|
Name |
Accession |
Description |
Interval |
E-value |
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
16-323 |
1.26e-106 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 327.54 E-value: 1.26e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 16 GCAPSPGAYDVKTLEVLKGPVSFQKSQRFKQQK--ESKQNLNVDKDTTLPASARKVKSSESK------------------ 75
Cdd:pfam15905 1 GCAPPPGSYDVKTSDALKGPVSFEKSQRFRKQKaaESQPNLNNSKDASTPATARKVKSLELKkksqknlkeskdqkelek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 76 -IRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSENGNQKNLRILSLE 154
Cdd:pfam15905 81 eIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSEDGTQKKMSSLSME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 155 LMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEISCASDQVEK 234
Cdd:pfam15905 161 LMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 235 YKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNENLNAEMQNLKQKFILEQ 314
Cdd:pfam15905 241 YKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEE 320
|
....*....
gi 217416398 315 QEREKLQQK 323
Cdd:pfam15905 321 QEHQKLQQK 329
|
|
| HMMR_C |
pfam15908 |
Hyaluronan mediated motility receptor C-terminal; HMMR_C is the C-terminal region of ... |
537-693 |
5.65e-63 |
|
Hyaluronan mediated motility receptor C-terminal; HMMR_C is the C-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464934 [Multi-domain] Cd Length: 157 Bit Score: 206.69 E-value: 5.65e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 537 RKQLEDEEGRKAEKENTTAELTEEINKWRLLYEELYNKTKPFQLQLDAFEVEKQALLNEHGAAQEQLNKIRDSYAKLLGH 616
Cdd:pfam15908 1 TKQLEMEEQRKARLENTVDELTEEIKKWRNLYEELYNKTKPFQEQLDAFEAEKNALLNENGAAQEELNKLSDAYAKLLGH 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 217416398 617 QNLKQKIKHVVKLKDENSQLKSEVSKLRCQLAKKKQSETKLQEELNKVLGIKHFDPSKAFHHESKENFALKTPLKEG 693
Cdd:pfam15908 81 QNQKQKIKHVVKLKEENTQLKQEVSKLRSQLAKEKQVQKKLQEQLNGAQGIRRFDPSKAFQHESKENFEPKTPLKEG 157
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
89-614 |
2.28e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 89 RIQDLETELEK----------------------MEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSENGNQK 146
Cdd:COG1196 190 RLEDILGELERqleplerqaekaeryrelkeelKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 147 N-LRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEI 225
Cdd:COG1196 270 EeLRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 226 SCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNENLNAEMQN 305
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 306 LKQKFILEQQEREKLQQKELQIDSLLQQEKELSSSLHQKLcsfqeemvKEKNLFEEELKQTLDELDKLQQKEEQAERLVK 385
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL--------EEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 386 QLEEEAKSRAEELKLLEEKLKGKE------AELEKSSAAHTQATLLLQEKYDSMVQSLEDVTAQFESYKALTASEIEDLK 459
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAvavligVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDK 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 460 LENSSLQEKAAKAGKN--------AEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITVSFLQKITDLQNQLKQ 531
Cdd:COG1196 582 IRARAALAAALARGAIgaavdlvaSDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 532 QEEDFRKQLEDEEGRKAEKEnttAELTEEINKWRLLYEELYNKTKPFQLQLDAFEVEKQALLNEHGAAQEQLNKIRDSYA 611
Cdd:COG1196 662 LTGGSRRELLAALLEAEAEL---EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
...
gi 217416398 612 KLL 614
Cdd:COG1196 739 EEL 741
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
209-395 |
1.40e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.78 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 209 IDEKSETEKLLEYIEEiscASDQVEKYKLDIAQL-EENLKEKNDEILSLKQSLEenivilsKQVEDLNVKCQLLEKeked 287
Cdd:PRK12704 24 VRKKIAEAKIKEAEEE---AKRILEEAKKEAEAIkKEALLEAKEEIHKLRNEFE-------KELRERRNELQKLEK---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 288 hvnRNREHNENLNAEMQNLKQKfileqqeREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTL 367
Cdd:PRK12704 90 ---RLLQKEENLDRKLELLEKR-------EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEIL 159
|
170 180
....*....|....*....|....*....
gi 217416398 368 deLDKLQQK-EEQAERLVKQLEEEAKSRA 395
Cdd:PRK12704 160 --LEKVEEEaRHEAAVLIKEIEEEAKEEA 186
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
67-376 |
1.65e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 67 RKVKSSESKIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSENGNQK 146
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 147 N--------LRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKL 218
Cdd:TIGR02168 764 EeleerleeAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 219 LEYIEEIScasDQVEKYKLDIAQLEENLKEkndeilslkqsLEENIVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNEN 298
Cdd:TIGR02168 844 EEQIEELS---EDIESLAAEIEELEELIEE-----------LESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 217416398 299 LNAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELSSSLhqklcsfQEEMVKEKNLFEEELKQTLDELDKLQQK 376
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT-------LEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
177-561 |
2.87e-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: 50.83 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 177 EMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEeiscasdQVEKYKLDIAQLEENLKEKNDEILSL 256
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE-------QLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 257 KQSLEENIVILSKQVEDLNVKCQLLEKEKEDhvnrNREHNENLNAEMQNLKQKFileQQEREKLQQKELQIDSLLQQEKE 336
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEE----AEEELAEAEAEIEELEAQI---EQLKEELKALREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 337 LSSSLHQKLcSFQEEMVKEKNLFEEELKQTLDELDKLqqkEEQAERLVKQLEEEAKSRAeelklleeKLKGKEAELEKSS 416
Cdd:TIGR02168 815 LNEEAANLR-ERLESLERRIAATERRLEDLEEQIEEL---SEDIESLAAEIEELEELIE--------ELESELEALLNER 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 417 AAHTQATLLLQEKYDSMVQSLEDVTAQF----ESYKALTAS------EIEDLKLENSSLQEKAAKAGK-NAEDVQHQILA 485
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRselrRELEELREKlaqlelRLEGLEVRIDNLQERLSEEYSlTLEEAEALENK 962
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217416398 486 TESSNQEyvrmlldLQTKSALKETEIKEITVSFLQKITDLQnQLKQQEEDFRKQLEDEEGRKAEKENTTAELTEEI 561
Cdd:TIGR02168 963 IEDDEEE-------ARRRLKRLENKIKELGPVNLAAIEEYE-ELKERYDFLTAQKEDLTEAKETLEEAIEEIDREA 1030
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
230-661 |
4.47e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 230 DQVEKYKLDIAQLEENLKEKNDEILSLKQsLEENIVILSKQVEDLNVKCQLLEKEKEDHvnrnrehneNLNAEMQNLKQK 309
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE-LEEELEELEAELEELREELEKLEKLLQLL---------PLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 310 FILEQQEREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLEE 389
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 390 EAKSRAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQEKYDSMVQSLEDVtaqFESYKALTASEIEDLKLENSSLQEKA 469
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSL---ILTIAGVLFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 470 AKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEI------TVSFLQKITDLQNQLKQQE-EDFRKQL-- 540
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELldrieeLQELLREAEELEEELQLEElEQEIAALla 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 541 ------EDEEGRKAEKENTTAELTEEINKWRLLYEELYNKTKPFQLQLDAFEVEKQA--LLNEHGAAQEQLNKIRDSYAK 612
Cdd:COG4717 378 eagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELeeLEEELEELEEELEELREELAE 457
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 217416398 613 LLGHQNLKQKIKHVVKLKDENSQLKSEVSKLRCQLAKKKQSETKLQEEL 661
Cdd:COG4717 458 LEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAR 506
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
310-478 |
4.55e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 310 FILEQQEREKLQQKELQIDSLLQQ-EKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLE 388
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEaKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 389 EEAKSRAEELKLLEEKLKGKEAELEKssaahtqatllLQEKYDSMVQSLEDvtaQFESYKALTASEIEDLKLEN--SSLQ 466
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEK-----------KEEELEELIEEQLQ---ELERISGLTAEEAKEILLEKveEEAR 168
|
170
....*....|..
