRK03918 482 LRELEKVLKK-ESELIKLKelaEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKlkgeIKSLKKELEklEELKKKLAE 560
|
410 420
....*....|....*....|
gi 2462558775 790 VKRKLLEEEEKNARLQKELG 809
Cdd:PRK03918 561 LEKKLDELEEELAELLKELE 580
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
407-814 |
5.91e-07 |
|
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: 53.26 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 407 SELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKL-- 484
Cdd:pfam01576 24 AESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMqq 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 485 -MNLLQERVKNEEPTTQ---------EGKIIELEQKCTGILEQ-GRFEREKLLNIQQQLTCSLRKVEEENQGalEMIKRL 553
Cdd:pfam01576 104 hIQDLEEQLDEEEAARQklqlekvttEAKIKKLEEDILLLEDQnSKLSKERKLLEERISEFTSNLAEEEEKA--KSLSKL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 554 KEENEKLNEFLELERHNNNMMAKTLEECRVTLEG------------------LKMENGSLKSHLQGEKQKATEASAV--- 612
Cdd:pfam01576 182 KNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGestdlqeqiaelqaqiaeLRAQLAKKEEELQAALARLEEETAQknn 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 613 ------EQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKdysyLKEICDHQAEQLSRTsl 686
Cdd:pfam01576 262 alkkirELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE----LRSKREQEVTELKKA-- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 687 kLQEKASESDAEIKDMKE----TIFELEDQVEQHRAVKlhnnqliSELESSVIKLEEQKSDLERQLKTLTkQMKEETEEW 762
Cdd:pfam01576 336 -LEEETRSHEAQLQEMRQkhtqALEELTEQLEQAKRNK-------ANLEKAKQALESENAELQAELRTLQ-QAKQDSEHK 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462558775 763 RRFQ----ADLQTAVVVANDIKCEA-------QQELRTVKRKLLEEEEKNARLQKELGDVQGH 814
Cdd:pfam01576 407 RKKLegqlQELQARLSESERQRAELaeklsklQSELESVSSLLNEAEGKNIKLSKDVSSLESQ 469
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
547-799 |
6.59e-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: 53.15 E-value: 6.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 547 LEMIKRLKEENEKLNEFL--ELERHNNNMMAKT--LEECRVTLEGLKMENGSLKSHLQGEKQKATEA----SAVEQTAEs 618
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLqsELRRIENRLDELSqeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELeedlSSLEQEIE- 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 619 cEVQEMLKVARAEKDLLELSCNELRQELLK-----ANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLK---LQE 690
Cdd:TIGR02169 755 -NVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEkeyLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 691 KASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQ 770
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913
|
250 260 270
....*....|....*....|....*....|..
gi 2462558775 771 TAVVVANDIKC---EAQQELRTVKRKLLEEEE 799
Cdd:TIGR02169 914 KKRKRLSELKAkleALEEELSEIEDPKGEDEE 945
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
411-805 |
7.31e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 411 LASLTEKIQKMEENH---HSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILET--SFHQHRERAEQLSQENEKLM 485
Cdd:COG4717 73 LKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 486 NLLQERVKNEEP-TTQEGKIIELEQKCTGILEQGRFEREKLLniqQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEfl 564
Cdd:COG4717 153 ERLEELRELEEElEELEAELAELQEELEELLEQLSLATEEEL---QDLAEELEELQQRLAELEEELEEAQEELEELEE-- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 565 ELERHNNNMMAKTLEEC-------------RVTLEGLKMENGSLKSHLQG----------------EKQKATEASAVEQT 615
Cdd:COG4717 228 ELEQLENELEAAALEERlkearlllliaaaLLALLGLGGSLLSLILTIAGvlflvlgllallflllAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 616 AESCEVQEMLKVARAE-KDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYS--YLKEICDHQAEQLSR---TSLKLQ 689
Cdd:COG4717 308 QALPALEELEEEELEElLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQLEELEQEIAALLAEagvEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 690 EKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEssvikLEEQKSDLERQLKTLTKQMKEETEEWRRFQADL 769
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELEEELEELEEELEELREELAELEAEL 462
|
410 420 430
....*....|....*....|....*....|....*.
gi 2462558775 770 QTAvvVANDIKCEAQQELRTVKRKLLEEEEKNARLQ 805
Cdd:COG4717 463 EQL--EEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
472-818 |
1.75e-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: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 472 ERAEQLSQENEKL---MNLLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTcSLRKVEEENQGALE 548
Cdd:COG1196 213 ERYRELKEELKELeaeLLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE-ELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 549 MIKRLKEENEKLNEFLELERHNNnmmaktleecRVTLEGLKMENGSLKSHLQGEKQKATEAsaveqtaescevQEMLKVA 628
Cdd:COG1196 292 ELLAELARLEQDIARLEERRREL----------EERLEELEEELAELEEELEELEEELEEL------------EEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 629 RAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFE 708
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR----AAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 709 LEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIK-CEAQQEL 787
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLeAEADYEG 505
|
330 340 350
....*....|....*....|....*....|.
