|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
184-521 |
1.52e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 184 HDRLQLQIQKREVENERLKEHIQSLETQIAkwnlqvkmnkqeavavkeASRQKAEALKKASKVYRQRLRHFTGDIEQLTS 263
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIA------------------ELEKALAELRKELEELEEELEQLRKELEELSR 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 264 QIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQI----SHLLEDLRKMET------HGKNSCEEILRKLH 333
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLeeaeEELAEAEAEIEEleaqieQLKEELKALREALD 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 334 SLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKNLLHEnkliI 413
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE----R 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 414 NKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVDGNYSLLTKLSLEEENh 493
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEN- 961
|
330 340
....*....|....*....|....*...
gi 564339144 494 liqlkceNLKEKLEQMDAENKELERKLA 521
Cdd:TIGR02168 962 -------KIEDDEEEARRRLKRLENKIK 982
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
247-629 |
4.97e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.75 E-value: 4.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 247 YRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAiektELEVQIETMKKQIShllEDLRKMETHgKNSCE 326
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE----TLEAEIEDLRETIA---ETEREREEL-AEEVR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 327 EILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQE--VEKRQKAL-----VEGYRTQVQKLEEAAAMVK 399
Cdd:PRK02224 283 DLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDrlEECRVAAQahneeAESLREDADDLEERAEELR 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 400 SRCKNL---LHENKLIINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQV 476
Cdd:PRK02224 363 EEAAELeseLEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 477 DGNYSLLTK-------LSLEEENHLIQLkcENLKEKLEQMDAENKELERKLADQEEFLKHSDlELREKAAECTALSRQLE 549
Cdd:PRK02224 443 EEAEALLEAgkcpecgQPVEGSPHVETI--EEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERRE 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 550 AA---LEEGRQKVSEEVEKMSS-RERAlqmkiSDLETELRKKNEEQNQLVGNMSTKAQHQDIC------LKEIQHSLEKS 619
Cdd:PRK02224 520 DLeelIAERRETIEEKRERAEElRERA-----AELEAEAEEKREAAAEAEEEAEEAREEVAELnsklaeLKERIESLERI 594
|
410
....*....|
gi 564339144 620 ETQNESIKNY 629
Cdd:PRK02224 595 RTLLAAIADA 604
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
166-483 |
5.28e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 166 EKESALKANRFSQSVKVVHDRLQ-LQIQKREVENERLKEHIQSLETQIAKWNLQVkmnkQEAVAVKEASRQKAEALKKAS 244
Cdd:COG1196 208 QAEKAERYRELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 245 KVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAvsasndwksryekiAIEKTELEVQIETMKKQISHLLEDLRKMETHGKNS 324
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRREL--------------EERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 325 CEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKN 404
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564339144 405 LLHENKLIINKKNTKLEKMRGQVEtHLEQVEQARNSITSAEQRLQECQENLQRCKEKcAEQALTIRELQGQVDGNYSLL 483
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAE-LEEEEEALLELLAELLEEAALLEAALAELLEE-LAEAAARLLLLLEAEADYEGF 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
199-556 |
7.83e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 7.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 199 ERLKEHIQSLETQIAKwnLqvkmnKQEAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSA 278
Cdd:COG1196 189 ERLEDILGELERQLEP--L-----ERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 279 SNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMEthgkNSCEEILRKLHSLEDENEALNIENVKLKSTLDALKD 358
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLE----QDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 359 EVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAmvksrcknllhenkliinKKNTKLEKMRGQVETHLEQVEQAR 438
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA------------------EAEEELEELAEELLEALRAAAELA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 439 NSITSAEQRLQECQENLQRCKEKCAEQALTIRELqgqvdgnysLLTKLSLEEENHLIQLKCENLKEKLEQMDAENKELER 518
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAEL---------EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
330 340 350
....*....|....*....|....*....|....*...
gi 564339144 519 KLADQEEFLKHSDLELREKAAEctALSRQLEAALEEGR 556
Cdd:COG1196 471 EAALLEAALAELLEELAEAAAR--LLLLLEAEADYEGF 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
226-556 |
8.58e-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: 62.00 E-value: 8.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 226 AVAVKEASRQKAEALKKASKVYRQRLrhftgdiEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKK 305
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEEL-------EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 306 QISHLLEdlrkmethgknsceeilrKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYR 385
Cdd:TIGR02168 303 QKQILRE------------------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 386 TQVQKLEEAaamvksrcknllhenkliINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEkcaeq 465
Cdd:TIGR02168 365 AELEELESR------------------LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ----- 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 466 alTIRELQGQVDGNYSLLTKLSLEEENHLIqlkcENLKEKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTALS 545
Cdd:TIGR02168 422 --EIEELLKKLEEAELKELQAELEELEEEL----EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
330
....*....|.
gi 564339144 546 RQLEAALEEGR 556
Cdd:TIGR02168 496 RLQENLEGFSE 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-606 |
1.22e-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: 61.61 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 192 QKREVEN--ERLKEHIQSLETQIAKWNLQVKMNKQEAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQE 269
Cdd:TIGR02168 173 RRKETERklERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 270 AKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMETHgknsCEEILRKLHSLEDENEALNIENVKL 349
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ----KQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 350 KSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAaamvksrcknllhenkliINKKNTKLEKMRGQVET 429
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR------------------LEELEEQLETLRSKVAQ 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 430 HLEQVEQARNSITSAEQRLQECQENLQRCKEkcaEQALTIRELQgqvdgnyslltklslEEENHLIQLKCENLKEKLEQM 509
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQ---EIEELLKKLE---------------EAELKELQAELEELEEELEEL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 510 DAENKELERKLADQeeflkhsdlelrekaaectalsRQLEAALEEGRQKVSEEVEKMSSRERALQmkisDLETELRKKNE 589
Cdd:TIGR02168 453 QEELERLEEALEEL----------------------REELEEAEQALDAAERELAQLQARLDSLE----RLQENLEGFSE 506
|
410
....*....|....*..
gi 564339144 590 EQNQLVGNMSTKAQHQD 606
Cdd:TIGR02168 507 GVKALLKNQSGLSGILG 523
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
295-586 |
2.47e-09 |
|
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: 60.47 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 295 ELEVQIETMKKQISHLLEDLRKMETH---GKNSCEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQ 371
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRldeLSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 372 EVEKRQKALVEGYRTQVQKLEEAAAMVKSRcknLLHENKLIINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQEC 451
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNDLEAR---LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 452 QENLQR----CKEKCAEQALTIRELQGQVDGNYSLLTKL-----SLEEENHLIQLKCENLKEKLEQMdaenKELERKLAD 522
Cdd:TIGR02169 835 IQELQEqridLKEQIKSIEKEIENLNGKKEELEEELEELeaalrDLESRLGDLKKERDELEAQLREL----ERKIEELEA 910
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564339144 523 QEEFLKHSDLELREKAAectALSRQLEAALEEGRQKVSEEVEKMSsrERALQMKISDLETELRK 586
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLE---ALEEELSEIEDPKGEDEEIPEEELS--LEDVQAELQRVEEEIRA 969
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
419-594 |
5.72e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 5.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 419 KLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVdgnYSLLTKLS-LEEENHLIQL 497
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE---YELLAELArLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 498 KCENLKEKLEQMDAENKELERKLADQEEflkhSDLELREKAAECTALSRQLEAALEEGRQKVSEEVEKMSSRERALQMKI 577
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEE----ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170
....*....|....*..
