|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
86-399 |
7.48e-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: 61.61 E-value: 7.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 86 LETQIAKWNLQVKMNKQEAVAvkEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDWKSRYE 165
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKI--AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 166 KIAIEKTELEVQIETMKKQI----SHLLEDLRKMET------HGKNSCEEILRKLHSLEDENEALNIENVKLKSTLDALK 235
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLeeaeEELAEAEAEIEEleaqieQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 236 DEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKNLLHEnkliINKKNTKLEKMRGQVETHLEQVEQA 315
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE----RASLEEALALLRSELEELSEELREL 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 316 RNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVDGNYSLLTKLSLEEENhliqlkceNLKEKLEQMDAENKELE 395
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEN--------KIEDDEEEARRRLKRLE 978
|
....
gi 1958752699 396 RKLA 399
Cdd:TIGR02168 979 NKIK 982
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
44-361 |
1.61e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 44 EKESALKANRFSQSVKVVHDRLQ-LQIQKREVENERLKEHIQSLETQIAKWNLQVkmnkQEAVAVKEASRQKAEALKKAS 122
Cdd:COG1196 208 QAEKAERYRELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 123 KVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAvsasndwksryekiAIEKTELEVQIETMKKQISHLLEDLRKMETHGKNS 202
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRREL--------------EERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 203 CEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKN 282
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752699 283 LLHENKLIINKKNTKLEKMRGQVEtHLEQVEQARNSITSAEQRLQECQENLQRCKEKcAEQALTIRELQGQVDGNYSLL 361
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAE-LEEEEEALLELLAELLEEAALLEAALAELLEE-LAEAAARLLLLLEAEADYEGF 506
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
125-507 |
2.09e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 125 YRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAiektELEVQIETMKKQIShllEDLRKMETHgKNSCE 204
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE----TLEAEIEDLRETIA---ETEREREEL-AEEVR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 205 EILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQE--VEKRQKAL-----VEGYRTQVQKLEEAAAMVK 277
Cdd:PRK02224 283 DLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDrlEECRVAAQahneeAESLREDADDLEERAEELR 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 278 SRCKNL---LHENKLIINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQV 354
Cdd:PRK02224 363 EEAAELeseLEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 355 DGNYSLLTK-------LSLEEENHLIQLkcENLKEKLEQMDAENKELERKLADQEEFLKHSDlELREKAAECTALSRQLE 427
Cdd:PRK02224 443 EEAEALLEAgkcpecgQPVEGSPHVETI--EEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERRE 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 428 AA---LEEGRQKVSEEVEKMSS-RERAlqmkiSDLETELRKKNEEQNQLVGNMSTKAQHQDIC------LKEIQHSLEKS 497
Cdd:PRK02224 520 DLeelIAERRETIEEKRERAEElRERA-----AELEAEAEEKREAAAEAEEEAEEAREEVAELnsklaeLKERIESLERI 594
|
410
....*....|
gi 1958752699 498 ETQNESIKNY 507
Cdd:PRK02224 595 RTLLAAIADA 604
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
77-434 |
2.87e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 77 ERLKEHIQSLETQIAKwnLqvkmnKQEAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSA 156
Cdd:COG1196 189 ERLEDILGELERQLEP--L-----ERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 157 SNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMEthgkNSCEEILRKLHSLEDENEALNIENVKLKSTLDALKD 236
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLE----QDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 237 EVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAmvksrcknllhenkliinKKNTKLEKMRGQVETHLEQVEQAR 316
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA------------------EAEEELEELAEELLEALRAAAELA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 317 NSITSAEQRLQECQENLQRCKEKCAEQALTIRELqgqvdgnysLLTKLSLEEENHLIQLKCENLKEKLEQMDAENKELER 396
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAEL---------EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958752699 397 KLADQEEFLKHSDLELREKAAEctALSRQLEAALEEGR 434
Cdd:COG1196 471 EAALLEAALAELLEELAEAAAR--LLLLLEAEADYEGF 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-434 |
4.57e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 104 AVAVKEASRQKAEALKKASKVYRQRLrhftgdiEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKK 183
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEEL-------EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 184 QISHLLEdlrkmethgknsceeilrKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYR 263
Cdd:TIGR02168 303 QKQILRE------------------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 264 TQVQKLEEAaamvksrcknllhenkliINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEkcaeq 343
Cdd:TIGR02168 365 AELEELESR------------------LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ----- 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 344 alTIRELQGQVDGNYSLLTKLSLEEENHLIqlkcENLKEKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTALS 423
Cdd:TIGR02168 422 --EIEELLKKLEEAELKELQAELEELEEEL----EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
330
....*....|.
gi 1958752699 424 RQLEAALEEGR 434
Cdd:TIGR02168 496 RLQENLEGFSE 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
70-484 |
8.87e-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: 58.14 E-value: 8.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 70 QKREVEN--ERLKEHIQSLETQIAKWNLQVKMNKQEAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQE 147
Cdd:TIGR02168 173 RRKETERklERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 148 AKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMETHgknsCEEILRKLHSLEDENEALNIENVKL 227
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ----KQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 228 KSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAaamvksrcknllhenkliINKKNTKLEKMRGQVET 307
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR------------------LEELEEQLETLRSKVAQ 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 308 HLEQVEQARNSITSAEQRLQECQENLQRCKEkcaEQALTIRELQgqvdgnyslltklslEEENHLIQLKCENLKEKLEQM 387
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQ---EIEELLKKLE---------------EAELKELQAELEELEEELEEL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 388 DAENKELERKLADQeeflkhsdlelrekaaectalsRQLEAALEEGRQKVSEEVEKMSSRERALQmkisDLETELRKKNE 467
Cdd:TIGR02168 453 QEELERLEEALEEL----------------------REELEEAEQALDAAERELAQLQARLDSLE----RLQENLEGFSE 506
|
410
....*....|....*..