gi 2462558775 788 RTVKRKLLEEEEKNARLQKELGDVQGHGRVV 818
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAY 536
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
620-821 |
2.27e-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: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 620 EVQEMLKVARAEKDLLELSCnELRQELLKANGEIKHVSSLLAKV-----EKDYSYLKEICDHQAEQLSRtslkLQEKASE 694
Cdd:COG4913 239 RAHEALEDAREQIELLEPIR-ELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELAR----LEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 695 SDAEIKDMKETIFELEDQVEQHRAVKLHN-NQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAV 773
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462558775 774 VVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVVTSR 821
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
411-808 |
2.37e-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: 51.51 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 411 LASLTEKIQKmeeNHHSTAEELQATLQELSD-QQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENE------K 483
Cdd:TIGR00618 181 LALMEFAKKK---SLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREaqeeqlK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 484 LMNLLQERVKNEEPTTQEGKIIELEQKCTGI-------------LEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMI 550
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAVLEETQERINRarkaaplaahikaVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 551 KRLKEENEKLNEFLELERHNnnmmAKTLEECRVTLEGLKMENgSLKSHLQGEKQKATEASAVEQTAesCEVQEMLKVARA 630
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHI----RDAHEVATSIREISCQQH-TLTQHIHTLQQQKTTLTQKLQSL--CKELDILQREQA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 631 EKDLLELSCNELRQELLKANGEI----KHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQ-----EKASESDAEIKD 701
Cdd:TIGR00618 411 TIDTRTSAFRDLQGQLAHAKKQQelqqRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQqlqtkEQIHLQETRKKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 702 MKETIfeLEDQVEQHRAVK---LHNNQ-------------LISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRF 765
Cdd:TIGR00618 491 VVLAR--LLELQEEPCPLCgscIHPNParqdidnpgpltrRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEI 568
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2462558775 766 QADLQTAVVVANDIKCEAQQeLRTVKRKLLEEEEKNARLQKEL 808
Cdd:TIGR00618 569 QQSFSILTQCDNRSKEDIPN-LQNITVRLQDLTEKLSEAEDML 610
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
548-808 |
5.77e-06 |
|
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: 50.12 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 548 EMIKRLKEENEKLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATE-ASAVEQTAESCEVQEMLK 626
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDlRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 627 varaeKDLLELS---CNELRQELLKANGEIKHVSSLLAKVEKDYSylKEIcdHQAEQLSRTSLK-----LQEKASESDAE 698
Cdd:pfam15921 162 -----EDMLEDSntqIEQLRKMMLSHEGVLQEIRSILVDFEEASG--KKI--YEHDSMSTMHFRslgsaISKILRELDTE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 699 IKDMKETIFELEDQVEQHRA---------VKLHNN---QLISELESSVIKLEE-------QKSDLERQLKTLTKQMKEET 759
Cdd:pfam15921 233 ISYLKGRIFPVEDQLEALKSesqnkiellLQQHQDrieQLISEHEVEITGLTEkassarsQANSIQSQLEIIQEQARNQN 312
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2462558775 760 EEWRRFQADLQTAVvvandikCEAQQELRTVKRKLleeEEKNARLQKEL 808
Cdd:pfam15921 313 SMYMRQLSDLESTV-------SQLRSELREAKRMY---EDKIEELEKQL 351
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
408-692 |
7.07e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 7.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 408 ELSLASLTEKIQKMEEnhhsTAEELQATLQELSDQqqmVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNL 487
Cdd:COG1196 238 EAELEELEAELEELEA----ELEELEAELAELEAE---LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 488 LQERVKNEEptTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELE 567
Cdd:COG1196 311 RRELEERLE--ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 568 ---RHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELScNELRQ 644
Cdd:COG1196 389 leaLRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL-ELLAE 467
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2462558775 645 ELLKANGEIKHVSSLLAKVEKDYS--YLKEICDHQAEQLSRTSLKLQEKA 692
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAArlLLLLEAEADYEGFLEGVKAALLLA 517
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
429-814 |
1.08e-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: 49.20 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 429 AEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhqhreRAEQLSQENEKLMNLLQErvkneEPTTQEGKIIELE 508
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHL--------QETRKKAVVLARLLELQE-----EPCPLCGSCIHPN 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 509 QKCTGILEQGRFER--EKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKL-NEFLELERHNN------NMMAKTLE 579
Cdd:TIGR00618 515 PARQDIDNPGPLTRrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIqQSFSILTQCDNrskediPNLQNITV 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 580 ECRVTLEGLKMENGSLKSHLQGEKQKATEASA---VEQTAESCEVQEMLKVARAEKDLLELSCNELRQELL--------- 647
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHALLRKLQPEQDlqdVRLHLQQCSQELALKLTALHALQLTLTQERVREHALsirvlpkel 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 648 ---------KANGEIKHVSSLLAKVEKDYSYLKEICDH------QAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQ 712
Cdd:TIGR00618 675 lasrqlalqKMQSEKEQLTYWKEMLAQCQTLLRELETHieeydrEFNEIENASSSLGSDLAAREDALNQSLKELMHQART 754
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 713 VEQHRAVKLHNNqliSELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKR 792
Cdd:TIGR00618 755 VLKARTEAHFNN---NEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEE 831
|
410 420
....*....|....*....|..
gi 2462558775 793 KLLEEEEKNARLQKELGDVQGH 814
Cdd:TIGR00618 832 QFLSRLEEKSATLGEITHQLLK 853
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
392-807 |
1.43e-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: 48.95 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 392 KSSKCSTAGSSPNSVSELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTA----------ENEKLVDEKT 461
Cdd:pfam05483 339 ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKfknnkeveleELKKILAEDE 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 462 ILETSFHQHRERAEQLSQENEKLMNLLQERVKN-EEPTTQEGKIIELEQKCTGILEQGR--FEREKLLNIQQQLTCSLRK 538
Cdd:pfam05483 419 KLLDEKKQFEKIAEELKGKEQELIFLLQAREKEiHDLEIQLTAIKTSEEHYLKEVEDLKteLEKEKLKNIELTAHCDKLL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 539 VEEEN--QGALEMIKRLKEENEKLNEFLELERHnnnmMAKTLEECRVTLEGLKMENGSLKSHLqgeKQKATEASAVEQTA 616
Cdd:pfam05483 499 LENKEltQEASDMTLELKKHQEDIINCKKQEER----MLKQIENLEEKEMNLRDELESVREEF---IQKGDEVKCKLDKS 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 617 ESCEVQEMLKVARAEKDL--LELSCNELRQELLKANGEIKHVSSLLAKVEKDYSY------LKEICDHQAE-QLSRTSLK 687
Cdd:pfam05483 572 EENARSIEYEVLKKEKQMkiLENKCNNLKKQIENKNKNIEELHQENKALKKKGSAenkqlnAYEIKVNKLElELASAKQK 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 688 LQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVI-KLEEQKSDLERQLKTLTKQMKEETEEWRRFQ 766
Cdd:pfam05483 652 FEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhKIAEMVALMEKHKHQYDKIIEERDSELGLYK 731
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2462558775 767 ADLQTAVVVANDIKCE---AQQELRTVKRKLLEEEEKNARLQKE 807
Cdd:pfam05483 732 NKEQEQSSAKAALEIElsnIKAELLSLKKQLEIEKEEKEKLKME 775
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
603-812 |
2.41e-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: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 603 KQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLS 682
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 683 RTSlklqekASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEw 762
Cdd:COG3883 97 RSG------GSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA- 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462558775 763 rrfQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQ 812
Cdd:COG3883 170 ---KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
430-756 |
2.45e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 430 EELQATLQELSDQQQMVQELTAENEKLVDEKTILETsfhQHRERAEQLSQENEKLMNLLQER-VKNEEPTTQEGKIIELE 508
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES---ENSEKQRELEEKQNEIEKLKKENqSYKQEIKNLESQINDLE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 509 QKctgileqgrFEREKLLNiqQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFL-ELERHNN------NMMAKTLEEC 581
Cdd:TIGR04523 398 SK---------IQNQEKLN--QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIkDLTNQDSvkeliiKNLDNTRESL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 582 RVTLEGLKMENGSLKSHLQGEKQ--KATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIkhvSSL 659
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKelKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI---SDL 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 660 LAKVEKDYSYLKEicdhqaEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEE 739
Cdd:TIGR04523 544 EDELNKDDFELKK------ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
|
330
....*....|....*..
