|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
343-537 |
6.98e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 343 LREELVHMQEDLRRLESEKEDLERDLNFKADQAQQYDRLLETVREQNRQLQMSLKESNNAQRTLESQLLTFQskdptkdf 422
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE-------- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 423 riKELEGSKRALEQENELLRKKLAGQcssSTIQIKTQELSREYEKMLNDLREEKDKE------LKSLRSQLIKIQSESTI 496
Cdd:COG1196 351 --EELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAAELAAQLeeleeaEEALLERLERLEEELEE 425
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1207161729 497 IQTTDTSSLELRISELLSKLEQRESVIRHQEEEIRRLKLQK 537
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
347-534 |
1.86e-06 |
|
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: 51.21 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 347 LVHMQEDLRRLESEKEDLERDLN---FKADQAQQYDRL---------------LETVREQNRQLQMSLKESNNAQRTLES 408
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKsleRQAEKAERYKELkaelrelelallvlrLEELREELEELQEELKEAEEELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 409 QLLTFQSKDPTKDFRIKELEGSKRALEQENELLRKKLAGQcsSSTIQIKTQELSR--EYEKMLNDLREEKDKELKSLRSQ 486
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL--EQQKQILRERLANleRQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1207161729 487 LIKIQSESTIIQtTDTSSLELRISELLSKLEQRESVIRHQEEEIRRLK 534
Cdd:TIGR02168 339 LAELEEKLEELK-EELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
214-534 |
2.26e-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: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 214 SESELVETSSIHEEVLDLKQLKNGIS---TEIKTEIQEPVAKLDN--RFFGELLAEVYRKNVDIQTcISEHVAKIRGRKH 288
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQselRRIENRLDELSQELSDasRKIGEIEKEIEQLEQEEEK-LKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 289 LLDSTI-DYKMEKEEFESLIPKgvSELTKQQIRYLLqtrmtADKTMHLVMTTFSSLREELVHMQEDLRRLESEKEDLERD 367
Cdd:TIGR02169 748 SLEQEIeNVKSELKELEARIEE--LEEDLHKLEEAL-----NDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 368 LNFKADQAQQYDRLLETVREQNRQLQMSLKESNNAQRTLESQLLTFQSKDPTKDFRIKELEGSKRALEQENELLRKKLag 447
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL-- 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 448 qcssSTIQIKTQELSREYEKM------LNDLREEKDKELKSLRSQLIKIQSESTiiQTTDTSSLELRISELLSKLEQRES 521
Cdd:TIGR02169 899 ----RELERKIEELEAQIEKKrkrlseLKAKLEALEEELSEIEDPKGEDEEIPE--EELSLEDVQAELQRVEEEIRALEP 972
|
330
....*....|....*..
gi 1207161729 522 V----IRHQEEEIRRLK 534
Cdd:TIGR02169 973 VnmlaIQEYEEVLKRLD 989
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
352-538 |
2.48e-06 |
|
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: 50.40 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 352 EDLRRLESEKEDLERDLNFKADQAQQYDRLLETVREQNRQLQMSLKESNNAQRTLESQLLTFQSKDPTKDFRIKELEGSK 431
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 432 RALEQENELLRKKLAGQCSS----------------------STIQIKTQELSREYEKMLNDLrEEKDKELKSLRSQLIK 489
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEikdltnqdsvkeliiknldntrESLETQLKVLSRSINKIKQNL-EQKQKELKSKEKELKK 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207161729 490 IQSESTIIQTTdTSSLELRISELLSKLEQRES------------------------------VIRHQEEEIRRLKLQKT 538
Cdd:TIGR04523 501 LNEEKKELEEK-VKDLTKKISSLKEKIEKLESekkekeskisdledelnkddfelkkenlekEIDEKNKEIEELKQTQK 578
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
312-546 |
2.33e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 312 SELTKQQIRYLLQTRMTADKTMHLVMTTFSSLREELVHMQEDLRRLESEKEDLE---RDLNFKADQAQQ-YDRLLETVRE 387
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRlelEELELELEEAQAeEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 388 QNRQLQMSLKESNNAQRT---LESQLLTFQSKDPTKDFRIKELEGSKRALEQENELLRKKLAgqcsssTIQIKTQELSRE 464
Cdd:COG1196 300 LEQDIARLEERRRELEERleeLEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA------EAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 465 YEKMLNDLREEKDKELKSLRSQLIKIQSESTIIQTTDtsSLELRISELLSKLEQRESVIRHQEEEIRRLKLQKTDSSSSS 544
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE--ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
..
