|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
191-509 |
1.97e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 191 EKESALKANRFSQSVKVVHDRLQ-LQIQKREVENERLKEHIQSLETQIAKWNLQVkmnkQEAVAVKEASRQKAEALKKAS 269
Cdd:COG1196 208 QAEKAERYRELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 270 KVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAvsasndwksryekiAIEKTELEVQIETMKKQISHLLEDLRKMETHGKNS 349
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRREL--------------EERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 350 CEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKN 429
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 430 LLHENKLIINKKNTKLEKMRGQVEtHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAE---QALTIRELQGQVSHRVE 506
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAE-LEEEEEALLELLAELLEEAALLEAALAELLEELAEaaaRLLLLLEAEADYEGFLE 508
|
...
gi 1958752701 507 SWK 509
Cdd:COG1196 509 GVK 511
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
209-502 |
1.77e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 209 HDRLQLQIQKREVENERLKEHIQSLETQIAkwnlqvkmnkqeavavkeASRQKAEALKKASKVYRQRLRHFTGDIEQLTS 288
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIA------------------ELEKALAELRKELEELEEELEQLRKELEELSR 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 289 QIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQI----SHLLEDLRKMET------HGKNSCEEILRKLH 358
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLeeaeEELAEAEAEIEEleaqieQLKEELKALREALD 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 359 SLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKNLLHEnkliI 438
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE----R 882
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958752701 439 NKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVS 502
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
224-500 |
4.35e-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: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 224 ERLKEHIQSLETQIAKwnLqvkmnKQEAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSA 303
Cdd:COG1196 189 ERLEDILGELERQLEP--L-----ERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 304 SNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKME---THGKNSCEEILRKLHSLEDENEALNIENVKLKSTLDA 380
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEqdiARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 381 LKDEVASVENEL----VELQEVEKRQKALVEGYRTQVQKLEE------AAAMVKSRCKNLLHENKLIINKKNTKLEKMRG 450
Cdd:COG1196 342 LEEELEEAEEELeeaeAELAEAEEALLEAEAELAEAEEELEElaeellEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958752701 451 QVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQ 500
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
251-498 |
1.70e-07 |
|
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: 54.29 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 251 AVAVKEASRQKAEALKKASKVYRQRLrhftgdiEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKK 330
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEEL-------EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 331 QISHLLEdlrkmethgknsceeilrKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYR 410
Cdd:TIGR02168 303 QKQILRE------------------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 411 TQVQKLEEAaamvksrcknllhenkliINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQ 490
Cdd:TIGR02168 365 AELEELESR------------------LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426
|
....*...
gi 1958752701 491 ALTIRELQ 498
Cdd:TIGR02168 427 LKKLEEAE 434
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
171-499 |
1.76e-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: 53.97 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 171 KKKVLEK-ETYIQELSCLFHnEKESALKANrfSQSVKVVHDRLQLQIQK-REVENErlKEHIQSLETQIAKWNLQVKmnk 248
Cdd:pfam15921 487 KKMTLESsERTVSDLTASLQ-EKERAIEAT--NAEITKLRSRVDLKLQElQHLKNE--GDHLRNVQTECEALKLQMA--- 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 249 qEAVAVKEASRQKAE---------------------ALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEA------- 300
Cdd:pfam15921 559 -EKDKVIEILRQQIEnmtqlvgqhgrtagamqvekaQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLelekvkl 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 301 VSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVKLKSTLDA 380
Cdd:pfam15921 638 VNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS 717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 381 LKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAA-------MVKSRCKNLLHENKLIINKKNT---KLEKMRG 450
Cdd:pfam15921 718 MEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTnankekhFLKEEKNKLSQELSTVATEKNKmagELEVLRS 797