gi 217416398 467 EKAAKAGKNAED 478
Cdd:PRK12704 169 HEAAVLIKEIEE 180
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
92-608 |
5.83e-06 |
|
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: 49.73 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 92 DLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSkfsengnqknlriLSLELMKLRNKRETKMRGMMA 171
Cdd:pfam15921 114 DLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKC-------------LKEDMLEDSNTQIEQLRKMML 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 172 KQEGMEMKLQVTQRSLEESQGK------------------------------IAQLEGKLVSIEKEKIDEKSETEKLLEY 221
Cdd:pfam15921 181 SHEGVLQEIRSILVDFEEASGKkiyehdsmstmhfrslgsaiskilreldteISYLKGRIFPVEDQLEALKSESQNKIEL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 222 IeeISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVK--CQLLEKEKEDHVNRN--REHNE 297
Cdd:pfam15921 261 L--LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMymRQLSDLESTVSQLRSelREAKR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 298 NLNAEMQNLKQKFILE-------QQEREKLQQKELQIDSLLQQekeLSSSLHQKLCSFQEEMVKEKNLFEEELKQTLD-- 368
Cdd:pfam15921 339 MYEDKIEELEKQLVLAnselteaRTERDQFSQESGNLDDQLQK---LLADLHKREKELSLEKEQNKRLWDRDTGNSITid 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 369 ----ELDKLQQKEEQAERLVKQLEEEAKsraeelklleeklkgkeAELEKSSAAhtqatllLQEKYDSMvQSLEDVTAQF 444
Cdd:pfam15921 416 hlrrELDDRNMEVQRLEALLKAMKSECQ-----------------GQMERQMAA-------IQGKNESL-EKVSSLTAQL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 445 ESYKALTASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYV----RMLLDLQTKSALK---------ETEI 511
Cdd:pfam15921 471 ESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITklrsRVDLKLQELQHLKnegdhlrnvQTEC 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 512 KEITVSFLQKITDLQnQLKQQEEDFrKQLEDEEGRKA-EKENTTAELTEEINKWRLLYEELY-------NKTKPFQLQLD 583
Cdd:pfam15921 551 EALKLQMAEKDKVIE-ILRQQIENM-TQLVGQHGRTAgAMQVEKAQLEKEINDRRLELQEFKilkdkkdAKIRELEARVS 628
|
570 580
....*....|....*....|....*
gi 217416398 584 AFEVEKQALLNehgAAQEQLNKIRD 608
Cdd:pfam15921 629 DLELEKVKLVN---AGSERLRAVKD 650
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
448-659 |
1.12e-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: 42.35 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 448 KALTASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITvsflQKITDLQN 527
Cdd:TIGR02168 227 LALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA----NEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 528 Q---LKQQEEDFRKQLEDEEGRKAEKENTTAELTEEINKWRLLYEELYNKTKPFQLQLDAFEVEKQALLNEHGAAQEQLN 604
Cdd:TIGR02168 303 QkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 217416398 605 KIRDSYAKLLghQNLKQKIKHVVKLKDENSQLKSEVSKLRCQLAK--KKQSETKLQE 659
Cdd:TIGR02168 383 TLRSKVAQLE--LQIASLNNEIERLEARLERLEDRRERLQQEIEEllKKLEEAELKE 437
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
451-664 |
3.41e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 451 TASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITvsflQKITDLQNQLK 530
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE----KEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 531 QQEEDFRKQLedeegRKAEKENTTAELTEEINK------------WRLLYEELYNKTKPFQLQLDAFEVEKQALLNEHGA 598
Cdd:COG4942 101 AQKEELAELL-----RALYRLGRQPPLALLLSPedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217416398 599 AQEQLNKIRDSYAKLLGHQNLKQKIkhvvklkdeNSQLKSEVSKLRCQLAKKKQSETKLQEELNKV 664
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKL---------LARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
16-323 |
1.26e-106 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 327.54 E-value: 1.26e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 16 GCAPSPGAYDVKTLEVLKGPVSFQKSQRFKQQK--ESKQNLNVDKDTTLPASARKVKSSESK------------------ 75
Cdd:pfam15905 1 GCAPPPGSYDVKTSDALKGPVSFEKSQRFRKQKaaESQPNLNNSKDASTPATARKVKSLELKkksqknlkeskdqkelek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 76 -IRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSENGNQKNLRILSLE 154
Cdd:pfam15905 81 eIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSEDGTQKKMSSLSME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 155 LMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEISCASDQVEK 234
Cdd:pfam15905 161 LMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 235 YKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNENLNAEMQNLKQKFILEQ 314
Cdd:pfam15905 241 YKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEE 320
|
....*....
gi 217416398 315 QEREKLQQK 323
Cdd:pfam15905 321 QEHQKLQQK 329
|
|
| HMMR_C |
pfam15908 |
Hyaluronan mediated motility receptor C-terminal; HMMR_C is the C-terminal region of ... |
537-693 |
5.65e-63 |
|
Hyaluronan mediated motility receptor C-terminal; HMMR_C is the C-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464934 [Multi-domain] Cd Length: 157 Bit Score: 206.69 E-value: 5.65e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 537 RKQLEDEEGRKAEKENTTAELTEEINKWRLLYEELYNKTKPFQLQLDAFEVEKQALLNEHGAAQEQLNKIRDSYAKLLGH 616
Cdd:pfam15908 1 TKQLEMEEQRKARLENTVDELTEEIKKWRNLYEELYNKTKPFQEQLDAFEAEKNALLNENGAAQEELNKLSDAYAKLLGH 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 217416398 617 QNLKQKIKHVVKLKDENSQLKSEVSKLRCQLAKKKQSETKLQEELNKVLGIKHFDPSKAFHHESKENFALKTPLKEG 693
Cdd:pfam15908 81 QNQKQKIKHVVKLKEENTQLKQEVSKLRSQLAKEKQVQKKLQEQLNGAQGIRRFDPSKAFQHESKENFEPKTPLKEG 157
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
89-614 |
2.28e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 89 RIQDLETELEK----------------------MEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSENGNQK 146
Cdd:COG1196 190 RLEDILGELERqleplerqaekaeryrelkeelKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 147 N-LRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEI 225
Cdd:COG1196 270 EeLRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 226 SCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNENLNAEMQN 305
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 306 LKQKFILEQQEREKLQQKELQIDSLLQQEKELSSSLHQKLcsfqeemvKEKNLFEEELKQTLDELDKLQQKEEQAERLVK 385
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL--------EEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 386 QLEEEAKSRAEELKLLEEKLKGKE------AELEKSSAAHTQATLLLQEKYDSMVQSLEDVTAQFESYKALTASEIEDLK 459
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAvavligVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDK 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 460 LENSSLQEKAAKAGKN--------AEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITVSFLQKITDLQNQLKQ 531
Cdd:COG1196 582 IRARAALAAALARGAIgaavdlvaSDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 532 QEEDFRKQLEDEEGRKAEKEnttAELTEEINKWRLLYEELYNKTKPFQLQLDAFEVEKQALLNEHGAAQEQLNKIRDSYA 611
Cdd:COG1196 662 LTGGSRRELLAALLEAEAEL---EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
...
gi 217416398 612 KLL 614
Cdd:COG1196 739 EEL 741
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
87-429 |
5.64e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 87 DRRIQDLETELEKMEA---RLNAALREktsLSANNATLEKQLIELTRTNELlkskfsengnQKNLRILSLELMKLRnkre 163
Cdd:COG1196 171 KERKEEAERKLEATEEnleRLEDILGE---LERQLEPLERQAEKAERYREL----------KEELKELEAELLLLK---- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 164 tkMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSE----TEKLLEYIEEISCASDQVEKYKLDI 239
Cdd:COG1196 234 --LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEleeaQAEEYELLAELARLEQDIARLEERR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 240 AQLEENLKEKNDEILSLKQ---SLEENIVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNENLNAEMQNLKQKFILEQQE 316
Cdd:COG1196 312 RELEERLEELEEELAELEEeleELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 317 REKLQQKELQIDSLLQQEKELSsslhQKLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRAE 396
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALL----ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
330 340 350
....*....|....*....|....*....|...