gi 2462558775 740 QKSDLERQLKTLTKQMK 756
Cdd:TIGR04523 618 ELEKAKKENEKLSSIIK 634
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
408-797 |
4.63e-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: 47.04 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 408 ELSLASLTEKIQKMEENHHSTAEeLQATLQELsdqQQMVQELTAENEKLVD-EKTILE-TSFHQHRERA-EQLSQENEKL 484
Cdd:pfam15921 447 ERQMAAIQGKNESLEKVSSLTAQ-LESTKEML---RKVVEELTAKKMTLESsERTVSDlTASLQEKERAiEATNAEITKL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 485 MNLLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNI-QQQLTCSLRKVEEENQGA----LEMIKRLKEENEK 559
Cdd:pfam15921 523 RSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEIlRQQIENMTQLVGQHGRTAgamqVEKAQLEKEINDR 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 560 LNEFLELERHNNNMMAKTLE-ECRVtleglkmengslkSHLQGEKQKATEASAveqtaescevqEMLKVARaekdllels 638
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRElEARV-------------SDLELEKVKLVNAGS-----------ERLRAVK--------- 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 639 cnELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRA 718
Cdd:pfam15921 650 --DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMK 727
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462558775 719 VKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQeLRTVKRKLLEE 797
Cdd:pfam15921 728 VAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEV-LRSQERRLKEK 805
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
437-795 |
5.02e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.75 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 437 QELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLM-NLLQERvkneeptTQEGKIIELeqkctgiL 515
Cdd:PRK04778 105 HEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRkSLLANR-------FSFGPALDE-------L 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 516 EqgrferEKLLNIQQQLTcslRKVEEENQG----ALEMIKRLKEENEKLNEFLE----LERHNNNMMAKTLEECRVTLEG 587
Cdd:PRK04778 171 E------KQLENLEEEFS---QFVELTESGdyveAREILDQLEEELAALEQIMEeipeLLKELQTELPDQLQELKAGYRE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 588 LKMENGSLKsHLQGEKqkateasaveqtaescEVQEML-KVARAEKDLLELSCNELRQELLKANGEIKHVSSLLakvEKD 666
Cdd:PRK04778 242 LVEEGYHLD-HLDIEK----------------EIQDLKeQIDENLALLEELDLDEAEEKNEEIQERIDQLYDIL---ERE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 667 YSYLKEIcDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQK---SD 743
Cdd:PRK04778 302 VKARKYV-EKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEiaySE 380
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2462558775 744 LERQLKTLTKQMKEETEEWRRFQADLQT---AVVVANDIKCEAQQELRTVKRKLL 795
Cdd:PRK04778 381 LQEELEEILKQLEEIEKEQEKLSEMLQGlrkDELEAREKLERYRNKLHEIKRYLE 435
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
429-807 |
5.41e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 429 AEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhqHRERAEQLSQENEKLMNLLQERVKNEEPTTQEgkiiELE 508
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE-----EKKKADEAKKKAEEAKKADEAKKKAEEAKKAE----EAK 1463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 509 QKCTgilEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNNNMMAKTLEECRVTLEGL 588
Cdd:PTZ00121 1464 KKAE---EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK 1540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 589 KMEngslkshlqgEKQKATEASAVEQTAESCEVQEMLKVARAEKD--LLELSCNELRQELLKANGEIKHVSSLLAKVEKD 666
Cdd:PTZ00121 1541 KAE----------EKKKADELKKAEELKKAEEKKKAEEAKKAEEDknMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 667 YSYLKEICDHQAEQLSrtslKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLE- 745
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELK----KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEd 1686
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462558775 746 ---------------RQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKN--ARLQKE 807
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 ... |
516-812 |
5.97e-05 |
|
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: 46.89 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 516 EQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNNNMMAKT----LEECRVTLEGLKME 591
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDylklNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 592 NGSLKSHLQGEKQKATEASAVEQTAESCEVQEMlKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKdysylk 671
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEK-KLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK------ 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 672 eicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQlKTL 751
Cdd:pfam02463 322 -----EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL-KEE 395
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462558775 752 TKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQ 812
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
550-808 |
6.83e-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: 46.59 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 550 IKRLKEENEKLNEFLELErhnnnmmaKTLEECRVTLEGLKMEngSLKSHLqgEKQKATEASAVEQ----TAESCEVQEML 625
Cdd:TIGR02168 202 LKSLERQAEKAERYKELK--------AELRELELALLVLRLE--ELREEL--EELQEELKEAEEEleelTAELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 626 KVARAEKDLLELSCNELRQELLKANGEI-------KHVSSLLAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAE 698
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALANEIsrleqqkQILRERLANLERQLEELEA----QLEELESKLDELAEELAELEEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 699 IKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQ----------MKEETEEWRRFQAD 768
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEierlearlerLEDRRERLQQEIEE 425
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2462558775 769 LQTAVVVANdiKCEAQQELRTVKRKLLEEEEKNARLQKEL 808
Cdd:TIGR02168 426 LLKKLEEAE--LKELQAELEELEEELEELQEELERLEEAL 463
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
641-823 |
1.69e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 641 ELRQELLKANGEIKHVSSLLAKVEKDYSYLKEIcdhqaeqlsRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAvk 720
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQER---------REALQRLAEYSWDEIDVASAEREIAELEAELERLDA-- 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 721 lhNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEK 800
Cdd:COG4913 683 --SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180
....*....|....*....|...