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1958752701 451 QVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCA----EQALTIRELQG 499
Cdd:pfam15921 798 QERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVrlklQHTLDVKELQG 850
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
251-475 |
2.35e-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: 52.84 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 251 AVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKK 330
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 331 QISHLLED----LRKMETHGKNSCEEILRKLHSLEDENEALNIenvkLKSTLDALKDEVASVENELVELQEVEKRQKALv 406
Cdd:COG4942 98 ELEAQKEElaelLRALYRLGRQPPLALLLSPEDFLDAVRRLQY----LKYLAPARREQAEELRADLAELAALRAELEAE- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752701 407 egyRTQVQKLEEAAAMVKSRCKNLLHENKLIINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQE 475
Cdd:COG4942 173 ---RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
111-503 |
7.98e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 111 SNLKKIFEQ-KDILSKELDTFNRVKLALEHliKQTDYEQTGPRPPCLLKDLSDSDSENRDLKKKVLEKETYIQELsclfh 189
Cdd:TIGR04523 221 SELKKQNNQlKDNIEKKQQEINEKTTEISN--TQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL----- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 190 NEKESALKANRFSQSVKVVHDRL-QLQIQKREVENE--RLKEHIQSLETQIAKWNLQVKMNKQEAVAVKEASRQKAEALK 266
Cdd:TIGR04523 294 KSEISDLNNQKEQDWNKELKSELkNQEKKLEEIQNQisQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 267 KASKVYRQRLRhftgDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHL---LEDLRKME 343
Cdd:TIGR04523 374 KLKKENQSYKQ----EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNnseIKDLTNQD 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 344 THGKNSCEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVEL----QEVEKRQKAL---VEGYRTQVQKL 416
Cdd:TIGR04523 450 SVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLneekKELEEKVKDLtkkISSLKEKIEKL 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 417 EEAAAMVKSRCKNLLHE-NKLIINKKNTKLEKMRGQVETHLEQVEQARNSITSA----EQRLQECQENLQRCKEKCAEQA 491
Cdd:TIGR04523 530 ESEKKEKESKISDLEDElNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKqeekQELIDQKEKEKKDLIKEIEEKE 609
|
410
....*....|..
gi 1958752701 492 LTIRELQGQVSH 503
Cdd:TIGR04523 610 KKISSLEKELEK 621
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
272-501 |
1.13e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 272 YRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAiektELEVQIETMKKQIShllEDLRKMETHgKNSCE 351
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE----TLEAEIEDLRETIA---ETEREREEL-AEEVR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 352 EILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQE--VEKRQKAL-----VEGYRTQVQKLEEAAAMVK 424
Cdd:PRK02224 283 DLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDrlEECRVAAQahneeAESLREDADDLEERAEELR 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 425 SRCKNL---LHENKLIINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQV 501
Cdd:PRK02224 363 EEAAELeseLEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV 442
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
205-502 |
1.81e-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: 50.84 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 205 VKVVHDRLQLQIQKREVENERL-KEHIQSLETQIAKwnlqvkmNKQEAVAVKEASRQKAEALKKASKVYRQrLRHFTGDI 283
Cdd:TIGR02169 182 VEENIERLDLIIDEKRQQLERLrREREKAERYQALL-------KEKREYEGYELLKEKEALERQKEAIERQ-LASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 284 EQLTSQIRDQEAKLSEA------VSASNDWKSRYEKIAIEKT--ELEVQIETMKKQISHLLEDLRKMETHGKNSCEEI-- 353
Cdd:TIGR02169 254 EKLTEEISELEKRLEEIeqlleeLNKKIKDLGEEEQLRVKEKigELEAEIASLERSIAEKERELEDAEERLAKLEAEIdk 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 354 -LRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELvelQEVEKRQKALVEGYRTQVQKLEEAaamvksrcKNLLH 432
Cdd:TIGR02169 334 lLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL---EEVDKEFAETRDELKDYREKLEKL--------KREIN 402
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 433 ENKLIINKKNTKLEKMRgqvethlEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVS 502
Cdd:TIGR02169 403 ELKRELDRLQEELQRLS-------EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
320-501 |
2.55e-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: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 320 ELEVQIETMKKQISHLLEDLRKMETH---GKNSCEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQ 396
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRldeLSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 397 EVEKRQKALVEGYRTQVQKLEEAAAMVKSRcknLLHENKLIINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQEC 476
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNDLEAR---LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180
....*....|....*....|....*....