gi 217416398 397 ELKLLEEKLKGKEAELEKSSAAHTQATLLLQEK 429
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
179-395 |
2.46e-08 |
|
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: 56.70 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 179 KLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEiscASDQVEKYKLDIAQLEENLKEKNDEILSLKQ 258
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA---LARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 259 SLEENIVILSKQVEDLNVKCQ------LLEKEKEDHVNRN----REHNENLNAEMQNLKQKFILEQQEREKLQQKELQID 328
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRqpplalLLSPEDFLDAVRRlqylKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 217416398 329 SLLQQEKELSSSLhQKLCSFQEEMVKEknlFEEELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRA 395
Cdd:COG4942 178 ALLAELEEERAAL-EALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
209-395 |
1.40e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.78 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 209 IDEKSETEKLLEYIEEiscASDQVEKYKLDIAQL-EENLKEKNDEILSLKQSLEenivilsKQVEDLNVKCQLLEKeked 287
Cdd:PRK12704 24 VRKKIAEAKIKEAEEE---AKRILEEAKKEAEAIkKEALLEAKEEIHKLRNEFE-------KELRERRNELQKLEK---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 288 hvnRNREHNENLNAEMQNLKQKfileqqeREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTL 367
Cdd:PRK12704 90 ---RLLQKEENLDRKLELLEKR-------EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEIL 159
|
170 180
....*....|....*....|....*....
gi 217416398 368 deLDKLQQK-EEQAERLVKQLEEEAKSRA 395
Cdd:PRK12704 160 --LEKVEEEaRHEAAVLIKEIEEEAKEEA 186
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
67-376 |
1.65e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 67 RKVKSSESKIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSENGNQK 146
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 147 N--------LRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKL 218
Cdd:TIGR02168 764 EeleerleeAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 219 LEYIEEIScasDQVEKYKLDIAQLEENLKEkndeilslkqsLEENIVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNEN 298
Cdd:TIGR02168 844 EEQIEELS---EDIESLAAEIEELEELIEE-----------LESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 217416398 299 LNAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELSSSLhqklcsfQEEMVKEKNLFEEELKQTLDELDKLQQK 376
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT-------LEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
154-483 |
3.70e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 154 ELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSEtekLLEYIEEISCASDQVE 233
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE---LKELEARIEELEEDLH 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 234 KYKLDIAQLEENL-KEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLEKEKedhvnrnrehnENLNAEMQNLKQKFIL 312
Cdd:TIGR02169 776 KLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK-----------EYLEKEIQELQEQRID 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 313 EQQEREKLQQkelQIDSLLQQEKELSSSLhqklcsfqEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLE---E 389
Cdd:TIGR02169 845 LKEQIKSIEK---EIENLNGKKEELEEEL--------EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEaqiE 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 390 EAKSRAEELKLLEEKLKGKEAELEKSSAAHTQ--ATLLLQEKYDSMVQSLEDVTAQFESYKALTASEIEDLKLENSSLQE 467
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEELSEIEDPKGEDEEipEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKE 993
|
330
....*....|....*.
gi 217416398 468 KAAKAGKNAEDVQHQI 483
Cdd:TIGR02169 994 KRAKLEEERKAILERI 1009
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
80-395 |
5.87e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 80 LQERGAQDRRIQDLETELEKMEA-----RLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSEngNQKNLRILSLE 154
Cdd:TIGR02169 203 LRREREKAERYQALLKEKREYEGyellkEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEE--IEQLLEELNKK 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 155 LMKLRNKR----ETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSI--EKEKIDEKSETEKLL--EYIEEIS 226
Cdd:TIGR02169 281 IKDLGEEEqlrvKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLlaEIEELEREIEEERKRrdKLTEEYA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 227 CASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEEniviLSKQVEDLNVKCQLLEKEKEdhvnRNREHNENLNAEMQNL 306
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK----LKREINELKRELDRLQEELQ----RLSEELADLNAAIAGI 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 307 KQKfILEQQEREKLQQKELQidsllQQEKELsSSLHQKLCSFQEEMVKEKnlfeEELKQTLDELDKLQQKEEQAERLVKQ 386
Cdd:TIGR02169 433 EAK-INELEEEKEDKALEIK-----KQEWKL-EQLAADLSKYEQELYDLK----EEYDRVEKELSKLQRELAEAEAQARA 501
|
....*....
gi 217416398 387 LEEEAKSRA 395
Cdd:TIGR02169 502 SEERVRGGR 510
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
82-395 |
8.84e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.43 E-value: 8.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 82 ERGAQDRRIQDLETELEKMEARLNAALREKtslsANNATLEKQlieltrtnellKSKFSENGNQKNLRILSLELMKLRNK 161
Cdd:pfam17380 294 EKMEQERLRQEKEEKAREVERRRKLEEAEK----ARQAEMDRQ-----------AAIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 162 REtKMRGMMAKQEGMEM-KLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEISCA-SDQVEKYKLDI 239
Cdd:pfam17380 359 KR-ELERIRQEEIAMEIsRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIrAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 240 AQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNENLNAEMQNLKQKFILEQQEREK 319
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKL 517
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217416398 320 LQQKELQIDSLLQQEKELSSSLHQKLcsfQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAErLVKQLEEEAKSRA 395
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRREAEEERR---KQQEMEERRRIQEQMRKATEERSRLEAMERERE-MMRQIVESEKARA 589
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
73-563 |
1.21e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 73 ESKIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSENgNQKNLRILS 152
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA-EEALLEAEA 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 153 LELMKLRNKRETKMRGMMAKQEgmemkLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEISCASDQV 232
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRA-----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 233 EKYKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNENLNAEMQNLKQKFIL 312
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 313 EQQEREKLQQKELQ--IDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLEEE 390
Cdd:COG1196 528 VLIGVEAAYEAALEaaLAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASD 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 391 AKSRAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQEkYDSMVQSLEDVTAQFESYKALTASEIEDLKLENSSLQEKAA 470
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR-LREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 471 KAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEikeitvsfLQKITDLQNQLKQQEEDFRKQLEDEEGRKAEK 550
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL--------EEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
490
....*....|...
gi 217416398 551 ENTTAELTEEINK 563
Cdd:COG1196 759 PPDLEELERELER 771
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
42-579 |
1.87e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 42 QRFKQQKESKQNLNVDKDTTLPASARKVKSSESKIRVLLQERGAQDRRIQDLET---ELEKMEARLNAALREKTSLSANN 118
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElkeEIEELEKELESLEGSKRKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 119 ATLEKQLIELTRTNELLKSKFSENGNQKNLRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLE 198
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 199 gKLVSIEKEKIDEKSETEKLLEYIEEISCASDQVEKYKLDIAQLE--------ENLKEKNDEILSLKQSLEENIVILSKQ 270
Cdd:PRK03918 342 -ELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTpeklekelEELEKAKEEIEEEISKITARIGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 271 VEDLNVKCQLLEKEKEDHVNRNR----EHNENL----NAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELsSSLH 342
Cdd:PRK03918 421 IKELKKAIEELKKAKGKCPVCGRelteEHRKELleeyTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL-IKLK 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 343 QKLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEAELEKSSAAHTQA 422
Cdd:PRK03918 500 ELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 423 TLLLQEKYDSMVQSLEDVTAQFESYKAL--TASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDL 500
Cdd:PRK03918 580 EELGFESVEELEERLKELEPFYNEYLELkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE 659
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 217416398 501 QTKSALKETEIKEITVSFLQKITDlqnQLKQQEEDFRKQLEDEEGRKAEKENTTAELtEEINKWRLLYEELYNKTKPFQ 579
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAELE---ELEKRREEIKKTLEKLKEELEEREKAKKEL-EKLEKALERVEELREKVKKYK 734
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
132-393 |
2.70e-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: 50.83 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 132 NELLKSKFSENGNQKNLRILSLELmklrNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDE 211
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAEL----QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 212 KSETEKLLEYIEEiscASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEEniviLSKQVEDLNVKCQLLEKEKEDHVNR 291
Cdd:TIGR02168 315 ERQLEELEAQLEE---LESKLDELAEELAELEEKLEELKEELESLEAELEE----LEAELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 292 NREHNEN---LNAEMQNLK-QKFILEQQEREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTL 367
Cdd:TIGR02168 388 VAQLELQiasLNNEIERLEaRLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR 467
|
250 260
....*....|....*....|....*.