gi 1958752699 468 EQNQLVGNMSTKAQHQD 484
Cdd:TIGR02168 507 GVKALLKNQSGLSGILG 523
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
297-472 |
1.30e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 297 KLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVdgnYSLLTKLS-LEEENHLIQL 375
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE---YELLAELArLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 376 KCENLKEKLEQMDAENKELERKLADQEEflkhSDLELREKAAECTALSRQLEAALEEGRQKVSEEVEKMSSRERALQMKI 455
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEE----ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170
....*....|....*..
gi 1958752699 456 SDLETELRKKNEEQNQL 472
Cdd:COG1196 386 EELLEALRAAAELAAQL 402
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
173-464 |
1.35e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 173 ELEVQIETMKKQISHLLEDLRKMETH---GKNSCEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQ 249
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRldeLSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 250 EVEKRQKALVEGYRTQVQKLEEAAAMVKSRcknLLHENKLIINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQEC 329
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNDLEAR---LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 330 QENLQR----CKEKCAEQALTIRELQGQVDGNYSLLTKL-----SLEEENHLIQLKCENLKEKLEQMdaenKELERKLAD 400
Cdd:TIGR02169 835 IQELQEqridLKEQIKSIEKEIENLNGKKEELEEELEELeaalrDLESRLGDLKKERDELEAQLREL----ERKIEELEA 910
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958752699 401 QEEFLKHSDLELREKAAectALSRQLEAALEEGRQKVSEEVEKMSsrERALQMKISDLETELRK 464
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLE---ALEEELSEIEDPKGEDEEIPEEELS--LEDVQAELQRVEEEIRA 969
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
311-499 |
5.06e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 311 QVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVDGNYSLLTKLSLEEEnhliqlkcENLKEKLEQMDAE 390
Cdd:COG4913 282 RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRL--------EQLEREIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 391 NKELERKLADQEEFLKHSDLELREKAAECTALSRQLEAALEEgrqkVSEEVEKMSSRERALQMKISDLETELRKKNEEQN 470
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA----LEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
170 180
....*....|....*....|....*....
gi 1958752699 471 QLVGNMSTKAQHQDICLKEIQHSLEKSET 499
Cdd:COG4913 430 SLERRKSNIPARLLALRDALAEALGLDEA 458
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
8-493 |
2.02e-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: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 8 CLLKD-LSDSDSENRDLKKKVLEKETYIQELSCLFHNEKESALKANRFSQSVKVVHDRLQlqiqkreveNERLKEHIQSL 86
Cdd:pfam15921 159 CLKEDmLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSL---------GSAISKILREL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 87 ETQIAKWNLQVKMNKQEAVAVKEASRQKAEALkkaskvyrqrLRHFTGDIEQLTSQ----IRDQEAKLSEAVSASNDWKS 162
Cdd:pfam15921 230 DTEISYLKGRIFPVEDQLEALKSESQNKIELL----------LQQHQDRIEQLISEheveITGLTEKASSARSQANSIQS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 163 RYEKIAIEKTELEV----QIETMKKQISHLLEDLRKMETHGKNSCEEILRKL-------HSLEDENEALNIENVKLKSTL 231
Cdd:pfam15921 300 QLEIIQEQARNQNSmymrQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLvlanselTEARTERDQFSQESGNLDDQL 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 232 DALKDEVASVENELVELQEVEKRQ--------------KALVEGYRTQVQKLEEAAAMVKSRCKNLLHENKLIINKKNTK 297
Cdd:pfam15921 380 QKLLADLHKREKELSLEKEQNKRLwdrdtgnsitidhlRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNES 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 298 LEK---MRGQVETH-------LEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVDGNYSLLTKLSLE 367
Cdd:pfam15921 460 LEKvssLTAQLESTkemlrkvVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 368 EEnHL--IQLKCENLKEKLEQMDAENKELERKLADQEEFLKHSDlelrEKAAECTALSRQLEAALEEGRQKVSE---EVE 442
Cdd:pfam15921 540 GD-HLrnVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHG----RTAGAMQVEKAQLEKEINDRRLELQEfkiLKD 614
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1958752699 443 KMSSRERALQMKISDLETELRKKNEEQNQLVGNMSTKAQHQDICLKEIQHS 493
Cdd:pfam15921 615 KKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTS 665
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
134-472 |
2.31e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 134 GDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMETHGKNSCEEI------- 206
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIeeleekv 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 207 --LRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQ--------------EVEKRQKAL---VEGYRTQVQ 267
Cdd:PRK03918 283 keLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEerikeleekeerleELKKKLKELekrLEELEERHE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 268 KLEEAAAMVK---SRCKNLLHENKLIINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCaeqA 344
Cdd:PRK03918 363 LYEEAKAKKEeleRLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC---P 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 345 LTIRELQGQVDGNysLLTKLSLEEENhlIQLKCENLKEKLEQMDAENKELERKLADQEEFLKhsdleLREKAAECTALSR 424
Cdd:PRK03918 440 VCGRELTEEHRKE--LLEEYTAELKR--IEKELKEIEEKERKLRKELRELEKVLKKESELIK-----LKELAEQLKELEE 510
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958752699 425 QLEAALEEGRQKVSEEVEKMSSRERALQMKISDLETELRKKNEEQNQL 472
Cdd:PRK03918 511 KLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
226-502 |
4.00e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 226 KLKSTLDALKDEVAsveneLVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRcKNLLHENKLIINKKNTKLEKMRGQV 305
Cdd:COG1196 217 ELKEELKELEAELL-----LLKLRELEAELEELEAELEELEAELEELEAELAEL-EAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 306 ETHLEQVEQARNSITSAEQRLQECQENLQRckekcaeQALTIRELQGQVDGNYSLLTKLSLEEENHLIQLkcENLKEKLE 385
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEE-------LEEELAELEEELEELEEELEELEEELEEAEEEL--EEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 386 QMDAENKELERKLADQEEflkhSDLELREKAAECTALSRQLEAALEEGRQKVSEEVEKMSSRERALQMKISDLETELRKK 465
