|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
289-645 |
1.17e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 289 LASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQE 368
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 369 rvKNEEPTTQEGKIIELEQKctgiLEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHN 448
Cdd:TIGR02168 759 --LEAEIEELEERLEEAEEE----LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 449 NNMMAKTLEECRVTLEGLKMENGSL-KSHLQGEKQKATEASAVEQ-TAESCEVQEMLKVARAEKDLLELSCNELRQELLK 526
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLaAEIEELEELIEELESELEAlLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 527 ANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLS-RTSLKLQ---EKASESDAEIKDMKETIFELEDQVEQHRAVKLHNN 602
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEeaeALENKIEDDEEEARRRLKRLENKIKELGPVNLAAI 992
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 119571305 603 QLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWR-RFQA 645
Cdd:TIGR02168 993 EEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREAReRFKD 1036
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
381-686 |
3.32e-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: 63.54 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 381 KIIELEQKCTGI---LEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNNNMMAKTLE 457
Cdd:TIGR02168 678 EIEELEEKIEELeekIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 458 ECRVTLEGLKMENGSLKSHLQgekqkateasavEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSL 537
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELA------------EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 538 LAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEE 617
Cdd:TIGR02168 826 LESLERRIAATER----RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119571305 618 QKSDLERQLKTLTKQMKEETEEWRRFQADLQtavvvandikcEAQQELRTVKRKLLEEEEKNARLQKEL 686
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLE-----------GLEVRIDNLQERLSEEYSLTLEEAEAL 959
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
286-690 |
7.66e-10 |
|
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: 62.35 E-value: 7.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 286 ELSLASLTEKIQKMEEnhhstaeeLQATLQELSDQQQmvqELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNL 365
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKS--------LESQISELKKQNN---QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 366 LQErvKNEEPTTQEGKIIELEQKCTGI-LEQGRFEREKLLNIQQQLTCSLRKVEEENQGA-------LEMIKRLKEENEK 437
Cdd:TIGR04523 269 LSE--KQKELEQNNKKIKELEKQLNQLkSEISDLNNQKEQDWNKELKSELKNQEKKLEEIqnqisqnNKIISQLNEQISQ 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 438 LNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKAT--EASAVEQTAESCEVQEMLKVARAEKDLLEL 515
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINdlESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 516 SCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTS------------------------LKLQEKAS 571
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSrsinkikqnleqkqkelkskekelKKLNEEKK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 572 ESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSdlERQLKTLTKQMKEETEEWRRFQADLQTAV 651
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQ 584
|
410 420 430
....*....|....*....|....*....|....*....
gi 119571305 652 VVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQ 690
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
428-686 |
1.52e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 428 IKRLKEENEKLNEFLELErhnnnmmaKTLEECRVTLEGLKMEngslksHLQGEKQKAtEASAVEQTAESCEVQEMLKVAR 507
Cdd:COG1196 202 LEPLERQAEKAERYRELK--------EELKELEAELLLLKLR------ELEAELEEL-EAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 508 AEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFEL 587
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE----RRRELEERLEELEEELAELEEELEELEEELEEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 588 EDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKcEAQQELRT 667
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL-ERLERLEE 421
|
250
....*....|....*....
gi 119571305 668 VKRKLLEEEEKNARLQKEL 686
Cdd:COG1196 422 ELEELEEALAELEEEEEEE 440
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
289-557 |
6.63e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 289 LASLTEKIQKMEENHHSTAEELQATLQELSD-------QQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEK 361
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEElrlevseLEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 362 LMNLLQE-----RVKNEEPTTQEGKIIELEQKCTGILEQGrferEKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENE 436
Cdd:TIGR02168 321 LEAQLEElesklDELAEELAELEEKLEELKEELESLEAEL----EELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 437 KLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELS 516
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 119571305 517 CNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAE 557
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
414-696 |
7.10e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 7.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 414 LRKVEEENQGALeMIKRLKEENEKLNEFLELERHNNNMMAKT---LEECRVTLEGLKMENGSLKSHLQgEKQKATEASAV 490
Cdd:TIGR02168 218 LKAELRELELAL-LVLRLEELREELEELQEELKEAEEELEELtaeLQELEEKLEELRLEVSELEEEIE-ELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 491 EQTaescEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQE-- 568
Cdd:TIGR02168 296 EIS----RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEle 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 569 -KASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQ--------MKEETEE 639
Cdd:TIGR02168 372 sRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKelqaeleeLEEELEE 451
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 119571305 640 WRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVV 696
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
286-546 |
4.97e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 286 ELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNL 365
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 366 LQERVKNEEptTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLtcsLRKVEEENQGALEMIKRLKEENEKLNEFLELE 445
Cdd:COG1196 332 LEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 446 RHNNNmMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELscNELRQELL 525
Cdd:COG1196 407 EAEEA-LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL--EAALAELL 483
|
250 260
....*....|....*....|.