gi 217416398 368 DELDKLQQKEEQAERLVKQLEEEAKS 393
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDS 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
177-561 |
2.87e-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: 50.83 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 177 EMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEeiscasdQVEKYKLDIAQLEENLKEKNDEILSL 256
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE-------QLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 257 KQSLEENIVILSKQVEDLNVKCQLLEKEKEDhvnrNREHNENLNAEMQNLKQKFileQQEREKLQQKELQIDSLLQQEKE 336
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEE----AEEELAEAEAEIEELEAQI---EQLKEELKALREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 337 LSSSLHQKLcSFQEEMVKEKNLFEEELKQTLDELDKLqqkEEQAERLVKQLEEEAKSRAeelklleeKLKGKEAELEKSS 416
Cdd:TIGR02168 815 LNEEAANLR-ERLESLERRIAATERRLEDLEEQIEEL---SEDIESLAAEIEELEELIE--------ELESELEALLNER 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 417 AAHTQATLLLQEKYDSMVQSLEDVTAQF----ESYKALTAS------EIEDLKLENSSLQEKAAKAGK-NAEDVQHQILA 485
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRselrRELEELREKlaqlelRLEGLEVRIDNLQERLSEEYSlTLEEAEALENK 962
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217416398 486 TESSNQEyvrmlldLQTKSALKETEIKEITVSFLQKITDLQnQLKQQEEDFRKQLEDEEGRKAEKENTTAELTEEI 561
Cdd:TIGR02168 963 IEDDEEE-------ARRRLKRLENKIKELGPVNLAAIEEYE-ELKERYDFLTAQKEDLTEAKETLEEAIEEIDREA 1030
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
79-317 |
3.35e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 50.67 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 79 LLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSENGnqKNLRILSLELMKL 158
Cdd:PLN02939 161 ILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLS--KELDVLKEENMLL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 159 RNK-----------RETKMRGMMAKQE--GMEMKLQVTQRSLEESQGKIAqlegKLVSIEKEKIDEKSETEKLLeyieeI 225
Cdd:PLN02939 239 KDDiqflkaelievAETEERVFKLEKErsLLDASLRELESKFIVAQEDVS----KLSPLQYDCWWEKVENLQDL-----L 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 226 SCASDQVEKYKLDIAQlEENLKEKNDEilsLKQSLEENIV--ILSKQVEDLNVKCQLLEK--EKEDH-VNRNREHNENLN 300
Cdd:PLN02939 310 DRATNQVEKAALVLDQ-NQDLRDKVDK---LEASLKEANVskFSSYKVELLQQKLKLLEErlQASDHeIHSYIQLYQESI 385
|
250
....*....|....*..
gi 217416398 301 AEMQNLKQKFILEQQER 317
Cdd:PLN02939 386 KEFQDTLSKLKEESKKR 402
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
350-664 |
4.38e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 350 EEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLEE-EAKSRAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQE 428
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREyEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 429 KYDSMVQSLEDVTAQFESYKALTASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKE 508
Cdd:TIGR02169 263 LEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 509 TEIKEITVSFLQKITDLQNqLKQQEEDFRKQLEDEEGRKAEKENTTAELTEEInkwrllyEELYNKTKPFQLQLDAFEVE 588
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAE-LKEELEDLRAELEEVDKEFAETRDELKDYREKL-------EKLKREINELKRELDRLQEE 414
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217416398 589 KQALLNEHGAAQEQLNKIRDSYAKLlgHQNLKQKIKHVVKLKDENSQLKSEVSKLRCQLAKKKQSETKLQEELNKV 664
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAKINEL--EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
230-661 |
4.47e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 230 DQVEKYKLDIAQLEENLKEKNDEILSLKQsLEENIVILSKQVEDLNVKCQLLEKEKEDHvnrnrehneNLNAEMQNLKQK 309
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE-LEEELEELEAELEELREELEKLEKLLQLL---------PLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 310 FILEQQEREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLEE 389
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 390 EAKSRAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQEKYDSMVQSLEDVtaqFESYKALTASEIEDLKLENSSLQEKA 469
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSL---ILTIAGVLFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 470 AKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEI------TVSFLQKITDLQNQLKQQE-EDFRKQL-- 540
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELldrieeLQELLREAEELEEELQLEElEQEIAALla 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 541 ------EDEEGRKAEKENTTAELTEEINKWRLLYEELYNKTKPFQLQLDAFEVEKQA--LLNEHGAAQEQLNKIRDSYAK 612
Cdd:COG4717 378 eagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELeeLEEELEELEEELEELREELAE 457
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 217416398 613 LLGHQNLKQKIKHVVKLKDENSQLKSEVSKLRCQLAKKKQSETKLQEEL 661
Cdd:COG4717 458 LEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAR 506
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
310-478 |
4.55e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 310 FILEQQEREKLQQKELQIDSLLQQ-EKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLE 388
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEaKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 389 EEAKSRAEELKLLEEKLKGKEAELEKssaahtqatllLQEKYDSMVQSLEDvtaQFESYKALTASEIEDLKLEN--SSLQ 466
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEK-----------KEEELEELIEEQLQ---ELERISGLTAEEAKEILLEKveEEAR 168
|
170
....*....|..
gi 217416398 467 EKAAKAGKNAED 478
Cdd:PRK12704 169 HEAAVLIKEIEE 180
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
42-613 |
5.21e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 42 QRFKQQKESKQNLNVDKDTTLPASARKVKSSESKIRVLLQERGAQDRRIQDL---E----TELEKMEARLNAALREKTSL 114
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeEyellAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 115 SANNATLEKQLIELTRTNELLKSKFSEngnqknlriLSLELMKLRNKRETKmrgmmakqegmEMKLQVTQRSLEESQGKI 194
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEE---------LEEELEEAEEELEEA-----------EAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 195 AQLEGKLVSIEKEKIDEKSETEKLLEYIEEiscasdqvekykldIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDL 274
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEE--------------LEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 275 nvkcQLLEKEKEDHVNRNREHNENLNAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVK 354
Cdd:COG1196 441 ----EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 355 EKNlfeEELKQTLDELDKLQQKEEQA-----ERLVKQLEEEAKSRAEELKLLEEKLKGKEAE---LEKSSAAHTQATLLL 426
Cdd:COG1196 517 AGL---RGLAGAVAVLIGVEAAYEAAleaalAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflpLDKIRARAALAAALA 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 427 QEKYDSMVQSLEDVTAQFESYKALTASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEyVRMLLDLQTKSAL 506
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG-GSLTGGSRRELLA 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 507 KETEIKEITVSFLQKITDLQNQLKQQEEDFRKQLEDEEGRKAEKENTTAELTEEINKWRLLYEELYNKTKPFQLQLDAFE 586
Cdd:COG1196 673 ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA 752
|
570 580
....*....|....*....|....*..