Cdd:COG1196 362 EAEEALLEAEAELAEAEE----ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958752699 466 NEEQNQLVGNMSTKAQHQDICLKEIQHSLEKSETQNE 502
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
104-328 |
2.29e-06 |
|
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: 49.76 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 104 AVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKK 183
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 184 QISHLLED----LRKMETHGKNSCEEILRKLHSLEDENEALNIenvkLKSTLDALKDEVASVENELVELQEVEKRQKALv 259
Cdd:COG4942 98 ELEAQKEElaelLRALYRLGRQPPLALLLSPEDFLDAVRRLQY----LKYLAPARREQAEELRADLAELAALRAELEAE- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752699 260 egyRTQVQKLEEAAAMVKSRCKNLLHENKLIINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQE 328
Cdd:COG4942 173 ---RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
243-473 |
6.92e-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: 48.91 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 243 NELVELQEVEKRQKALVEGYRTQVQKLEEAAAMvKSRCKNLLHEnkliinKKNTKLEKMRGQVETHLEQVEQARNSITSA 322
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREK-AERYQALLKE------KREYEGYELLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 323 EQRLQECQENLQRCKEKCAEQALTIRELQGQVDgnyslltKLSLEEENhliqlkceNLKEKLEQMDAENKELERKLADQE 402
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIK-------DLGEEEQL--------RVKEKIGELEAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958752699 403 EFLKHSD-------LELREKAAECTALSRQLEAALEEgRQKVSEEVEKMSSRERALQMKISDLETELRKKNEEQNQLV 473
Cdd:TIGR02169 315 RELEDAEerlakleAEIDKLLAEIEELEREIEEERKR-RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
63-469 |
1.11e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 63 DRLQLQIQKREVENERLKEHIQSLETQIAKWNLQVKMNKQEAVAVKEAS---RQKAEALKKASKVYRQRLRHFTGDIEQL 139
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAeelREEAAELESELEEAREAVEDRREEIEEL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 140 TSQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMET---HGK--------------NS 202
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleAGKcpecgqpvegsphvET 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 203 CEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASvENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKN 282
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 283 L-------------LHENKLIINKKNTKLEKMRGQVETHLEQVEQARNS---ITSAEQRLQECQE--------NLQRcKE 338
Cdd:PRK02224 549 LeaeaeekreaaaeAEEEAEEAREEVAELNSKLAELKERIESLERIRTLlaaIADAEDEIERLREkrealaelNDER-RE 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 339 KCAEQALTIRELQGQVDGNYslLTKLSLEEENHLIQLkcENLKEKLEQMDAENKELERKLADQEEFLKHSDlELREKAAE 418
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEAR--IEEAREDKERAEEYL--EQVEEKLDELREERDDLQAEIGAVENELEELE-ELRERREA 702
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1958752699 419 CTALSRQLEAALEEgrqkvSEEVEKMSSRERAlqmkisdletELRKKNEEQ 469
Cdd:PRK02224 703 LENRVEALEALYDE-----AEELESMYGDLRA----------ELRQRNVET 738
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
63-500 |
1.19e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 63 DRLQLQIQKREVENERLKEHIQSLETQIakwnlQVKMNKQ-EAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTS 141
Cdd:pfam15921 415 DHLRRELDDRNMEVQRLEALLKAMKSEC-----QGQMERQmAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKM 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 142 QIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMEtHGKNSCEEILRKLHSLEDENEAL- 220
Cdd:pfam15921 490 TLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR-NVQTECEALKLQMAEKDKVIEILr 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 221 -NIENV-----KLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEeaaamvkSRCKNLLHENKLIINKK 294
Cdd:pfam15921 569 qQIENMtqlvgQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE-------ARVSDLELEKVKLVNAG 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 295 NTKLEKMRG---QVETHLEQVEQARNSITSAEQRLQECQENLqrcKEKCAEQALTIRELQGQVDGNYSLL-----TKLSL 366
Cdd:pfam15921 642 SERLRAVKDikqERDQLLNEVKTSRNELNSLSEDYEVLKRNF---RNKSEEMETTTNKLKMQLKSAQSELeqtrnTLKSM 718
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 367 EEENHLIQLKCENLKEKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTALSRQLEAALEEgRQKVSEEVEKMSS 446
Cdd:pfam15921 719 EGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE-KNKMAGELEVLRS 797
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1958752699 447 RERALQMKISDLETELRKKNEEQNQLVGNMstKAQHQDICLKEIQHSLEKSETQ 500
Cdd:pfam15921 798 QERRLKEKVANMEVALDKASLQFAECQDII--QRQEQESVRLKLQHTLDVKELQ 849
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
101-417 |
2.07e-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: 47.37 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 101 KQEAVAVKEASRQKAEALKKASKVYRQrLRHFTGDIEQLTSQIRDQEAKLSEA------VSASNDWKSRYEKIAIEKT-- 172
Cdd:TIGR02169 219 EKREYEGYELLKEKEALERQKEAIERQ-LASLEEELEKLTEEISELEKRLEEIeqlleeLNKKIKDLGEEEQLRVKEKig 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 173 ELEVQIETMKKQISHLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVE 252
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 253 KRQKALVEGYRTQVQKLEEAaamvksrcKNLLHENKLIINKKNTKLEKMRgqvethlEQVEQARNSITSAEQRLQECQEN 332
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKL--------KREINELKRELDRLQEELQRLS-------EELADLNAAIAGIEAKINELEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 333 LQRCKEKCAEQALTIRELQGQVDGnyslltklsleeenhlIQLKCENLKEKLEQMDAENKELERKLADQEEFLKHSDLEL 412
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLAADLSK----------------YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
....*
gi 1958752699 413 REKAA 417
Cdd:TIGR02169 507 RGGRA 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
64-452 |
2.48e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 64 RLQLQIQKREVENERLKEHIQSLETQIAkwnlqvkmnkQEAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQI 143