gi 1958752701 477 QENLQR----CKEKCAEQALTIRELQGQV 501
Cdd:TIGR02169 835 IQELQEqridLKEQIKSIEKEIENLNGKK 863
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
113-502 |
5.34e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 113 LKKIFEQKDILSKELDTFNRVKLALEHLIKQTDYEQTGPRPPclLKDLSDSDSENRDLKKKVLEKETYIQELSCLFHNEK 192
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE--IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 193 ESALKANRFSQSVKVVHDRLQ-----------LQIQKREVEN--ERLKEHIQSLETQIAKWNLQVKMNKQEAVAVKEASR 259
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKeleekeerleeLKKKLKELEKrlEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 260 QKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSA------------SNDWKSRYEKIAIEKTELEVQIET 327
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgreltEEHRKELLEEYTAELKRIEKELKE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 328 MKKQISHLLEDLRKMETHGKNSCE-----EILRKLHSLEDENEALNIENV--------KLKSTLDALKDEVASVENELVE 394
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESEliklkELAEQLKELEEKLKKYNLEELekkaeeyeKLKEKLIKLKGEIKSLKKELEK 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 395 LQEVEKRQKALVEgyrtQVQKLEEAAAMVKSRCKNLLHENKLIINKKNTKLEKMrgqvetHLEQVE--QARNSITSAEQR 472
Cdd:PRK03918 551 LEELKKKLAELEK----KLDELEEELAELLKELEELGFESVEELEERLKELEPF------YNEYLElkDAEKELEREEKE 620
|
410 420 430
....*....|....*....|....*....|
gi 1958752701 473 LQECQENLQRCKEKCAEQALTIRELQGQVS 502
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKELE 650
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
176-419 |
1.45e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 176 EKETYIQELSCLFHNEKESALKANRFSQsvkvvhdrlQLQIQKREVENERLKEHIQSLETQIAKwnLQVKMNKQEAVAVK 255
Cdd:COG3206 132 VKGSNVIEISYTSPDPELAAAVANALAE---------AYLEQNLELRREEARKALEFLEEQLPE--LRKELEEAEAALEE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 256 EASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDW----------------KSRYEKIAIEKT 319
Cdd:COG3206 201 FRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGpdalpellqspviqqlRAQLAELEAELA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 320 ELEV-------QIETMKKQISHLLEDLRkmethgknscEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENEL 392
Cdd:COG3206 281 ELSArytpnhpDVIALRAQIAALRAQLQ----------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELE 350
|
250 260
....*....|....*....|....*..
gi 1958752701 393 VELQEVEKRQKALVEGYRTQVQKLEEA 419
Cdd:COG3206 351 AELRRLEREVEVARELYESLLQRLEEA 377
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
111-475 |
2.61e-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: 46.94 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 111 SNLKKIFEQKDILSKELDTFNRVKLALEHLIKQtdyeqtgprppcLLKDLSDSDSENRDLKKKVLEKETYIQELSclfhN 190
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQ------------LKKELTNSESENSEKQRELEEKQNEIEKLK----K 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 191 EKESALKANrfsQSVKVVHDRLQLQIQKREVENERLKEHIQSLETQIAKWNLQVKMNKQEAVAVKEASR---QKAEALKK 267
Cdd:TIGR04523 378 ENQSYKQEI---KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKdltNQDSVKEL 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 268 ASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMETHGK 347
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 348 nsceEILRKLHSLEDENEALNIEN----------------VKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRT 411
Cdd:TIGR04523 535 ----EKESKISDLEDELNKDDFELkkenlekeideknkeiEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEK 610
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958752701 412 QVQKLEEAAAMVKSRCKNLLhenkLIINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQE 475
Cdd:TIGR04523 611 KISSLEKELEKAKKENEKLS----SIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKE 670
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
29-505 |
2.84e-05 |
|
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: 46.96 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 29 APEKHRSRASQAAQAVPRLSGYLPQPSVLRDYRFKGDVSSTKTELEAALREAELASCSV-------------ELLLPLLK 95
Cdd:TIGR00606 547 KDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQnknhinneleskeEQLSSYED 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 96 NTVEGIGLEHANLSASNLKKIFEQKdilSKELDTFNRVKLALEHLIKQTDYEQTGPRPPC--LLKDLSDSDSENRDLKKK 173
Cdd:TIGR00606 627 KLFDVCGSQDEESDLERLKEEIEKS---SKQRAMLAGATAVYSQFITQLTDENQSCCPVCqrVFQTEAELQEFISDLQSK 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 174 VLEKETYIQELsclfhnEKESALKANRFSQSVKVVHDRlQLQIQKREVENERLKEHIQSLETQIA--KWNLQVKMNKQEA 251
Cdd:TIGR00606 704 LRLAPDKLKST------ESELKKKEKRRDEMLGLAPGR-QSIIDLKEKEIPELRNKLQKVNRDIQrlKNDIEEQETLLGT 776
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 252 VAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLS--EAVSASNDWKSRYEKIAIEKTELEVQIETMK 329
Cdd:TIGR00606 777 IMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTvqQVNQEKQEKQHELDTVVSKIELNRKLIQDQQ 856
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 330 KQISHLLEDLRKMETHgKNSCEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEvekRQKALVEGY 409
Cdd:TIGR00606 857 EQIQHLKSKTNELKSE-KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQ---EKEELISSK 932
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 410 RTQVQKLEEAAAMVKSRCKNLLHENKLIINKKNTKLEKMRGQVETHLEQVEQarnSITSAEQRLQECQENLQRCKEKCAE 489
Cdd:TIGR00606 933 ETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNA---QLEECEKHQEKINEDMRLMRQDIDT 1009
|
490
....*....|....*.