gi 217416398 587 VEKQALLNEHGAAQEQLNKIRDSYAKL 613
Cdd:COG1196 753 LEELPEPPDLEELERELERLEREIEAL 779
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
92-608 |
5.83e-06 |
|
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: 49.73 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 92 DLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSkfsengnqknlriLSLELMKLRNKRETKMRGMMA 171
Cdd:pfam15921 114 DLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKC-------------LKEDMLEDSNTQIEQLRKMML 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 172 KQEGMEMKLQVTQRSLEESQGK------------------------------IAQLEGKLVSIEKEKIDEKSETEKLLEY 221
Cdd:pfam15921 181 SHEGVLQEIRSILVDFEEASGKkiyehdsmstmhfrslgsaiskilreldteISYLKGRIFPVEDQLEALKSESQNKIEL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 222 IeeISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVK--CQLLEKEKEDHVNRN--REHNE 297
Cdd:pfam15921 261 L--LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMymRQLSDLESTVSQLRSelREAKR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 298 NLNAEMQNLKQKFILE-------QQEREKLQQKELQIDSLLQQekeLSSSLHQKLCSFQEEMVKEKNLFEEELKQTLD-- 368
Cdd:pfam15921 339 MYEDKIEELEKQLVLAnselteaRTERDQFSQESGNLDDQLQK---LLADLHKREKELSLEKEQNKRLWDRDTGNSITid 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 369 ----ELDKLQQKEEQAERLVKQLEEEAKsraeelklleeklkgkeAELEKSSAAhtqatllLQEKYDSMvQSLEDVTAQF 444
Cdd:pfam15921 416 hlrrELDDRNMEVQRLEALLKAMKSECQ-----------------GQMERQMAA-------IQGKNESL-EKVSSLTAQL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 445 ESYKALTASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYV----RMLLDLQTKSALK---------ETEI 511
Cdd:pfam15921 471 ESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITklrsRVDLKLQELQHLKnegdhlrnvQTEC 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 512 KEITVSFLQKITDLQnQLKQQEEDFrKQLEDEEGRKA-EKENTTAELTEEINKWRLLYEELY-------NKTKPFQLQLD 583
Cdd:pfam15921 551 EALKLQMAEKDKVIE-ILRQQIENM-TQLVGQHGRTAgAMQVEKAQLEKEINDRRLELQEFKilkdkkdAKIRELEARVS 628
|
570 580
....*....|....*....|....*
gi 217416398 584 AFEVEKQALLNehgAAQEQLNKIRD 608
Cdd:pfam15921 629 DLELEKVKLVN---AGSERLRAVKD 650
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
360-666 |
1.37e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 360 EEELKQTLDELDKLQQKEEQAERLVKQLEEEAKS-------RAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQEKYDS 432
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLEPLERQAEKaeryrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 433 MVQSLEDVTAQFESYKAltasEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIK 512
Cdd:COG1196 258 LEAELAELEAELEELRL----ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 513 EITVSfLQKITDLQNQLKQQEEDFRKQLEDEEGRKAEKENTTAELTEEINKWRLLYEELYNKTKPFQLQLDAFEVEKQAL 592
Cdd:COG1196 334 ELEEE-LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 217416398 593 LNEHGAAQEQLNKIRDSYAKLLghQNLKQKIKHVVKLKDENSQLKSEVSKLRCQLAKKKQSETKLQEELNKVLG 666
Cdd:COG1196 413 LERLERLEEELEELEEALAELE--EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
148-472 |
1.42e-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: 48.53 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 148 LRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEIsc 227
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI-- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 228 asdqvekyKLDIAQLEENLKEK-NDEILSLKQSLEEniviLSKQVEdlnvKCQLLEKEKEDHVNRNREHNENLNAEMQNL 306
Cdd:TIGR02169 271 --------EQLLEELNKKIKDLgEEEQLRVKEKIGE----LEAEIA----SLERSIAEKERELEDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 307 KQKfiLEQQEREkLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEeLKQTLDELDKLQQKEEQAERLVKQ 386
Cdd:TIGR02169 335 LAE--IEELERE-IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE-LKDYREKLEKLKREINELKRELDR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 387 LEEEAKSRAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQEKYDSMVQSLEDVTAQFESYKALTAsEIEDLKLENSSLQ 466
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE-EYDRVEKELSKLQ 489
|
....*.
gi 217416398 467 EKAAKA 472
Cdd:TIGR02169 490 RELAEA 495
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
34-262 |
1.76e-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: 47.45 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 34 GPVSFQKSQRFKQQKESKQNLNVDKDttlpASARKVKSSESKIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTS 113
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIA----ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 114 LSANNATLEKQLIELTRTNELLKSKFSENGNQKNLR-ILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQG 192
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 217416398 193 KIAQLEGKLVSIEKEKIDEKSETEKLLEYIEE-ISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEE 262
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKlLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
291-542 |
2.03e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 291 RNREHNENLNAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELSS---------SLHQKLCSFQEEMvkeknlfeE 361
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvaSAEREIAELEAEL--------E 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 362 ELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQekydsmVQSLEDVT 441
Cdd:COG4913 679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR------LELRALLE 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 442 AQFESY--KALTASEIEDLKLENSSLQEKAAKAGKNAEDVQHQIL-----------ATESSNQEYVRMLLDLQT------ 502
Cdd:COG4913 753 ERFAAAlgDAVERELRENLEERIDALRARLNRAEEELERAMRAFNrewpaetadldADLESLPEYLALLDRLEEdglpey 832
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 217416398 503 ----KSALKETEIkeitvsflQKITDLQNQLKQQEEDFRKQLED 542
Cdd:COG4913 833 eerfKELLNENSI--------EFVADLLSKLRRAIREIKERIDP 868
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
181-552 |
2.14e-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: 48.13 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 181 QVTQRSLEESQGKIAQLEGKLVSIEK--EKIDEKSE-TEKLLEYIEEISCAsdQVEKYKLDIAQLEENLKEKNDEILSLK 257
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERqlKSLERQAEkAERYKELKAELREL--ELALLVLRLEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 258 Q---SLEENIVILSKQVEDLNVKCQLLEKEKEDhvnrnrehnenLNAEMQNLKQKfileqqereklqqkelqIDSLLQQE 334
Cdd:TIGR02168 253 EeleELTAELQELEEKLEELRLEVSELEEEIEE-----------LQKELYALANE-----------------ISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 335 KELSSSLHQklcsfqeemvkeknlFEEELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEA---E 411
Cdd:TIGR02168 305 QILRERLAN---------------LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAeleE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 412 LEKSSAAHTQATLLLQEKYDSMVQSLEDVTAQFESYKAltasEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQ 491
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA----RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 217416398 492 EyvRMLLDLQTKSALKETEIKEITVSFLQKITDLQnQLKQQEEDFRKQLEDEEGRKAEKEN 552
Cdd:TIGR02168 446 E--EELEELQEELERLEEALEELREELEEAEQALD-AAERELAQLQARLDSLERLQENLEG 503
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
132-667 |
4.80e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.64 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 132 NELLKSKFSENGNQKNLRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKlvsiekekidE 211
Cdd:pfam05483 208 NARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEK----------T 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 212 KSETEKLLEYIEEISCASDQVEKYKLDIAQleenlkekndeILSLKQSLEENIVILSKQVedlnvkCQLLEKEKEDHVNR 291
Cdd:pfam05483 278 KLQDENLKELIEKKDHLTKELEDIKMSLQR-----------SMSTQKALEEDLQIATKTI------CQLTEEKEAQMEEL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 292 NREHNENLNAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELssslhQKLCSFQEEMVKEKNLFE---EELKQTLD 368
Cdd:pfam05483 341 NKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMEL-----QKKSSELEEMTKFKNNKEvelEELKKILA 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 369 ELDKLQQKEEQAERLVkqleEEAKSRAEELKLLEEKLKGKEAELEKSSAAHTQAtlllQEKYDSMVQSLEDVTAQFESYK 448
Cdd:pfam05483 416 EDEKLLDEKKQFEKIA----EELKGKEQELIFLLQAREKEIHDLEIQLTAIKTS----EEHYLKEVEDLKTELEKEKLKN 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 449 ALTASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITVSFLQKITDLQNQ 528
Cdd:pfam05483 488 IELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCK 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 529 LKQQEEDFRK---QLEDEEGRKAEKENTTAELTEEINKWRLLYEELYNKTKPFQ-------LQLDAFEVEKQALLNEHGA 598
Cdd:pfam05483 568 LDKSEENARSieyEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKkkgsaenKQLNAYEIKVNKLELELAS 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 599 AQEQLNKIRDSYA-----KLLGHQNLKQKIKHVVKLKDENSQLKSEVSKlRCQ---------LAKKKQSETKLQEELNKV 664
Cdd:pfam05483 648 AKQKFEEIIDNYQkeiedKKISEEKLLEEVEKAKAIADEAVKLQKEIDK-RCQhkiaemvalMEKHKHQYDKIIEERDSE 726
|
...
gi 217416398 665 LGI 667
Cdd:pfam05483 727 LGL 729
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
72-391 |
5.28e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 72 SESKIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSE--------NG 143
Cdd:PRK02224 263 LRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEcrvaaqahNE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 144 NQKNLRILSLELmklrnkrETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIE 223
Cdd:PRK02224 343 EAESLREDADDL-------EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 224 EISCASDQVEKyklDIAQLEENLKEKNDEILSLKQSLEENivilskqvedlnvKCQLLEKEKED--HVNR---NREHNEN 298
Cdd:PRK02224 416 ELREERDELRE---REAELEATLRTARERVEEAEALLEAG-------------KCPECGQPVEGspHVETieeDRERVEE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 299 LNAEMQNLKqkfileqQEREKLQQKELQIDSLLQQEKELSSSLHQ-----KLCSFQEEMVKEKNLFEEELKQTLDELD-K 372
Cdd:PRK02224 480 LEAELEDLE-------EEVEEVEERLERAEDLVEAEDRIERLEERredleELIAERRETIEEKRERAEELRERAAELEaE 552
|
330
....*....|....*....