Cdd:COG4913 278 RAALRLWFAQRRLELLEAELEELRAELA----------RLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 144 RDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLrkmethgknscEEILRKLHSLEDENEAlniE 223
Cdd:COG4913 348 ERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL-----------EEELEALEEALAEAEA---A 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 224 NVKLKSTLDALKDEVASVEN-------------------------------ELVELQEVEKRQKALVEGY-RTQ------ 265
Cdd:COG4913 414 LRDLRRELRELEAEIASLERrksniparllalrdalaealgldeaelpfvgELIEVRPEEERWRGAIERVlGGFaltllv 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 266 -VQKLEEAAAMVKS----------RCKNLLHENKLIINKKNTKLEKM-------RGQVETHL------------EQVEQA 315
Cdd:COG4913 494 pPEHYAAALRWVNRlhlrgrlvyeRVRTGLPDPERPRLDPDSLAGKLdfkphpfRAWLEAELgrrfdyvcvdspEELRRH 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 316 RNSIT----------------------------SAEQRLQECQENLQRCKEKCAEQALTIRELQGQVDGN------YSLL 361
Cdd:COG4913 574 PRAITragqvkgngtrhekddrrrirsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALqerreaLQRL 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 362 TKLSLEEENHL-IQLKCENLKEKLEQMDAEN---KELERKLADQEEFLKHSDLELREKAAECTALSRQLEAALEEgRQKV 437
Cdd:COG4913 654 AEYSWDEIDVAsAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE-LDEL 732
|
490
....*....|....*
gi 1958752699 438 SEEVEKMSSRERALQ 452
Cdd:COG4913 733 QDRLEAAEDLARLEL 747
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
29-272 |
4.46e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 29 EKETYIQELSCLFHNEKESALKANRFSQsvkvvhdrlQLQIQKREVENERLKEHIQSLETQIAKwnLQVKMNKQEAVAVK 108
Cdd:COG3206 132 VKGSNVIEISYTSPDPELAAAVANALAE---------AYLEQNLELRREEARKALEFLEEQLPE--LRKELEEAEAALEE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 109 EASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLS--EAVSASNDWKSRYEKIAIEKTELEVQIETMKKQIS 186
Cdd:COG3206 201 FRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAalRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 187 HLLEDL-----------RKMETHGKNSCEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQ 255
Cdd:COG3206 281 ELSARYtpnhpdvialrAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREV 360
|
250
....*....|....*..
gi 1958752699 256 KALVEGYRTQVQKLEEA 272
Cdd:COG3206 361 EVARELYESLLQRLEEA 377
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
261-513 |
8.62e-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: 45.43 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 261 GYRTQVQKLEEAAAMVKSRCKNLLHEnkliINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKC 340
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKA----LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 341 AEQALTIRELQGQVDGNYSLLTKLSLEEENHLIQLkcENLKEKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECT 420
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEI--EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 421 ALSRQLEAA------LEEGRQKVSEEVEKMSSRERALQMKISDLETELRKKNEEQNQL----------VGNMSTKAQHQD 484
Cdd:TIGR02168 828 SLERRIAATerrledLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLeealallrseLEELSEELRELE 907
|
250 260
....*....|....*....|....*....
gi 1958752699 485 ICLKEIQHSLEKSETQNESIKNYLQFLQI 513
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEV 936
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
231-503 |
1.06e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 231 LDALKDEVASVENELVELQevekRQKALVEGYRTQVQKLEEA----AAMVKSRCKNLLHENKLIINKKNTKLEKMRGQVE 306
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLE----RQAEKAERYKELKAELRELelalLVLRLEELREELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 307 THLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEqaltirelqgqvdgnyslltklsLEEENHLIQLKCENLKEKLEQ 386
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALANEISR-----------------------LEQQKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 387 MDAENKELERKLADQEEFLKHSDLELREKAAECTALsrqlEAALEEGRqkvsEEVEKMSSRERALQMKISDLETELRKKN 466
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESL----EAELEELE----AELEELESRLEELEEQLETLRSKVAQLE 392
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958752699 467 EEQNQLvgnmSTKAQHQDICLKEIQHSLEKSETQNES 503
Cdd:TIGR02168 393 LQIASL----NNEIERLEARLERLEDRRERLQQEIEE 425
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
68-472 |
2.32e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 68 QIQKREVENERLKEHIQSLETQIAKWNLQVKmNKQEAVAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQE 147
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIK-KKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 148 AKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMETHGKNSCEEILRKLHSLEDENEALN---IEN 224
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSekqKEL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 225 VKLKSTLDALKDEVASVENELVELQ-------------EVEKRQKALVE------GYRTQVQKLEEAAAMVKSRCKNLLH 285
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNnqkeqdwnkelksELKNQEKKLEEiqnqisQNNKIISQLNEQISQLKKELTNSES 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 286 ENKLI---INKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVDGNYSLLT 362
Cdd:TIGR04523 357 ENSEKqreLEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 363 KL-----SLEEENHLIQLKCENLKEKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTALSRQlEAALEEGRQKV 437
Cdd:TIGR04523 437 KNnseikDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE-KKELEEKVKDL 515
|
410 420 430
....*....|....*....|....*....|....*
gi 1958752699 438 SEEVEKMSSRERALQMKISDLETELRKKNEEQNQL 472
Cdd:TIGR04523 516 TKKISSLKEKIEKLESEKKEKESKISDLEDELNKD 550
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
376-472 |
2.76e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 376 KCENLKEKLEQMDAENKELERKLADQEEFLKHSDLELREkaaectalsrqleaALEEGRQKVSEEvEKMSSRERalqmKI 455
Cdd:COG2433 414 EIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSE--------------ARSEERREIRKD-REISRLDR----EI 474
|
90
....*....|....*..