gi 1958752701 490 QALTIRELQGQVSHRV 505
Cdd:TIGR00606 1010 QKIQERWLQDNLTLRK 1025
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
208-502 |
2.97e-05 |
|
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: 46.76 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 208 VHDRLQLQ-IQKREVENERLKEHIQSLETQIAKwnLQVKMNKQEAVAVKEASRQkaEALKKASKVYRQRLRHFTGDIEQ- 285
Cdd:pfam12128 227 IRDIQAIAgIMKIRPEFTKLQQEFNTLESAELR--LSHLHFGYKSDETLIASRQ--EERQETSAELNQLLRTLDDQWKEk 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 286 ---LTSQIRDQEAKLSEA---VSASNDWKSRYEKIAIEKTELEV--------QIETMKKQISHLLEDLRKME----THGK 347
Cdd:pfam12128 303 rdeLNGELSAADAAVAKDrseLEALEDQHGAFLDADIETAAADQeqlpswqsELENLEERLKALTGKHQDVTakynRRRS 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 348 NSCEEILRKLHSLEDENEALNIENVKLKStldALKDEVASVENELVELQEVEKRQkalvegYRTQVQKLEEAAAMVKSRC 427
Cdd:pfam12128 383 KIKEQNNRDIAGIKDKLAKIREARDRQLA---VAEDDLQALESELREQLEAGKLE------FNEEEYRLKSRLGELKLRL 453
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958752701 428 KNLLHENKLIINKKN--TKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVS 502
Cdd:pfam12128 454 NQATATPELLLQLENfdERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLF 530
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
110-405 |
5.37e-05 |
|
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: 46.21 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 110 ASNLKKIFEQKDILSKELDTFNRVKLALEHLIkqtdyEQTGPRPPCLLKDLSDsdsENRDLKKKVLEKETYIQELSCLFH 189
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEI-----SELEKRLEEIEQLLEE---LNKKIKDLGEEEQLRVKEKIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 190 NEKESALKANRFSQSVKvvhDRLQLQIQKREVENERLKEHIQSLETQIAKWNL---QVKMNKQEAVAVKEASRQKAEALK 266
Cdd:TIGR02169 301 AEIASLERSIAEKEREL---EDAEERLAKLEAEIDKLLAEIEELEREIEEERKrrdKLTEEYAELKEELEDLRAELEEVD 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 267 KASKVYRQRLRHFTGDIEQLTSQIrdqeaklseavsasNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMEThg 346
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREI--------------NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE-- 441
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752701 347 knsceeilrklhSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKAL 405
Cdd:TIGR02169 442 ------------EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
211-390 |
8.90e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 211 RLQLQIQKREVENERLKEHIQSLETQIAkwnlqvkmnkQEAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQI 290
Cdd:COG4913 278 RAALRLWFAQRRLELLEAELEELRAELA----------RLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 291 RDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLrkmethgknscEEILRKLHSLEDENEAlniE 370
Cdd:COG4913 348 ERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL-----------EEELEALEEALAEAEA---A 413
|
170 180
....*....|....*....|
gi 1958752701 371 NVKLKSTLDALKDEVASVEN 390
Cdd:COG4913 414 LRDLRRELRELEAEIASLER 433
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
155-502 |
9.78e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.11 E-value: 9.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 155 CLLKD-LSDSDSENRDLKKKVLEKETYIQELSCLFHNEKESALKANRFSQSVKVVHDR-LQLQIQK--REVENE--RLKE 228
Cdd:pfam15921 159 CLKEDmLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRsLGSAISKilRELDTEisYLKG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 229 HIQSLETQIAkwnlqvkmnkqeavAVKEASRQKAEALkkaskvyrqrLRHFTGDIEQLTSQ----IRDQEAKLSEAVSAS 304
Cdd:pfam15921 239 RIFPVEDQLE--------------ALKSESQNKIELL----------LQQHQDRIEQLISEheveITGLTEKASSARSQA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 305 NDWKSRYEKIAIEKTELEV----QIETMKKQISHLLEDLRKMETHGKNSCEEILRKL-------HSLEDENEALNIENVK 373
Cdd:pfam15921 295 NSIQSQLEIIQEQARNQNSmymrQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLvlanselTEARTERDQFSQESGN 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 374 LKSTLDALKDEVASVENELVELQEVEKRQ--------------KALVEGYRTQVQKLEEAAAMVKSRCKNLLHENKLIIN 439
Cdd:pfam15921 375 LDDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnsitidhlRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQ 454
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958752701 440 KKNTKLEK---MRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVS 502
Cdd:pfam15921 455 GKNESLEKvssLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEIT 520
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