gi 119571305 526 KANGEIKHVSSLLAKVEKDYS 546
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYE 504
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
286-691 |
2.10e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 286 ELSLASLTEKIQKMEENHH---STAEELQATLQELSDQQQMVQELTAENEKLVD-------EKTILETSFHQHRERAEQL 355
Cdd:PRK02224 212 ESELAELDEEIERYEEQREqarETRDEADEVLEEHEERREELETLEAEIEDLREtiaeterEREELAEEVRDLRERLEEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 356 SQENEKLmnLLQERVKNEEPTTQEGKIIELEQKCTGI---LEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLK 432
Cdd:PRK02224 292 EEERDDL--LAEAGLDDADAEAVEARREELEDRDEELrdrLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 433 EENEKLNEFLELERHNNNMMAKTLEECR-------VTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESC--EVQEML 503
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRerfgdapVDLGNAEDFLEELREERDELREREAELEATLRTARERveEAEALL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 504 KV---------------------ARAEKDLLELSCNELRQELLKANGEIKHVSSLlAKVEKDYSYLKE-------ICDHQ 555
Cdd:PRK02224 450 EAgkcpecgqpvegsphvetieeDRERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEErredleeLIAER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 556 AEQLSRTSLKLQEK---ASESDAEIKDMKETIFELEDQVEQHR-AVKLHNNQL---------ISELESSVIKLEEQKSDL 622
Cdd:PRK02224 529 RETIEEKRERAEELrerAAELEAEAEEKREAAAEAEEEAEEAReEVAELNSKLaelkeriesLERIRTLLAAIADAEDEI 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 623 ER------QLKTLTKQMKEETEEWRRFQADLQ-----TAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQG 691
Cdd:PRK02224 609 ERlrekreALAELNDERRERLAEKRERKRELEaefdeARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
278-639 |
2.99e-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: 53.92 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 278 GSSPNSVSEL-SLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLS 356
Cdd:TIGR02169 664 GGILFSRSEPaELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 357 qenEKLMNLLQERVKNE-EPTTQEGKIIELEQKCTGI-LEQGRFEREKLLNIQQQLTCSLRKVEEENQgalEMIKRLKEE 434
Cdd:TIGR02169 744 ---EDLSSLEQEIENVKsELKELEARIEELEEDLHKLeEALNDLEARLSHSRIPEIQAELSKLEEEVS---RIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 435 NEKLNEfLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKaTEASAVEQTAESCEVQEMLKVARAEKDLLE 514
Cdd:TIGR02169 818 EQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE-LEEELEELEAALRDLESRLGDLKKERDELE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 515 LSCNELRQELLKANGEI----KHVSSLLAKVEKDYSYLKEICDHQAEQLSrtslklqekASESDAEIKDMKETIFELEDQ 590
Cdd:TIGR02169 896 AQLRELERKIEELEAQIekkrKRLSELKAKLEALEEELSEIEDPKGEDEE---------IPEEELSLEDVQAELQRVEEE 966
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 119571305 591 VEQHRAVklhNNQLISELESSVIKLEEQKSDLERqLKTLTKQMKEETEE 639
Cdd:TIGR02169 967 IRALEPV---NMLAIQEYEEVLKRLDELKEKRAK-LEEERKAILERIEE 1011
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
295-684 |
5.96e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 295 KIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETsFHQHRERAEQLSQENEKlmnlLQERVKNEE 374
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKKEELER----LKKRLTGLT 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 375 PTTQEGKIIELEQKCTGIleqgrfeREKLLNIQQQLTcSLRKVEEENQGALEMIKRLKEENEKLNEFLElERHNNNMMA- 453
Cdd:PRK03918 386 PEKLEKELEELEKAKEEI-------EEEISKITARIG-ELKKEIKELKKAIEELKKAKGKCPVCGRELT-EEHRKELLEe 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 454 ---------KTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELScnELRQEL 524
Cdd:PRK03918 457 ytaelkrieKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYE--KLKEKL 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 525 LKANGEIKHVSSLLAKV---EKDYSYLKEICDHQAEQLSRTSLKLQEKASESdaeIKDMKETIFELE----------DQV 591
Cdd:PRK03918 535 IKLKGEIKSLKKELEKLeelKKKLAELEKKLDELEEELAELLKELEELGFES---VEELEERLKELEpfyneylelkDAE 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 592 EQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLT-----------KQMKEETEEWRRFQADLQTAVVVANDIKCE 660
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEelekkyseeeyEELREEYLELSRELAGLRAELEELEKRREE 691
|
410 420
....*....|....*....|....
gi 119571305 661 AQQELRTVKRKLLEEEEKNARLQK 684
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKELEK 715
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
498-699 |
1.61e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 498 EVQEMLKVARAEKDLLELSCnELRQELLKANGEIKHVSSLLAKV-----EKDYSYLKEICDHQAEQLSRtslkLQEKASE 572
Cdd:COG4913 239 RAHEALEDAREQIELLEPIR-ELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELAR----LEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 573 SDAEIKDMKETIFELEDQVEQHRAVKLHN-NQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAV 651
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 119571305 652 VVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVVTSR 699
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
425-677 |
1.84e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 425 LEMIKRLKEENEKLNEFL--ELERHNNNMMAKT--LEECRVTLEGLKMENGSLKSHLQGEKQKATEA----SAVEQTAEs 496
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLqsELRRIENRLDELSqeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELeedlSSLEQEIE- 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 497 cEVQEMLKVARAEKDLLELSCNELRQELLK-----ANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLK---LQE 568
Cdd:TIGR02169 755 -NVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEkeyLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 569 KASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQ 648
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913
|
250 260 270
....*....|....*....|....*....|..
gi 119571305 649 TAVVVANDIKC---EAQQELRTVKRKLLEEEE 677
Cdd:TIGR02169 914 KKRKRLSELKAkleALEEELSEIEDPKGEDEE 945
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
350-708 |
1.97e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 350 ERAEQLSQENEKL---MNLLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTcSLRKVEEENQGALE 426
Cdd:COG1196 213 ERYRELKEELKELeaeLLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE-ELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 427 MIKRLKEENEKLNEFLELERHNNnmmaktleecRVTLEGLKMENGSLKSHLQGEKQKATEAsaveqtaescevQEMLKVA 506
Cdd:COG1196 292 ELLAELARLEQDIARLEERRREL----------EERLEELEEELAELEEELEELEEELEEL------------EEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 507 RAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFE 586
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR----AAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 587 LEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIK-CEAQQEL 665
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLeAEADYEG 505
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 119571305 666 RTVKRKLLEEEEKNARLQKELGDVQGHGRVVTsRAAPPSLGSV 708
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE-AALEAALAAA 547
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
293-687 |
2.13e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 293 TEKIQKMEENHHstaEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhQHRERAEQLSQENEKL---MNLLQER 369
Cdd:PRK03918 188 TENIEELIKEKE---KELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLegsKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 370 VKN------------EEPTTQEGKIIELEQKCTGILEQGRFeREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEK 437
Cdd:PRK03918 261 IREleerieelkkeiEELEEKVKELKELKEKAEEYIKLSEF-YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 438 LNEFLELERHNNNMMAKtLEECRVTLEGLKMENGSLKSHLQGEKQKATEasaveqtaescEVQEMLKVARAEKDLLELSC 517
Cdd:PRK03918 340 LEELKKKLKELEKRLEE-LEERHELYEEAKAKKEELERLKKRLTGLTPE-----------KLEKELEELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 518 NELRQELLKANGEIKHVSSLLAKVEKdysyLKEICDHQAEQLSRTSLKlqEKASESDAEIKDMKETIFELEDQVEQHRAV 597
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKK----AKGKCPVCGRELTEEHRK--ELLEEYTAELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 598 KLHNNQLISElESSVIKLEEQKSDLERQLKTLTKQMKEETEE-WRRFQADLQTAVVVANDIKC---------EAQQELRT 667
Cdd:PRK03918 482 LRELEKVLKK-ESELIKLKELAEQLKELEEKLKKYNLEELEKkAEEYEKLKEKLIKLKGEIKSlkkelekleELKKKLAE 560
|
410 420
....*....|....*....|
gi 119571305 668 VKRKLLEEEEKNARLQKELG 687
Cdd:PRK03918 561 LEKKLDELEEELAELLKELE 580
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
289-683 |
4.11e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 289 LASLTEKIQKMEENH---HSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILET--SFHQHRERAEQLSQENEKLM 363
Cdd:COG4717 73 LKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 364 NLLQERVKNEEP-TTQEGKIIELEQKCTGILEQGRFEREKLLniqQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEfl 442
Cdd:COG4717 153 ERLEELRELEEElEELEAELAELQEELEELLEQLSLATEEEL---QDLAEELEELQQRLAELEEELEEAQEELEELEE-- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 443 ELERHNNNMMAKTLEEC-------------RVTLEGLKMENGSLKSHLQG----------------EKQKATEASAVEQT 493
Cdd:COG4717 228 ELEQLENELEAAALEERlkearlllliaaaLLALLGLGGSLLSLILTIAGvlflvlgllallflllAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 494 AESCEVQEMLKVARAE-KDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYS--YLKEICDHQAEQLSR---TSLKLQ 567
Cdd:COG4717 308 QALPALEELEEEELEElLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQLEELEQEIAALLAEagvEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 568 EKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEssvikLEEQKSDLERQLKTLTKQMKEETEEWRRFQADL 647
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELEEELEELEEELEELREELAELEAEL 462
|
410 420 430
....*....|....*....|....*....|....*.