gi 2462558775 801 NARLQKELGDVQGHGRVVTSRAA 823
Cdd:COG4913 761 DAVERELRENLEERIDALRARLN 783
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
418-708 |
1.86e-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: 45.34 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 418 IQKMEENHHSTAEELQATLQELSDQQQMvQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQERVKNEEP 497
Cdd:TIGR00618 600 TEKLSEAEDMLACEQHALLRKLQPEQDL-QDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASR 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 498 TTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFL-ELERHNNNMMAK 576
Cdd:TIGR00618 679 QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLkELMHQARTVLKA 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 577 TLEECRVTLEGLKME--NGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIK 654
Cdd:TIGR00618 759 RTEAHFNNNEEVTAAlqTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLE 838
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2462558775 655 HVSSLLAKVEKDYSYLKEiCDHQAEQLSRTSLKLQEKasESDAEIKDMKETIFE 708
Cdd:TIGR00618 839 EKSATLGEITHQLLKYEE-CSKQLAQLTQEQAKIIQL--SDKLNGINQIKIQFD 889
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
430-817 |
2.50e-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: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 430 EELQATLQELsdqqQMVQELTAENEKLVDEKtiletsfhqhRERAEQLSQENEKLMNL--LQERVKNEEPTTQEGKIIEL 507
Cdd:TIGR02169 170 RKKEKALEEL----EEVEENIERLDLIIDEK----------RQQLERLRREREKAERYqaLLKEKREYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 508 EQKctgiLEQGRFEREKLLNIQQQLTcslRKVEEENQGALEMIKRLKEENEKLNEFLELERhnnNMMAKTLEECRVTLEG 587
Cdd:TIGR02169 236 ERQ----KEAIERQLASLEEELEKLT---EEISELEKRLEEIEQLLEELNKKIKDLGEEEQ---LRVKEKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 588 LKMENGSLKSHLQ--GEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAK-VE 664
Cdd:TIGR02169 306 LERSIAEKERELEdaEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAEtRD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 665 KDYSYLKEICD--HQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKS 742
Cdd:TIGR02169 386 ELKDYREKLEKlkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462558775 743 DLERQLKTLTKQMKEETEEWRRFQADLQTAvvvandiKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRV 817
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQRELAEA-------EAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSV 533
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
481-812 |
2.61e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.68 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 481 NEKLMNLLQERVKNEEPTTQEGKiieLEQKCTGILEQGRFEREKL-LNIQQQLTCSLRKVEEENQgalEMIKRLKEENEK 559
Cdd:COG5022 775 QVIQHGFRLRRLVDYELKWRLFI---KLQPLLSLLGSRKEYRSYLaCIIKLQKTIKREKKLRETE---EVEFSLKAEVLI 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 560 LNEFLELERHNnnmMAKTLEECRVTLEGL-KMENgsLKSHLQGEKQKATEASAVEQTAEscevqemlkvaRAEKDLLELS 638
Cdd:COG5022 849 QKFGRSLKAKK---RFSLLKKETIYLQSAqRVEL--AERQLQELKIDVKSISSLKLVNL-----------ELESEIIELK 912
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 639 CNElrQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTsLKLQEkasesdaEIKDMKETIFELEDQVEQHRA 718
Cdd:COG5022 913 KSL--SSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPEL-NKLHE-------VESKLKETSEEYEDLLKKSTI 982
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 719 VKLHNNQLISELESSVIKLEEQKSDLERqLKTLTKQMKEEteewRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEE 798
Cdd:COG5022 983 LVREGNKANSELKNFKKELAELSKQYGA-LQESTKQLKEL----PVEVAELQSASKIISSESTELSILKPLQKLKGLLLL 1057
|
330
....*....|....
gi 2462558775 799 EKNaRLQKELGDVQ 812
Cdd:COG5022 1058 ENN-QLQARYKALK 1070
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
471-807 |
3.84e-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: 44.19 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 471 RERAEQLSQENEKLMNLLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMI 550
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 551 KRLKEENEKLNEFLELERHNNNMMAKTLEEcrvtlEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARA 630
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEK-----KLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 631 EKDLLELSCNELRQELLKANGEIKhvsSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELE 710
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIK---REAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 711 DQVEQHRAVKLHNNQLISELESSVI--KLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELR 788
Cdd:pfam02463 404 EKEAQLLLELARQLEDLLKEEKKEEleILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQ 483
|
330
....*....|....*....
gi 2462558775 789 TVKRKLLEEEEKNARLQKE 807
Cdd:pfam02463 484 EQLELLLSRQKLEERSQKE 502
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
413-757 |
4.08e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 413 SLTEKIQKMEENH---HSTAEELQATLQE----LSDQQQMVQELTAE----NEKLVDEKTILETSFHQHRERAEQLSQEN 481
Cdd:PRK02224 346 SLREDADDLEERAeelREEAAELESELEEareaVEDRREEIEELEEEieelRERFGDAPVDLGNAEDFLEELREERDELR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 482 EKLMNL------LQERVKNEEPTTQEGKIIELEQKCTG-----ILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEM- 549
Cdd:PRK02224 426 EREAELeatlrtARERVEEAEALLEAGKCPECGQPVEGsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLv 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 550 -----IKRLKEENEKLNEFLELERhnnnmmaKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEAsavEQTAEscEVQEM 624
Cdd:PRK02224 506 eaedrIERLEERREDLEELIAERR-------ETIEEKRERAEELRERAAELEAEAEEKREAAAEA---EEEAE--EAREE 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 625 LKvaraekdllelSCNELRQELLKANGEIKHVSSLLAKVEKdysylkeiCDHQAEQLSRTSLKLQEKASESDAEIKDMKE 704
Cdd:PRK02224 574 VA-----------ELNSKLAELKERIESLERIRTLLAAIAD--------AEDEIERLREKREALAELNDERRERLAEKRE 634
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462558775 705 TIFELEDQVEQHRAVKLHNN-----QLISELESSVIKLEEQKSDLERQLKTLTKQMKE 757
Cdd:PRK02224 635 RKRELEAEFDEARIEEAREDkeraeEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
412-771 |
5.30e-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: 43.88 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 412 ASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQER 491
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 492 VKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTC------------SLRKVEEENQGALEMIKRLKEENEK 559
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAklqgsdldrtvqQVNQEKQEKQHELDTVVSKIELNRK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 560 LNE-----FLELERHNNNM------MAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAES--CEVQEMLK 626
Cdd:TIGR00606 851 LIQdqqeqIQHLKSKTNELkseklqIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKdqQEKEELIS 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 627 VARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEI-----------CDHQAEQLSR---------TSL 686
Cdd:TIGR00606 931 SKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETelntvnaqleeCEKHQEKINEdmrlmrqdiDTQ 1010
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 687 KLQEKASESDAEIKDMKETIFELEDQVEQHraVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQ 766
Cdd:TIGR00606 1011 KIQERWLQDNLTLRKRENELKEVEEELKQH--LKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFK 1088
|
....*
gi 2462558775 767 ADLQT 771
Cdd:TIGR00606 1089 KELRE 1093
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
521-811 |
5.84e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 521 EREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNnnmmAKTLEECRVTLEGLKMENGSLKSHLQ 600
Cdd:PRK03918 180 RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKE----VKELEELKEEIEELEKELESLEGSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 601 G--EKQKATEASAVEQTAESCEVQEmlKVARAEK-DLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDhQ 677
Cdd:PRK03918 256 KleEKIRELEERIEELKKEIEELEE--KVKELKElKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-E 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 678 AEQLSRTSLKLQEKASESDAEIKDMK------ETIFELEDQVEQHRAVKLHNNqlISELESSVIKLEEQKSDLERQLKTL 751
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEELEerhelyEEAKAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKI 410
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462558775 752 TkqmkEETEEWRRFQADLQTAVvvaNDIKcEAQQELRTVKRKLLEEEEKN--ARLQKELGDV 811
Cdd:PRK03918 411 T----ARIGELKKEIKELKKAI---EELK-KAKGKCPVCGRELTEEHRKEllEEYTAELKRI 464
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
411-813 |
6.05e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 411 LASLTEKIQKMEENHH---STAEELQATLQELSDQQQMVQEltaENEKLVDEKTILETSFHQHRERAEQLSQENEKL--- 484
Cdd:TIGR02169 352 RDKLTEEYAELKEELEdlrAELEEVDKEFAETRDELKDYRE---KLEKLKREINELKRELDRLQEELQRLSEELADLnaa 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 485 -------MNLLQERV--KNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCS-------------------- 535
Cdd:TIGR02169 429 iagieakINELEEEKedKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLqrelaeaeaqaraseervrg 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 536 ---------------------LRKVEEENQGALEM--------------------IKRLKEENEKLNEFLELER------ 568
Cdd:TIGR02169 509 graveevlkasiqgvhgtvaqLGSVGERYATAIEVaagnrlnnvvveddavakeaIELLKRRKAGRATFLPLNKmrderr 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 569 -------------------------------HNNNMMAKTLEECR--------VTLEGL------KMENGSLKSHLQGEK 603
Cdd:TIGR02169 589 dlsilsedgvigfavdlvefdpkyepafkyvFGDTLVVEDIEAARrlmgkyrmVTLEGElfeksgAMTGGSRAPRGGILF 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 604 QKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSR 683
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 684 TSLKLQEKASESD---AEIKDMKETIFELEDQVEQHRAVKLHnnQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETE 760
Cdd:TIGR02169 749 LEQEIENVKSELKeleARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTL 826
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462558775 761 EWRRFQADLQTAVVVANDIK------CEAQQELRTVKRKLLEEEEKNA----RLQKELGDVQG 813
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKeqiksiEKEIENLNGKKEELEEELEELEaalrDLESRLGDLKK 889
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
396-637 |
6.39e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 396 CSTAGSSPNSVSELS--LASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRER 473
Cdd:COG4942 12 ALAAAAQADAAAEAEaeLEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 474 AEQLSQENEKLMNLLQERVKNeepttqegkiieleqkctgILEQGRFEREKLLNIQQQLTCSLRkveeenqgALEMIKRL 553
Cdd:COG4942 92 IAELRAELEAQKEELAELLRA-------------------LYRLGRQPPLALLLSPEDFLDAVR--------RLQYLKYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 554 KEENEKLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKD 633
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
....