gi 1958752699 456 SDLETELRKKNEEQNQL 472
Cdd:COG2433 475 ERLERELEEERERIEEL 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
272-468 |
5.43e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 272 AAAMVKSRCKNLLHENKLIINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQ 351
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 352 GQVDGNYSLLTKL-----------------------SLEEENHLIQLKCENLKEKLEQMDAENKELERKLADQEEFLKHS 408
Cdd:COG4942 97 AELEAQKEELAELlralyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958752699 409 DLELREKAAECTALS------RQLEAALEEGRQKVSEEVEKMSSRERALQMKISDLETELRKKNEE 468
Cdd:COG4942 177 EALLAELEEERAALEalkaerQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
65-468 |
7.68e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 65 LQLQIQKREVENERLKEHIQSLETQIAKWNLQVKMNKQEAVAVKEASRQKAE--ALKKASKVYRQRLRHFTGDIEQLTSQ 142
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 143 IRDQEAKLSEAvsasNDWKSRYEKIAIEKTELEVQIETMKK------QISHLLEDLRKMETH-GKNSCEEILRKLHSLED 215
Cdd:PRK03918 323 INGIEERIKEL----EEKEERLEELKKKLKELEKRLEELEErhelyeEAKAKKEELERLKKRlTGLTPEKLEKELEELEK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 216 ENEALNIENVKLKSTLDALKDEVASVENELVELQEVekRQKALVEGYRTQVQKLEEAAAMVKSRCKNLLHENKLIINKKN 295
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIEELKKA--KGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 296 tKLEKMRGQVETHLEQVEQARNSITSAEQrLQECQENLQRCKEKCAEQALTirelqgqvdgNYSLLTKLSLEEENHLIQL 375
Cdd:PRK03918 477 -KLRKELRELEKVLKKESELIKLKELAEQ-LKELEEKLKKYNLEELEKKAE----------EYEKLKEKLIKLKGEIKSL 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 376 KCEnlKEKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTalsRQLEAALEEGRQKVSE--EVEKMSSRERALQM 453
Cdd:PRK03918 545 KKE--LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESV---EELEERLKELEPFYNEylELKDAEKELEREEK 619
|
410
....*....|....*
gi 1958752699 454 KISDLETELRKKNEE 468
Cdd:PRK03918 620 ELKKLEEELDKAFEE 634
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
13-482 |
1.21e-03 |
|
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: 41.58 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 13 LSDSDSENRDLKKKVLEKETYIQELSCLFHNEKESALKANRFSQSVKVVHDRLQLQIQKREVENERLKEHIQSLETQIAK 92
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 93 WNLQVKMNKQEAVAVKE---ASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDWKSRYEKIAI 169
Cdd:TIGR02168 342 LEEKLEELKEELESLEAeleELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 170 EKTELEVQIETMKKQ-ISHLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVEL 248
Cdd:TIGR02168 422 EIEELLKKLEEAELKeLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 249 QEVEKRQKALV--------------------EGYRTQVQK-LEEAAAMVKSRCKN-------LLHENKL----------- 289
Cdd:TIGR02168 502 EGFSEGVKALLknqsglsgilgvlselisvdEGYEAAIEAaLGGRLQAVVVENLNaakkaiaFLKQNELgrvtflpldsi 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 290 ----IINKKNTKLEKMRGQVETHLEQVEQA----------------------------------------------RNSI 319
Cdd:TIGR02168 582 kgteIQGNDREILKNIEGFLGVAKDLVKFDpklrkalsyllggvlvvddldnalelakklrpgyrivtldgdlvrpGGVI 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 320 T----SAEQRLQECQENLQRCKEKCAEQALTIRELQGQVDGNYSLLTklSLEEENHLIQLKCENLKEKLEQMDAENKELE 395
Cdd:TIGR02168 662 TggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELE--ELEEELEQLRKELEELSRQISALRKDLARLE 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 396 RKLADQEEFLKHSDLELREKAAECTALSRQLE------AALEEGRQKVSEEVEKMS-------SRERALQMKISDLETEL 462
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEeaeeelAEAEAEIEELEAQIEQLKeelkalrEALDELRAELTLLNEEA 819
|
570 580
....*....|....*....|
gi 1958752699 463 RKKNEEQNQLVGNMSTKAQH 482
Cdd:TIGR02168 820 ANLRERLESLERRIAATERR 839
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
231-446 |
1.44e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 231 LDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRcknllhenkliinKKNTKLEKMRGQVETHLE 310
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE-------------IDVASAEREIAELEAELE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 311 QVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVDGnyslltklsleeenhlIQLKCENLKEKLEQMDAE 390
Cdd:COG4913 679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ----------------AEEELDELQDRLEAAEDL 742
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958752699 391 NKELERKLADqEEFLKHSDLELREKAAEctALSRQLEAALEEGRQKVSEEVEKMSS 446
Cdd:COG4913 743 ARLELRALLE-ERFAAALGDAVERELRE--NLEERIDALRARLNRAEEELERAMRA 795
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
11-506 |
1.55e-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: 41.16 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 11 KDLSDSDSENRDLKKKVL----EKETYIQELSCLFHNEKESALKANRFSQSVKVV------HDRLQLQIQKREVENERLK 80
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEelenELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLkkkiqkNKSLESQISELKKQNNQLK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 81 EHIQSLETQIAKWNLQVKMNKQEAVAVKEASRQKAEALKKASKvyrqRLRHFTGDIEQLTSQIRDQEAKLSE-----AVS 155
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK----ELEQNNKKIKELEKQLNQLKSEISDlnnqkEQD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 156 ASNDWKSRYEKIAIEKTELEVQIETMKKQISHL---LEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVKLKSTLD 232
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLneqISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 233 ALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKNLLHENKLIINK---KNTKLEKMRGQVETHL 309
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvKELIIKNLDNTRESLE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 310 EQVEQARNSITSAEQRLQECQENLqrcKEKCAEQALTIRElqgqvdgnyslltKLSLEEENHLIQLKCENLKEKLEQMDA 389
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKEL---KSKEKELKKLNEE-------------KKELEEKVKDLTKKISSLKEKIEKLES 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 390 ENKELERKLADQEEFLKHSDLELREKAaectalsrqleaaLEEGRQKVSEEVEKMSSRERALQMKISDLETELRKKNEEQ 469
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELKKEN-------------LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEK 598
|
490 500 510
....*....|....*....|....*....|....*..