gi 119571305 648 QTAvvVANDIKCEAQQELRTVKRKLLEEEEKNARLQ 683
Cdd:COG4717 463 EQL--EEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
286-570 |
8.19e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 8.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 286 ELSLASLTEKIQKMEEnhhsTAEELQATLQELSDQqqmVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNL 365
Cdd:COG1196 238 EAELEELEAELEELEA----ELEELEAELAELEAE---LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 366 LQERVKNEEptTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELE 445
Cdd:COG1196 311 RRELEERLE--ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 446 ---RHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELScNELRQ 522
Cdd:COG1196 389 leaLRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL-ELLAE 467
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 119571305 523 ELLKANGEIKHVSSLLAKVEKDYS--YLKEICDHQAEQLSRTSLKLQEKA 570
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAArlLLLLEAEADYEGFLEGVKAALLLA 517
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
285-692 |
1.17e-05 |
|
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: 49.02 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 285 SELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKL-- 362
Cdd:pfam01576 24 AESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMqq 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 363 -MNLLQERVKNEEPTTQ---------EGKIIELEQKCTGILEQ-GRFEREKLLNIQQQLTCSLRKVEEENQGalEMIKRL 431
Cdd:pfam01576 104 hIQDLEEQLDEEEAARQklqlekvttEAKIKKLEEDILLLEDQnSKLSKERKLLEERISEFTSNLAEEEEKA--KSLSKL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 432 KEENEKLNEFLELERHNNNMMAKTLEECRVTLEG------------------LKMENGSLKSHLQGEKQKATEASAV--- 490
Cdd:pfam01576 182 KNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGestdlqeqiaelqaqiaeLRAQLAKKEEELQAALARLEEETAQknn 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 491 ------EQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKdysyLKEICDHQAEQLSRTsl 564
Cdd:pfam01576 262 alkkirELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE----LRSKREQEVTELKKA-- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 565 kLQEKASESDAEIKDMKE----TIFELEDQVEQHRAVKlhnnqliSELESSVIKLEEQKSDLERQLKTLTKQMKEETEEW 640
Cdd:pfam01576 336 -LEEETRSHEAQLQEMRQkhtqALEELTEQLEQAKRNK-------ANLEKAKQALESENAELQAELRTLQQAKQDSEHKR 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119571305 641 RRFQADLQTAVVVANDIK----------CEAQQELRTVKRKLLEEEEKNARLQKELGDVQGH 692
Cdd:pfam01576 408 KKLEGQLQELQARLSESErqraelaeklSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQ 469
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
481-707 |
1.57e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 481 KQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLS 560
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 561 RTSlklqekASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEw 640
Cdd:COG3883 97 RSG------GSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA- 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119571305 641 rrfQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVVTSRAAPPSLGS 707
Cdd:COG3883 170 ---KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
283-685 |
1.75e-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: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 283 SVSELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQL-SQENEK 361
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIkNKLLKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 362 LMNLLQERVKNEEPTTQEGKIIELEQKctgileqgrfeREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEF 441
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKSLESQISELKKQ-----------NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 442 L-----ELERHNNNMMAKT--LEECRVTLEGLKME-----NGSLKSHLQGEKQKATEA-SAVEQTAESC-EVQEMLKVAR 507
Cdd:TIGR04523 269 LsekqkELEQNNKKIKELEkqLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIqNQISQNNKIIsQLNEQISQLK 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 508 AEKDLLELSCNELRQELLKANGEIKHVssllaKVEKDySYLKEICD--HQAEQLSRTSLKLQEKASESDAEIKDMKETIF 585
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKL-----KKENQ-SYKQEIKNleSQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 586 ELEDQVEQHRAVKLHNNQLISELES-------SVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVvvandik 658
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNqdsvkelIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE------- 495
|
410 420
....*....|....*....|....*..