gi 2462558775 634 LLEL 637
Cdd:COG4942 225 LEAL 228
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
575-780 |
9.21e-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: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 575 AKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAES--CEVQEMLKVARAEKDLLELSCNELRQELLKANGE 652
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERriAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 653 IKHVSSLLAKV-------------------------EKDYSYLKEICDH---QAEQLSRTSLKLQEKASESDAEIKDMKE 704
Cdd:COG4942 99 LEAQKEELAELlralyrlgrqpplalllspedfldaVRRLQYLKYLAPArreQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462558775 705 TIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIK 780
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
575-807 |
1.05e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 575 AKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAEscevqEMLKVARAEKDLLELscNELRQELLKANGEIK 654
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-----DEIDVASAEREIAEL--EAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 655 HVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASE--------SDAEIKDMKETIFELEDQVEQHrAVKLHNNQL 726
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEldelqdrlEAAEDLARLELRALLEERFAAA-LGDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 727 ISELESSVIKLEEQKSDLERQLktlTKQMKEETEEWRRFQADLQTAVVVANDIkceaQQELRTVKRKLLEE-EEKNARLQ 805
Cdd:COG4913 768 RENLEERIDALRARLNRAEEEL---ERAMRAFNREWPAETADLDADLESLPEY----LALLDRLEEDGLPEyEERFKELL 840
|
..
gi 2462558775 806 KE 807
Cdd:COG4913 841 NE 842
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
422-813 |
1.08e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 422 EENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFH----------QHRERAEQLSQENEKLMNLLQER 491
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQaetelcaeaeEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 492 VKNEEPTTQ---------EGKIIELEQKctgiLEQGRFEREKLLNIQQQLTCSLRKVEEE------------------NQ 544
Cdd:pfam01576 84 LEEEEERSQqlqnekkkmQQHIQDLEEQ----LDEEEAARQKLQLEKVTTEAKIKKLEEDillledqnsklskerkllEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 545 GALEMIKRLKEENEKLNEFLELeRHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEkqkATEASavEQTAESCEVQEM 624
Cdd:pfam01576 160 RISEFTSNLAEEEEKAKSLSKL-KNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGE---STDLQ--EQIAELQAQIAE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 625 LKVARAEKDllelscNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEIC-DHQAEQLSRTSLKLQEK--ASESDAEIKD 701
Cdd:pfam01576 234 LRAQLAKKE------EELQAALARLEEETAQKNNALKKIRELEAQISELQeDLESERAARNKAEKQRRdlGEELEALKTE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 702 MKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKC 781
Cdd:pfam01576 308 LEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENA 387
|
410 420 430
....*....|....*....|....*....|..
gi 2462558775 782 EAQQELRTVKRKLLEEEEKNARLQKELGDVQG 813
Cdd:pfam01576 388 ELQAELRTLQQAKQDSEHKRKKLEGQLQELQA 419
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
602-808 |
1.08e-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: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 602 EKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQL 681
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 682 SRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQ---LKTLTKQMKEE 758
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAEraeLEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462558775 759 TEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKEL 808
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
407-690 |
1.15e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 407 SELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRER---AEQLSQENEK 483
Cdd:pfam15921 494 SERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKdkvIEILRQQIEN 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 484 LMNL-----------------LQERVKNEEPTTQEGKII---------ELEQKCTGIleqgRFEREKLLNIQQQLTCSLR 537
Cdd:pfam15921 574 MTQLvgqhgrtagamqvekaqLEKEINDRRLELQEFKILkdkkdakirELEARVSDL----ELEKVKLVNAGSERLRAVK 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 538 KVEEENQGALEMIKRLKEENEKLNEFLELERHNnnmMAKTLEECRVTLEGLKMENGSLKSHLQGEK-------------- 603
Cdd:pfam15921 650 DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN---FRNKSEEMETTTNKLKMQLKSAQSELEQTRntlksmegsdgham 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 604 ------QKATEASAVEQTAESCEVQ---EMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEIC 674
Cdd:pfam15921 727 kvamgmQKQITAKRGQIDALQSKIQfleEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKV 806
|
330
....*....|....*.
gi 2462558775 675 DHQAEQLSRTSLKLQE 690
Cdd:pfam15921 807 ANMEVALDKASLQFAE 822
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
592-758 |
1.36e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 592 NGSLKSHLQGEKQKATEASAVEQTAEScEVQEMLKVARAE-KDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYL 670
Cdd:PRK12705 18 LGVLVVLLKKRQRLAKEAERILQEAQK-EAEEKLEAALLEaKELLLRERNQQRQEARREREELQREEERLVQKEEQLDAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 671 KEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRavklhNNQLISELEssvikleeqkSDLERQLKT 750
Cdd:PRK12705 97 AEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQA-----RKLLLKLLD----------AELEEEKAQ 161
|
....*...