gi 1958752699 470 NQLVGNMSTKAQHQDICLKEIQHSLEKSETQNESIKN 506
Cdd:TIGR04523 599 KDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
204-271 |
2.22e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 2.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752699 204 EEILRKLHSLEDENEALNIE-NVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEE 271
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEqDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQ 482
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
69-498 |
2.45e-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: 40.59 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 69 IQKREVENERLKEHIQSLETQIAKwnLQVKMNKQEAVAVKEASRQkaEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEA 148
Cdd:pfam12128 236 IMKIRPEFTKLQQEFNTLESAELR--LSHLHFGYKSDETLIASRQ--EERQETSAELNQLLRTLDDQWKEKRDELNGELS 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 149 KLSEAVS-------ASNDWKSRYEKIAIEKTELEV--------QIETMKKQISHLLEDLRKME----THGKNSCEEILRK 209
Cdd:pfam12128 312 AADAAVAkdrseleALEDQHGAFLDADIETAAADQeqlpswqsELENLEERLKALTGKHQDVTakynRRRSKIKEQNNRD 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 210 LHSLEDENEALNIENVKLKStldALKDEVASVENELVELQEVEKRQkalvegYRTQVQKLEEAAAMVKSRCKNLLHENKL 289
Cdd:pfam12128 392 IAGIKDKLAKIREARDRQLA---VAEDDLQALESELREQLEAGKLE------FNEEEYRLKSRLGELKLRLNQATATPEL 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 290 IINKKN--TKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVDG----------- 356
Cdd:pfam12128 463 LLQLENfdERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPqagtllhflrk 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 357 -------------NYSLLTKLSLEEENHLIQLKCEN----LKEKLEQMD-----AENKELERKLA-------DQEEFLKH 407
Cdd:pfam12128 543 eapdweqsigkviSPELLHRTDLDPEVWDGSVGGELnlygVKLDLKRIDvpewaASEEELRERLDkaeealqSAREKQAA 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 408 SDLELREKAAECTALSRQLEAAL------EEGRQKVSEEVEKMSSR-ERALQMKISDLETELRKKNEEQNQLVGNMSTKA 480
Cdd:pfam12128 623 AEEQLVQANGELEKASREETFARtalknaRLDLRRLFDEKQSEKDKkNKALAERKDSANERLNSLEAQLKQLDKKHQAWL 702
|
490
....*....|....*...
gi 1958752699 481 QHQDICLKEiqHSLEKSE 498
Cdd:pfam12128 703 EEQKEQKRE--ARTEKQA 718
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
286-472 |
3.34e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 286 ENKLIINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRckekcaeqaltireLQGQVDGNYSLLTKLS 365
Cdd:COG3206 195 EAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA--------------LRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 366 leeENHLIQlkceNLKEKLEQmdaenkeLERKLADQEEFLKHSDLELREKAAECTALSRQLEAALEEGRQKVSEEVEKMS 445
Cdd:COG3206 261 ---QSPVIQ----QLRAQLAE-------LEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQ 326
|
170 180
....*....|....*....|....*..
gi 1958752699 446 SRERALQMKISDLETELRKKNEEQNQL 472
Cdd:COG3206 327 AREASLQAQLAQLEARLAELPELEAEL 353
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
66-349 |
4.00e-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: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 66 QLQIQKREVENERLKEHIQSLETQIAKWNLQVKMNKQEavavkeaSRQKAEALKKASKVYRQRLRhftgDIEQLTSQIRD 145
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL-------NQQKDEQIKKLQQEKELLEK----EIERLKETIIK 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 146 QEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMETHGKNSCEEIL---RKLHSLEDENEALNI 222
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKklnEEKKELEEKVKDLTK 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 223 ENVKLKSTLDALKDEVASVENELVELQE--VEKRQKALVEGYRTQVQKLEEAAAMVKSRCKNLLHEN---KLIINKKNTK 297
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDelNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQeekQELIDQKEKE 597
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958752699 298 LEKMRGQVETHLEQVEQARNSITSAE---QRLQECQENLQRCKEKCAEQALTIRE 349
Cdd:TIGR04523 598 KKDLIKEIEEKEKKISSLEKELEKAKkenEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
322-472 |
4.19e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 322 AEQRLQECQENLQRCKEKcaeqaltIRELQGQVDgnyslltKLSLEEEnhlIQLKCENLKEKLEQMDAE-----NKELER 396
Cdd:COG1196 177 AERKLEATEENLERLEDI-------LGELERQLE-------PLERQAE---KAERYRELKEELKELEAEllllkLRELEA 239
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958752699 397 KLADQEEFLKHSDLELREKAAEctalSRQLEAALEEGRQKVSE---EVEKMSSRERALQMKISDLETELRKKNEEQNQL 472
Cdd:COG1196 240 ELEELEAELEELEAELEELEAE----LAELEAELEELRLELEElelELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
65-509 |
4.28e-03 |
|
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: 39.72 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 65 LQLQIQKREVENERLKEHIQSLETQiAKWNLQVKMNKQEAVAVKEAsrqkaEALKKASKVYRQRLRHFTGDIEQLTSQIR 144
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKELEFEIQSQ-EQDSEIVKNSKSELARIPEL-----EKELERLREHNKHLNENIENKLLLKEEVE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 145 DQEAKLSEavsaSNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMETHgKNSCEEILRKLHSLEDENEALNIEN 224
Cdd:pfam05557 232 DLKRKLER----EEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDL-SRRIEQLQQREIVLKEENSSLTSSA 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 225 VKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQV----QKLEEAAAMVKSRCKNLLHEN-KLIINKKNTKLE 299
Cdd:pfam05557 307 RQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltKERDGYRAILESYDKELTMSNySPQLLERIEEAE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 300 KMRGQVETHLEQVEQarnsitsaeqRLQECQENLQRCKEKCAEQALTIRELQGQVDGNYSLLTKLSLEEenhliqlkcen 379
Cdd:pfam05557 387 DMTQKMQAHNEEMEA----------QLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDS----------- 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 380 LKEKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTALSRQLEAALEEGRQKvSEEVEKmssreraLQMKISDLE 459
Cdd:pfam05557 446 LRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQR-KNQLEK-------LQAEIERLK 517
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1958752699 460 TELRKKNEEQNQLVGNMSTKAQHQDICLKEIQHSLEKSETQNESIKNYLQ 509
Cdd:pfam05557 518 RLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQRLKEVFQ 567
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
322-454 |
4.40e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 322 AEQRLQECQENLQRCKEKCAEQALT-IRELQGQVDGNYSLLTKLSLEEENHLIQlKCENLKEKLEQMDAENKELErklaD 400
Cdd:PRK12704 40 AKRILEEAKKEAEAIKKEALLEAKEeIHKLRNEFEKELRERRNELQKLEKRLLQ-KEENLDRKLELLEKREEELE----K 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958752699 401 QEEFLKHSDLELREKAAECTALSRQLEAALE--------EGRQKVSEEVEKMSSRERALQMK 454
Cdd:PRK12704 115 KEKELEQKQQELEKKEEELEELIEEQLQELErisgltaeEAKEILLEKVEEEARHEAAVLIK 176
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
108-509 |