gi 217416398 373 LQQKEEQAERLVKQLEEEA 391
Cdd:PRK02224 553 AEEKREAAAEAEEEAEEAR 571
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
67-664 |
6.37e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 6.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 67 RKVKSSESKIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLkskfsengNQK 146
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI--------EEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 147 NLRILSLElmklrnkretkmrgmmAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKsETEKLLEYIEEIS 226
Cdd:PRK03918 244 EKELESLE----------------GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE-EYIKLSEFYEEYL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 227 CASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEE---NIVILSKQVEDLNVKCQLLEKEKEDHVNRNR-------EHN 296
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKELEEKEERLEElkkKLKELEKRLEELEERHELYEEAKAKKEELERlkkrltgLTP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 297 ENLNAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELSSSLHQK-----LCSFQEEMVKEKNLFEE---ELKQTLD 368
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEEytaELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 369 ELDKLQQKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEAE-------LEKSSAAHTQATLLLQE--KYDSMVQSLED 439
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEeklkkynLEELEKKAEEYEKLKEKliKLKGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 440 ---VTAQFESYKALTASEIEDLKLENSSLQEKAAKAG-KNAEDVQHQILATESSNQEYVRM------LLDLQTKSALKET 509
Cdd:PRK03918 547 eleKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELkdaekeLEREEKELKKLEE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 510 EIKEITVSFLQKITDLQnQLKQQEEDFRKQLEDEEGRKAEKENTtaELTEEINKWRLLYEELYNKTKPFQLQLDAFEVEK 589
Cdd:PRK03918 627 ELDKAFEELAETEKRLE-ELRKELEELEKKYSEEEYEELREEYL--ELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 217416398 590 QallnEHGAAQEQLNKIRDSYAKLlghQNLKQKIKHVVKLKDENSQLKSE--VSKLRCQLAKKKQSETKLQEELNKV 664
Cdd:PRK03918 704 E----EREKAKKELEKLEKALERV---EELREKVKKYKALLKERALSKVGeiASEIFEELTEGKYSGVRVKAEENKV 773
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
68-285 |
9.13e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.69 E-value: 9.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 68 KVKSSESKIRVLLQERGAQ-----DRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELtrtnELLKSkfsen 142
Cdd:PRK05771 61 KLRSYLPKLNPLREEKKKVsvkslEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERL----EPWGN----- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 143 gnqknlriLSLELMKLRNKRETKMR-GMMAKQEGMEMKLQVTQRSLEEsqgkIAQLEGK---LVSIEKEKIDEKSETEKL 218
Cdd:PRK05771 132 --------FDLDLSLLLGFKYVSVFvGTVPEDKLEELKLESDVENVEY----ISTDKGYvyvVVVVLKELSDEVEEELKK 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 217416398 219 LEY----IEEISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEENIV----ILSKQVEDLNVKCQLLEKEK 285
Cdd:PRK05771 200 LGFerleLEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLalyeYLEIELERAEALSKFLKTDK 274
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
206-556 |
9.24e-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: 45.83 E-value: 9.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 206 KEKIDEKSETEKLLE-YIEEISCASDQVEKYKLDIAQLEENLKEKND----EILSLKQSLEENIVILSKQVEDLNVKCQL 280
Cdd:TIGR02169 176 LEELEEVEENIERLDlIIDEKRQQLERLRREREKAERYQALLKEKREyegyELLKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 281 LEKEKEDHVNRNREHNENLNAEMQNLKQKFILEQQE-REKLQQKELQIDSLLQQEKELSSSlhqklcsfQEEMVKEKNLF 359
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEIASLERSIAEKERE--------LEDAEERLAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 360 EEELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRAEELKLLEEKLkgkeAELEKSSAAhtqatllLQEKYDSMVQSLED 439
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL----EEVDKEFAE-------TRDELKDYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 440 VTaqfesykaltaSEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITvsfl 519
Cdd:TIGR02169 397 LK-----------REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA---- 461
|
330 340 350
....*....|....*....|....*....|....*..
gi 217416398 520 QKITDLQNQLKQQEEDFRKqLEDEEgRKAEKENTTAE 556
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDR-VEKEL-SKLQRELAEAE 496
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
42-564 |
1.27e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 42 QRFKQQKESKQNLnVDKDTTLPASARKVKSSESKIRVLLQERGAQDRRIQDLETElEKMEARLNAALREKTSLSANNATL 121
Cdd:TIGR00618 379 QHIHTLQQQKTTL-TQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQ-QELQQRYAELCAAAITCTAQCEKL 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 122 EKqlIELTRTNELLKSKFSENGNQKNLRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQG---KIAQLE 198
Cdd:TIGR00618 457 EK--IHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPltrRMQRGE 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 199 GKLVSIEKEKIDEKSETEKLLEYIEEISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKC 278
Cdd:TIGR00618 535 QTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQ 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 279 QLLEKEKEDHVNRNREHNENLNAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNL 358
Cdd:TIGR00618 615 HALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTY 694
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 359 FEEELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRaeelklleeklkgkEAELEKSSAAHTQATLLLQEKYDSMVQSLE 438
Cdd:TIGR00618 695 WKEMLAQCQTLLRELETHIEEYDREFNEIENASSSL--------------GSDLAAREDALNQSLKELMHQARTVLKART 760
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 439 DvtAQFESYKALTASEIEDLKLENssLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITVSF 518
Cdd:TIGR00618 761 E--AHFNNNEEVTAALQTGAELSH--LAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSR 836
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 217416398 519 LQKITDLQNQLKQQEEdfrkQLEDEEGRKAEKENTTAELTEEINKW 564
Cdd:TIGR00618 837 LEEKSATLGEITHQLL----KYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
42-287 |
1.48e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 42 QRFKQQKESKQNLNVDKDTTLPASARKVKSSESKIRVLLQERGAQDRRIQDLETELEKMEARLNAAL-----REKTSLSA 116
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiqAELSKLEE 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 117 NNATLEKQLIEL-TRTNELLKSKFSENGNQKNLRILSLELMKLRNKREtkmrgmmAKQEGMEMKLQVTQRSLEESQGKIA 195
Cdd:TIGR02169 806 EVSRIEARLREIeQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE-------KEIENLNGKKEELEEELEELEAALR 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 196 QLEGKLVSIEKEKIDEKSETEKLLEYIEEISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEEnIVILSKQVEDLN 275
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE-IPEEELSLEDVQ 957
|
250
....*....|..
gi 217416398 276 VKCQLLEKEKED 287
Cdd:TIGR02169 958 AELQRVEEEIRA 969
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
297-562 |
1.65e-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: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 297 ENLNAEMQNLKQKFILEQQEREKLQQKELQID---SLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTLDELDKL 373
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSrqiSALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 374 QQKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEAEL-----------------EKSSAAHTQATLLLQEKYDSMVQS 436
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaanlrerleslERRIAATERRLEDLEEQIEELSED 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 437 LEDVTAQFESYKALTA---SEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKE 513
Cdd:TIGR02168 854 IESLAAEIEELEELIEeleSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 217416398 514 ITVSFLQKITDLQNQLKQQEEDFRKQLEDEEGRKAEKENTTAELTEEIN 562
Cdd:TIGR02168 934 LEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
314-561 |
1.87e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 314 QQEREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQ---EEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLEEE 390
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEkeiEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 391 AKSRAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQEKY----DSMVQSLEDVTAQFESYKALTASEIEDLKLENSSLQ 466
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEvsriEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 467 EKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITvSFLQKITDLQNQLKQQEEDFRKQLEDEEGR 546
Cdd:TIGR02169 847 EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE-AQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
250
....*....|....*
gi 217416398 547 KAEKENTTAELTEEI 561
Cdd:TIGR02169 926 LEALEEELSEIEDPK 940
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
205-692 |
2.01e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 205 EKEKIDEKSETEKLLEYIEEISCASDQVEKyKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLEKE 284
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKK-KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 285 KEDHVNRNREHNEnlnaEMQNLKQKFILEQQEREKLQQKElqidsllqQEKELSSSLHQKlcsfQEEMVKEKNLFEE-EL 363
Cdd:PTZ00121 1379 KADAAKKKAEEKK----KADEAKKKAEEDKKKADELKKAA--------AAKKKADEAKKK----AEEKKKADEAKKKaEE 1442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 364 KQTLDELDKLQQKEEQAERLVKQLEEEAKS---RAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQEKYDSMVQSLEDV 440
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEAKKKAEEAKKAdeaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 441 TAQfESYKALTASEIEDLKlenSSLQEKAAKAGKNAEDVQ--HQILATESSNQEYVRMLLDLQTKSALKETE---IKEIT 515
Cdd:PTZ00121 1523 KAD-EAKKAEEAKKADEAK---KAEEKKKADELKKAEELKkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEearIEEVM 1598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 516 VSFLQKITDLQNQLKQQEEDFRK--QLEDEEGRKAEKENTTAELTEEINKW-RLLYEELYNKTKPFQLQLDAFEVEKQA- 591
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKaeELKKAEEEKKKVEQLKKKEAEEKKKAeELKKAEEENKIKAAEEAKKAEEDKKKAe 1678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 592 ----LLNEHGAAQEQLNKIRDSYAK---LLGHQNLKQKIKHVVKLKDENSQLKSEVSKLRCQLAKKKQSETKLQE-ELNK 663
Cdd:PTZ00121 1679 eakkAEEDEKKAAEALKKEAEEAKKaeeLKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEeEKKK 1758
|
490 500
....*....|....*....|....*....
