|
Name |
Accession |
Description |
Interval |
E-value |
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
16-339 |
1.68e-114 |
|
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: 348.34 E-value: 1.68e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 16 GCAPSPGAYDVKTLEVLKGPVSFQKSQRFKQQK--ESKQNLNVDKDTTLPASARKVKSSESKKESQKND---KDLKILEK 90
Cdd:pfam15905 1 GCAPPPGSYDVKTSDALKGPVSFEKSQRFRKQKaaESQPNLNNSKDASTPATARKVKSLELKKKSQKNLkesKDQKELEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 91 EIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSENGNQKNLRILSLE 170
Cdd:pfam15905 81 EIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSEDGTQKKMSSLSME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 171 LMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEISCASDQVEK 250
Cdd:pfam15905 161 LMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 251 YKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNENLNAEMQNLKQKFILEQ 330
Cdd:pfam15905 241 YKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEE 320
|
....*....
gi 217272802 331 QEREKLQQK 339
Cdd:pfam15905 321 QEHQKLQQK 329
|
|
| HMMR_C |
pfam15908 |
Hyaluronan mediated motility receptor C-terminal; HMMR_C is the C-terminal region of ... |
553-709 |
3.50e-62 |
|
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: 204.76 E-value: 3.50e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 553 RKQLEDEEGRKAEKENTTAELTEEINKWRLLYEELYNKTKPFQLQLDAFEVEKQALLNEHGAAQEQLNKIRDSYAKLLGH 632
Cdd:pfam15908 1 TKQLEMEEQRKARLENTVDELTEEIKKWRNLYEELYNKTKPFQEQLDAFEAEKNALLNENGAAQEELNKLSDAYAKLLGH 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 217272802 633 QNLKQKIKHVVKLKDENSQLKSEVSKLRCQLAKKKQSETKLQEELNKVLGIKHFDPSKAFHHESKENFALKTPLKEG 709
Cdd:pfam15908 81 QNQKQKIKHVVKLKEENTQLKQEVSKLRSQLAKEKQVQKKLQEQLNGAQGIRRFDPSKAFQHESKENFEPKTPLKEG 157
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
105-630 |
2.83e-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: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 105 RIQDLETELEK----------------------MEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSENGNQK 162
Cdd:COG1196 190 RLEDILGELERqleplerqaekaeryrelkeelKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 163 N-LRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEI 241
Cdd:COG1196 270 EeLRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 242 SCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNENLNAEMQN 321
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 322 LKQKFILEQQEREKLQQKELQIDSLLQQEKELSSSLHQKLcsfqeemvKEKNLFEEELKQTLDELDKLQQKEEQAERLVK 401
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL--------EEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 402 QLEEEAKSRAEELKLLEEKLKGKE------AELEKSSAAHTQATLLLQEKYDSMVQSLEDVTAQFESYKALTASEIEDLK 475
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAvavligVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDK 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 476 LENSSLQEKAAKAGKN--------AEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITVSFLQKITDLQNQLKQ 547
Cdd:COG1196 582 IRARAALAAALARGAIgaavdlvaSDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 548 QEEDFRKQLEDEEGRKAEKEnttAELTEEINKWRLLYEELYNKTKPFQLQLDAFEVEKQALLNEHGAAQEQLNKIRDSYA 627
Cdd:COG1196 662 LTGGSRRELLAALLEAEAEL---EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
...
gi 217272802 628 KLL 630
Cdd:COG1196 739 EEL 741
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
79-392 |
1.12e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 79 QKNDKDLKILEKEIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKfsen 158
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER---- 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 159 gnQKNLRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSE----TEKL 234
Cdd:TIGR02168 749 --IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 235 LEYIEEISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEE---NIVILSKQVEDLNVKCQLLEKEKEDHVNRNREH 311
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEElesELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 312 NENLNAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELSSSLhqklcsfQEEMVKEKNLFEEELKQTLDELDKLQQ 391
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT-------LEEAEALENKIEDDEEEARRRLKRLEN 979
|
.