189-367 |
4.55e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 189 HNEKESALKA-NRFSQSVKVVHDRLQLQIQKREVENERLKEHIQSLETQIAKWNLQVKmNKQEAVAVKEASRQKAEALKK 267
Cdd:TIGR02168 805 LDELRAELTLlNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE-ELEELIEELESELEALLNERA 883
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 268 ASKVYRQRLRHftgDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHL----LEDLRKME 343
Cdd:TIGR02168 884 SLEEALALLRS---ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEysltLEEAEALE 960
|
170 180
....*....|....*....|....
gi 1958752701 344 THGKNSCEEILRKLHSLEDENEAL 367
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKEL 984
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
210-421 |
6.90e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 210 DRLQLQIQKREVENERLKEHIQSLETQIAKWNLQVKmnkqeavavkeASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQ 289
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIA-----------ALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 290 IRDQEAKLSEAVSASndwksrYEKIAIEKTELEVQIETMkKQISHLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNI 369
Cdd:COG4942 99 LEAQKEELAELLRAL------YRLGRQPPLALLLSPEDF-LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958752701 370 ENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAA 421
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
281-487 |
1.23e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 281 GDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMETHGKNSCEEI------- 353
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIeeleekv 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 354 --LRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQ--------------EVEKRQKAL---VEGYRTQVQ 414
Cdd:PRK03918 283 keLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEerikeleekeerleELKKKLKELekrLEELEERHE 362
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958752701 415 KLEEAAAMVK---SRCKNLLHENKLIINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKC 487
Cdd:PRK03918 363 LYEEAKAKKEeleRLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC 438
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
266-486 |
1.24e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 266 KKASKVYRQRLRHFTGDIEQLtsqirdqeAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMEth 345
Cdd:COG4717 53 KEADELFKPQGRKPELNLKEL--------KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 346 gknsceeILRKLHSLEDENEALNIEnvklkstLDALKDEVASVENELVELQEVEKRQKALvegyRTQVQKLEEAAAMVKS 425
Cdd:COG4717 123 -------KLLQLLPLYQELEALEAE-------LAELPERLEELEERLEELRELEEELEEL----EAELAELQEELEELLE 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752701 426 RCKNLLHENkliINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEK 486
Cdd:COG4717 185 QLSLATEEE---LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
351-418 |
1.36e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 1.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752701 351 EEILRKLHSLEDENEALNIE-NVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEE 418
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEqDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQ 482
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
250-509 |
2.17e-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: 40.98 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 250 EAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQI-ETM 328
Cdd:pfam12128 594 EWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKnKAL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 329 KKQISHLLEDLRKMETHGK-NSCEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQ-KALV 406
Cdd:pfam12128 674 AERKDSANERLNSLEAQLKqLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAElKALE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 407 EGYRTQVQKLEeaaamvksrcknllhenklIINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQE--CQENlQRCK 484
Cdd:pfam12128 754 TWYKRDLASLG-------------------VDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQEtwLQRR-PRLA 813
|
250 260
....*....|....*....|....*
gi 1958752701 485 EKCAEQALTIRELQGQVSHRVESWK 509
Cdd:pfam12128 814 TQLSNIERAISELQQQLARLIADTK 838
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
216-430 |
2.21e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 216 IQKREVENERLKEHIQSLETQIAKWNLQVKMNKQEAvavkEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEA 295