gi 564339144 578 SDLETELRKKNEEQNQL 594
Cdd:COG1196 386 EELLEALRAAAELAAQL 402
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
130-615 |
1.29e-08 |
|
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: 58.21 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 130 CLLKD-LSDSDSENRDLKKKVLEKETYIQELSCLFHNEKESALKANRFSQSVKVVHDRLQlqiqkreveNERLKEHIQSL 208
Cdd:pfam15921 159 CLKEDmLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSL---------GSAISKILREL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 209 ETQIAKWNLQVKMNKQEAVAVKEASRQKAEALkkaskvyrqrLRHFTGDIEQLTSQ----IRDQEAKLSEAVSASNDWKS 284
Cdd:pfam15921 230 DTEISYLKGRIFPVEDQLEALKSESQNKIELL----------LQQHQDRIEQLISEheveITGLTEKASSARSQANSIQS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 285 RYEKIAIEKTELEV----QIETMKKQISHLLEDLRKMETHGKNSCEEILRKL-------HSLEDENEALNIENVKLKSTL 353
Cdd:pfam15921 300 QLEIIQEQARNQNSmymrQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLvlanselTEARTERDQFSQESGNLDDQL 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 354 DALKDEVASVENELVELQEVEKRQ--------------KALVEGYRTQVQKLEEAAAMVKSRCKNLLHENKLIINKKNTK 419
Cdd:pfam15921 380 QKLLADLHKREKELSLEKEQNKRLwdrdtgnsitidhlRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNES 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 420 LEK---MRGQVETH-------LEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVDGNYSLLTKLSLE 489
Cdd:pfam15921 460 LEKvssLTAQLESTkemlrkvVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 490 EEnHL--IQLKCENLKEKLEQMDAENKELERKLADQEEFLKHSDlelrEKAAECTALSRQLEAALEEGRQKVSE---EVE 564
Cdd:pfam15921 540 GD-HLrnVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHG----RTAGAMQVEKAQLEKEINDRRLELQEfkiLKD 614
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 564339144 565 KMSSRERALQMKISDLETELRKKNEEQNQLVGNMSTKAQHQDICLKEIQHS 615
Cdd:pfam15921 615 KKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTS 665
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
256-594 |
2.90e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 256 GDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMETHGKNSCEEI------- 328
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIeeleekv 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 329 --LRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQ--------------EVEKRQKAL---VEGYRTQVQ 389
Cdd:PRK03918 283 keLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEerikeleekeerleELKKKLKELekrLEELEERHE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 390 KLEEAAAMVK---SRCKNLLHENKLIINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCaeqA 466
Cdd:PRK03918 363 LYEEAKAKKEeleRLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC---P 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 467 LTIRELQGQVDGNysLLTKLSLEEENhlIQLKCENLKEKLEQMDAENKELERKLADQEEFLKhsdleLREKAAECTALSR 546
Cdd:PRK03918 440 VCGRELTEEHRKE--LLEEYTAELKR--IEKELKEIEEKERKLRKELRELEKVLKKESELIK-----LKELAEQLKELEE 510
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 564339144 547 QLEAALEEGRQKVSEEVEKMSSRERALQMKISDLETELRKKNEEQNQL 594
Cdd:PRK03918 511 KLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
433-621 |
3.61e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 433 QVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVDGNYSLLTKLSLEEEnhliqlkcENLKEKLEQMDAE 512
Cdd:COG4913 282 RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRL--------EQLEREIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 513 NKELERKLADQEEFLKHSDLELREKAAECTALSRQLEAALEEgrqkVSEEVEKMSSRERALQMKISDLETELRKKNEEQN 592
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA----LEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
170 180
....*....|....*....|....*....
gi 564339144 593 QLVGNMSTKAQHQDICLKEIQHSLEKSET 621
Cdd:COG4913 430 SLERRKSNIPARLLALRDALAEALGLDEA 458
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
348-624 |
1.60e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 348 KLKSTLDALKDEVAsveneLVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRcKNLLHENKLIINKKNTKLEKMRGQV 427
Cdd:COG1196 217 ELKEELKELEAELL-----LLKLRELEAELEELEAELEELEAELEELEAELAEL-EAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 428 ETHLEQVEQARNSITSAEQRLQECQENLQRckekcaeQALTIRELQGQVDGNYSLLTKLSLEEENHLIQLkcENLKEKLE 507
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEE-------LEEELAELEEELEELEEELEELEEELEEAEEEL--EEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 508 QMDAENKELERKLADQEEflkhSDLELREKAAECTALSRQLEAALEEGRQKVSEEVEKMSSRERALQMKISDLETELRKK 587
Cdd:COG1196 362 EAEEALLEAEAELAEAEE----ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270
....*....|....*....|....*....|....*..
gi 564339144 588 NEEQNQLVGNMSTKAQHQDICLKEIQHSLEKSETQNE 624
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
226-450 |
8.77e-07 |
|
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: 51.69 E-value: 8.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 226 AVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKK 305
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 306 QISHLLED----LRKMETHGKNSCEEILRKLHSLEDENEALNIenvkLKSTLDALKDEVASVENELVELQEVEKRQKALv 381
Cdd:COG4942 98 ELEAQKEElaelLRALYRLGRQPPLALLLSPEDFLDAVRRLQY----LKYLAPARREQAEELRADLAELAALRAELEAE- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564339144 382 egyRTQVQKLEEAAAMVKSRCKNLLHENKLIINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQE 450
Cdd:COG4942 173 ---RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
133-622 |
9.04e-07 |
|
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: 52.43 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 133 KDLSDSDSENRDLKKKVLEKETYIQELSCLFHNEKESALKANRFSQSVKVvhDRLQLQIQKREVENERLKEHIQSLETQI 212
Cdd:pfam15921 365 RDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITI--DHLRRELDDRNMEVQRLEALLKAMKSEC 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 213 akwnlQVKMNKQ-EAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAI 291
Cdd:pfam15921 443 -----QGQMERQmAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNA 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 292 EKTELEVQIETMKKQISHLLEDLRKMEtHGKNSCEEILRKLHSLEDENEAL--NIENV-----KLKSTLDALKDEVASVE 364
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKNEGDHLR-NVQTECEALKLQMAEKDKVIEILrqQIENMtqlvgQHGRTAGAMQVEKAQLE 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 365 NELVELQEVEKRQKALVEGYRTQVQKLEeaaamvkSRCKNLLHENKLIINKKNTKLEKMRG---QVETHLEQVEQARNSI 441
Cdd:pfam15921 597 KEINDRRLELQEFKILKDKKDAKIRELE-------ARVSDLELEKVKLVNAGSERLRAVKDikqERDQLLNEVKTSRNEL 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 442 TSAEQRLQECQENLqrcKEKCAEQALTIRELQGQVDGNYSLL-----TKLSLE-EENHLIQLKC---ENLKEKLEQMDAe 512
Cdd:pfam15921 670 NSLSEDYEVLKRNF---RNKSEEMETTTNKLKMQLKSAQSELeqtrnTLKSMEgSDGHAMKVAMgmqKQITAKRGQIDA- 745
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 513 nkeLERKLADQEEFLKHSDLELREKAAECTALSRQLEAALEEgRQKVSEEVEKMSSRERALQMKISDLETELRKKNEEQN 592
Cdd:pfam15921 746 ---LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE-KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFA 821
|