gi 2462558775 751 LTKQMKEE 758
Cdd:PRK12705 162 RVKKIEEE 169
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
606-812 |
1.59e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 606 ATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRTS 685
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA----ELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 686 LKLQEKASESDAEIKDM------------------KETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQ 747
Cdd:COG4942 93 AELRAELEAQKEELAELlralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462558775 748 LKTLTKQMKEETEEwrrfQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQ 812
Cdd:COG4942 173 RAELEALLAELEEE----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
431-774 |
2.00e-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: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 431 ELQATLQELSDQ-QQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQERVKNEEPTTQEGKIIE-LE 508
Cdd:pfam01576 226 ELQAQIAELRAQlAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEaLK 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 509 QKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEE----NQGALEMIKRLKEENEKLNEFLELERHNNnmmaKTLEECRVT 584
Cdd:pfam01576 306 TELEDTLDTTAAQQELRSKREQEVTELKKALEEEtrshEAQLQEMRQKHTQALEELTEQLEQAKRNK----ANLEKAKQA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 585 LEGlkmENGSLKSHLQGEKQKATEASAVEQTAEScEVQE-MLKVARAEKDLlelscNELRQELLKANGEIKHVSSLLAKV 663
Cdd:pfam01576 382 LES---ENAELQAELRTLQQAKQDSEHKRKKLEG-QLQElQARLSESERQR-----AELAEKLSKLQSELESVSSLLNEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 664 EKDYSYLKEICDHQAEQLSRTSLKLQEKASES---DAEIKDMKETIFELEDQVEQH--------RAVKLHNNQL------ 726
Cdd:pfam01576 453 EGKNIKLSKDVSSLESQLQDTQELLQEETRQKlnlSTRLRQLEDERNSLQEQLEEEeeakrnveRQLSTLQAQLsdmkkk 532
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2462558775 727 ISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEW-------RRFQADLQTAVV 774
Cdd:pfam01576 533 LEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYdklektkNRLQQELDDLLV 587
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
408-761 |
2.08e-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: 41.88 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 408 ELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNL 487
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 488 LQERVKNEEPTTQEGKIIELEQKctgileqgrferEKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELE 567
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELAL------------KLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSE 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 568 RHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQgEKQKATEASAVEQTAESCEVQEMLKVARAEKDllelscnelrqELL 647
Cdd:TIGR00618 689 KEQLTYWKEMLAQCQTLLRELETHIEEYDREFN-EIENASSSLGSDLAAREDALNQSLKELMHQAR-----------TVL 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 648 KANGEIKHVSSLLAKVE----KDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDmKETIFELEDQVEQHRAVKLHN 723
Cdd:TIGR00618 757 KARTEAHFNNNEEVTAAlqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPS-DEDILNLQCETLVQEEEQFLS 835
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2462558775 724 nqLISELESSVIKLEEQKSDLE---RQLKTLTKQMKEETEE 761
Cdd:TIGR00618 836 --RLEEKSATLGEITHQLLKYEecsKQLAQLTQEQAKIIQL 874
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
410-808 |
2.26e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 410 SLASLTEKIQKMEE-NHHSTAEELQATLQELSDQqqmVQELTAENEKLVDEKTILETSFHQHRERAEQLS---QENEKLM 485
Cdd:PRK02224 188 SLDQLKAQIEEKEEkDLHERLNGLESELAELDEE---IERYEEQREQARETRDEADEVLEEHEERREELEtleAEIEDLR 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 486 NLLQERVKN-----EEPTTQEGKIIELEQKCTGILEQGRFE----------REKLLNIQQQLTCSLRKVEEENQGALEMI 550
Cdd:PRK02224 265 ETIAETEREreelaEEVRDLRERLEELEEERDDLLAEAGLDdadaeavearREELEDRDEELRDRLEECRVAAQAHNEEA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 551 KRLKEENEKLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLkshlqgEKQKATEASAVEQTAESCE-VQEMLKVAR 629
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL------EEEIEELRERFGDAPVDLGnAEDFLEELR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 630 AEKDLLELSCNELRQELLKANGEIKHVSSLLAKVE--------KDYSYLKEICDHqaeqlsrtslklQEKASESDAEIKD 701
Cdd:PRK02224 419 EERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvEGSPHVETIEED------------RERVEELEAELED 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 702 MKETIFELEDQVEqhRAVKLhnnqliSELESSVIKLEEQKSDLERQL---KTLTKQMKEETEEWRRFQADLQTAVVVAND 778
Cdd:PRK02224 487 LEEEVEEVEERLE--RAEDL------VEAEDRIERLEERREDLEELIaerRETIEEKRERAEELRERAAELEAEAEEKRE 558
|
410 420 430
....*....|....*....|....*....|
gi 2462558775 779 IKCEAQQELRTVKRKLLEEEEKNARLQKEL 808
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAELNSKLAELKERI 588
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
476-808 |
2.32e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.63 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 476 QLSQENEKLMNL---LQERVKNEEPTTQEG-KIIELEQKCtgiLEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIK 551
Cdd:pfam05483 82 KLYKEAEKIKKWkvsIEAELKQKENKLQENrKIIEAQRKA---IQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 552 RLKE----ENEKLNEFlELERH---------NNNM--MAKTLEECRVTLEGLKME-NGSLK------SHLQGEKQKATEA 609
Cdd:pfam05483 159 LLKEtcarSAEKTKKY-EYEREetrqvymdlNNNIekMILAFEELRVQAENARLEmHFKLKedhekiQHLEEEYKKEIND 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 610 SAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEIcdhqaeQLSRTSLKLQ 689
Cdd:pfam05483 238 KEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDI------KMSLQRSMST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 690 EKASESDAEI--KDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQA 767
Cdd:pfam05483 312 QKALEEDLQIatKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSS 391
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2462558775 768 DLQTAVVVANDIKCEAqQELRTV---KRKLLEEEEKNARLQKEL 808
Cdd:pfam05483 392 ELEEMTKFKNNKEVEL-EELKKIlaeDEKLLDEKKQFEKIAEEL 434
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
465-803 |
2.37e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 465 TSFHQHRERAE-QLSQENEKLMNLLQERVKNEEPTT--QEGKIIEL---EQKCTGILEQGRFER----EKLLNIQQQLTC 534
Cdd:PLN02939 91 TSSDDDHNRASmQRDEAIAAIDNEQQTNSKDGEQLSdfQLEDLVGMiqnAEKNILLLNQARLQAledlEKILTEKEALQG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 535 SLRKVEEENQGALEMIKRLKEEN---EKLNEFLELERHNNNMMAKTLEECRVT----LEGLKMENGSLKSHLQGEKqkaT 607
Cdd:PLN02939 171 KINILEMRLSETDARIKLAAQEKihvEILEEQLEKLRNELLIRGATEGLCVHSlskeLDVLKEENMLLKDDIQFLK---A 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 608 EASAVEQTAESCEVQEmlkvarAEKDLLELSCNELRQELLKANGEIKHVSSL-----LAKVEKdysyLKEICDHQAEQLS 682
Cdd:PLN02939 248 ELIEVAETEERVFKLE------KERSLLDASLRELESKFIVAQEDVSKLSPLqydcwWEKVEN----LQDLLDRATNQVE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 683 RTSLKLQEKasesdaeiKDMKETIFELEDQVEqhravklhnnqliselESSVIKLEEQKSDLerqlktLTKQMKEETEEW 762
Cdd:PLN02939 318 KAALVLDQN--------QDLRDKVDKLEASLK----------------EANVSKFSSYKVEL------LQQKLKLLEERL 367
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2462558775 763 RRFQADLQTAVVVANDIKCEAQQELrtvkRKLLEEEEKNAR 803
Cdd:PLN02939 368 QASDHEIHSYIQLYQESIKEFQDTL----SKLKEESKKRSL 404
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
411-809 |
2.44e-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: 41.57 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 411 LASLTEKIQKMEEN-HHSTAEELQATLQELSDQQQMVQELTAENEklvdektilETSFHQHRERAEQLSQENEKLMNLLQ 489
Cdd:TIGR00606 593 LAKLNKELASLEQNkNHINNELESKEEQLSSYEDKLFDVCGSQDE---------ESDLERLKEEIEKSSKQRAMLAGATA 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 490 ERVKNEEPTTQEgkiielEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERH 569
Cdd:TIGR00606 664 VYSQFITQLTDE------NQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQS 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 570 NNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESC--------EVQEMLK---------VARAEK 632
Cdd:TIGR00606 738 IIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCltdvtimeRFQMELKdverkiaqqAAKLQG 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 633 DLLELSCNELRQELLKANGEIKHVSS---LLAKVEKDY--------SYLKEICDHQAeQLSRTSLKLQEKASESDAEIKD 701
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQEKQHELDTVVSkieLNRKLIQDQqeqiqhlkSKTNELKSEKL-QIGTNLQRRQQFEEQLVELSTE 896
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 702 MKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAvvvANDIKC 781
Cdd:TIGR00606 897 VQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDG---KDDYLK 973
|
410 420
....*....|....*....|....*...