4.67e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 108 KEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAVSaSNDWKSRYEKIAiEKTELEVQIETMKKQISH 187
Cdd:TIGR00606 586 INQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCG-SQDEESDLERLK-EEIEKSSKQRAMLAGATA 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 188 LLEDLRKMETHGKNSCEEILRKLHSLEDEneaLNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQ 267
Cdd:TIGR00606 664 VYSQFITQLTDENQSCCPVCQRVFQTEAE---LQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIID 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 268 KLEEAAAMVKSRCKNLLHEnkliINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQrLQECQENLQRCKEKCAEQAlti 347
Cdd:TIGR00606 741 LKEKEIPELRNKLQKVNRD----IQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTI-MERFQMELKDVERKIAQQA--- 812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 348 RELQGqVDGNyslltkLSLEEENHLIQLKcenlKEKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTALSRQLE 427
Cdd:TIGR00606 813 AKLQG-SDLD------RTVQQVNQEKQEK----QHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQ 881
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 428 --AALEEGRQKVSEEVEKMSSRERALQMKISDLETELRKKNEEQNQLVGNMSTKAQHQDICLKEIQHSLEKSETQNESIK 505
Cdd:TIGR00606 882 rrQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIE 961
|
....
gi 1958752699 506 NYLQ 509
Cdd:TIGR00606 962 NKIQ 965
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
173-506 |
4.83e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 39.84 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 173 ELEVQIETMKKQISHLLEDLRKMETHGKNsceEILRKLHSLEDENEALNIENVKLKSTLDALKDEV--ASVENELVELQE 250
Cdd:PLN03229 433 ELEGEVEKLKEQILKAKESSSKPSELALN---EMIEKLKKEIDLEYTEAVIAMGLQERLENLREEFskANSQDQLMHPVL 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 251 VEKRQKALVEGYRTQVQKLEEAAAMVKSRCKNLLHENKLIINKKNtKLEKMRGQVETHLEQVEQArnsitsaeqrlQECQ 330
Cdd:PLN03229 510 MEKIEKLKDEFNKRLSRAPNYLSLKYKLDMLNEFSRAKALSEKKS-KAEKLKAEINKKFKEVMDR-----------PEIK 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 331 ENLQRCKEKCAEQAL-TIRELQgqvdgnyslltklsleeenhliqlkcENLKEKLEQMdaeNKELERKLAdqeEFLKHSD 409
Cdd:PLN03229 578 EKMEALKAEVASSGAsSGDELD--------------------------DDLKEKVEKM---KKEIELELA---GVLKSMG 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 410 LEL-----REKAAECTALSRQLEAALEEGRQKVSEEVEKM---------------------SSRERALQMKISDLETELR 463
Cdd:PLN03229 626 LEVigvtkKNKDTAEQTPPPNLQEKIESLNEEINKKIERVirssdlkskiellklevakasKTPDVTEKEKIEALEQQIK 705
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958752699 464 KKNEEqnqlVGNMSTKAQHQDICLKEIQHSLEKSETQNESIKN 506
Cdd:PLN03229 706 QKIAE----ALNSSELKEKFEELEAELAAARETAAESNGSLKN 744
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
63-274 |
5.09e-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: 39.36 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 63 DRLQLQIQKREVENERLKEHIQSLETQIAKWNLQVKmnkqeavavkeASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQ 142
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIA-----------ALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 143 IRDQEAKLSEAVSASndwksrYEKIAIEKTELEVQIETMkKQISHLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNI 222
Cdd:COG4942 99 LEAQKEELAELLRAL------YRLGRQPPLALLLSPEDF-LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958752699 223 ENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAA 274
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
236-512 |
5.16e-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: 39.67 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 236 DEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKNLLHENKLIINKKNTKLEKMRGQVETHLEQ---- 311
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISElekr 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 312 VEQARNSITSAEQRLQECQENLQ-RCKEKCAEQALTIRELQGQVDGNYSLLTKLS-----LEEENHLIQLKCENLKEKLE 385
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIASLERSIAEKERELEDAEerlakLEAEIDKLLAEIEELEREIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 386 -------QMDAENKELERKLADQEEFLKHSDLELREKAAECTALSRQLEAALEEgRQKVSEEVEKMSSRERALQMKISDL 458
Cdd:TIGR02169 347 eerkrrdKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE-INELKRELDRLQEELQRLSEELADL 425
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958752699 459 ETELRKKNEEQNQLVGNMSTKA---QHQDICLKEIQHSLEKSETQNESIKNYLQFLQ 512
Cdd:TIGR02169 426 NAAIAGIEAKINELEEEKEDKAleiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
141-506 |
5.50e-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: 39.62 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 141 SQIRDQEAKLSEAVSASNDWKSRYEKIAIEKTELEVQIETMKKQISHLLEDLRKMETHGK---NSCEEILRKLHSLEDEN 217
Cdd:TIGR04523 96 DKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEklnNKYNDLKKQKEELENEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 218 EALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVegyrTQVQKLEEAAAMVKSrcknllhenklIINKKNTK 297
Cdd:TIGR04523 176 NLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLE----SQISELKKQNNQLKD-----------NIEKKQQE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 298 LEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVdgnySLLTKLSLEEENHLIQLKC 377
Cdd:TIGR04523 241 INEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEI----SDLNNQKEQDWNKELKSEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 378 ENLKEKLEQMDAENKELERKLADQEEFLKHSDLELREKAAECTALSRQLEAALEEGRQKVSEEVEKMSSRERaLQMKISD 457
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN-LESQIND 395
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958752699 458 LETELRKKNEEQNQLVGNMSTKAQHQDICLKEIQHSLEKSETQNESIKN 506
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
46-390 |
5.93e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.50 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 46 ESALKANRFSQSVKVVHDRLQLQIQKREVENERLKEHIQSLETQIAKWNLQ--VKMNKQEAVAVKEASRQKAEALKKASK 123
Cdd:PLN02939 81 RTVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEdlVGMIQNAEKNILLLNQARLQALEDLEK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 124 VYRQRlrhftgdiEQLTSQIRDQEAKLSEAVSASNdwKSRYEKIAIEKteLEVQIETMKKQISHLLEDLRKMEthgknsc 203
Cdd:PLN02939 161 ILTEK--------EALQGKINILEMRLSETDARIK--LAAQEKIHVEI--LEEQLEKLRNELLIRGATEGLCV------- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 204 eeilrklHSLEDENEALNIENVKLKSTLDALKDevasvenELVELQEVEKRqkalvegyrtqVQKLEEAAAMVKSRCKNL 283
Cdd:PLN02939 222 -------HSLSKELDVLKEENMLLKDDIQFLKA-------ELIEVAETEER-----------VFKLEKERSLLDASLREL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 284 lhENKLIINKKN-TKLEKMrgQVETHLEQVEQARNSITSAEQRLQECQENLQRCkekcaeqaltiRELQGQVDgnyslLT 362
Cdd:PLN02939 277 --ESKFIVAQEDvSKLSPL--QYDCWWEKVENLQDLLDRATNQVEKAALVLDQN-----------QDLRDKVD-----KL 336
|
330 340 350
....*....|....*....|....*....|....*..