490 500 510
....*....|....*....|....*....|
gi 564339144 593 QLVGNMstKAQHQDICLKEIQHSLEKSETQ 622
Cdd:pfam15921 822 ECQDII--QRQEQESVRLKLQHTLDVKELQ 849
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
365-595 |
1.59e-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: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 365 NELVELQEVEKRQKALVEGYRTQVQKLEEAAAMvKSRCKNLLHEnkliinKKNTKLEKMRGQVETHLEQVEQARNSITSA 444
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREK-AERYQALLKE------KREYEGYELLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 445 EQRLQECQENLQRCKEKCAEQALTIRELQGQVDgnyslltKLSLEEENhliqlkceNLKEKLEQMDAENKELERKLADQE 524
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIK-------DLGEEEQL--------RVKEKIGELEAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564339144 525 EFLKHSD-------LELREKAAECTALSRQLEAALEEgRQKVSEEVEKMSSRERALQMKISDLETELRKKNEEQNQLV 595
Cdd:TIGR02169 315 RELEDAEerlakleAEIDKLLAEIEELEREIEEERKR-RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
185-591 |
2.49e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 185 DRLQLQIQKREVENERLKEHIQSLETQIAKWNLQVKMNKQEAVAVKEAS---RQKAEALKKASKVYRQRLRHFTGDIEQL 261
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAeelREEAAELESELEEAREAVEDRREEIEEL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 262 TSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMET---HGK--------------NS 324
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleAGKcpecgqpvegsphvET 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 325 CEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASvENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKN 404
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 405 L-------------LHENKLIINKKNTKLEKMRGQVETHLEQVEQARNS---ITSAEQRLQECQE--------NLQRcKE 460
Cdd:PRK02224 549 LeaeaeekreaaaeAEEEAEEAREEVAELNSKLAELKERIESLERIRTLlaaIADAEDEIERLREkrealaelNDER-RE 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 461 KCAEQALTIRELQGQVDGNYslLTKLSLEEENHLIQLkcENLKEKLEQMDAENKELERKLADQEEFLKHSDlELREKAAE 540
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEAR--IEEAREDKERAEEYL--EQVEEKLDELREERDDLQAEIGAVENELEELE-ELRERREA 702
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 564339144 541 CTALSRQLEAALEEgrqkvSEEVEKMSSRERAlqmkisdletELRKKNEEQ 591
Cdd:PRK02224 703 LENRVEALEALYDE-----AEELESMYGDLRA----------ELRQRNVET 738
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
223-539 |
3.35e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 223 KQEAVAVKEASRQKAEALKKASKVYRQrLRHFTGDIEQLTSQIRDQEAKLSEA------VSASNDWKSRYEKIAIEKT-- 294
Cdd:TIGR02169 219 EKREYEGYELLKEKEALERQKEAIERQ-LASLEEELEKLTEEISELEKRLEEIeqlleeLNKKIKDLGEEEQLRVKEKig 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 295 ELEVQIETMKKQISHLLEDLRKMETHGKNSCEEI---LRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELvelQ 371
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIdklLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL---E 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 372 EVEKRQKALVEGYRTQVQKLEEAaamvksrcKNLLHENKLIINKKNTKLEKMRgqvethlEQVEQARNSITSAEQRLQEC 451
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKL--------KREINELKRELDRLQEELQRLS-------EELADLNAAIAGIEAKINEL 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 452 QENLQrckekcaEQALTIRELQGQVDgnySLLTKLSLEEENHliqlkcENLKEKLEQMDAENKELERKLADQEEFLKHSD 531
Cdd:TIGR02169 440 EEEKE-------DKALEIKKQEWKLE---QLAADLSKYEQEL------YDLKEEYDRVEKELSKLQRELAEAEAQARASE 503
|
....*...
gi 564339144 532 LELREKAA 539
Cdd:TIGR02169 504 ERVRGGRA 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
186-593 |
5.83e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 186 RLQLQIQKREVENERLKEHIQSLETQIAkwnlqvkmnkQEAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQI 265
Cdd:COG4913 278 RAALRLWFAQRRLELLEAELEELRAELA----------RLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 266 RDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLrkmethgknscEEILRKLHSLEDENEAlniE 345
Cdd:COG4913 348 ERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL-----------EEELEALEEALAEAEA---A 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 346 NVKLKSTLDALKDEVASVEN-------------------------------ELVELQEVEKRQKALVEGY-RTQ------ 387
Cdd:COG4913 414 LRDLRRELRELEAEIASLERrksniparllalrdalaealgldeaelpfvgELIEVRPEEERWRGAIERVlGGFaltllv 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 388 -VQKLEEAAAMVKS----------RCKNLLHENKLIINKKNTKLEKM-------RGQVETHL------------EQVEQA 437
Cdd:COG4913 494 pPEHYAAALRWVNRlhlrgrlvyeRVRTGLPDPERPRLDPDSLAGKLdfkphpfRAWLEAELgrrfdyvcvdspEELRRH 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 438 RNSIT----------------------------SAEQRLQECQENLQRCKEKCAEQALTIRELQGQVDGN------YSLL 483
Cdd:COG4913 574 PRAITragqvkgngtrhekddrrrirsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALqerreaLQRL 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 484 TKLSLEEENHL-IQLKCENLKEKLEQMDAEN---KELERKLADQEEFLKHSDLELREKAAECTALSRQLEAALEEgRQKV 559
Cdd:COG4913 654 AEYSWDEIDVAsAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE-LDEL 732
|
490 500 510
....*....|....*....|....*....|....
gi 564339144 560 SEEVEKMSSRERALQmkISDLETELRKKNEEQNQ 593
Cdd:COG4913 733 QDRLEAAEDLARLEL--RALLEERFAAALGDAVE 764
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
89-633 |
8.78e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 8.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 89 KKIFEQKDILSKELDTFNRVKLALEHLIKQTDyeqtgprppcLLKDLSDSDSENRDLKKKVLEKETYIQELScLFHNEKE 168
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQIE----------LLEPIRELAERYAAARERLAELEYLRAALR-LWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 169 SALKANRfsqsvkvvHDRLQLQIQKREVENERLKEHIQSLETQIAkwNLQVKMNKQEAVAVKEASRQKAEALKKASKVyR 248
Cdd:COG4913 290 LELLEAE--------LEELRAELARLEAELERLEARLDALREELD--ELEAQIRGNGGDRLEQLEREIERLERELEER-E 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 249 QRLRHFTGDIEQLTSQIRDQEAKL----SEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMETHGKNs 324
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSN- 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 325 ceeILRKLHSLEDE-NEALNIENVKLKstldalkdeVASvenELVELQEVEKRQKALVEGY-RTQ-------VQKLEEAA 395
Cdd:COG4913 438 ---IPARLLALRDAlAEALGLDEAELP---------FVG---ELIEVRPEEERWRGAIERVlGGFaltllvpPEHYAAAL 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 396 AMVKSRcKNLLHENKLIINKKNTKLEKMRGQVETHLEQVEQARNSITS-AEQRLQE-----C---QENLQRckekcAEQA 466
Cdd:COG4913 503 RWVNRL-HLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAwLEAELGRrfdyvCvdsPEELRR-----HPRA 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 467 LTIrelQGQVDGNYSLLTK--LSLEEENHLIQlkcENLKEKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTAL 544
Cdd:COG4913 577 ITR---AGQVKGNGTRHEKddRRRIRSRYVLG---FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 545 SR------------QLEAALEEGRQKVsEEVEKMSSRERALQMKISDLETELRKKNEEQNQLVGNMSTKAQHQDICLKEI 612
Cdd:COG4913 651 QRlaeyswdeidvaSAEREIAELEAEL-ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
|
570 580
....*....|....*....|.