gi 217416398 664 VLGIKHFDPSKAFHHESKENFALKTPLKE 692
Cdd:PTZ00121 1759 IAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
223-390 |
2.28e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.46 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 223 EEISCASDQVEKYKLDIAQL-----EENLKEKNDEILSLKQSLEENIviLSKQVEDLNVKcqllekEKEDHVNRNREHNE 297
Cdd:pfam06160 237 KEIQQLEEQLEENLALLENLeldeaEEALEEIEERIDQLYDLLEKEV--DAKKYVEKNLP------EIEDYLEHAEEQNK 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 298 NLNAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELSSSLHQK------LCSFQEEMVKEKNLFEEELKQTLDELD 371
Cdd:pfam06160 309 ELKEELERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVERLEEKevayseLQEELEEILEQLEEIEEEQEEFKESLQ 388
|
170
....*....|....*....
gi 217416398 372 KLQQKEEQAERLVKQLEEE 390
Cdd:pfam06160 389 SLRKDELEAREKLDEFKLE 407
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
212-443 |
2.33e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 212 KSETEKLLEYIEEiscasdQVEKYKLDIAQLEENL---KEKNDEIlslkqSLEENIVILSKQVEDLNVKCQLLEKEKEDH 288
Cdd:COG3206 170 REEARKALEFLEE------QLPELRKELEEAEAALeefRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 289 VNRNREHNENLNAEMQNLKQkfILEQQEREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTLD 368
Cdd:COG3206 239 EARLAALRAQLGSGPDALPE--LLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 217416398 369 ELDKLQQKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEAELEkssaahtqatlLLQEKYDSMVQSLEDVTAQ 443
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE-----------VARELYESLLQRLEEARLA 380
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
152-390 |
2.72e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 152 SLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEISCASDQ 231
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 232 VEKYKLDIAQLEENLKEKNDEILSLKQSLEEniviLSKQVEDLNVkcqlLEKEKEDHVNRNREHNENLNAEMQNLKQKFI 311
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEE----LEEKVKELKE----LKEKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 312 LEQQER------EKLQQKELQIDSLLQQEKELS---SSLHQKLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAER 382
Cdd:PRK03918 319 LEEEINgieeriKELEEKEERLEELKKKLKELEkrlEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK 398
|
....*...
gi 217416398 383 LVKQLEEE 390
Cdd:PRK03918 399 AKEEIEEE 406
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
66-561 |
3.83e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 66 ARKVKSSESKIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRT-------------- 131
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAElaeaeeeleelaee 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 132 -NELLKSKFSENGNQKNLRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKID 210
Cdd:COG1196 388 lLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 211 EKSETEKLLEYIEEISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKCQ---LLEKEKED 287
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYeaaLEAALAAA 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 288 HVNRNREHNENLNAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTL 367
Cdd:COG1196 548 LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 368 DELDkLQQKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQEKYDSMVQSLEDVTAQFESY 447
Cdd:COG1196 628 VAAR-LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 448 KALTASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALkETEIKEITvsflQKITDLQN 527
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL-ERELERLE----REIEALGP 781
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 217416398 528 -------QLKQQEEDFR---KQLEDEEGRKAEKENTTAELTEEI 561
Cdd:COG1196 782 vnllaieEYEELEERYDflsEQREDLEEARETLEEAIEEIDRET 825
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
216-459 |
5.16e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 216 EKLLEYIEEISCASDQVEKYKLDIAQLEEnLKEKNDEILSLKQSLEENIVILSK-QVEDLNVKCQLLEKEKEdhvnRNRE 294
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEYLRAAlRLWFAQRRLELLEAELE----ELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 295 HNENLNAEMQNLKQKFILEQQEREKLQQKELQIDslLQQEKELssslhqklcsfqeemvkeknlfEEELKQTLDELDKLQ 374
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNG--GDRLEQL----------------------EREIERLERELEERE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 375 QKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEAELEKSSAAhtqatllLQEKYDSMVQSLEDVTAQFESykalTASE 454
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA-------LEEALAEAEAALRDLRRELRE----LEAE 427
|
....*
gi 217416398 455 IEDLK 459
Cdd:COG4913 428 IASLE 432
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
45-661 |
1.10e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 45 KQQKESKQNLNVDKDTTLPASARKVKSSESKIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQ 124
Cdd:TIGR04523 46 KNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 125 LIELTRT-NELLKSKFSENGNQKNLRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVS 203
Cdd:TIGR04523 126 LNKLEKQkKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 204 IEKEKIDEKSETEKLLEYIEEISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLeK 283
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI-K 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 284 EKEDHVNRNREHNENLNAEMQNLKQKFILEQ--QEREKLQQKELQIDSLLQQEKELSSSLhQKLCSFQEEMVKEKNLFEE 361
Cdd:TIGR04523 285 ELEKQLNQLKSEISDLNNQKEQDWNKELKSElkNQEKKLEEIQNQISQNNKIISQLNEQI-SQLKKELTNSESENSEKQR 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 362 ELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEAELEKssaahtqatllLQEKYDSMVQSLEDVT 441
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK-----------LQQEKELLEKEIERLK 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 442 AQFESYKaltaSEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITvsflQK 521
Cdd:TIGR04523 433 ETIIKNN----SEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN----EE 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 522 ITDLQNQ---LKQQEEDFRKQLEDEEGRKAEKENTTAELTEEINK--WRLLYEELYNKTKPFQLQLDAFEVEKQALLNEH 596
Cdd:TIGR04523 505 KKELEEKvkdLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQ 584
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 217416398 597 GAAQEQLNKIRDSYAKLLghQNLKQKIKHVVKLKDENSQLKSEVSKLRCQLAKKKQSETKLQEEL 661
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLI--KEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
448-659 |
1.12e-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: 42.35 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 448 KALTASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITvsflQKITDLQN 527
Cdd:TIGR02168 227 LALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA----NEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 528 Q---LKQQEEDFRKQLEDEEGRKAEKENTTAELTEEINKWRLLYEELYNKTKPFQLQLDAFEVEKQALLNEHGAAQEQLN 604
Cdd:TIGR02168 303 QkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 217416398 605 KIRDSYAKLLghQNLKQKIKHVVKLKDENSQLKSEVSKLRCQLAK--KKQSETKLQE 659
Cdd:TIGR02168 383 TLRSKVAQLE--LQIASLNNEIERLEARLERLEDRRERLQQEIEEllKKLEEAELKE 437
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
73-390 |
1.33e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 73 ESKIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSE-NGNQKNLRIL 151
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDElREREAELEAT 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 152 SLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEkekiDEKSETEKLLEYIEEISCASDQ 231
Cdd:PRK02224 435 LRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLE----EEVEEVEERLERAEDLVEAEDR 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 232 VEKYKLDIAQLEENLKEKNDEILSLKQSLEEniviLSKQVEDLNVKCQllekEKEDHVNRNREHNENLNAEMQNLKQKFI 311
Cdd:PRK02224 511 IERLEERREDLEELIAERRETIEEKRERAEE----LRERAAELEAEAE----EKREAAAEAEEEAEEAREEVAELNSKLA 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 312 LEQQEREKLQQKELQIDSLLQQEKELSSsLHQKLCSFQE------EMVKEKNLFEEELKQTLDE--LDKLQQKEEQAERL 383
Cdd:PRK02224 583 ELKERIESLERIRTLLAAIADAEDEIER-LREKREALAElnderrERLAEKRERKRELEAEFDEarIEEAREDKERAEEY 661
|
....*..