gi 217272802 392 K 392
Cdd:TIGR02168 980 K 980
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
225-411 |
1.72e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.40 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 225 IDEKSETEKLLEYIEEiscASDQVEKYKLDIAQL-EENLKEKNDEILSLKQSLEenivilsKQVEDLNVKCQLLEKeked 303
Cdd:PRK12704 24 VRKKIAEAKIKEAEEE---AKRILEEAKKEAEAIkKEALLEAKEEIHKLRNEFE-------KELRERRNELQKLEK---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 304 hvnRNREHNENLNAEMQNLKQKfileqqeREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTL 383
Cdd:PRK12704 90 ---RLLQKEENLDRKLELLEKR-------EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEIL 159
|
170 180
....*....|....*....|....*....
gi 217272802 384 deLDKLQQK-EEQAERLVKQLEEEAKSRA 411
Cdd:PRK12704 160 --LEKVEEEaRHEAAVLIKEIEEEAKEEA 186
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
193-577 |
4.34e-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: 50.44 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 193 EMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEeiscasdQVEKYKLDIAQLEENLKEKNDEILSL 272
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE-------QLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 273 KQSLEENIVILSKQVEDLNVKCQLLEKEKEDhvnrNREHNENLNAEMQNLKQKFileQQEREKLQQKELQIDSLLQQEKE 352
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEE----AEEELAEAEAEIEELEAQI---EQLKEELKALREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 353 LSSSLHQKLcSFQEEMVKEKNLFEEELKQTLDELDKLqqkEEQAERLVKQLEEEAKSRAeelklleeKLKGKEAELEKSS 432
Cdd:TIGR02168 815 LNEEAANLR-ERLESLERRIAATERRLEDLEEQIEEL---SEDIESLAAEIEELEELIE--------ELESELEALLNER 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 433 AAHTQATLLLQEKYDSMVQSLEDVTAQF----ESYKALTAS------EIEDLKLENSSLQEKAAKAGK-NAEDVQHQILA 501
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRselrRELEELREKlaqlelRLEGLEVRIDNLQERLSEEYSlTLEEAEALENK 962
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217272802 502 TESSNQEyvrmlldLQTKSALKETEIKEITVSFLQKITDLQnQLKQQEEDFRKQLEDEEGRKAEKENTTAELTEEI 577
Cdd:TIGR02168 963 IEDDEEE-------ARRRLKRLENKIKELGPVNLAAIEEYE-ELKERYDFLTAQKEDLTEAKETLEEAIEEIDREA 1030
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
246-679 |
5.72e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 246 DQVEKYKLDIAQLEENLKEKNDEILSLKQsLEENIVILSKQVEDLNVKCQLLEKEKEDHvnrnrehneNLNAEMQNLKQK 325
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE-LEEELEELEAELEELREELEKLEKLLQLL---------PLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 326 FILEQQEREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLEE 405
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 406 EAKSRAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQEKYDSMVQSLEDVtaqFESYKALTASEIEDLKLENSSLQEKA 485
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSL---ILTIAGVLFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 486 AKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEitvsFLQKITDLQnQLKQQEEDFRKQLEDEEGRKAE 565
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLE----LLDRIEELQ-ELLREAEELEEELQLEELEQEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 566 KENTTAELTEEINKWRLLYEELynktkpfqlqldafeVEKQALLNEHGAAQEQLNKIRDSYAKLLGHQNLKQkikhvvkL 645
Cdd:COG4717 373 AALLAEAGVEDEEELRAALEQA---------------EEYQELKEELEELEEQLEELLGELEELLEALDEEE-------L 430
|
410 420 430
....*....|....*....|....*....|....
gi 217272802 646 KDENSQLKSEVSKLRCQLAKKKQSETKLQEELNK 679
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELEAELEQ 464
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
326-494 |
5.92e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 326 FILEQQEREKLQQKELQIDSLLQQ-EKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLE 404
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEaKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 405 EEAKSRAEELKLLEEKLKGKEAELEKssaahtqatllLQEKYDSMVQSLEDvtaQFESYKALTASEIEDLKLEN--SSLQ 482
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEK-----------KEEELEELIEEQLQ---ELERISGLTAEEAKEILLEKveEEAR 168
|
170
....*....|..