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI----ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 296 KLSEAvsasndwKSRYEkiaiektELEVQIETMKKQISHLLEDLRKMETHGKnsceEILRKLHSLEDENEALNIENvKLK 375
Cdd:TIGR02169 897 QLREL-------ERKIE-------ELEAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGEDEEIPEEELSLE-DVQ 957
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752701 376 STLDALKDEVASVE--NELV--ELQEVEKRQKALVEgyrtQVQKLEEAAAMVKSRCKNL 430
Cdd:TIGR02169 958 AELQRVEEEIRALEpvNMLAiqEYEEVLKRLDELKE----KRAKLEEERKAILERIEEY 1012
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
212-498 |
2.60e-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: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 212 LQLQIQKREVENERLKEHIQSLETQIAkwNLQVKMNKQEAVAVkeASRQKAEALKKASKVYR----------QRLRHFTG 281
Cdd:COG3096 373 AAEQLAEAEARLEAAEEEVDSLKSQLA--DYQQALDVQQTRAI--QYQQAVQALEKARALCGlpdltpenaeDYLAAFRA 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 282 DIEQLTSQIRDQEAKLSEAVSASNDWKSRYEkiAIEKTELEVQIETMKKQISHLLEDLRKMETHGKN------SCEEILR 355
Cdd:COG3096 449 KEQQATEEVLELEQKLSVADAARRQFEKAYE--LVCKIAGEVERSQAWQTARELLRRYRSQQALAQRlqqlraQLAELEQ 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 356 KLHSLEDENEALNIENVKLKSTLDAlKDEVASVENEL-VELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSrcknlLHEN 434
Cdd:COG3096 527 RLRQQQNAERLLEEFCQRIGQQLDA-AEELEELLAELeAQLEELEEQAAEAVEQRSELRQQLEQLRARIKE-----LAAR 600
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958752701 435 KLIINKKNTKLEKMRGQVETHLEQveqaRNSITSAEQRLQECQENLQRCKEKCAEQ----ALTIRELQ 498
Cdd:COG3096 601 APAWLAAQDALERLREQSGEALAD----SQEVTAAMQQLLEREREATVERDELAARkqalESQIERLS 664
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
215-478 |
3.49e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 215 QIQKREVENERLKEHIQSLETQIAKWNLQVKmNKQEAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQE 294
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIK-KKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 295 AKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMETHGKNSCEEIL-------------------- 354
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNqlkdeqnkikkqlsekqkel 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 355 ----RKLHSLED-----ENEALNIENVKLKSTLDALKDEVASVENELVELQ-EVEKRQKalvegyrtQVQKLEEAAAMVK 424
Cdd:TIGR04523 277 eqnnKKIKELEKqlnqlKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQnQISQNNK--------IISQLNEQISQLK 348
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958752701 425 SRCKNLLHENKLI---INKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQE 478
Cdd:TIGR04523 349 KELTNSESENSEKqreLEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK 405
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
71-299 |
4.22e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 71 TELEAALREAELASCSVELLLPLlkntvegiglehanlsasnlKKIFEQKDILSKELDTFNRVKLALEHLIKQTDYEQtg 150
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPI--------------------RELAERYAAARERLAELEYLRAALRLWFAQRRLEL-- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 151 prppcLLKDLSDSDSENRDLKKKVLEKETYIQELsclfhNEKESALKANRFSQSVKVVhDRLQLQIQKREVENERLKEHI 230
Cdd:COG4913 293 -----LEAELEELRAELARLEAELERLEARLDAL-----REELDELEAQIRGNGGDRL-EQLEREIERLERELEERERRR 361
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752701 231 QSLETQIAKWNLQVKMNKQEAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSE 299
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
210-501 |
4.91e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 210 DRLQLQIQKREVENERLKEHIQSLETQIAKWNLQVKMNKQEAVAVKEAS---RQKAEALKKASKVYRQRLRHFTGDIEQL 286
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAeelREEAAELESELEEAREAVEDRREEIEEL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 287 TSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMET---HGK--------------NS 349
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleAGKcpecgqpvegsphvET 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 350 CEEILRKLHSLEDENEALNIENVKLKSTLDALKD------------EVASVENELVELQEV---EKRQKAlvEGYRTQVQ 414
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDlveaedrierleERREDLEELIAERREtieEKRERA--EELRERAA 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 415 KLE-------EAAAMVKSRCKNLLHENKlIINKKNTKLEKMR---GQVETHLEQVEQARNSITSAEQRLQECQE-NLQRc 483
Cdd:PRK02224 548 ELEaeaeekrEAAAEAEEEAEEAREEVA-ELNSKLAELKERIeslERIRTLLAAIADAEDEIERLREKREALAElNDER- 625
|
330
....*....|....*...