gi 119571305 659 ceaqQELRTVKRKLLEEEEKNARLQKE 685
Cdd:TIGR04523 496 ----KELKKLNEEKKELEEKVKDLTKK 518
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
426-686 |
5.34e-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: 46.65 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 426 EMIKRLKEENEKLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATE-ASAVEQTAESCEVQEMLK 504
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDlRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 505 varaeKDLLELS---CNELRQELLKANGEIKHVSSLLAKVEKDYSylKEIcdHQAEQLSRTSLK-----LQEKASESDAE 576
Cdd:pfam15921 162 -----EDMLEDSntqIEQLRKMMLSHEGVLQEIRSILVDFEEASG--KKI--YEHDSMSTMHFRslgsaISKILRELDTE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 577 IKDMKETIFELEDQVEQHRA---------VKLHNN---QLISELESSVIKLEE-------QKSDLERQLKTLTKQMKEET 637
Cdd:pfam15921 233 ISYLKGRIFPVEDQLEALKSesqnkiellLQQHQDrieQLISEHEVEITGLTEkassarsQANSIQSQLEIIQEQARNQN 312
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 119571305 638 EEWRRFQADLQTAVvvandikCEAQQELRTVKRKLleeEEKNARLQKEL 686
Cdd:pfam15921 313 SMYMRQLSDLESTV-------SQLRSELREAKRMY---EDKIEELEKQL 351
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
289-686 |
6.05e-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: 46.50 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 289 LASLTEKIQKmeeNHHSTAEELQATLQELSD-QQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENE------K 361
Cdd:TIGR00618 181 LALMEFAKKK---SLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREaqeeqlK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 362 LMNLLQERVKNEEPTTQEGKIIELEQKCTGI-------------LEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMI 428
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAVLEETQERINRarkaaplaahikaVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 429 KRLKEENEKLNEFLELERHNnnmmAKTLEECRVTLEGLKMENgSLKSHLQGEKQKATEASAVEQTAesCEVQEMLKVARA 508
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHI----RDAHEVATSIREISCQQH-TLTQHIHTLQQQKTTLTQKLQSL--CKELDILQREQA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 509 EKDLLELSCNELRQELLKANGEI----KHVSSLLAKVEKDYSYLKEICDHQAEQLSRT---SLKLQEKASESDAEIKDMK 581
Cdd:TIGR00618 411 TIDTRTSAFRDLQGQLAHAKKQQelqqRYAELCAAAITCTAQCEKLEKIHLQESAQSLkerEQQLQTKEQIHLQETRKKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 582 ETIFELEDQVEQHRAVK---LHNNQ-------------LISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQA 645
Cdd:TIGR00618 491 VVLARLLELQEEPCPLCgscIHPNParqdidnpgpltrRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ 570
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 119571305 646 DLQTAVVVANDIKCEAQQeLRTVKRKLLEEEEKNARLQKEL 686
Cdd:TIGR00618 571 SFSILTQCDNRSKEDIPN-LQNITVRLQDLTEKLSEAEDML 610
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
519-701 |
1.18e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 519 ELRQELLKANGEIKHVSSLLAKVEKDYSYLKEIcdhqaeqlsRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAvk 598
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQER---------REALQRLAEYSWDEIDVASAEREIAELEAELERLDA-- 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 599 lhNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEK 678
Cdd:COG4913 683 --SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180
....*....|....*....|...
gi 119571305 679 NARLQKELGDVQGHGRVVTSRAA 701
Cdd:COG4913 761 DAVERELRENLEERIDALRARLN 783
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
307-692 |
1.23e-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: 45.73 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 307 AEELQATLQELSDQQQMVQELTAENEKLVDEKTIL--ETSFHQHRERAEQLSQENEKLM-----NLLQERVKNEEPTTQE 379
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHlqETRKKAVVLARLLELQEEPCPLcgsciHPNPARQDIDNPGPLT 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 380 GKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEM---IKRLKEENEKLNEFLELERHNNNMMAK-- 454
Cdd:TIGR00618 528 RRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILtqcDNRSKEDIPNLQNITVRLQDLTEKLSEae 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 455 --TLEECRVTLEGLKMENGSLKSHL---QGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANG 529
Cdd:TIGR00618 608 dmLACEQHALLRKLQPEQDLQDVRLhlqQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQS 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 530 EIKHVSSLLAKVEKDYSYLKEICDH------QAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNq 603
Cdd:TIGR00618 688 EKEQLTYWKEMLAQCQTLLRELETHieeydrEFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNN- 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 604 liSELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQ 683
Cdd:TIGR00618 767 --NEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATL 844
|
....*....
gi 119571305 684 KELGDVQGH 692
Cdd:TIGR00618 845 GEITHQLLK 853
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
428-686 |
1.74e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 428 IKRLKEENEKLNEFLELErhnnnmmaKTLEECRVTLEGLKMEngSLKSHLQgEKQKATEASAVEQTAESCEVQE------ 501
Cdd:TIGR02168 202 LKSLERQAEKAERYKELK--------AELRELELALLVLRLE--ELREELE-ELQEELKEAEEELEELTAELQEleekle 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 502 --MLKVARAEKDLLELS--CNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEI 577
Cdd:TIGR02168 271 elRLEVSELEEEIEELQkeLYALANEISRLEQQKQILRERLANLERQLEELEA----QLEELESKLDELAEELAELEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 578 KDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQ----------MKEETEEWRRFQADL 647
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEierlearlerLEDRRERLQQEIEEL 426
|
250 260 270
....*....|....*....|....*....|....*....
gi 119571305 648 QTAVVVANdiKCEAQQELRTVKRKLLEEEEKNARLQKEL 686
Cdd:TIGR02168 427 LKKLEEAE--LKELQAELEELEEELEELQEELERLEEAL 463
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
307-679 |
3.25e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 307 AEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhqHRERAEQLSQENEKLMNLLQERVKNEEPTTQEgkiiELE 386
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE-----EKKKADEAKKKAEEAKKADEAKKKAEEAKKAE----EAK 1463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 387 QKCTgilEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNNNMMAKTLEECRVTLEGL 466
Cdd:PTZ00121 1464 KKAE---EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK 1540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 467 KMEngslkshlqgEKQKATEASAVEQTAESCEVQEMLKVARAEKD--LLELSCNELRQELLKANGEIKHVSSLLAKVEKD 544
Cdd:PTZ00121 1541 KAE----------EKKKADELKKAEELKKAEEKKKAEEAKKAEEDknMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 545 YSYLKEICDHQAEQLSrtslKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLE- 623
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELK----KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEd 1686
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119571305 624 ---------------RQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKN 679
Cdd:PTZ00121 1687 ekkaaealkkeaeeaKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
504-673 |
4.46e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 504 KVARAEKDLLELSCNELRQELLKANGEIKHVSSLLakvEKDYSYLKEIcDHQAEQLSRTSLKLQEKASESDAEIKDMKET 583
Cdd:PRK04778 264 QIDENLALLEELDLDEAEEKNEEIQERIDQLYDIL---EREVKARKYV-EKNSDTLPDFLEHAKEQNKELKEEIDRVKQS 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 584 IFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQK---SDLERQLKTLTKQMKEETEEWRRFQADLQT---AVVVANDI 657
Cdd:PRK04778 340 YTLNESELESVRQLEKQLESLEKQYDEITERIAEQEiaySELQEELEEILKQLEEIEKEQEKLSEMLQGlrkDELEAREK 419
|
170
....*....|....*.