gi 217272802 483 EKAAKAGKNAED 494
Cdd:PRK12704 169 HEAAVLIKEIEE 180
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
108-624 |
9.68e-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: 49.35 E-value: 9.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 108 DLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSkfsengnqknlriLSLELMKLRNKRETKMRGMMA 187
Cdd:pfam15921 114 DLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKC-------------LKEDMLEDSNTQIEQLRKMML 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 188 KQEGMEMKLQVTQRSLEESQGK------------------------------IAQLEGKLVSIEKEKIDEKSETEKLLEY 237
Cdd:pfam15921 181 SHEGVLQEIRSILVDFEEASGKkiyehdsmstmhfrslgsaiskilreldteISYLKGRIFPVEDQLEALKSESQNKIEL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 238 IeeISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVK--CQLLEKEKEDHVNRN--REHNE 313
Cdd:pfam15921 261 L--LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMymRQLSDLESTVSQLRSelREAKR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 314 NLNAEMQNLKQKFILE-------QQEREKLQQKELQIDSLLQQekeLSSSLHQKLCSFQEEMVKEKNLFEEELKQTLD-- 384
Cdd:pfam15921 339 MYEDKIEELEKQLVLAnselteaRTERDQFSQESGNLDDQLQK---LLADLHKREKELSLEKEQNKRLWDRDTGNSITid 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 385 ----ELDKLQQKEEQAERLVKQLEEEAKsraeelklleeklkgkeAELEKSSAAhtqatllLQEKYDSMvQSLEDVTAQF 460
Cdd:pfam15921 416 hlrrELDDRNMEVQRLEALLKAMKSECQ-----------------GQMERQMAA-------IQGKNESL-EKVSSLTAQL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 461 ESYKALTASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYV----RMLLDLQTKSALK---------ETEI 527
Cdd:pfam15921 471 ESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITklrsRVDLKLQELQHLKnegdhlrnvQTEC 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 528 KEITVSFLQKITDLQnQLKQQEEDFrKQLEDEEGRKA-EKENTTAELTEEINKWRLLYEELY-------NKTKPFQLQLD 599
Cdd:pfam15921 551 EALKLQMAEKDKVIE-ILRQQIENM-TQLVGQHGRTAgAMQVEKAQLEKEINDRRLELQEFKilkdkkdAKIRELEARVS 628
|
570 580
....*....|....*....|....*
gi 217272802 600 AFEVEKQALLNehgAAQEQLNKIRD 624
Cdd:pfam15921 629 DLELEKVKLVN---AGSERLRAVKD 650
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
464-675 |
1.37e-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: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 464 KALTASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITvsflQKITDLQN 543
Cdd:TIGR02168 227 LALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA----NEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 544 Q---LKQQEEDFRKQLEDEEGRKAEKENTTAELTEEINKWRLLYEELYNKTKPFQLQLDAFEVEKQALLNEHGAAQEQLN 620
Cdd:TIGR02168 303 QkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 217272802 621 KIRDSYAKLLghQNLKQKIKHVVKLKDENSQLKSEVSKLRCQLAK--KKQSETKLQE 675
Cdd:TIGR02168 383 TLRSKVAQLE--LQIASLNNEIERLEARLERLEDRRERLQQEIEEllKKLEEAELKE 437
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
467-680 |
3.99e-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: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 467 TASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITvsflQKITDLQNQLK 546
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE----KEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 547 QQEEDFRKQLedeegRKAEKENTTAELTEEINK------------WRLLYEELYNKTKPFQLQLDAFEVEKQALLNEHGA 614
Cdd:COG4942 101 AQKEELAELL-----RALYRLGRQPPLALLLSPedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217272802 615 AQEQLNKIRDSYAKLLGHQNLKQKIkhvvklkdeNSQLKSEVSKLRCQLAKKKQSETKLQEELNKV 680
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 ... |
16-339 |
1.68e-114 |
|
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: 348.34 E-value: 1.68e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 16 GCAPSPGAYDVKTLEVLKGPVSFQKSQRFKQQK--ESKQNLNVDKDTTLPASARKVKSSESKKESQKND---KDLKILEK 90
Cdd:pfam15905 1 GCAPPPGSYDVKTSDALKGPVSFEKSQRFRKQKaaESQPNLNNSKDASTPATARKVKSLELKKKSQKNLkesKDQKELEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 91 EIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSENGNQKNLRILSLE 170
Cdd:pfam15905 81 EIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSEDGTQKKMSSLSME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 171 LMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEISCASDQVEK 250
Cdd:pfam15905 161 LMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 251 YKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNENLNAEMQNLKQKFILEQ 330
Cdd:pfam15905 241 YKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEE 320
|
....*....