gi 1207161729 545 TR 546
Cdd:COG1196 452 AE 453
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
341-480 |
5.66e-05 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 44.12 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 341 SSLREELVHMQEDLRRLESEKEDLERDLNFKADQaqqydrlLETVREQNRQLQMSLKESNNAQR-TLESQLLTFQSKDPT 419
Cdd:pfam15619 63 ARHNEEVRVLRERLRRLQEKERDLERKLKEKEAE-------LLRLRDQLKRLEKLSEDKNLAEReELQKKLEQLEAKLED 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207161729 420 KDFRIKELEgskRALEQENELLRKKLAGQ-CSSSTIQIKTQELSREYEKmLNDLREEKDKEL 480
Cdd:pfam15619 136 KDEKIQDLE---RKLELENKSFRRQLAAEkKKHKEAQEEVKILQEEIER-LQQKLKEKEREL 193
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
315-521 |
7.89e-05 |
|
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: 45.14 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 315 TKQQIRYLLQTRMTADKTMHLVMTTFSSLREELVHMQEDLRRLESEKEDLERDLnfkADQAQQYDRLLETVREQNRQLQM 394
Cdd:COG4942 46 LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL---EAQKEELAELLRALYRLGRQPPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 395 SLKESNNAQRTLESQLLTFQSKDPTKDFRIKELEGSKRALEQENELLRKKLAgqcsssTIQIKTQELSREYEKmLNDLRE 474
Cdd:COG4942 123 ALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA------ELEALLAELEEERAA-LEALKA 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207161729 475 EKDKELKSLRSQLIKIQSESTIIQtTDTSSLELRISELLSKLEQRES 521
Cdd:COG4942 196 ERQKLLARLEKELAELAAELAELQ-QEAEELEALIARLEAEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
299-534 |
3.47e-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: 43.89 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 299 EKEEFESLIpkgvSELTKQQIRyLLQTRMTADKTMHLVMTTFSSLREELVHMQEDLRRLESEKEDLERDLNFKADQAQQY 378
Cdd:TIGR02168 685 KIEELEEKI----AELEKALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 379 DRLLETVREQNRQLQMSLKESNNAQRTLESQLLTFQSKDPTKDFRIKELEGSKRALEQENELLRKKLAG-QCSSSTIQIK 457
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESlERRIAATERR 839
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207161729 458 TQELSREYEKMLNDLrEEKDKELKSLRSQLIKIQSESTIIqTTDTSSLELRISELLSKLEQRESVIRHQEEEIRRLK 534
Cdd:TIGR02168 840 LEDLEEQIEELSEDI-ESLAAEIEELEELIEELESELEAL-LNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
271-527 |
4.87e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 271 DIQTCISEHVAKIRGRKHLLDSTIDYKMEKEEFESLIPKGVSELTKQQIRYLLQTRMTADKTMHL---------VMTTFS 341
Cdd:pfam15921 441 ECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLqekeraieaTNAEIT 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 342 SLR-------EELVHMQ---EDLRRLESEKEDLERDLNFKaDQA-----QQYDRLLETVREQNRQLQMSLKESNNAQRTL 406
Cdd:pfam15921 521 KLRsrvdlklQELQHLKnegDHLRNVQTECEALKLQMAEK-DKVieilrQQIENMTQLVGQHGRTAGAMQVEKAQLEKEI 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 407 ESQLLTFQS----KDpTKDFRIKELEGSKRALEQEnellRKKLAGQCSSSTIQIKtqELSREYEKMLNDLREEKDkELKS 482
Cdd:pfam15921 600 NDRRLELQEfkilKD-KKDAKIRELEARVSDLELE----KVKLVNAGSERLRAVK--DIKQERDQLLNEVKTSRN-ELNS 671
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1207161729 483 LRS--QLIK--IQSESTIIQTTdTSSLELRISELLSKLEQRESVIRHQE 527
Cdd:pfam15921 672 LSEdyEVLKrnFRNKSEEMETT-TNKLKMQLKSAQSELEQTRNTLKSME 719
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
340-427 |
5.02e-04 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 42.41 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 340 FSSLREELVHMQEDLRRLESEKEDLERDLNFKADQAQQYDRLLETVREQNRQLQMSLKESNNAQRTLESQLLTFQSKDPT 419
Cdd:COG4026 130 YNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKRLL 209
|
....*...