gi 119571305 658 KCEAQQELRTVKRKLL 673
Cdd:PRK04778 420 LERYRNKLHEIKRYLE 435
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
286-675 |
4.72e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 286 ELSLASLTEKIQKMEENHHSTAEeLQATLQELsdqQQMVQELTAENEKLVD-EKTILE-TSFHQHRERA-EQLSQENEKL 362
Cdd:pfam15921 447 ERQMAAIQGKNESLEKVSSLTAQ-LESTKEML---RKVVEELTAKKMTLESsERTVSDlTASLQEKERAiEATNAEITKL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 363 MNLLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNI-QQQLTCSLRKVEEENQGA----LEMIKRLKEENEK 437
Cdd:pfam15921 523 RSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEIlRQQIENMTQLVGQHGRTAgamqVEKAQLEKEINDR 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 438 LNEFLELERHNNNMMAKTLE-ECRVtleglkmengslkSHLQGEKQKATEASAveqtaescevqEMLKVARaekdllels 516
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRElEARV-------------SDLELEKVKLVNAGS-----------ERLRAVK--------- 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 517 cnELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRA 596
Cdd:pfam15921 650 --DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMK 727
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119571305 597 VKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQeLRTVKRKLLEE 675
Cdd:pfam15921 728 VAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEV-LRSQERRLKEK 805
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
484-707 |
5.73e-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: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 484 ATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRTS 563
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA----ELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 564 LKLQEKASESDAEIKDM------------------KETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQ 625
Cdd:COG4942 93 AELRAELEAQKEELAELlralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 626 LKTLTKQMKEETEEwrrfQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVVTSRAAPPSL 705
Cdd:COG4942 173 RAELEALLAELEEE----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
..
gi 119571305 706 GS 707
Cdd:COG4942 249 AA 250
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
274-515 |
5.98e-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: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 274 CSTAGSSPNSVSELS--LASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRER 351
Cdd:COG4942 12 ALAAAAQADAAAEAEaeLEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 352 AEQLSQENEKLMNLLQERVKNeepttqegkiieleqkctgILEQGRFEREKLLNIQQQLTCSLRkveeenqgALEMIKRL 431
Cdd:COG4942 92 IAELRAELEAQKEELAELLRA-------------------LYRLGRQPPLALLLSPEDFLDAVR--------RLQYLKYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 432 KEENEKLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKD 511
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
....
gi 119571305 512 LLEL 515
Cdd:COG4942 225 LEAL 228
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
270-685 |
6.67e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 270 KSSKCSTAGSSPNSVSELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTA----------ENEKLVDEKT 339
Cdd:pfam05483 339 ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKfknnkeveleELKKILAEDE 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 340 ILETSFHQHRERAEQLSQENEKLMNLLQERVKN-EEPTTQEGKIIELEQKCTGILEQGR--FEREKLLNIQQQLTCSLRK 416
Cdd:pfam05483 419 KLLDEKKQFEKIAEELKGKEQELIFLLQAREKEiHDLEIQLTAIKTSEEHYLKEVEDLKteLEKEKLKNIELTAHCDKLL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 417 VEEEN--QGALEMIKRLKEENEKLNEFLELERHnnnmMAKTLEECRVTLEGLKMENGSLKSHLqgeKQKATEASAVEQTA 494
Cdd:pfam05483 499 LENKEltQEASDMTLELKKHQEDIINCKKQEER----MLKQIENLEEKEMNLRDELESVREEF---IQKGDEVKCKLDKS 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 495 ESCEVQEMLKVARAEKDL--LELSCNELRQELLKANGEIKHVSSLLAKVEKDYSY------LKEICDHQAE-QLSRTSLK 565
Cdd:pfam05483 572 EENARSIEYEVLKKEKQMkiLENKCNNLKKQIENKNKNIEELHQENKALKKKGSAenkqlnAYEIKVNKLElELASAKQK 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 566 LQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVI-KLEEQKSDLERQLKTLTKQMKEETEEWRRFQ 644
Cdd:pfam05483 652 FEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhKIAEMVALMEKHKHQYDKIIEERDSELGLYK 731
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 119571305 645 ADLQTAVVVANDIKCE---AQQELRTVKRKLLEEEEKNARLQKE 685
Cdd:pfam05483 732 NKEQEQSSAKAALEIElsnIKAELLSLKKQLEIEKEEKEKLKME 775
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
308-695 |
7.07e-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: 43.13 E-value: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 308 EELQATLQELsdqqQMVQELTAENEKLVDEKtiletsfhqhRERAEQLSQENEKLMNLLQERVKNEEpttQEGKIIELEQ 387
Cdd:TIGR02169 170 RKKEKALEEL----EEVEENIERLDLIIDEK----------RQQLERLRREREKAERYQALLKEKRE---YEGYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 388 KCTgiLEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERhnnNMMAKTLEECRVTLEGLK 467
Cdd:TIGR02169 233 EAL--ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ---LRVKEKIGELEAEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 468 MENGSLKSHLQ--GEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAK-VEKD 544
Cdd:TIGR02169 308 RSIAEKERELEdaEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAEtRDEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 545 YSYLKEICD--HQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDL 622
Cdd:TIGR02169 388 KDYREKLEKlkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119571305 623 ERQLKTLTKQMKEETEEWRRFQADLQTAvvvandiKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRV 695
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQRELAEA-------EAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSV 533
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
394-690 |
7.27e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 394 EQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNNNMMAKT----LEECRVTLEGLKME 469
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDylklNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 470 NGSLKSHLQGEKQKATEASAVEQTAESCEVQEMlKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKdysylk 549
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEK-KLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK------ 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 550 eicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQlKTL 629
Cdd:pfam02463 322 -----EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL-KEE 395
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119571305 630 TKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQ 690
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
453-685 |
7.77e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 453 AKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAEscevqEMLKVARAEKDLLELscNELRQELLKANGEIK 532
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-----DEIDVASAEREIAEL--EAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 533 HVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASE--------SDAEIKDMKETIFELEDQVEQHrAVKLHNNQL 604
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEldelqdrlEAAEDLARLELRALLEERFAAA-LGDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 605 ISELESSVIKLEEQKSDLERQLktlTKQMKEETEEWRRFQADLQTAVVVANDIkceaQQELRTVKRKLLEE-EEKNARLQ 683
Cdd:COG4913 768 RENLEERIDALRARLNRAEEEL---ERAMRAFNREWPAETADLDADLESLPEY----LALLDRLEEDGLPEyEERFKELL 840
|
..