gi 1958752701 484 KEKCAEQALTIRELQGQV 501
Cdd:PRK02224 626 RERLAEKRERKRELEAEF 643
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
222-492 |
5.27e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.50 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 222 ENERLKEHIQSLETQIAKWNLQVKMNKQEAVAVKEASRQkaeaLKKASKVYRQRLRHFTGDIEQLTSQIRDQEaklSEAV 301
Cdd:PLN02939 164 EKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQ----LEKLRNELLIRGATEGLCVHSLSKELDVLK---EENM 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 302 SASNDWKSRYEKIaIEKTELEVQIETMKKQISHLLEDLRKMETHGKNSCEEILrKLHSLEDENEALNIENvkLKSTLDAL 381
Cdd:PLN02939 237 LLKDDIQFLKAEL-IEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVS-KLSPLQYDCWWEKVEN--LQDLLDRA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 382 KDEVasvENELVELQEVEKrqkalvegYRTQVQKLEEAAAMVKSrcknllheNKLIINKKNTKLEKMRgQVETHLEQVEQ 461
Cdd:PLN02939 313 TNQV---EKAALVLDQNQD--------LRDKVDKLEASLKEANV--------SKFSSYKVELLQQKLK-LLEERLQASDH 372
|
250 260 270
....*....|....*....|....*....|..
gi 1958752701 462 ARNS-ITSAEQRLQECQENLQRCKEKCAEQAL 492
Cdd:PLN02939 373 EIHSyIQLYQESIKEFQDTLSKLKEESKKRSL 404
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
317-472 |
5.42e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 317 EKTELEVQIEtMKKQISHLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNienvKLKSTLDALKDEVASvenelvELQ 396
Cdd:PRK12704 56 KEALLEAKEE-IHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLE----KREEELEKKEKELEQ------KQQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 397 EVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKNLLHENKliinKKNTKLEKMRGQVETHLEQVEQ----ARNSITSAEQR 472
Cdd:PRK12704 125 ELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEKV----EEEARHEAAVLIKEIEEEAKEEadkkAKEILAQAIQR 200
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
273-491 |
5.75e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 273 RQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMethgknscee 352
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 353 ilrkLHSLEDENEALNIENVKLKSTldalkdEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKsrcknllh 432
Cdd:COG3883 92 ----ARALYRSGGSVSYLDVLLGSE------SFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELE-------- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752701 433 ENKLIINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQA 491
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
104-506 |
5.92e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 39.32 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 104 EHANLSASNLKKIFEQKDILSKELDTFnRVKLALEHLIKQTDYE--QTGPRPPCLLKDLSDSDSENRDLKKK-----VLE 176
Cdd:pfam05483 275 EKTKLQDENLKELIEKKDHLTKELEDI-KMSLQRSMSTQKALEEdlQIATKTICQLTEEKEAQMEELNKAKAahsfvVTE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 177 KETYIQELSCLFHNEKEsalKANRFSQSVKVVHDRLQLQIQK----------REVENERLKEHIQSLET------QIAKW 240
Cdd:pfam05483 354 FEATTCSLEELLRTEQQ---RLEKNEDQLKIITMELQKKSSEleemtkfknnKEVELEELKKILAEDEKlldekkQFEKI 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 241 NLQVKMNKQEAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTE 320
Cdd:pfam05483 431 AEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASD 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 321 LEV---------------------QIETMKKQISHLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVKLKSTLD 379
Cdd:pfam05483 511 MTLelkkhqediinckkqeermlkQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMK 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 380 ALKDEV----ASVENELVELQEVEKRQKAL----------VEGYRTQVQKLEEAAAMVKSRCKNllhenklIINKKNTKL 445
Cdd:pfam05483 591 ILENKCnnlkKQIENKNKNIEELHQENKALkkkgsaenkqLNAYEIKVNKLELELASAKQKFEE-------IIDNYQKEI 663