gi 564339144 613 QHSLEKSETQNESIKNYLQFL 633
Cdd:COG4913 730 DELQDRLEAAEDLARLELRAL 750
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
133-628 |
2.81e-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: 47.32 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 133 KDLSDSDSENRDLKKKVL----EKETYIQELSCLFHNEKESALKANRFSQSVKVV------HDRLQLQIQKREVENERLK 202
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEelenELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLkkkiqkNKSLESQISELKKQNNQLK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 203 EHIQSLETQIAKWNLQVKMNKQEAVAVKEASRQKAEALKKASKvyrqRLRHFTGDIEQLTSQIRDQEAKLSE-----AVS 277
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK----ELEQNNKKIKELEKQLNQLKSEISDlnnqkEQD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 278 ASNDWKSRYEKIAIEKTELEVQIETMKKQISHL---LEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVKLKSTLD 354
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLneqISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 355 ALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKNLLHENKLIINK---KNTKLEKMRGQVETHL 431
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvKELIIKNLDNTRESLE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 432 EQVEQARNSITSAEQRLQECQENLqrcKEKCAEQALTIRElqgqvdgnyslltKLSLEEENHLIQLKCENLKEKLEQMDA 511
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKEL---KSKEKELKKLNEE-------------KKELEEKVKDLTKKISSLKEKIEKLES 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 512 ENKELERKLADQEEFLKHSDLELREKAaectalsrqleaaLEEGRQKVSEEVEKMSSRERALQMKISDLETELRKKNEEQ 591
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELKKEN-------------LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEK 598
|
490 500 510
....*....|....*....|....*....|....*..
gi 564339144 592 NQLVGNMSTKAQHQDICLKEIQHSLEKSETQNESIKN 628
Cdd:TIGR04523 599 KDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
353-625 |
2.86e-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: 47.36 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 353 LDALKDEVASVENELVELQevekRQKALVEGYRTQVQKLEEA----AAMVKSRCKNLLHENKLIINKKNTKLEKMRGQVE 428
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLE----RQAEKAERYKELKAELRELelalLVLRLEELREELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 429 THLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEqaltirelqgqvdgnyslltklsLEEENHLIQLKCENLKEKLEQ 508
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALANEISR-----------------------LEQQKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 509 MDAENKELERKLADQEEFLKHSDLELREKAAECTALsrqlEAALEEGRqkvsEEVEKMSSRERALQMKISDLETELRKKN 588
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESL----EAELEELE----AELEELESRLEELEEQLETLRSKVAQLE 392
|
250 260 270
....*....|....*....|....*....|....*..
gi 564339144 589 EEQNQLvgnmSTKAQHQDICLKEIQHSLEKSETQNES 625
Cdd:TIGR02168 393 LQIASL----NNEIERLEARLERLEDRRERLQQEIEE 425
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
98-604 |
3.06e-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: 47.36 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 98 LSKELDTFNRVKLALEHLIKQTDYEQTGprppcLLKDLSDSDSENRDLKKKVLEKETYIQELSCLFHNEKESALKANRFS 177
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQE-----LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 178 QSVKVVHDRLQLQIQKREVENERLKEHIQSLETQIAkwnlQVKMNKQEAVAVKEASRQKAEALKKASKVYRQRLRHFTGD 257
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLE----ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 258 IEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQ-ISHLLEDLRKMETHGKNSCEEILRKLHSLE 336
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKeLQAELEELEEELEELQEELERLEEALEELR 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 337 DENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKALV--------------------EGYRTQVQK-LEEAA 395
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLknqsglsgilgvlselisvdEGYEAAIEAaLGGRL 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 396 AMVKSRCKN-------LLHENKL---------------IINKKNTKLEKMRGQVETHLEQVEQA---------------- 437
Cdd:TIGR02168 548 QAVVVENLNaakkaiaFLKQNELgrvtflpldsikgteIQGNDREILKNIEGFLGVAKDLVKFDpklrkalsyllggvlv 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 438 ------------------------------RNSIT----SAEQRLQECQENLQRCKEKCAEQALTIRELQGQVDGNYSLL 483
Cdd:TIGR02168 628 vddldnalelakklrpgyrivtldgdlvrpGGVITggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 484 TklSLEEENHLIQLKCENLKEKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTALSRQLE------AALEEGRQ 557
Cdd:TIGR02168 708 E--ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEeaeeelAEAEAEIE 785
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 564339144 558 KVSEEVEKMS-------SRERALQMKISDLETELRKKNEEQNQLVGNMSTKAQH 604
Cdd:TIGR02168 786 ELEAQIEQLKeelkalrEALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
383-635 |
3.25e-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: 47.36 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 383 GYRTQVQKLEEAAAMVKSRCKNLLHEnkliINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKC 462
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKA----LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 463 AEQALTIRELQGQVDGNYSLLTKLSLEEENHLIQLkcENLKEKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECT 542
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEI--EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 543 ALSRQLEAA------LEEGRQKVSEEVEKMSSRERALQMKISDLETELRKKNEEQNQL----------VGNMSTKAQHQD 606
Cdd:TIGR02168 828 SLERRIAATerrledLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLeealallrseLEELSEELRELE 907
|
250 260
....*....|....*....|....*....
gi 564339144 607 ICLKEIQHSLEKSETQNESIKNYLQFLQI 635
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEV 936
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
151-394 |
3.48e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 151 EKETYIQELSCLFHNEKESALKANRFSQsvkvvhdrlQLQIQKREVENERLKEHIQSLETQIAKwnLQVKMNKQEAVAVK 230
Cdd:COG3206 132 VKGSNVIEISYTSPDPELAAAVANALAE---------AYLEQNLELRREEARKALEFLEEQLPE--LRKELEEAEAALEE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 231 EASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLS--EAVSASNDWKSRYEKIAIEKTELEVQIETMKKQIS 308
Cdd:COG3206 201 FRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAalRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 309 HLLEDL-----------RKMETHGKNSCEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQ 377
Cdd:COG3206 281 ELSARYtpnhpdvialrAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREV 360
|
250
....*....|....*..