gi 119571305 684 KE 685
Cdd:COG4913 841 NE 842
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
453-658 |
7.97e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 453 AKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAES--CEVQEMLKVARAEKDLLELSCNELRQELLKANGE 530
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERriAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 531 IKHVSSLLAKV-------------------------EKDYSYLKEICDH---QAEQLSRTSLKLQEKASESDAEIKDMKE 582
Cdd:COG4942 99 LEAQKEELAELlralyrlgrqpplalllspedfldaVRRLQYLKYLAPArreQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119571305 583 TIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIK 658
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
296-586 |
8.34e-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: 42.65 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 296 IQKMEENHHSTAEELQATLQELSDQQQMvQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQERVKNEEP 375
Cdd:TIGR00618 600 TEKLSEAEDMLACEQHALLRKLQPEQDL-QDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASR 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 376 TTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFL-ELERHNNNMMAK 454
Cdd:TIGR00618 679 QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLkELMHQARTVLKA 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 455 TLEECRVTLEGLKME--NGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIK 532
Cdd:TIGR00618 759 RTEAHFNNNEEVTAAlqTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLE 838
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 119571305 533 HVSSLLAKVEKDYSYLKEiCDHQAEQLSRTSLKLQEKasESDAEIKDMKETIFE 586
Cdd:TIGR00618 839 EKSATLGEITHQLLKYEE-CSKQLAQLTQEQAKIIQL--SDKLNGINQIKIQFD 889
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
480-686 |
9.49e-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: 42.06 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 480 EKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQL 559
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 560 SRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQ---LKTLTKQMKEE 636
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAEraeLEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 119571305 637 TEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKEL 686
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
291-635 |
1.06e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 291 SLTEKIQKMEENH---HSTAEELQATLQE----LSDQQQMVQELTAE----NEKLVDEKTILETSFHQHRERAEQLSQEN 359
Cdd:PRK02224 346 SLREDADDLEERAeelREEAAELESELEEareaVEDRREEIEELEEEieelRERFGDAPVDLGNAEDFLEELREERDELR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 360 EKLMNL------LQERVKNEEPTTQEGKIIELEQKCTG-----ILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEM- 427
Cdd:PRK02224 426 EREAELeatlrtARERVEEAEALLEAGKCPECGQPVEGsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLv 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 428 -----IKRLKEENEKLNEFLELERhnnnmmaKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEAsavEQTAEscEVQEM 502
Cdd:PRK02224 506 eaedrIERLEERREDLEELIAERR-------ETIEEKRERAEELRERAAELEAEAEEKREAAAEA---EEEAE--EAREE 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 503 LKvaraekdllelSCNELRQELLKANGEIKHVSSLLAKVEKdysylkeiCDHQAEQLSRTSLKLQEKASESDAEIKDMKE 582
Cdd:PRK02224 574 VA-----------ELNSKLAELKERIESLERIRTLLAAIAD--------AEDEIERLREKREALAELNDERRERLAEKRE 634
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 119571305 583 TIFELEDQVEQHRAVKLHNN-----QLISELESSVIKLEEQKSDLERQLKTLTKQMKE 635
Cdd:PRK02224 635 RKRELEAEFDEARIEEAREDkeraeEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
359-690 |
1.18e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 359 NEKLMNLLQERVKNEEPTTQEGKiieLEQKCTGILEQGRFEREKL-LNIQQQLTCSLRKVEEENQgalEMIKRLKEENEK 437
Cdd:COG5022 775 QVIQHGFRLRRLVDYELKWRLFI---KLQPLLSLLGSRKEYRSYLaCIIKLQKTIKREKKLRETE---EVEFSLKAEVLI 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 438 LNEFLELERHNnnmMAKTLEECRVTLEGL-KMENgsLKSHLQGEKQKATEASAVEQTAEscevqemlkvaRAEKDLLELS 516
Cdd:COG5022 849 QKFGRSLKAKK---RFSLLKKETIYLQSAqRVEL--AERQLQELKIDVKSISSLKLVNL-----------ELESEIIELK 912
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 517 CNElrQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTsLKLQEkasesdaEIKDMKETIFELEDQVEQHRA 596
Cdd:COG5022 913 KSL--SSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPEL-NKLHE-------VESKLKETSEEYEDLLKKSTI 982
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 597 VKLHNNQLISELESSVIKLEEQKSDLERqLKTLTKQMKEEteewRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEE 676
Cdd:COG5022 983 LVREGNKANSELKNFKKELAELSKQYGA-LQESTKQLKEL----PVEVAELQSASKIISSESTELSILKPLQKLKGLLLL 1057
|
330
....*....|....
gi 119571305 677 EKNaRLQKELGDVQ 690
Cdd:COG5022 1058 ENN-QLQARYKALK 1070
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
470-636 |
1.70e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 470 NGSLKSHLQGEKQKATEASAVEQTAEScEVQEMLKVARAE-KDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYL 548
Cdd:PRK12705 18 LGVLVVLLKKRQRLAKEAERILQEAQK-EAEEKLEAALLEaKELLLRERNQQRQEARREREELQREEERLVQKEEQLDAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 549 KEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRavklhNNQLISELEssvikleeqkSDLERQLKT 628
Cdd:PRK12705 97 AEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQA-----RKLLLKLLD----------AELEEEKAQ 161
|
....*...
gi 119571305 629 LTKQMKEE 636
Cdd:PRK12705 162 RVKKIEEE 169
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
349-685 |
2.86e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 349 RERAEQLSQENEKLMNLLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMI 428
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 429 KRLKEENEKLNEFLELERHNNNMMAKTLEEcrvtlEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARA 508
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEK-----KLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 509 EKDLLELSCNELRQELLKANGEIKhvsSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELE 588
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIK---REAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 589 DQVEQHRAVKLHNNQLISELESSVI--KLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELR 666
Cdd:pfam02463 404 EKEAQLLLELARQLEDLLKEEKKEEleILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQ 483
|
330
....*....|....*....