gi 2462558775 782 EAQQELRTVKRKLLEEEEKNARLQKELG 809
Cdd:TIGR00606 974 QKETELNTVNAQLEECEKHQEKINEDMR 1001
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
515-768 |
2.45e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.95 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 515 LEQGRFEREKLLniqQQLTCSLRKVEEENQGALEMIKRLKEENEKLN-EFLELERHNNNMMAKTLEE-CRVTLEGLKMEN 592
Cdd:pfam15905 85 LVQERGEQDKRL---QALEEELEKVEAKLNAAVREKTSLSASVASLEkQLLELTRVNELLKAKFSEDgTQKKMSSLSMEL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 593 GSLKSHLQGeKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQE----------LLKANGEIKHVSSLLAK 662
Cdd:pfam15905 162 MKLRNKLEA-KMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEkieeksetekLLEYITELSCVSEQVEK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 663 VEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEdqveqhravklhnnqliSELESSVIKLEEQKS 742
Cdd:pfam15905 241 YKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLE-----------------SEKEELLREYEEKEQ 303
|
250 260
....*....|....*....|....*.
gi 2462558775 743 DLERQLKTLTKQMKEETEEWRRFQAD 768
Cdd:pfam15905 304 TLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
724-807 |
3.44e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 724 NQLISELESSVIKLEEQKSDLE---RQLKTLTKQMKEETEEWR-RFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEE 799
Cdd:PRK00409 519 NELIASLEELERELEQKAEEAEallKEAEKLKEELEEKKEKLQeEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQK 598
|
....*...
gi 2462558775 800 KNARLQKE 807
Cdd:PRK00409 599 GGYASVKA 606
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
9-212 |
4.19e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 40.92 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 9 GAGREPRGHLIQSCYVID---RRNRGSERDRPTKSSMRSAAKPwnpaiRAGGHGPDRVRPLPAASSGMKSSKSSTSLAFE 85
Cdd:PHA03307 202 ASPRPPRRSSPISASASSpapAPGRSAADDAGASSSDSSSSES-----SGCGWGPENECPLPRPAPITLPTRIWEASGWN 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 86 SRLSRLKRASSEDTLNKPGSTAASGVVRLKKTATAGAISELTESRLRSGTGAfttTKRTGiPAPREFSVTVSRERSVPRG 165
Cdd:PHA03307 277 GPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSS---TSSSS-ESSRGAAVSPGPSPSRSPS 352
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462558775 166 PSNPRKSVSSPTSSNTPTPTKHLRTPS-TKPKQENEGGEKAALESQVR 212
Cdd:PHA03307 353 PSRPPPPADPSSPRKRPRPSRAPSSPAaSAGRPTRRRARAAVAGRARR 400
|
|
| PRK10884 |
PRK10884 |
SH3 domain-containing protein; Provisional |
688-812 |
4.45e-03 |
|
SH3 domain-containing protein; Provisional
Pssm-ID: 182809 [Multi-domain] Cd Length: 206 Bit Score: 39.25 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 688 LQEKASESDAEIKDMKEtifeledqveqhRAVKLHNNQLiseleSSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQA 767
Cdd:PRK10884 59 LQVNANTNYAQIRDSKG------------RTAWIPLKQL-----STTPSLRTRVPDLENQVKTLTDKLNNIDNTWNQRTA 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2462558775 768 DLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQ 812
Cdd:PRK10884 122 EMQQKVAQSDSVINGLKEENQKLKNQLIVAQKKVDAANLQLDDKQ 166
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
514-806 |
4.82e-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: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 514 ILEQGRFEREKLLNIQQ--QLTCSLRKVEEENQGAL---EMIKRLKEENEKLNEFLELERHNNNMMAKTLEECRVTLEGL 588
Cdd:TIGR00618 148 LLPQGEFAQFLKAKSKEkkELLMNLFPLDQYTQLALmefAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 589 -------KMENGSLKSHLQGEKQKATEASAVEQTAEscEVQEMLKVARAEKDLLELSCNEL--RQELLKANGEIKHVSSL 659
Cdd:TIGR00618 228 lkhlreaLQQTQQSHAYLTQKREAQEEQLKKQQLLK--QLRARIEELRAQEAVLEETQERInrARKAAPLAAHIKAVTQI 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 660 LAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESdaEIKDMKETIF----ELEDQVEQHRAVKLHNNQLISELEsSVI 735
Cdd:TIGR00618 306 EQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIE--EQRRLLQTLHsqeiHIRDAHEVATSIREISCQQHTLTQ-HIH 382
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462558775 736 KLEEQKSDLERQLKTLTKQMKEETEEWRRF------QADLQTAVVVANDiKCEAQQELRTVKRKLLEEEEKNARLQK 806
Cdd:TIGR00618 383 TLQQQKTTLTQKLQSLCKELDILQREQATIdtrtsaFRDLQGQLAHAKK-QQELQQRYAELCAAAITCTAQCEKLEK 458
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
404-809 |
5.00e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 404 NSVSELSlASLTEKIQKMEENHHS----TAEELQATLQElsDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLsQ 479
Cdd:PRK04863 796 EELAERY-ATLSFDVQKLQRLHQAfsrfIGSHLAVAFEA--DPEAELRQLNRRRVELERALADHESQEQQQRSQLEQA-K 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 480 ENEKLMNLLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFERE--KLLNIQQQLTCSLRKVEEEnqgaLEMIKRLKEEN 557
Cdd:PRK04863 872 EGLSALNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFVQQhgNALAQLEPIVSVLQSDPEQ----FEQLKQDYQQA 947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 558 EKlneflelERHNNNMMAKTLEECRVTLEGLKMENgslkshlqgekqkateasAVEQTAESCEVQEMLkvaRAEKDLLEL 637
Cdd:PRK04863 948 QQ-------TQRDAKQQAFALTEVVQRRAHFSYED------------------AAEMLAKNSDLNEKL---RQRLEQAEQ 999
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 638 SCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDmketifELEDQVEQHR 717
Cdd:PRK04863 1000 ERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARARRD------ELHARLSANR 1073
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 718 AVKlhnNQLiselessviklEEQKSDLERQLKTLTKQMKEETEEWRrfqaDLQTAVVVANDIKCEAQQELRT--VKRKLL 795
Cdd:PRK04863 1074 SRR---NQL-----------EKQLTFCEAEMDNLTKKLRKLERDYH----EMREQVVNAKAGWCAVLRLVKDngVERRLH 1135
|
410 420
....*....|....*....|.