gi 217272802 331 QEREKLQQK 339
Cdd:pfam15905 321 QEHQKLQQK 329
|
|
| HMMR_C |
pfam15908 |
Hyaluronan mediated motility receptor C-terminal; HMMR_C is the C-terminal region of ... |
553-709 |
3.50e-62 |
|
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: 204.76 E-value: 3.50e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 553 RKQLEDEEGRKAEKENTTAELTEEINKWRLLYEELYNKTKPFQLQLDAFEVEKQALLNEHGAAQEQLNKIRDSYAKLLGH 632
Cdd:pfam15908 1 TKQLEMEEQRKARLENTVDELTEEIKKWRNLYEELYNKTKPFQEQLDAFEAEKNALLNENGAAQEELNKLSDAYAKLLGH 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 217272802 633 QNLKQKIKHVVKLKDENSQLKSEVSKLRCQLAKKKQSETKLQEELNKVLGIKHFDPSKAFHHESKENFALKTPLKEG 709
Cdd:pfam15908 81 QNQKQKIKHVVKLKEENTQLKQEVSKLRSQLAKEKQVQKKLQEQLNGAQGIRRFDPSKAFQHESKENFEPKTPLKEG 157
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
105-630 |
2.83e-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: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 105 RIQDLETELEK----------------------MEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSENGNQK 162
Cdd:COG1196 190 RLEDILGELERqleplerqaekaeryrelkeelKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 163 N-LRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEI 241
Cdd:COG1196 270 EeLRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 242 SCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNENLNAEMQN 321
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 322 LKQKFILEQQEREKLQQKELQIDSLLQQEKELSSSLHQKLcsfqeemvKEKNLFEEELKQTLDELDKLQQKEEQAERLVK 401
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL--------EEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 402 QLEEEAKSRAEELKLLEEKLKGKE------AELEKSSAAHTQATLLLQEKYDSMVQSLEDVTAQFESYKALTASEIEDLK 475
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAvavligVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDK 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 476 LENSSLQEKAAKAGKN--------AEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITVSFLQKITDLQNQLKQ 547
Cdd:COG1196 582 IRARAALAAALARGAIgaavdlvaSDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 548 QEEDFRKQLEDEEGRKAEKEnttAELTEEINKWRLLYEELYNKTKPFQLQLDAFEVEKQALLNEHGAAQEQLNKIRDSYA 627
Cdd:COG1196 662 LTGGSRRELLAALLEAEAEL---EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
...
gi 217272802 628 KLL 630
Cdd:COG1196 739 EEL 741
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
103-445 |
6.81e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 6.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 103 DRRIQDLETELEKMEA---RLNAALREktsLSANNATLEKQLIELTRTNELlkskfsengnQKNLRILSLELMKLRnkre 179
Cdd:COG1196 171 KERKEEAERKLEATEEnleRLEDILGE---LERQLEPLERQAEKAERYREL----------KEELKELEAELLLLK---- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 180 tkMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSE----TEKLLEYIEEISCASDQVEKYKLDI 255
Cdd:COG1196 234 --LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEleeaQAEEYELLAELARLEQDIARLEERR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 256 AQLEENLKEKNDEILSLKQ---SLEENIVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNENLNAEMQNLKQKFILEQQE 332
Cdd:COG1196 312 RELEERLEELEEELAELEEeleELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 333 REKLQQKELQIDSLLQQEKELSsslhQKLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRAE 412
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALL----ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
330 340 350
....*....|....*....|....*....|...