gi 119571305 667 TVKRKLLEEEEKNARLQKE 685
Cdd:pfam02463 484 EQLELLLSRQKLEERSQKE 502
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
308-634 |
3.10e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 308 EELQATLQELSDQQQMVQELTAENEKLVDEKTILETsfhQHRERAEQLSQENEKLMNLLQER-VKNEEPTTQEGKIIELE 386
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES---ENSEKQRELEEKQNEIEKLKKENqSYKQEIKNLESQINDLE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 387 QKCtgileqgrferEKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFL-ELERHNN------NMMAKTLEEC 459
Cdd:TIGR04523 398 SKI-----------QNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIkDLTNQDSvkeliiKNLDNTRESL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 460 RVTLEGLKMENGSLKSHLQGEKQ--KATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIkhvSSL 537
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKelKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI---SDL 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 538 LAKVEKDYSYLKEicdhqaEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEE 617
Cdd:TIGR04523 544 EDELNKDDFELKK------ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
|
330
....*....|....*..
gi 119571305 618 QKSDLERQLKTLTKQMK 634
Cdd:TIGR04523 618 ELEKAKKENEKLSSIIK 634
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
289-691 |
3.81e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 289 LASLTEKIQKMEENHH---STAEELQATLQELSDQQQMVQEltaENEKLVDEKTILETSFHQHRERAEQLSQENEKL--- 362
Cdd:TIGR02169 352 RDKLTEEYAELKEELEdlrAELEEVDKEFAETRDELKDYRE---KLEKLKREINELKRELDRLQEELQRLSEELADLnaa 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 363 -------MNLLQERV--KNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCS-------------------- 413
Cdd:TIGR02169 429 iagieakINELEEEKedKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLqrelaeaeaqaraseervrg 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 414 ---------------------LRKVEEENQGALEM--------------------IKRLKEENEKLNEFLELER------ 446
Cdd:TIGR02169 509 graveevlkasiqgvhgtvaqLGSVGERYATAIEVaagnrlnnvvveddavakeaIELLKRRKAGRATFLPLNKmrderr 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 447 -------------------------------HNNNMMAKTLEECR--------VTLEGL------KMENGSLKSHLQGEK 481
Cdd:TIGR02169 589 dlsilsedgvigfavdlvefdpkyepafkyvFGDTLVVEDIEAARrlmgkyrmVTLEGElfeksgAMTGGSRAPRGGILF 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 482 QKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSR 561
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 562 TSLKLQEKASESD---AEIKDMKETIFELEDQVEQHRAVKLHnnQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETE 638
Cdd:TIGR02169 749 LEQEIENVKSELKeleARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTL 826
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119571305 639 EWRRFQADLQTAVVVANDIK------CEAQQELRTVKRKLLEEEEKNA----RLQKELGDVQG 691
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKeqiksiEKEIENLNGKKEELEEELEELEaalrDLESRLGDLKK 889
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
290-649 |
4.05e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 290 ASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQER 369
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 370 VKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTC------------SLRKVEEENQGALEMIKRLKEENEK 437
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAklqgsdldrtvqQVNQEKQEKQHELDTVVSKIELNRK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 438 LNE-----FLELERHNNNM------MAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAES--CEVQEMLK 504
Cdd:TIGR00606 851 LIQdqqeqIQHLKSKTNELkseklqIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKdqQEKEELIS 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 505 VARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEI-----------CDHQAEQLSR---------TSL 564
Cdd:TIGR00606 931 SKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETelntvnaqleeCEKHQEKINEdmrlmrqdiDTQ 1010
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 565 KLQEKASESDAEIKDMKETIFELEDQVEQHraVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQ 644
Cdd:TIGR00606 1011 KIQERWLQDNLTLRKRENELKEVEEELKQH--LKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFK 1088
|
....*
gi 119571305 645 ADLQT 649
Cdd:TIGR00606 1089 KELRE 1093
|
|
| PRK10884 |
PRK10884 |
SH3 domain-containing protein; Provisional |
566-690 |
4.25e-03 |
|
SH3 domain-containing protein; Provisional
Pssm-ID: 182809 [Multi-domain] Cd Length: 206 Bit Score: 39.25 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 566 LQEKASESDAEIKDMKEtifeledqveqhRAVKLHNNQLiseleSSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQA 645
Cdd:PRK10884 59 LQVNANTNYAQIRDSKG------------RTAWIPLKQL-----STTPSLRTRVPDLENQVKTLTDKLNNIDNTWNQRTA 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 119571305 646 DLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQ 690
Cdd:PRK10884 122 EMQQKVAQSDSVINGLKEENQKLKNQLIVAQKKVDAANLQLDDKQ 166
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
602-685 |
4.29e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 602 NQLISELESSVIKLEEQKSDLE---RQLKTLTKQMKEETEEWR-RFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEE 677
Cdd:PRK00409 519 NELIASLEELERELEQKAEEAEallKEAEKLKEELEEKKEKLQeEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQK 598
|
....*...
gi 119571305 678 KNARLQKE 685
Cdd:PRK00409 599 GGYASVKA 606
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
399-679 |
4.50e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 399 EREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNnnmmAKTLEECRVTLEGLKMENGSLKSHLQ 478
Cdd:PRK03918 180 RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKE----VKELEELKEEIEELEKELESLEGSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 479 G--EKQKATEASAVEQTAESCEVQEmlKVARAEK-DLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDhQ 555
Cdd:PRK03918 256 KleEKIRELEERIEELKKEIEELEE--KVKELKElKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-E 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 556 AEQLSRTSLKLQEKASESDAEIKDMK------ETIFELEDQVEQHRAVKLHNNqlISELESSVIKLEEQKSDLERQLKTL 629
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEELEerhelyEEAKAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKI 410
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 119571305 630 TkqmkEETEEWRRFQADLQTAVvvaNDIKcEAQQELRTVKRKLLEEEEKN 679