gi 1958752699 363 KLSLEEEN---------HLIQLKCENLKEKLEQMDAE 390
Cdd:PLN02939 337 EASLKEANvskfssykvELLQQKLKLLEERLQASDHE 373
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
10-466 |
7.75e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 10 LKDLSDSDSENRDLKKKVLEKETYIQELSclfhnEKESALKANRFSQSVKVVHDRLQLQIQKREVENERLKEHIQSLETQ 89
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELE-----AELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 90 IAKW-NLQVKMNKQEAvAVKEASRQKAEALKKASKVYRQRLRHFTGDIEQLTSQIRDQEAKLSEAvsasndwksryekia 168
Cdd:COG4717 155 LEELrELEEELEELEA-ELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA--------------- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 169 iektelEVQIETMKKQISHLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVKLKSTLDALKDEVASVeneLVEL 248
Cdd:COG4717 219 ------QEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL---LALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 249 QEVEKRQKALVEGYRTQVQKLEEAAAMVKSRCKNLLHENKLIINKKNTKLEKMRGQVETHLEQVEQARNSITSA--EQRL 326
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqlEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 327 QECQENLQRCK-------EKCAEQALTIRELQGQVDGNYSLLTKLSLEEENHLIQLKCENLKEKLEQMDAENKELERKLA 399
Cdd:COG4717 370 QEIAALLAEAGvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELE 449
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958752699 400 DQEEflKHSDLELREKAAECTALSRQLEAALEEGRQKVSEEVEKMSSReRALQMKISDLETELRKKN 466
Cdd:COG4717 450 ELRE--ELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAAL-KLALELLEEAREEYREER 513
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
126-403 |
7.87e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 126 RQRLRHFTGDIEQLTSQIRDQEAKLSEAVSASNDWKSR---YEKIAiEKTELEVQIETMKKQISHLLEDLRKMEthgKNS 202
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERreaLQRLA-EYSWDEIDVASAEREIAELEAELERLD---ASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 203 CEeilrkLHSLEDENEALNIENVKLKSTLDALKDEVASVENELVELQEVEKRQKALVEGYRTQVQKLEEAAamvksrckn 282
Cdd:COG4913 685 DD-----LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--------- 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 283 llhenkliinkkntkLEKMRGQV---ETHLEQVEQARNSITSAEQRLQECQENLQRCKEK-CAEQALTIRELQGQVDGNY 358
Cdd:COG4913 751 ---------------LEERFAAAlgdAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLP 815
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1958752699 359 SLLTKLSLEEENHLIQLKCENLKEKLEQMDAENKELERKLADQEE 403
Cdd:COG4913 816 EYLALLDRLEEDGLPEYEERFKELLNENSIEFVADLLSKLRRAIR 860
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
309-467 |
8.84e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 38.52 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 309 LEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQALTIRELQGQVDGNYSLLTK-----------------LSLEEE-- 369
Cdd:PRK11637 74 LAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAqldaafrqgehtglqliLSGEESqr 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 370 -----------NHLIQLKCENLKEKLEQMDAENKELERKLADQEEFLkhSDLELREKAAECTALSRQ-----LEAALEEG 433
Cdd:PRK11637 154 gerilayfgylNQARQETIAELKQTREELAAQKAELEEKQSQQKTLL--YEQQAQQQKLEQARNERKktltgLESSLQKD 231
|
170 180 190
....*....|....*....|....*....|....
gi 1958752699 434 RQKVSEevekMSSRERALQMKISDLETELRKKNE 467
Cdd:PRK11637 232 QQQLSE----LRANESRLRDSIARAEREAKARAE 261
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
264-452 |
9.84e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.27 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 264 TQVQKLEEAAAMVKSRCKNLLHEnkliINKKNTKLEKMRGQVETHLEQVEQARNSITSAEQRLQECQENLQRCKEKCAEQ 343
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAE----LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 344 ALTIRELQGQVD---------------GNYSLLTKLS----------------LEEENHLIQLKCENLKEKLEQMDAENK 392
Cdd:COG3883 92 ARALYRSGGSVSyldvllgsesfsdflDRLSALSKIAdadadlleelkadkaeLEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752699 393 ELERKLADQEEFLKHSDLELREKAAECTALSRQLEAALEEGRQKVSEEVEKMSSRERALQ 452
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| |