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752701 446 EKMRGQVETHLEQVEQARNSITSAEQRLQECQenlQRCKEKCAEQALTIRELQGQVSHRVE 506
Cdd:pfam05483 664 EDKKISEEKLLEEVEKAKAIADEAVKLQKEID---KRCQHKIAEMVALMEKHKHQYDKIIE 721
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
317-509 |
6.36e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 317 EKTELEVQIETMKKQISHLLEDLRKMEThgknsceeILRKLHSLEDENEALN--IENVKLKSTLDALKDEVASVENELvE 394
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALED--------AREQIELLEPIRELAEryAAARERLAELEYLRAALRLWFAQR-R 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 395 LQEVEKRQKALvegyRTQVQKLEEAAAMVKSRCKNLlhenkliinkkNTKLEKMRGQVETH-LEQVEQARNSITSAEQRL 473
Cdd:COG4913 290 LELLEAELEEL----RAELARLEAELERLEARLDAL-----------REELDELEAQIRGNgGDRLEQLEREIERLEREL 354
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958752701 474 QECQENLQRCKEKCAEQALTI-------RELQGQVSHRVESWK 509
Cdd:COG4913 355 EERERRRARLEALLAALGLPLpasaeefAALRAEAAALLEALE 397
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
305-507 |
6.51e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 38.75 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 305 NDWKSRYEKIAIEKTELEVQIETMKKqishLLEDLRK---METHGKNSCEEilrKLHSLEDENEALNIENVKLKSTLDAL 381
Cdd:pfam00038 57 EDLRRQLDTLTVERARLQLELDNLRL----AAEDFRQkyeDELNLRTSAEN---DLVGLRKDLDEATLARVDLEAKIESL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 382 KDEVASV----ENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKNLLHENKLIINKK-NTKLEKMRGQVETHL 456
Cdd:pfam00038 130 KEELAFLkknhEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWyQSKLEELQQAAARNG 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958752701 457 EQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVSHRVES 507
Cdd:pfam00038 210 DALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLAD 260
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
315-504 |
7.05e-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: 38.59 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 315 AIEKTELEVQIETMKKQISHLLEDLRKMethgKNSCEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVE 394
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 395 LQEVEKRQKALVEGYRTQVQKLEEAAAMvksrcKNLLHENKliINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQ 474
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPL-----ALLLSPED--FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190
....*....|....*....|....*....|
gi 1958752701 475 ECQENLQRCKEKCAEQALTIRELQGQVSHR 504
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAER 197
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
113-304 |
7.63e-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: 38.59 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 113 LKKIFEQKDILSKELDTFNRVKLALEHLIKQTDYEQTGprppcLLKDLSDSDSENRDLKKKVLEKETYIQE--------- 183
Cdd:COG4942 43 LAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-----LEAELAELEKEIAELRAELEAQKEELAEllralyrlg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 184 ----LSCLFHNEkeSALKANRFSQSVKVVHDRLQLQIQKREVENERLKEHIQSLETQIAKWNLQVKMNKQEAVAVKEASR 259
Cdd:COG4942 118 rqppLALLLSPE--DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958752701 260 QKAEALKKASK---VYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSAS 304
Cdd:COG4942 196 ERQKLLARLEKelaELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
351-452 |
9.21e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 36.91 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752701 351 EEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCknl 430
Cdd:pfam11559 55 ESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQIKTQF--- 131
|
90 100
....*....|....*....|..
gi 1958752701 431 LHENKliinKKNTKLEKMRGQV 452
Cdd:pfam11559 132 AHEVK----KRDREIEKLKERL 149
|
|
| |