gi 1207161729 420 KDFRIKEL 427
Cdd:COG4026 210 EVFSLEEL 217
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
343-534 |
5.43e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 343 LREELVHMQEDLRRLESEKEDL--ERDLNFKADQAQQYDRLLETVREQNRQLQMSLKESNNAQRTLESQLLTFQSKDPT- 419
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEl 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 420 -KDFRIKELEGSKRALEQENELLRKKLAGQcssstiQIKTQELSREYEKMLNDLREEKDKELKSLRSQLIKIQSEstiiq 498
Cdd:COG3206 260 lQSPVIQQLRAQLAELEAELAELSARYTPN------HPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAR----- 328
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207161729 499 ttdtsslELRISELLSKLEQRESVIRHQEEEIRRLK 534
Cdd:COG3206 329 -------EASLQAQLAQLEARLAELPELEAELRRLE 357
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
330-539 |
5.79e-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: 43.09 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 330 DKTMHLVMTTFSSLREELVHMQEDLRRLESEKEDLERDLNFKADQAQQYDRLLETVREQNRQLQMSL---KESNNAQRTL 406
Cdd:TIGR04523 137 KKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlKKKIQKNKSL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 407 ESQLLTFQSKDPTKDFRIKELEGSKRALEQENELLRKKLAgQCSSSTIQIKTQELSREYE-KMLNDLREEKDKELKSLRS 485
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN-QLKDEQNKIKKQLSEKQKElEQNNKKIKELEKQLNQLKS 295
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207161729 486 QL--IKIQSESTIIQT--TDTSSLELRISELLSKLEQRESVIRHQEEEIRRLKLQKTD 539
Cdd:TIGR04523 296 EIsdLNNQKEQDWNKElkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTN 353
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
354-539 |
6.43e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 354 LRRLESEKEDLER--DLNF-----------KADQAQQYDRLLEtvREQNRQLQMSLKESNNAQRTLESQlltfqskdptk 420
Cdd:COG1196 178 ERKLEATEENLERleDILGelerqleplerQAEKAERYRELKE--ELKELEAELLLLKLRELEAELEEL----------- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 421 DFRIKELEGSKRALEQENELLRKKLAgqcsssTIQIKTQELSREYEKMLNDLREekdkelksLRSQLIKIQSEStIIQTT 500
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELE------ELRLELEELELELEEAQAEEYE--------LLAELARLEQDI-ARLEE 309
|
170 180 190
....*....|....*....|....*....|....*....