Cdd:PRK03918 411 T----ARIGELKKEIKELKKAI---EELK-KAKGKCPVCGRELTEEHRKE 452
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
343-681 |
4.62e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.27 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 343 TSFHQHRERAE-QLSQENEKLMNLLQERVKNEEPTT--QEGKIIEL---EQKCTGILEQGRFER----EKLLNIQQQLTC 412
Cdd:PLN02939 91 TSSDDDHNRASmQRDEAIAAIDNEQQTNSKDGEQLSdfQLEDLVGMiqnAEKNILLLNQARLQAledlEKILTEKEALQG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 413 SLRKVEEENQGALEMIKRLKEEN---EKLNEFLELERHNNNMMAKTLEECRVT----LEGLKMENGSLKSHLQGEKqkaT 485
Cdd:PLN02939 171 KINILEMRLSETDARIKLAAQEKihvEILEEQLEKLRNELLIRGATEGLCVHSlskeLDVLKEENMLLKDDIQFLK---A 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 486 EASAVEQTAESCEVQEmlkvarAEKDLLELSCNELRQELLKANGEIKHVSSL-----LAKVEKdysyLKEICDHQAEQLS 560
Cdd:PLN02939 248 ELIEVAETEERVFKLE------KERSLLDASLRELESKFIVAQEDVSKLSPLqydcwWEKVEN----LQDLLDRATNQVE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 561 RTSLKLQEKasesdaeiKDMKETIFELEDQVEqhravklhnnqliselESSVIKLEEQKSDLerqlktLTKQMKEETEEW 640
Cdd:PLN02939 318 KAALVLDQN--------QDLRDKVDKLEASLK----------------EANVSKFSSYKVEL------LQQKLKLLEERL 367
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 119571305 641 RRFQADLQTAVVVANDIKCEAQQELrtvkRKLLEEEEKNAR 681
Cdd:PLN02939 368 QASDHEIHSYIQLYQESIKEFQDTL----SKLKEESKKRSL 404
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
288-686 |
5.62e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 288 SLASLTEKIQKMEE-NHHSTAEELQATLQELSDQqqmVQELTAENEKLVDEKTILETSFHQHRERAEQLS---QENEKLM 363
Cdd:PRK02224 188 SLDQLKAQIEEKEEkDLHERLNGLESELAELDEE---IERYEEQREQARETRDEADEVLEEHEERREELEtleAEIEDLR 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 364 NLLQERVKN-----EEPTTQEGKIIELEQKCTGILEQGRFE----------REKLLNIQQQLTCSLRKVEEENQGALEMI 428
Cdd:PRK02224 265 ETIAETEREreelaEEVRDLRERLEELEEERDDLLAEAGLDdadaeavearREELEDRDEELRDRLEECRVAAQAHNEEA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 429 KRLKEENEKLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLkshlqgEKQKATEASAVEQTAESCE-VQEMLKVAR 507
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL------EEEIEELRERFGDAPVDLGnAEDFLEELR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 508 AEKDLLELSCNELRQELLKANGEIKHVSSLLAKVE--------KDYSYLKEICDHqaeqlsrtslklQEKASESDAEIKD 579
Cdd:PRK02224 419 EERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvEGSPHVETIEED------------RERVEELEAELED 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 580 MKETIFELEDQVEqhRAVKLhnnqliSELESSVIKLEEQKSDLERQL---KTLTKQMKEETEEWRRFQADLQTAVVVAND 656
Cdd:PRK02224 487 LEEEVEEVEERLE--RAEDL------VEAEDRIERLEERREDLEELIaerRETIEEKRERAEELRERAAELEAEAEEKRE 558
|
410 420 430
....*....|....*....|....*....|
gi 119571305 657 IKCEAQQELRTVKRKLLEEEEKNARLQKEL 686
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAELNSKLAELKERI 588
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
285-568 |
7.01e-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: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 285 SELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRER---AEQLSQENEK 361
Cdd:pfam15921 494 SERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKdkvIEILRQQIEN 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 362 LMNL-----------------LQERVKNEEPTTQEGKII---------ELEQKCTGIleqgRFEREKLLNIQQQLTCSLR 415
Cdd:pfam15921 574 MTQLvgqhgrtagamqvekaqLEKEINDRRLELQEFKILkdkkdakirELEARVSDL----ELEKVKLVNAGSERLRAVK 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 416 KVEEENQGALEMIKRLKEENEKLNEFLELERHNnnmMAKTLEECRVTLEGLKMENGSLKSHLQGEK-------------- 481
Cdd:pfam15921 650 DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN---FRNKSEEMETTTNKLKMQLKSAQSELEQTRntlksmegsdgham 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 482 ------QKATEASAVEQTAESCEVQ---EMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEIC 552
Cdd:pfam15921 727 kvamgmQKQITAKRGQIDALQSKIQfleEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKV 806
|
330
....*....|....*.
gi 119571305 553 DHQAEQLSRTSLKLQE 568
Cdd:pfam15921 807 ANMEVALDKASLQFAE 822
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
292-459 |
7.54e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 39.31 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 292 LTEKIQKMEENHHSTAEELQATLQeLSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQERVK 371
Cdd:PRK12705 31 LAKEAERILQEAQKEAEEKLEAAL-LEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 372 NEEP-TTQEGKIIELEQKCTGILEQ-GRFEREKllniQQQLTCSLRKVEEENQGALEmIKRLKEENEklnefLELERHNN 449
Cdd:PRK12705 110 REKAlSARELELEELEKQLDNELYRvAGLTPEQ----ARKLLLKLLDAELEEEKAQR-VKKIEEEAD-----LEAERKAQ 179
|
170
....*....|
gi 119571305 450 NMMAKTLEEC 459
Cdd:PRK12705 180 NILAQAMQRI 189
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
282-687 |
7.82e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.56 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 282 NSVSELSlASLTEKIQKMEENHHS----TAEELQATLQElsDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLsQ 357
Cdd:PRK04863 796 EELAERY-ATLSFDVQKLQRLHQAfsrfIGSHLAVAFEA--DPEAELRQLNRRRVELERALADHESQEQQQRSQLEQA-K 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 358 ENEKLMNLLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFERE--KLLNIQQQLTCSLRKVEEEnqgaLEMIKRLKEEN 435
Cdd:PRK04863 872 EGLSALNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFVQQhgNALAQLEPIVSVLQSDPEQ----FEQLKQDYQQA 947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 436 EKlneflelERHNNNMMAKTLEECRVTLEGLKMENgslkshlqgekqkateasAVEQTAESCEVQEMLkvaRAEKDLLEL 515
Cdd:PRK04863 948 QQ-------TQRDAKQQAFALTEVVQRRAHFSYED------------------AAEMLAKNSDLNEKL---RQRLEQAEQ 999
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 516 SCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDmketifELEDQVEQHR 595
Cdd:PRK04863 1000 ERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARARRD------ELHARLSANR 1073
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119571305 596 AVKlhnNQLiselessviklEEQKSDLERQLKTLTKQMKEETEEWRrfqaDLQTAVVVANDIKCEAQQELRT--VKRKLL 673
Cdd:PRK04863 1074 SRR---NQL-----------EKQLTFCEAEMDNLTKKLRKLERDYH----EMREQVVNAKAGWCAVLRLVKDngVERRLH 1135
|
410 420
....*....|....*....|.
gi 119571305 674 EEE-------EKNARLQKELG 687
Cdd:PRK04863 1136 RRElaylsadELRSMSDKALG 1156
|
|
| |