gi 217272802 413 ELKLLEEKLKGKEAELEKSSAAHTQATLLLQEK 445
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
70-629 |
4.50e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 70 KSSESKKESQKNDKDLKILEKEIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNE 149
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 150 LLKSKFSENGNQKNLRILSLELMKLRNKRETkmrgmmAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKS 229
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAE------EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 230 ETEKLLEYIEEiscasdqvekykldIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLnvkcQLLEKEKEDHVNRNR 309
Cdd:COG1196 394 AAAELAAQLEE--------------LEEAEEALLERLERLEEELEELEEALAELEEEEEEE----EEALEEAAEEEAELE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 310 EHNENLNAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTLDELDKL 389
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAA 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 390 QQKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQEKYDSMVQSLEDVTAQFES-YKALTA 468
Cdd:COG1196 536 YEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLrEADARY 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 469 SEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATE---SSNQEYVRMLLDLQTKSALKETEIKEITVSFLQKITDLQNQL 545
Cdd:COG1196 616 YVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTlegEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 546 KQQEEDFRKQLEDEEGRKAEKENTTAELTEEINKWRLLYEELYNKTKPFQLQLDAFEVEKQALLNEHGAAQEQLNKIRDS 625
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
....
gi 217272802 626 YAKL 629
Cdd:COG1196 776 IEAL 779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
79-392 |
1.12e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 79 QKNDKDLKILEKEIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKfsen 158
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER---- 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 159 gnQKNLRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSE----TEKL 234
Cdd:TIGR02168 749 --IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 235 LEYIEEISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEE---NIVILSKQVEDLNVKCQLLEKEKEDHVNRNREH 311
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEElesELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 312 NENLNAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELSSSLhqklcsfQEEMVKEKNLFEEELKQTLDELDKLQQ 391
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT-------LEEAEALENKIEDDEEEARRRLKRLEN 979
|
.
gi 217272802 392 K 392
Cdd:TIGR02168 980 K 980
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
195-411 |
2.97e-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: 56.31 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 195 KLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEiscASDQVEKYKLDIAQLEENLKEKNDEILSLKQ 274
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA---LARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 275 SLEENIVILSKQVEDLNVKCQ------LLEKEKEDHVNRN----REHNENLNAEMQNLKQKFILEQQEREKLQQKELQID 344
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRqpplalLLSPEDFLDAVRRlqylKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 217272802 345 SLLQQEKELSSSLhQKLCSFQEEMVKEknlFEEELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRA 411
Cdd:COG4942 178 ALLAELEEERAAL-EALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
43-678 |
6.85e-08 |
|
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: 56.22 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 43 RFKQQKESKQNLNVDKDttlpASARKVKSSESK---KESQKNDKDLKI--LEKEIRVLLQERGAQDRRIQDLETELEKME 117
Cdd:TIGR02168 233 RLEELREELEELQEELK----EAEEELEELTAElqeLEEKLEELRLEVseLEEEIEELQKELYALANEISRLEQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 118 ARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSEngNQKNLRILSLELMKLRNKRETKMRGMMAKQEGMEM--- 194
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE--LKEELESLEAELEELEAELEELESRLEELEEQLETlrs 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 195 KLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEE--ISCASDQVEKYKLDIAQLEENLKEKNDEILSL 272
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLEEALEEL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 273 KQSLEEN---IVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNENLNAEMQ------------NLKQKF----------I 327
Cdd:TIGR02168 467 REELEEAeqaLDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEGYeaaieaalggR 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 328 LEQQEREKLQQKELQIDSLLQQEK------ELSSSLHQKLCSFQEEMVKEKNLFEEELK--------------------- 380
Cdd:TIGR02168 547 LQAVVVENLNAAKKAIAFLKQNELgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKdlvkfdpklrkalsyllggvl 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 381 --QTLDELDKLQQKEEQAERLVKQLEEEAKSR------AEELKLLEEKLKGKEAELEKSSAAHTQATLLLQEKYDSMVQS 452
Cdd:TIGR02168 627 vvDDLDNALELAKKLRPGYRIVTLDGDLVRPGgvitggSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKE 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 453 LEDVTAQFESYKALTASEIEDLKLENSSLQEKAAKAGKNAEDVQhQILATESSNQEYVRMLLDLQTKSALKETEIKEITV 532
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA-QLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 533 SFLQKITDLQNQLKQQEE---DFRKQLEDEEGRKAEKENTTAELTEEINKWRLLYEELYNKTK--------------PFQ 595
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREaldELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEelsedieslaaeieELE 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 596 LQLDAFEVEKQALLNEHGAAQEQLNKIRDSYAKLlgHQNLKQKIKHVVKLKDENSQLKSEVSKLRCQLAKKKQSETKLQE 675
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEEALALLRSELEEL--SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
...