gi 1207161729 501 DTSSLELRISELLSKLEQRESVIRHQEEEIRRLKLQKTD 539
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
463-534 |
7.57e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 7.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207161729 463 REYEKMLNDLREEKDKELKSLRSQLIKIQSESTIIQTTDT--SSLELRISELLSKLEQRESVIRHQEEEIRRLK 534
Cdd:COG2433 426 EAEVEELEAELEEKDERIERLERELSEARSEERREIRKDReiSRLDREIERLERELEEERERIEELKRKLERLK 499
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
341-532 |
1.09e-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: 41.67 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 341 SSLREELVHMQEDLRRLESEKEDLERDLNFKADQAQQYDRLLETVREQNRQLQMSLKESNNAQRTLESQL---------- 410
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaellralyrl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 411 -------LTFQSKDPTKDFRIKELEGS-KRALEQENELLRKKLAgqcsssTIQIKTQELSREYEKmLNDLREEKDKELKS 482
Cdd:COG4942 117 grqpplaLLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLA------ELAALRAELEAERAE-LEALLAELEEERAA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207161729 483 LRSQLIKIQSESTIIQtTDTSSLELRISELLSKLEQRESVIRHQEEEIRR 532
Cdd:COG4942 190 LEALKAERQKLLARLE-KELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
323-531 |
1.89e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.35 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 323 LQTRMTADKtmHLVMTTFSSLRE--ELVHMQEDLRRLESEKEDLERDLNFKADQAQQYDRLLETVREQNRQLQMSLKESN 400
Cdd:pfam10174 142 MELRIETQK--QTLGARDESIKKllEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRN 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 401 NAQRTlESQLLTFQSKDPTKDFRIKELEGSKRALEQENELLRKKLAGQCSSSTIQIKTQELSREYEKMLNDLREEKDKEL 480
Cdd:pfam10174 220 QLQPD-PAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQEL 298
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1207161729 481 KSLRSQLIKIQS--ESTIIQTTDTSSLELRISELLSKLEQRESVIRHQEEEIR 531
Cdd:pfam10174 299 SKKESELLALQTklETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALR 351
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
352-538 |
2.23e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 352 EDLRRLESEKEDLERDLNFKADQAQQYDRLLETVREQNRQLQMSLKESNNAQRTLESQLLTFQSKDPTKDFRIKELEGS- 430
Cdd:pfam15921 643 ERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSd 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 431 ----KRALEQENELLRKKLAGQCSSSTIQIkTQELSREYEKMLNDLREEKDK---ELKSLRSQLIKIQSESTIIQTTD-- 501
Cdd:pfam15921 723 ghamKVAMGMQKQITAKRGQIDALQSKIQF-LEEAMTNANKEKHFLKEEKNKlsqELSTVATEKNKMAGELEVLRSQErr 801
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1207161729 502 ----TSSLELRISELLSKLEQRESVIRHQEEEIRRLKLQKT 538
Cdd:pfam15921 802 lkekVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHT 842
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
338-493 |
2.79e-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: 40.81 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 338 TTFSSLREELVHMQEDLRRLESEKEDLERDLNFKADQAQQYDRLLETVREQNRQLQMSLKESNNAQRTLESQL------- 410
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELeallner 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 411 -------LTFQSKDPTKDFRIKELEGSKRALEQENELLRKKLAG---QCSSSTIQIKT--QELSREYEKMLND---LREE 475
Cdd:TIGR02168 883 asleealALLRSELEELSEELRELESKRSELRRELEELREKLAQlelRLEGLEVRIDNlqERLSEEYSLTLEEaeaLENK 962
|
170
....*....|....*...
gi 1207161729 476 KDKELKSLRSQLIKIQSE 493
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENK 980
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
341-521 |
2.85e-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: 40.49 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 341 SSLREELVHMQEDLRR----LESEKEDLERDLNFKADQAQQYDRLLETVREQNRQLQMSLKESNNAQRTLESQLLTFQSK 416
Cdd:pfam05557 12 SQLQNEKKQMELEHKRarieLEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 417 DPTKDFRIKELEGSKRALEQENELLRKKLAGQcsssTIQIKTQELSREYEKMLNDLREEKDKELKSLRSQLIKIQSESti 496
Cdd:pfam05557 92 LNEKESQLADAREVISCLKNELSELRRQIQRA----ELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSL-- 165
|
170 180
....*....|....*....|....*