gi 2462558775 796 EEE-------EKNARLQKELG 809
Cdd:PRK04863 1136 RRElaylsadELRSMSDKALG 1156
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
620-819 |
5.32e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 620 EVQEMLKVARAEKDllelSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEIcdHQAEQLSRTSLKLQEKASESDAEI 699
Cdd:COG4717 75 ELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEKLEKL--LQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 700 KDMKETIFELEDQVEQhravklhnnqlISELESSVIKLEEQKSDLERQLKTLT----KQMKEETEEWRRFQADLQTAVVV 775
Cdd:COG4717 149 EELEERLEELRELEEE-----------LEELEAELAELQEELEELLEQLSLATeeelQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462558775 776 ANDIKCEAQQELRTVKRKLLEEEEKNaRLQKELGDVQGHGRVVT 819
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEE-RLKEARLLLLIAAALLA 260
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
414-581 |
6.22e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 414 LTEKIQKMEENHHSTAEELQATLQeLSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQERVK 493
Cdd:PRK12705 31 LAKEAERILQEAQKEAEEKLEAAL-LEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 494 NEEP-TTQEGKIIELEQKCTGILEQ-GRFEREKllniQQQLTCSLRKVEEENQGALEmIKRLKEENEklnefLELERHNN 571
Cdd:PRK12705 110 REKAlSARELELEELEKQLDNELYRvAGLTPEQ----ARKLLLKLLDAELEEEKAQR-VKKIEEEAD-----LEAERKAQ 179
|
170
....*....|
gi 2462558775 572 NMMAKTLEEC 581
Cdd:PRK12705 180 NILAQAMQRI 189
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
429-772 |
7.77e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.82 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 429 AEELQATLQELSDQQQMVQELTAENEKLVDEKTILET----SFHQHRERAEQLSQENEKLMNLLQERVKNEEPTTQE--- 501
Cdd:pfam12128 300 KEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDadieTAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKynr 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 502 ----------GKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEE-----NQGALEMIKRLKEENEKLN----- 561
Cdd:pfam12128 380 rrskikeqnnRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAgklefNEEEYRLKSRLGELKLRLNqatat 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 562 -EFLELERHNN---NMMAKTLEECRVTLEGLKMENGSLKSHL--QGEKQKATEASAVEQTAESCEVQEML---------- 625
Cdd:pfam12128 460 pELLLQLENFDeriERAREEQEAANAEVERLQSELRQARKRRdqASEALRQASRRLEERQSALDELELQLfpqagtllhf 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 626 -------------KVARAE----------------KDLLELSCNELRQELLKANGEIKHVSSL---LAKVEKDYSYLKEI 673
Cdd:pfam12128 540 lrkeapdweqsigKVISPEllhrtdldpevwdgsvGGELNLYGVKLDLKRIDVPEWAASEEELrerLDKAEEALQSAREK 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 674 CDHQAEQLSRTSLKLQE-KASESDAE--IKDMKETIFELEDQveqHRAVKLHNNQLISELESSViklEEQKSDLERQLKT 750
Cdd:pfam12128 620 QAAAEEQLVQANGELEKaSREETFARtaLKNARLDLRRLFDE---KQSEKDKKNKALAERKDSA---NERLNSLEAQLKQ 693
|
410 420
....*....|....*....|..
gi 2462558775 751 LTKQMKEETEEWRRFQADLQTA 772
Cdd:pfam12128 694 LDKKHQAWLEEQKEQKREARTE 715
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
404-803 |
8.52e-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: 39.72 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 404 NSVSELSLASLTEKIQKMEENHHSTAEELQATLQELSDQqqmVQELTAENEKLVdektilETSFHQHRERAEQLSQENE- 482
Cdd:pfam15921 208 DSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQ---LEALKSESQNKI------ELLLQQHQDRIEQLISEHEv 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 483 --------------------KLMNLLQERVKN------------------------EEPTTQEGKIIELEQK---CTGIL 515
Cdd:pfam15921 279 eitgltekassarsqansiqSQLEIIQEQARNqnsmymrqlsdlestvsqlrselrEAKRMYEDKIEELEKQlvlANSEL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 516 EQGRFEREKL------LNIQ-QQLTCSLRKVEEENQGALEMIKRLKEE---NEKLNEFLELERHNNNMMAKTLEecrVTL 585
Cdd:pfam15921 359 TEARTERDQFsqesgnLDDQlQKLLADLHKREKELSLEKEQNKRLWDRdtgNSITIDHLRRELDDRNMEVQRLE---ALL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 586 EGLKME-NGSLKSHL---QGEKQKATEASAVEQTAESceVQEMLK------------VARAEKDLLEL--SCNELRQELL 647
Cdd:pfam15921 436 KAMKSEcQGQMERQMaaiQGKNESLEKVSSLTAQLES--TKEMLRkvveeltakkmtLESSERTVSDLtaSLQEKERAIE 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 648 KANGEIKHVSSLLAKVEKDYSYLKEICDH-QAEQLSRTSLKLQekASESDAEIKDMKETIFELEDQVEQH----RAVKLH 722
Cdd:pfam15921 514 ATNAEITKLRSRVDLKLQELQHLKNEGDHlRNVQTECEALKLQ--MAEKDKVIEILRQQIENMTQLVGQHgrtaGAMQVE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558775 723 NNQLISELESSVIKLEEqksdlerqLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVK--RKLLEEEEK 800
Cdd:pfam15921 592 KAQLEKEINDRRLELQE--------FKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKqeRDQLLNEVK 663
|
...
gi 2462558775 801 NAR 803
Cdd:pfam15921 664 TSR 666
|
|
| |