gi 564339144 378 KALVEGYRTQVQKLEEA 394
Cdd:COG3206 361 EVARELYESLLQRLEEA 377
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
187-590 |
9.79e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 187 LQLQIQKREVENERLKEHIQSLETQIAKWNLQVKMNKQEAVAVKE--ASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQ 264
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 265 IRDQEAKLSEAvsasNDWKSRYEKIAIEKTELEVQIETMKK------QISHLLEDLRKMETH-GKNSCEEILRKLHSLED 337
Cdd:PRK03918 323 INGIEERIKEL----EEKEERLEELKKKLKELEKRLEELEErhelyeEAKAKKEELERLKKRlTGLTPEKLEKELEELEK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 338 ENEALNIENVKLKSTLDALKDEVASVENELVELQEVekRQKALVEGYRTQVQKLEEAAAMVKSRCKNLLHENKLIINKKN 417
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIEELKKA--KGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 418 tKLEKMRGQVETHLEQVEQARNSITSAEQrLQECQENLQRCKEKCAEQALTirelqgqvdgNYSLLTKLSLEEENHLIQL 497
Cdd:PRK03918 477 -KLRKELRELEKVLKKESELIKLKELAEQ-LKELEEKLKKYNLEELEKKAE----------EYEKLKEKLIKLKGEIKSL 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 498 KCEnlKEKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTalsRQLEAALEEGRQKVSE--EVEKMSSRERALQM 575
Cdd:PRK03918 545 KKE--LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESV---EELEERLKELEPFYNEylELKDAEKELEREEK 619
|
410
....*....|....*
gi 564339144 576 KISDLETELRKKNEE 590
Cdd:PRK03918 620 ELKKLEEELDKAFEE 634
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
394-590 |
2.09e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 394 AAAMVKSRCKNLLHENKLIINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQ 473
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 474 GQVDGNYSLLTKL-----------------------SLEEENHLIQLKCENLKEKLEQMDAENKELERKLADQEEFLKHS 530
Cdd:COG4942 97 AELEAQKEELAELlralyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564339144 531 DLELREKAAECTALS------RQLEAALEEGRQKVSEEVEKMSSRERALQMKISDLETELRKKNEE 590
Cdd:COG4942 177 EALLAELEEERAALEalkaerQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
188-471 |
2.22e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 188 QLQIQKREVENERLKEHIQSLETQIAKWNLQVKMNKQEavavkeaSRQKAEALKKASKVYRQRLRhftgDIEQLTSQIRD 267
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL-------NQQKDEQIKKLQQEKELLEK----EIERLKETIIK 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 268 QEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMETHGKNSCEEIL---RKLHSLEDENEALNI 344
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKklnEEKKELEEKVKDLTK 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 345 ENVKLKSTLDALKDEVASVENELVELQE--VEKRQKALVEGYRTQVQKLEEAAAMVKSRCKNLLHEN---KLIINKKNTK 419
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDelNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQeekQELIDQKEKE 597
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 564339144 420 LEKMRGQVETHLEQVEQARNSITSAE---QRLQECQENLQRCKEKCAEQALTIRE 471
Cdd:TIGR04523 598 KKDLIKEIEEKEKKISSLEKELEKAKkenEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
498-594 |
2.54e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 498 KCENLKEKLEQMDAENKELERKLADQEEFLKHSDLELREkaaectalsrqleaALEEGRQKVSEEvEKMSSRERalqmKI 577
Cdd:COG2433 414 EIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSE--------------ARSEERREIRKD-REISRLDR----EI 474
|
90
....*....|....*..
gi 564339144 578 SDLETELRKKNEEQNQL 594
Cdd:COG2433 475 ERLERELEEERERIEEL 491
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
191-628 |
2.91e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 191 IQKREVENERLKEHIQSLETQIakwnlqvkMNKQEAVAVKEASRQKAEALKKAS----KVYRQRLRHFTGDIEQLTSQIR 266
Cdd:TIGR04523 28 ANKQDTEEKQLEKKLKTIKNEL--------KNKEKELKNLDKNLNKDEEKINNSnnkiKILEQQIKDLNDKLKKNKDKIN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 267 DQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMETHGK---NSCEEILRKLHSLEDENEALN 343
Cdd:TIGR04523 100 KLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEklnNKYNDLKKQKEELENELNLLE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 344 IENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVegyrTQVQKLEEAAAMVKSrcknllhenklIINKKNTKLEKM 423
Cdd:TIGR04523 180 KEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLE----SQISELKKQNNQLKD-----------NIEKKQQEINEK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 424 RGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVdgnySLLTKLSLEEENHLIQLKCENLK 503
Cdd:TIGR04523 245 TTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEI----SDLNNQKEQDWNKELKSELKNQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 504 EKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTALSRQLEAALEEGRQKVSEEVEKMSSRERaLQMKISDLETE 583
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN-LESQINDLESK 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 564339144 584 LRKKNEEQNQLVGNMSTKAQHQDICLKEIQHSLEKSETQNESIKN 628
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
187-631 |
3.13e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.96 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 187 LQLQIQKREVENERLKEHIQSLETQiAKWNLQVKMNKQEAVAVKEAsrqkaEALKKASKVYRQRLRHFTGDIEQLTSQIR 266
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKELEFEIQSQ-EQDSEIVKNSKSELARIPEL-----EKELERLREHNKHLNENIENKLLLKEEVE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 267 DQEAKLSEavsaSNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMETHgKNSCEEILRKLHSLEDENEALNIEN 346
Cdd:pfam05557 232 DLKRKLER----EEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDL-SRRIEQLQQREIVLKEENSSLTSSA 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 347 VKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQV----QKLEEAAAMVKSRCKNLLHEN-KLIINKKNTKLE 421
Cdd:pfam05557 307 RQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltKERDGYRAILESYDKELTMSNySPQLLERIEEAE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 422 KMRGQVETHLEQVEQarnsitsaeqRLQECQENLQRCKEKCAEQALTIRELQGQVDGNYSLLTKLSLEEenhliqlkcen 501
Cdd:pfam05557 387 DMTQKMQAHNEEMEA----------QLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDS----------- 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 502 LKEKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTALSRQLEAALEEGRQKvSEEVEKmssreraLQMKISDLE 581
Cdd:pfam05557 446 LRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQR-KNQLEK-------LQAEIERLK 517
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 564339144 582 TELRKKNEEQNQLVGNMSTKAQHQDICLKEIQHSLEKSETQNESIKNYLQ 631
Cdd:pfam05557 518 RLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQRLKEVFQ 567
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
183-620 |
3.46e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 183 VHDRLQLQ-IQKREVENERLKEHIQSLETQIAKwnLQVKMNKQEAVAVKEASRQkaEALKKASKVYRQRLRHFTGDIEQ- 260
Cdd:pfam12128 227 IRDIQAIAgIMKIRPEFTKLQQEFNTLESAELR--LSHLHFGYKSDETLIASRQ--EERQETSAELNQLLRTLDDQWKEk 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 261 ---LTSQIRDQEAKLSEA---VSASNDWKSRYEKIAIEKTELEV--------QIETMKKQISHLLEDLRKME----THGK 322
Cdd:pfam12128 303 rdeLNGELSAADAAVAKDrseLEALEDQHGAFLDADIETAAADQeqlpswqsELENLEERLKALTGKHQDVTakynRRRS 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 323 NSCEEILRKLHSLEDENEALNIENVKLKStldALKDEVASVENELVELQEVEKRQkalvegYRTQVQKLEEAAAMVKSRC 402
Cdd:pfam12128 383 KIKEQNNRDIAGIKDKLAKIREARDRQLA---VAEDDLQALESELREQLEAGKLE------FNEEEYRLKSRLGELKLRL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 403 KNLLHENKLIINKKN--TKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVDG-- 478
Cdd:pfam12128 454 NQATATPELLLQLENfdERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPqa 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 479 ----------------------NYSLLTKLSLEEENHLIQLKCEN----LKEKLEQMD-----AENKELERKLA------ 521
Cdd:pfam12128 534 gtllhflrkeapdweqsigkviSPELLHRTDLDPEVWDGSVGGELnlygVKLDLKRIDvpewaASEEELRERLDkaeeal 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 522 -DQEEFLKHSDLELREKAAECTALSRQLEAAL------EEGRQKVSEEVEKMSSR-ERALQMKISDLETELRKKNEEQNQ 593
Cdd:pfam12128 614 qSAREKQAAAEEQLVQANGELEKASREETFARtalknaRLDLRRLFDEKQSEKDKkNKALAERKDSANERLNSLEAQLKQ 693
|
490 500
....*....|....*....|....*..