gi 217272802 676 ELN 678
Cdd:TIGR02168 944 RLS 946
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
66-579 |
1.06e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 66 ARKVKSSESKKESQKNDKDLKILEKEIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELT 145
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 146 RTNELLKSKFSENgNQKNLRILSLELMKLRNKRETKMRGMMAKQEgmemkLQVTQRSLEESQGKIAQLEGKLVSIEKEKI 225
Cdd:COG1196 351 EELEEAEAELAEA-EEALLEAEAELAEAEEELEELAEELLEALRA-----AAELAAQLEELEEAEEALLERLERLEEELE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 226 DEKSETEKLLEYIEEISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLEKEKEDHV 305
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 306 NRNREHNENLNAEMQNLKQKFILEQQEREKLQQKELQ--IDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTL 383
Cdd:COG1196 505 GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEaaLAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRA 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 384 DELDKLQQKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQEkYDSMVQSLEDVTAQFESY 463
Cdd:COG1196 585 RAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR-LREVTLEGEGGSAGGSLT 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 464 KALTASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEikeitvsfLQKITDLQN 543
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL--------EEQLEAERE 735
|
490 500 510
....*....|....*....|....*....|....*.
gi 217272802 544 QLKQQEEDFRKQLEDEEGRKAEKENTTAELTEEINK 579
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
225-411 |
1.72e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.40 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 225 IDEKSETEKLLEYIEEiscASDQVEKYKLDIAQL-EENLKEKNDEILSLKQSLEenivilsKQVEDLNVKCQLLEKeked 303
Cdd:PRK12704 24 VRKKIAEAKIKEAEEE---AKRILEEAKKEAEAIkKEALLEAKEEIHKLRNEFE-------KELRERRNELQKLEK---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 304 hvnRNREHNENLNAEMQNLKQKfileqqeREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTL 383
Cdd:PRK12704 90 ---RLLQKEENLDRKLELLEKR-------EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEIL 159
|
170 180
....*....|....*....|....*....
gi 217272802 384 deLDKLQQK-EEQAERLVKQLEEEAKSRA 411
Cdd:PRK12704 160 --LEKVEEEaRHEAAVLIKEIEEEAKEEA 186
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
99-406 |
2.07e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 99 RGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSEngnqknLRILSLELMKLRNKR 178
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA------LRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 179 ETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVS----IEKEKIDEKSETEKLLEYIEEISCASDQVEKYKLD 254
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEleaqIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 255 IAQLEENLKEKNDEILSLKQSLE---ENIVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNENLNAEMQNLkqkfileQQ 331
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEelsEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL-------EE 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 332 EREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFE---EELKQTLDELDKLQQK----EEQAERLVKQLE 404
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQErlsEEYSLTLEEAEALENKieddEEEARRRLKRLE 978
|
..
gi 217272802 405 EE 406
Cdd:TIGR02168 979 NK 980
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
66-411 |
2.48e-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: 54.30 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 66 ARKVKSSESKKESQKNDKDLKILEKEIRV---LLQERGAQDRRIQDLETELEKMEA-----RLNAALREKTSLSANNATL 137
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQqleRLRREREKAERYQALLKEKREYEGyellkEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 138 EKQLIELTRTNELLKSKFSEngNQKNLRILSLELMKLRNKR----ETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQL 213
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEE--IEQLLEELNKKIKDLGEEEqlrvKEKIGELEAEIASLERSIAEKERELEDAEERLAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 214 EGKLVSI--EKEKIDEKSETEKLL--EYIEEISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEEniviLSKQVED 289
Cdd:TIGR02169 328 EAEIDKLlaEIEELEREIEEERKRrdKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK----LKREINE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 290 LNVKCQLLEKEKEdhvnRNREHNENLNAEMQNLKQKfILEQQEREKLQQKELQidsllQQEKELsSSLHQKLCSFQEEMV 369
Cdd:TIGR02169 404 LKRELDRLQEELQ----RLSEELADLNAAIAGIEAK-INELEEEKEDKALEIK-----KQEWKL-EQLAADLSKYEQELY 472
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 217272802 370 KEKnlfeEELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRA 411
Cdd:TIGR02169 473 DLK----EEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
170-499 |
5.71e-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: 5.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 170 ELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSEtekLLEYIEEISCASDQVE 249
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE---LKELEARIEELEEDLH 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 250 KYKLDIAQLEENL-KEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLEKEKedhvnrnrehnENLNAEMQNLKQKFIL 328
Cdd:TIGR02169 776 KLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK-----------EYLEKEIQELQEQRID 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 329 EQQEREKLQQkelQIDSLLQQEKELSSSLhqklcsfqEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLE---E 405
Cdd:TIGR02169 845 LKEQIKSIEK---EIENLNGKKEELEEEL--------EELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEaqiE 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 406 EAKSRAEELKLLEEKLKGKEAELEKSSAAHTQ--ATLLLQEKYDSMVQSLEDVTAQFESYKALTASEIEDLKLENSSLQE 483
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEELSEIEDPKGEDEEipEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKE 993
|
330
....*....|....*.