gi 217416398 384 VKQLEEE 390
Cdd:PRK02224 662 LEQVEEK 668
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
79-379 |
1.51e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 79 LLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIElTRTNELLKSKFSENGN-----QKNLRILSL 153
Cdd:PRK11281 71 LLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLS-TLSLRQLESRLAQTLDqlqnaQNDLAEYNS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 154 ELMKLRNKRETkmrgmmakqegmemklqvTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLeyieeiscasdQVE 233
Cdd:PRK11281 150 QLVSLQTQPER------------------AQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLL-----------QAE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 234 KYKLDiAQLEENlkekndeilslKQSLEEN---IVILSKQVEDLNVKCQLLEKEKEDhvnrnreHNENLNAEMQNLKQKF 310
Cdd:PRK11281 201 QALLN-AQNDLQ-----------RKSLEGNtqlQDLLQKQRDYLTARIQRLEHQLQL-------LQEAINSKRLTLSEKT 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 217416398 311 ILEQQEREKLQQkeLQIDSLLQQEKELSSSLHQKLCSFQEEMvkeKNLFEEEL--KQTLDELDKLQQK-EEQ 379
Cdd:PRK11281 262 VQEAQSQDEAAR--IQANPLVAQELEINLQLSQRLLKATEKL---NTLTQQNLrvKNWLDRLTQSERNiKEQ 328
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
67-560 |
3.32e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 67 RKVKSSESKIRVLLQERGAQDRRIQDLETELEKMEARLNAaLREKTSLSANNAtleKQLIE----LTRTNE-----LLKS 137
Cdd:pfam05483 233 KEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQ-LEEKTKLQDENL---KELIEkkdhLTKELEdikmsLQRS 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 138 KFSENGNQKNLRILSLELMKLRNKRETKMRGMMAKQEG--------------MEMKLQVTQRSLE--ESQGKIAQLEGKL 201
Cdd:pfam05483 309 MSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAhsfvvtefeattcsLEELLRTEQQRLEknEDQLKIITMELQK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 202 VSIEKEKIDE-KSETEKLLEYIEEISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEENIVIL------------- 267
Cdd:pfam05483 389 KSSELEEMTKfKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLeiqltaiktseeh 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 268 -SKQVEDLNVKCQ---LLEKEKEDHVNRNREHNENLNAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELSSSLHQ 343
Cdd:pfam05483 469 yLKEVEDLKTELEkekLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRD 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 344 KLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLEEEA---KSRAEELKLLEEKLKGKEAELEKSSAAHT 420
Cdd:pfam05483 549 ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCnnlKKQIENKNKNIEELHQENKALKKKGSAEN 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 421 QATLLLQEKYDSMVQSLEDVTAQFESYKALTASEIEDLKLENSSLQEKAAKAGKNAEDV-----------QHQILA---- 485
Cdd:pfam05483 629 KQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAvklqkeidkrcQHKIAEmval 708
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 217416398 486 TESSNQEYVRMLLDLQTKSAL---KETEIKEITVSFLQKITDLQNQLKQQEEDFRKQLEDEEGRKAEKENTTAELTEE 560
Cdd:pfam05483 709 MEKHKHQYDKIIEERDSELGLyknKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
451-664 |
3.41e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 451 TASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITvsflQKITDLQNQLK 530
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE----KEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 531 QQEEDFRKQLedeegRKAEKENTTAELTEEINK------------WRLLYEELYNKTKPFQLQLDAFEVEKQALLNEHGA 598
Cdd:COG4942 101 AQKEELAELL-----RALYRLGRQPPLALLLSPedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217416398 599 AQEQLNKIRDSYAKLLGHQNLKQKIkhvvklkdeNSQLKSEVSKLRCQLAKKKQSETKLQEELNKV 664
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKL---------LARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
318-539 |
3.50e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 318 EKLQQKELQIDSLLQQEKELSSSLhQKLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRAEE 397
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKEL-AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 398 LKLLEEKLKGKEAELEKSSAAHTQATLLLQEKYDSMVQSLEDVTAQFESYKALTA---SEIEDLKLENSSLQEKAAKAGK 474
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEelrADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 217416398 475 NAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEItvsfLQKITDLQNQLKQQEEDFRKQ 539
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL----QQEAEELEALIARLEAEAAAA 239
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
73-225 |
3.84e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 73 ESKIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSENGNQKNLRILS 152
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217416398 153 LELMKLRNKR---ETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLvsiEKEKIDEKSETEKLLEYIEEI 225
Cdd:COG1579 96 KEIESLKRRIsdlEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAELEELEAEREEL 168
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
42-388 |
4.06e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 42 QRFKQQKESKQNLNVDKDTTLpasARKVKSSESKIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATL 121
Cdd:COG5022 828 REKKLRETEEVEFSLKAEVLI---QKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLEL 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 122 EKQLIELTR---TNELLKSKFSENgnqknlriLSLELMKLRNKRETKM-RGMMAKQEGMEMKLQVTQRSLEESQGKIAQL 197
Cdd:COG5022 905 ESEIIELKKslsSDLIENLEFKTE--------LIARLKKLLNNIDLEEgPSIEYVKLPELNKLHEVESKLKETSEEYEDL 976
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 198 EGKLVSIEKEKIDEKSETEKLLEYIEEISCASDQVEKYKldiaqleENLKEKNDEILSLKQsleeNIVILSKQVEDLNVK 277
Cdd:COG5022 977 LKKSTILVREGNKANSELKNFKKELAELSKQYGALQEST-------KQLKELPVEVAELQS----ASKIISSESTELSIL 1045
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 278 cqlleKEKEDHVNRNREHNENLNAEMQNLKQKfileqqeREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKN 357
Cdd:COG5022 1046 -----KPLQKLKGLLLLENNQLQARYKALKLR-------RENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPAN 1113
|
330 340 350
....*....|....*....|....*....|.
gi 217416398 358 LFEEELKQTLdELDKLQQKEEQAERLVKQLE 388
Cdd:COG5022 1114 VLQFIVAQMI-KLNLLQEISKFLSQLVNTLE 1143
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
172-663 |
7.03e-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: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 172 KQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEI----SCASDQVEKYKLDIAQLEENLK 247
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLndklKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 248 EKND-------EILSLKQSLEEN----------IVILSKQVEDLNVKCQLLEKEKEDHVNRNREhnenLNAEMQNLKQKF 310
Cdd:TIGR04523 114 NDKEqknklevELNKLEKQKKENkknidkflteIKKKEKELEKLNNKYNDLKKQKEELENELNL----LEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 311 ILEQQEREKLQQKELQIDSLLQQEKELSS---SLHQKLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQL 387
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQKNKSLESqisELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 388 E------EEAKSRAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQ-EKYDSMVQSLEDVTAQFESYKALTASEIEDLKL 460
Cdd:TIGR04523 270 SekqkelEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSElKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 461 ENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITVSFLQKITDLQNqLKQQEEDFRKQL 540
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK-LQQEKELLEKEI 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 541 EDEEGRKAEKENTTAELTEEINKWRLLYEELYNKTKPFQLQLDAFEVEkqallnehgaaqeqLNKIRDSYAKLlgHQNLK 620
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRS--------------INKIKQNLEQK--QKELK 492
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 217416398 621 QKIKHVVKLKDENSQLKSEVSKLRCQLAKKKQSETKLQEELNK 663
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
160-571 |
8.15e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.57 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 160 NKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEISCASDQVEKYKLDI 239
Cdd:pfam02463 629 LKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRE 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 240 AQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNENLNAEMQNLKQKFILEQQEREK 319
Cdd:pfam02463 709 KEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKV 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 320 LQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRAEELK 399
Cdd:pfam02463 789 EEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEEL 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 400 LLEEKLKGKEAELEKSSAAHTQATLLLQEKYDSMVQSLEDVTAQFESYKALTASEIEDLKLENSSLQEKAAKAGKNAEDV 479
Cdd:pfam02463 869 LQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEK 948
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416398 480 QHQILATESSNQEYVRMLLDLQTKSALKETEIKEITVSFLQKITDLQNQLKQQEEDFRKQLEDEEGRKAEKENTTAELTE 559
Cdd:pfam02463 949 EKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVS 1028
|
410
....*....|..
gi 217416398 560 EINKWRLLYEEL 571
Cdd:pfam02463 1029 INKGWNKVFFYL 1040
|
|
| |