gi 564339144 594 LVGNMSTKAQHQDICLKEiqHSLEKSE 620
Cdd:pfam12128 694 LDKKHQAWLEEQKEQKRE--ARTEKQA 718
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
230-631 |
4.62e-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: 43.50 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 230 KEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSaSNDWKSRYEKIAiEKTELEVQIETMKKQISH 309
Cdd:TIGR00606 586 INQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCG-SQDEESDLERLK-EEIEKSSKQRAMLAGATA 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 310 LLEDLRKMETHGKNSCEEILRKLHSLEDEneaLNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQ 389
Cdd:TIGR00606 664 VYSQFITQLTDENQSCCPVCQRVFQTEAE---LQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIID 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 390 KLEEAAAMVKSRCKNLLHEnkliINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQrLQECQENLQRCKEKCAEQAlti 469
Cdd:TIGR00606 741 LKEKEIPELRNKLQKVNRD----IQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTI-MERFQMELKDVERKIAQQA--- 812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 470 RELQGqVDGNyslltkLSLEEENHLIQLKcenlKEKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTALSRQLE 549
Cdd:TIGR00606 813 AKLQG-SDLD------RTVQQVNQEKQEK----QHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQ 881
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 550 --AALEEGRQKVSEEVEKMSSRERALQMKISDLETELRKKNEEQNQLVGNMSTKAQHQDICLKEIQHSLEKSETQNESIK 627
Cdd:TIGR00606 882 rrQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIE 961
|
....
gi 564339144 628 NYLQ 631
Cdd:TIGR00606 962 NKIQ 965
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
353-568 |
1.00e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 353 LDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRcknllhenkliinKKNTKLEKMRGQVETHLE 432
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE-------------IDVASAEREIAELEAELE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 433 QVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVDGnyslltklsleeenhlIQLKCENLKEKLEQMDAE 512
Cdd:COG4913 679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ----------------AEEELDELQDRLEAAEDL 742
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564339144 513 NKELERKLADqEEFLKHSDLELREKAAEctALSRQLEAALEEGRQKVSEEVEKMSS 568
Cdd:COG4913 743 ARLELRALLE-ERFAAALGDAVERELRE--NLEERIDALRARLNRAEEELERAMRA 795
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
132-588 |
1.05e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 132 LKDLSDSDSENRDLKKKVLEKETYIQELSclfhnEKESALKANRFSQSVKVVHDRLQLQIQKREVENERLKEHIQSLETQ 211
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELE-----AELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 212 IAKW-NLQVKMNKQEAvAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAvsasndwksryekia 290
Cdd:COG4717 155 LEELrELEEELEELEA-ELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA--------------- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 291 iektelEVQIETMKKQISHLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVeneLVEL 370
Cdd:COG4717 219 ------QEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL---LALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 371 QEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKNLLHENKLIINKKNTKLEKMRGQVETHLEQVEQARNSITSA--EQRL 448
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqlEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 449 QECQENLQRCK-------EKCAEQALTIRELQGQVDGNYSLLTKLSLEEENHLIQLKCENLKEKLEQMDAENKELERKLA 521
Cdd:COG4717 370 QEIAALLAEAGvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELE 449
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564339144 522 DQEEflKHSDLELREKAAECTALSRQLEAALEEGRQKVSEEVEKMSSReRALQMKISDLETELRKKN 588
Cdd:COG4717 450 ELRE--ELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAAL-KLALELLEEAREEYREER 513
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
193-627 |
1.46e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 193 KREVENERLKEHIQSLETQIAKWNLQVKMNKQEAVAVK-EASRQKAEALKKASKVYRQ--RLRHFTGDIEQLTSQIRDQE 269
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKkEEAKKKADAAKKKAEEKKKadEAKKKAEEDKKKADELKKAA 1414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 270 A---------KLSEAVSASNDWKSRYEKiAIEKTELEVQIETMKK--QISHLLEDLRKMETHGKNS-----CEEILRKLH 333
Cdd:PTZ00121 1415 AakkkadeakKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKaeEAKKKAEEAKKADEAKKKAeeakkADEAKKKAE 1493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 334 SLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKNLLHENKLII 413
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE 1573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 414 NKKNTKLEKMRgqvetHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVDGNYSLLTKLSLEEENH 493
Cdd:PTZ00121 1574 EDKNMALRKAE-----EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 494 LIQLKCENLKEKLEQMDAENKELERKLADQEefLKHSDlELREKAAECTALSRQLEAALEEGRQKVSEEVEKMSSRERAL 573
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAEE--AKKAE-EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE 1725
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 564339144 574 QMKISDLEtELRKKNEEQNQLVGNMSTKAQHQdiclKEIQHSLEKSETQNESIK 627
Cdd:PTZ00121 1726 EENKIKAE-EAKKEAEEDKKKAEEAKKDEEEK----KKIAHLKKEEEKKAEEIR 1774
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
358-634 |
1.65e-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: 41.59 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 358 DEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKNLLHENKLIINKKNTKLEKMRGQVETHLEQ---- 433
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISElekr 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 434 VEQARNSITSAEQRLQECQENLQ-RCKEKCAEQALTIRELQGQVDGNYSLLTKLS-----LEEENHLIQLKCENLKEKLE 507
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIASLERSIAEKERELEDAEerlakLEAEIDKLLAEIEELEREIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 508 -------QMDAENKELERKLADQEEFLKHSDLELREKAAECTALSRQLEAALEEgRQKVSEEVEKMSSRERALQMKISDL 580
Cdd:TIGR02169 347 eerkrrdKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE-INELKRELDRLQEELQRLSEELADL 425
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 564339144 581 ETELRKKNEEQNQLVGNMSTKA---QHQDICLKEIQHSLEKSETQNESIKNYLQFLQ 634
Cdd:TIGR02169 426 NAAIAGIEAKINELEEEKEDKAleiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
444-594 |
1.91e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 444 AEQRLQECQENLQRCKEKcaeqaltIRELQGQVDgnyslltKLSLEEEnhlIQLKCENLKEKLEQMDAE-----NKELER 518
Cdd:COG1196 177 AERKLEATEENLERLEDI-------LGELERQLE-------PLERQAE---KAERYRELKEELKELEAEllllkLRELEA 239
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564339144 519 KLADQEEFLKHSDLELREKAAEctalSRQLEAALEEGRQKVSE---EVEKMSSRERALQMKISDLETELRKKNEEQNQL 594
Cdd:COG1196 240 ELEELEAELEELEAELEELEAE----LAELEAELEELRLELEElelELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
185-396 |
2.12e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 185 DRLQLQIQKREVENERLKEHIQSLETQIAKWNLQVKmnkqeavavkeASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQ 264
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIA-----------ALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 265 IRDQEAKLSEAVSASndwksrYEKIAIEKTELEVQIETMkKQISHLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNI 344
Cdd:COG4942 99 LEAQKEELAELLRAL------YRLGRQPPLALLLSPEDF-LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564339144 345 ENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAA 396
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
386-574 |
2.47e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 386 TQVQKLEEAAAMVKSRCKNLLHEnkliINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQ 465
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAE----LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 466 ALTIRELQGQVD---------------GNYSLLTKLS----------------LEEENHLIQLKCENLKEKLEQMDAENK 514
Cdd:COG3883 92 ARALYRSGGSVSyldvllgsesfsdflDRLSALSKIAdadadlleelkadkaeLEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 515 ELERKLADQEEFLKHSDLELREKAAECTALSRQLEAALEEGRQKVSEEVEKMSSRERALQ 574
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
326-393 |
2.49e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 2.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564339144 326 EEILRKLHSLEDENEALNIE-NVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEE 393
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEqDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQ 482
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
408-594 |
2.71e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 408 ENKLIINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRckekcaeqaltireLQGQVDGNYSLLTKLS 487
Cdd:COG3206 195 EAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA--------------LRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 488 leeENHLIQlkceNLKEKLEQmdaenkeLERKLADQEEFLKHSDLELREKAAECTALSRQLEAALEEGRQKVSEEVEKMS 567
Cdd:COG3206 261 ---QSPVIQ----QLRAQLAE-------LEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQ 326
|
170 180
....*....|....*....|....*..