gi 1207161729 497 iqttdtSSLELRISELLSKLEQRES 521
Cdd:pfam05557 166 ------AEAEQRIKELEFEIQSQEQ 184
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
301-531 |
4.69e-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: 40.04 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 301 EEFESLIPKGVSELTKQQIRYLLQTRMTADKTMHLVMttfssLREELVHMQEDLRRLESEKEDLERDLNFKADQAQQYDR 380
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQI-----LRERLANLERQLEELEAQLEELESKLDELAEELAELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 381 LLETVREQNRQLQMSLKESNNAQRTLESQLLTFQSKDPTKDFRIKELEGSKRALEQENELLRKKLAGqcSSSTIQIKTQE 460
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER--LEDRRERLQQE 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207161729 461 LSREYEKMLNDLREEKDKELKSLRSQLIKIQSESTIIQTTdtsslELRISELLSKLEQRESVIRHQEEEIR 531
Cdd:TIGR02168 423 IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA-----LEELREELEEAEQALDAAERELAQLQ 488
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
357-494 |
4.99e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.23 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 357 LESEKEDLERDLNFKADQAQQYDRLLETVREQNRQLQMSLKESNNAQRTLESQLLTFQSKDPTKDFRIKElegSKRALEQ 436
Cdd:smart00787 142 LEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKE---KLKKLLQ 218
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207161729 437 ENELLRKKLAG-----QCSSSTIQIKTQELS------REYEKMLNDLREEKDKELKSLRSQLIKIQSES 494
Cdd:smart00787 219 EIMIKVKKLEEleeelQELESKIEDLTNKKSelnteiAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
355-535 |
5.90e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 355 RRLESEKEDLERDLNFKADQAQQYDRLLETVREQNRQLQMSLKESN-NAQRTLESQLLTFQSKDPTKDFRIK-ELEGSKR 432
Cdd:COG4717 319 EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQlEELEQEIAALLAEAGVEDEEELRAAlEQAEEYQ 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 433 ALEQENELLRKKLAGQCSSSTIQIKTQELSREYEKM--LNDLREEKDKELKSLRSQLIKIQSEstiIQTTDTSSlelRIS 510
Cdd:COG4717 399 ELKEELEELEEQLEELLGELEELLEALDEEELEEELeeLEEELEELEEELEELREELAELEAE---LEQLEEDG---ELA 472
|
170 180
....*....|....*....|....*
gi 1207161729 511 ELLSKLEQRESVIRHQEEEIRRLKL 535
Cdd:COG4717 473 ELLQELEELKAELRELAEEWAALKL 497
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
338-536 |
5.97e-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: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 338 TTFSSLREELVHMQEDLRRLESEKEDLERDLNFKADQAQQYDRLLETVREQNRQLQMSLKESNNAQRTLESQLLTFQSKD 417
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 418 PTKDFRIKELEGSKRALEQE-----------NELLRKKLAGQCSSSTIQIKTQELSREYEKMLNDLREEKDK---ELKSL 483
Cdd:TIGR04523 113 KNDKEQKNKLEVELNKLEKQkkenkknidkfLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNiqkNIDKI 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207161729 484 RSQLIKIQSESTIIQT--TDTSSLELRISELLSKLEQRESVIRHQEEEIRRLKLQ 536
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTE 247
|
|
| atpG |
CHL00118 |
ATP synthase CF0 B' subunit; Validated |
431-517 |
6.67e-03 |
|
ATP synthase CF0 B' subunit; Validated
Pssm-ID: 214369 [Multi-domain] Cd Length: 156 Bit Score: 37.66 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 431 KRALEQENELLRKKLAgqcSSSTIQIKTQELSREYEKMLNDLREEKDKELKSLRSQ--------LIKIQSESTIIQTTDT 502
Cdd:CHL00118 48 LKVLDERKEYIRKNLT---KASEILAKANELTKQYEQELSKARKEAQLEITQSQKEakeiveneLKQAQKYIDSLLNEAT 124
|
90
....*....|....*
gi 1207161729 503 SSLELRISELLSKLE 517
Cdd:CHL00118 125 KQLEAQKEKALKSLE 139
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
352-546 |
6.71e-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: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 352 EDLRRLESEKEDLER--DLNFKADQAQQYDRLLEtVREQNRQLQMSLKESNNAQRTLESqlLTFQSKDptkdfRIKELEG 429
Cdd:TIGR02169 198 QQLERLRREREKAERyqALLKEKREYEGYELLKE-KEALERQKEAIERQLASLEEELEK--LTEEISE-----LEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 430 SKRALEQENELLRKKlaGQCSSSTIQIKTQELSREYEKmLNDLREEKDKELKSLRSQLIKIQSESTIIQtTDTSSLELRI 509
Cdd:TIGR02169 270 IEQLLEELNKKIKDL--GEEEQLRVKEKIGELEAEIAS-LERSIAEKERELEDAEERLAKLEAEIDKLL-AEIEELEREI 345
|
170 180 190
....*....|....*....|....*....|....*....