gi 564339144 568 SRERALQMKISDLETELRKKNEEQNQL 594
Cdd:COG3206 327 AREASLQAQLAQLEARLAELPELEAEL 353
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
444-576 |
2.73e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 444 AEQRLQECQENLQRCKEKCAEQALT-IRELQGQVDGNYSLLTKLSLEEENHLIQlKCENLKEKLEQMDAENKELErklaD 522
Cdd:PRK12704 40 AKRILEEAKKEAEAIKKEALLEAKEeIHKLRNEFEKELRERRNELQKLEKRLLQ-KEENLDRKLELLEKREEELE----K 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564339144 523 QEEFLKHSDLELREKAAECTALSRQLEAALE--------EGRQKVSEEVEKMSSRERALQMK 576
Cdd:PRK12704 115 KEKELEQKQQELEKKEEELEELIEEQLQELErisgltaeEAKEILLEKVEEEARHEAAVLIK 176
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
295-628 |
3.20e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.61 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 295 ELEVQIETMKKQISHLLEDLRKMETHGKNsceEILRKLHSLEDENEALNIENVKLKSTLDALKDEV--ASVENELVELQE 372
Cdd:PLN03229 433 ELEGEVEKLKEQILKAKESSSKPSELALN---EMIEKLKKEIDLEYTEAVIAMGLQERLENLREEFskANSQDQLMHPVL 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 373 VEKRQKALVEGYRTQVQKLEEAAAMVKSRCKNLLHENKLIINKKNtKLEKMRGQVETHLEQVEQArnsitsaeqrlQECQ 452
Cdd:PLN03229 510 MEKIEKLKDEFNKRLSRAPNYLSLKYKLDMLNEFSRAKALSEKKS-KAEKLKAEINKKFKEVMDR-----------PEIK 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 453 ENLQRCKEKCAEQAL-TIRELQgqvdgnyslltklsleeenhliqlkcENLKEKLEQMdaeNKELERKLAdqeEFLKHSD 531
Cdd:PLN03229 578 EKMEALKAEVASSGAsSGDELD--------------------------DDLKEKVEKM---KKEIELELA---GVLKSMG 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 532 LEL-----REKAAECTALSRQLEAALEEGRQKVSEEVEKM---------------------SSRERALQMKISDLETELR 585
Cdd:PLN03229 626 LEVigvtkKNKDTAEQTPPPNLQEKIESLNEEINKKIERVirssdlkskiellklevakasKTPDVTEKEKIEALEQQIK 705
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 564339144 586 KKNEEqnqlVGNMSTKAQHQDICLKEIQHSLEKSETQNESIKN 628
Cdd:PLN03229 706 QKIAE----ALNSSELKEKFEELEAELAAARETAAESNGSLKN 744
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
431-589 |
3.40e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.45 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 431 LEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVDGNYSLLTK-----------------LSLEEE-- 491
Cdd:PRK11637 74 LAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAqldaafrqgehtglqliLSGEESqr 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 492 -----------NHLIQLKCENLKEKLEQMDAENKELERKLADQEEFLkhSDLELREKAAECTALSRQ-----LEAALEEG 555
Cdd:PRK11637 154 gerilayfgylNQARQETIAELKQTREELAAQKAELEEKQSQQKTLL--YEQQAQQQKLEQARNERKktltgLESSLQKD 231
|
170 180 190
....*....|....*....|....*....|....
gi 564339144 556 RQKVSEevekMSSRERALQMKISDLETELRKKNE 589
Cdd:PRK11637 232 QQQLSE----LRANESRLRDSIARAEREAKARAE 261
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
187-611 |
3.46e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 187 LQLQIQKREVENERLKEHIQSLETQIAKWNLQVKM-----NKQEAVAV--------KEASRQKAEALKKASKVYRQRLRH 253
Cdd:pfam01576 143 LEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSlsklkNKHEAMISdleerlkkEEKGRQELEKAKRKLEGESTDLQE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 254 FTGDIEQLTSQIRDQEAKLSEAVSASNDwksRYEKIAIEKTELEVQIETMKKQISHLLEDLrKMETHGKNSCEEILRklh 333
Cdd:pfam01576 223 QIAELQAQIAELRAQLAKKEEELQAALA---RLEEETAQKNNALKKIRELEAQISELQEDL-ESERAARNKAEKQRR--- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 334 SLEDENEALNIENVKLKSTLDALKDEVASVENELVELQ-----EVEKRQKALVEGYRTQVQKLEEAAAMVKS--RCKNLL 406
Cdd:pfam01576 296 DLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKkaleeETRSHEAQLQEMRQKHTQALEELTEQLEQakRNKANL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 407 HENKLIINKKNTKLEKMRGQVETHLEQVEQARNSitsAEQRLQECQENLQRCKEKCAEQALTIRELQGQVDGNYSLLTKL 486
Cdd:pfam01576 376 EKAKQALESENAELQAELRTLQQAKQDSEHKRKK---LEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEA 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 487 ------------SLEEENHLIQLKCE-------NLKEKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTALSRQ 547
Cdd:pfam01576 453 egkniklskdvsSLESQLQDTQELLQeetrqklNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKK 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 548 LEA------ALEEGRQKVSEEVEKMSSRERALQMKISDLETELRKKNEE----------QNQLVGNMSTKAQHQDICLKE 611
Cdd:pfam01576 533 LEEdagtleALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQElddllvdldhQRQLVSNLEKKQKKFDQMLAE 612
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
194-564 |
3.65e-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: 40.48 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 194 REVENERLKEHIQSLET------QIAKWNLQVKMNKQEAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRD 267
Cdd:pfam05483 403 KEVELEELKKILAEDEKlldekkQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 268 QEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENV 347
Cdd:pfam05483 483 EKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGD 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 348 KLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQK----LEEAAAMVKSRCKNLLHENKLIiNKKNTKLEKM 423
Cdd:pfam05483 563 EVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENknknIEELHQENKALKKKGSAENKQL-NAYEIKVNKL 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 424 RGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVDgnysLLTKLSLEEENHLIQLKCENLK 503
Cdd:pfam05483 642 ELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEID----KRCQHKIAEMVALMEKHKHQYD 717
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564339144 504 EKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTALSRQLEAALEEGRQKVSEEVE 564
Cdd:pfam05483 718 KIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
258-586 |
3.87e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.71 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 258 IEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIA---------------IEKTELEVQIETMKKQISHLLEDLRKMETHGK 322
Cdd:COG3096 838 LAALRQRRSELERELAQHRAQEQQLRQQLDQLKeqlqllnkllpqanlLADETLADRLEELREELDAAQEAQAFIQQHGK 917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 323 N--SCEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASvenelveLQEVEKRQKALveGYRTQVQKLEEAAAMVKs 400
Cdd:COG3096 918 AlaQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFA-------LSEVVQRRPHF--SYEDAVGLLGENSDLNE- 987
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 401 rcknllhenkliinKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRL-----------QECQENLQRCKE------KCA 463
Cdd:COG3096 988 --------------KLRARLEQAEEARREAREQLRQAQAQYSQYNQVLaslkssrdakqQTLQELEQELEElgvqadAEA 1053
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 464 EQALTIR--ELQGQVDGNYSLLTklSLEEENHLIQLKCENLKEKLeqmdaenKELERKLADQEEFL-------------- 527
Cdd:COG3096 1054 EERARIRrdELHEELSQNRSRRS--QLEKQLTRCEAEMDSLQKRL-------RKAERDYKQEREQVvqakagwcavlrla 1124
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 528 KHSDLELREKAAECTALSrqleaaleegrqkvSEEVEKMS-SRERALQMKISDLEtELRK 586
Cdd:COG3096 1125 RDNDVERRLHRRELAYLS--------------ADELRSMSdKALGALRLAVADNE-HLRD 1169
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
131-573 |
4.06e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 131 LLKDLSDSDSENRDLKKKVLEKETYIQELSCLFHNEKESALKANRFSQSVKVVHDRLQLQIQKREVENERLKEHIQSLET 210
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 211 QIAKWNLQVKMNKQEAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIA 290
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 291 IEKTELEVQIEtMKKQISHLLEDLRkmETHGKNSCEEILRKLHSLEDENEALniENVKLKSTLDALKDEVASVENELVEL 370
Cdd:COG1196 488 EAAARLLLLLE-AEADYEGFLEGVK--AALLLAGLRGLAGAVAVLIGVEAAY--EAALEAALAAALQNIVVEDDEVAAAA 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 371 QEVEKRQKA------------------------LVEGYRTQVQKLEEAAAMVKSRCKNLLHENKLIINKKNTKLEKMRGQ 426
Cdd:COG1196 563 IEYLKAAKAgratflpldkiraraalaaalargAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTL 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 427 VETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQvdgnyslltkLSLEEENHLIQLKCENLKEKL 506
Cdd:COG1196 643 AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE----------ELELEEALLAEEEEERELAEA 712
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564339144 507 EQMDAENKELERKLADQEEFLKHSDLELREKAAECTALSRQLEAALEEGRQKVSEEVEKMSSRERAL 573
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
168-512 |
4.32e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.27 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 168 ESALKANRFSQSVKVVHDRLQLQIQKREVENERLKEHIQSLETQIAKWNLQ--VKMNKQEAVAVKEASRQKAEALKKASK 245
Cdd:PLN02939 81 RTVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEdlVGMIQNAEKNILLLNQARLQALEDLEK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 246 VYRQRlrhftgdiEQLTSQIRDQEAKLSEAVSASNdwKSRYEKIAIEKteLEVQIETMKKQISHLLEDLRKMEthgknsc 325
Cdd:PLN02939 161 ILTEK--------EALQGKINILEMRLSETDARIK--LAAQEKIHVEI--LEEQLEKLRNELLIRGATEGLCV------- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 326 eeilrklHSLEDENEALNIENVKLKSTLDALKDevasvenELVELQEVEKRqkalvegyrtqVQKLEEAAAMVKSRCKNL 405
Cdd:PLN02939 222 -------HSLSKELDVLKEENMLLKDDIQFLKA-------ELIEVAETEER-----------VFKLEKERSLLDASLREL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 406 lhENKLIINKKN-TKLEKMrgQVETHLEQVEQARNSITSAEQRLQECQENLQRCkekcaeqaltiRELQGQVDgnyslLT 484
Cdd:PLN02939 277 --ESKFIVAQEDvSKLSPL--QYDCWWEKVENLQDLLDRATNQVEKAALVLDQN-----------QDLRDKVD-----KL 336
|
330 340 350
....*....|....*....|....*....|....*..
gi 564339144 485 KLSLEEEN---------HLIQLKCENLKEKLEQMDAE 512
Cdd:PLN02939 337 EASLKEANvskfssykvELLQQKLKLLEERLQASDHE 373
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
248-525 |
4.56e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 248 RQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDWKSR---YEKIAiEKTELEVQIETMKKQISHLLEDLRKMEthgKNS 324
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERreaLQRLA-EYSWDEIDVASAEREIAELEAELERLD---ASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 325 CEeilrkLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAamvksrckn 404
Cdd:COG4913 685 DD-----LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--------- 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 405 llhenkliinkkntkLEKMRGQV---ETHLEQVEQARNSITSAEQRLQECQENLQRCKEK-CAEQALTIRELQGQVDGNY 480
Cdd:COG4913 751 ---------------LEERFAAAlgdAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLP 815
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 564339144 481 SLLTKLSLEEENHLIQLKCENLKEKLEQMDAENKELERKLADQEE 525
Cdd:COG4913 816 EYLALLDRLEEDGLPEYEERFKELLNENSIEFVADLLSKLRRAIR 860
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
88-581 |
5.77e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 88 LKKIFEQKDILSKELDTFNRVKLALEHLIKQTDYEQTGPRPPclLKDLSDSDSENRDLKKKVLEKETYIQELSCLFHNEK 167
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE--IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 168 ESALKANRFSQSVKVVHDRLQ-----------LQIQKREVEN--ERLKEHIQSLETQIAKWNLQVKMNKQEAVAVKEASR 234
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKeleekeerleeLKKKLKELEKrlEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 235 QKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSA------------SNDWKSRYEKIAIEKTELEVQIET 302
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgreltEEHRKELLEEYTAELKRIEKELKE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 303 MKKQISHLLEDLRKMETHGKNSCE-----EILRKLHSLEDENEALNIENV--------KLKSTLDALKDEVASVENELVE 369
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESEliklkELAEQLKELEEKLKKYNLEELekkaeeyeKLKEKLIKLKGEIKSLKKELEK 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 370 LQEVEKRQKALVEgyrtQVQKLEEAAAMVKSRCKNLLHENKLIINKKNTKLEKMRGQVethleqveqarNSITSAEQRLQ 449
Cdd:PRK03918 551 LEELKKKLAELEK----KLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEY-----------LELKDAEKELE 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 450 ECQENLQRCKEKcaeqaltirelqgqvdgnyslltklsleeenhliqlkcenLKEKLEQMDAENKELERKLADQEEFLK- 528
Cdd:PRK03918 616 REEKELKKLEEE----------------------------------------LDKAFEELAETEKRLEELRKELEELEKk 655
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 564339144 529 HSDLELREKAAECTALSRQLEAA------LEEGRQKVSEEVEKMSSRERALQMKISDLE 581
Cdd:PRK03918 656 YSEEEYEELREEYLELSRELAGLraeleeLEKRREEIKKTLEKLKEELEEREKAKKELE 714
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
225-580 |
7.90e-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: 39.44 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 225 EAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQI-ETM 303
Cdd:pfam12128 594 EWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKnKAL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 304 KKQISHLLEDLRKMETHGK-NSCEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQ-KALV 381
Cdd:pfam12128 674 AERKDSANERLNSLEAQLKqLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAElKALE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 382 EGYRTQVQKLEeaaamvksrcknllhenklIINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQE--CQENlQRCK 459
Cdd:pfam12128 754 TWYKRDLASLG-------------------VDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQEtwLQRR-PRLA 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564339144 460 EKCAEQALTIRELQGQvdgnyslLTKLSLEEENHLIQLKCEnlKEKLEQMDAENKELERKLADQEEFLkhSDLELREKAA 539
Cdd:pfam12128 814 TQLSNIERAISELQQQ-------LARLIADTKLRRAKLEME--RKASEKQQVRLSENLRGLRCEMSKL--ATLKEDANSE 882
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 564339144 540 ECTALSRQLEAALEEGRQKVSEEVEKMSSRERALQMKISDL 580
Cdd:pfam12128 883 QAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADH 923
|
|
| |