gi 1207161729 510 SELLSKLEQRESVI--RHQEEEIRRLKLQKTDSSSSSTR 546
Cdd:TIGR02169 346 EEERKRRDKLTEEYaeLKEELEDLRAELEEVDKEFAETR 384
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
343-492 |
7.38e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 343 LREELVHMQEDLRRLE---------SEKEDLERDLNFKADQAQQYDRLLETVREQNRQLQMSLKESNNAQRTLESQLltf 413
Cdd:COG4717 107 LEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELL--- 183
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207161729 414 QSKDPTKDFRIKELEGSKRALEQENELLRKKLAgqcsssTIQIKTQELSREYEKMLNDLREEKDKELKSLRSQLIKIQS 492
Cdd:COG4717 184 EQLSLATEEELQDLAEELEELQQRLAELEEELE------EAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAA 256
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
343-486 |
7.98e-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: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 343 LREELVHMQEDLRRLESEKEDLERDLnfkADQAQQYDRL-----------LETVREQNRQLQMSLKESNNAQRTLESQLL 411
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARL---DALREELDELeaqirgnggdrLEQLEREIERLERELEERERRRARLEALLA 369
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207161729 412 TFQSKDPT--KDF--RIKELEGSKRALEQENELLRKKLAgqcssstiqiktqELSREYEKMLNDLReEKDKELKSLRSQ 486
Cdd:COG4913 370 ALGLPLPAsaEEFaaLRAEAAALLEALEEELEALEEALA-------------EAEAALRDLRRELR-ELEAEIASLERR 434
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
352-536 |
8.40e-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: 39.23 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 352 EDLRRLESEKEDLERDLNFKADQAQQYDRLLETVREQNRQLQMSLKESNNAQRTLESQLLTFQSKDPTKDFRIKELEGSK 431
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTR 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 432 RALEQENELLR------------------------KKLAGQCSSSTIQIKT----QELSREYEKMLNDLREEKDKELKSL 483
Cdd:TIGR04523 464 ESLETQLKVLSrsinkikqnleqkqkelkskekelKKLNEEKKELEEKVKDltkkISSLKEKIEKLESEKKEKESKISDL 543
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207161729 484 RSQLIKIQSEST------IIQTTDT--SSLELRISELLSKLEQRESVIRHQEEEIRRLKLQ 536
Cdd:TIGR04523 544 EDELNKDDFELKkenlekEIDEKNKeiEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE 604
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
345-534 |
8.52e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 345 EELVHMQEDLRRLESEKEDLERDLNFKADQAQQYDRLLETVREQNRqlqMSLKESNNAQRTLESQLLTFQSKDPTKDFRI 424
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELER---LKKRLTGLTPEKLEKELEELEKAKEEIEEEI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 425 KELEGSKRALEQENELLR------KKLAGQCSSSTIQIKTQ---ELSREYEKMLNDLREEK---DKELKSLRSQLIKIQS 492
Cdd:PRK03918 408 SKITARIGELKKEIKELKkaieelKKAKGKCPVCGRELTEEhrkELLEEYTAELKRIEKELkeiEEKERKLRKELRELEK 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207161729 493 ----ESTIIQTTDTS----SLELRISEL-LSKLEQRESVIRHQEEEIRRLK 534
Cdd:PRK03918 488 vlkkESELIKLKELAeqlkELEEKLKKYnLEELEKKAEEYEKLKEKLIKLK 538
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
351-538 |
9.02e-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: 9.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 351 QEDLRRLESEKEDLERDLnfkADQAQQYDRLLETVREQNRQlqmsLKESNNAQRTLESQLLTFQSkdptkdfRIKELEGS 430
Cdd:COG4942 26 EAELEQLQQEIAELEKEL---AALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEA-------ELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207161729 431 KRALEQENELLRKKLA---------GQCSSSTIQIKTQELSR-----EYEKMLNDLREEKDKELKSLRSQLIKIQSEsti 496
Cdd:COG4942 92 IAELRAELEAQKEELAellralyrlGRQPPLALLLSPEDFLDavrrlQYLKYLAPARREQAEELRADLAELAALRAE--- 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1207161729 497 iQTTDTSSLELRISELLSKLEQRESVIRHQEEEIRRLKLQKT 538
Cdd:COG4942 169 -LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209
|
|
| |