gi 217272802 484 KAAKAGKNAEDVQHQI 499
Cdd:TIGR02169 994 KRAKLEEERKAILERI 1009
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
98-411 |
9.85e-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: 9.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 98 ERGAQDRRIQDLETELEKMEARLNAALREKtslsANNATLEKQlieltrtnellKSKFSENGNQKNLRILSLELMKLRNK 177
Cdd:pfam17380 294 EKMEQERLRQEKEEKAREVERRRKLEEAEK----ARQAEMDRQ-----------AAIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 178 REtKMRGMMAKQEGMEM-KLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEISCA-SDQVEKYKLDI 255
Cdd:pfam17380 359 KR-ELERIRQEEIAMEIsRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIrAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 256 AQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNENLNAEMQNLKQKFILEQQEREK 335
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKL 517
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217272802 336 LQQKELQIDSLLQQEKELSSSLHQKLcsfQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAErLVKQLEEEAKSRA 411
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRREAEEERR---KQQEMEERRRIQEQMRKATEERSRLEAMERERE-MMRQIVESEKARA 589
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
64-278 |
1.26e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 64 ASARKVKSSESKKESQKNDKDLKILEKEIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIE 143
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 144 LTRTNELLKSKFSENGNQKNLR-ILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEK 222
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLAlLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 217272802 223 EKIDEKSETEKLLEYIEE-ISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEE 278
Cdd:COG4942 182 ELEEERAALEALKAERQKlLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
95-333 |
3.77e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 50.67 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 95 LLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSENGnqKNLRILSLELMKL 174
Cdd:PLN02939 161 ILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLS--KELDVLKEENMLL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 175 RNK-----------RETKMRGMMAKQE--GMEMKLQVTQRSLEESQGKIAqlegKLVSIEKEKIDEKSETEKLLeyieeI 241
Cdd:PLN02939 239 KDDiqflkaelievAETEERVFKLEKErsLLDASLRELESKFIVAQEDVS----KLSPLQYDCWWEKVENLQDL-----L 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 242 SCASDQVEKYKLDIAQlEENLKEKNDEilsLKQSLEENIV--ILSKQVEDLNVKCQLLEK--EKEDH-VNRNREHNENLN 316
Cdd:PLN02939 310 DRATNQVEKAALVLDQ-NQDLRDKVDK---LEASLKEANVskFSSYKVELLQQKLKLLEErlQASDHeIHSYIQLYQESI 385
|
250
....*....|....*..
gi 217272802 317 AEMQNLKQKFILEQQER 333
Cdd:PLN02939 386 KEFQDTLSKLKEESKKR 402
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
72-595 |
3.86e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 72 SESKKESQKNDKDLKILEKEIRVLLQERGAQDRRIQDLET---ELEKMEARLNAALREKTSLSANNATLEKQLIELTRTN 148
Cdd:PRK03918 196 KEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElkeEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 149 ELLKSKFSENGNQKNLRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEgKLVSIEKEKIDEK 228
Cdd:PRK03918 276 EELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 229 SETEKLLEYIEEISCASDQVEKYKLDIAQLE--------ENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLEKE 300
Cdd:PRK03918 355 EELEERHELYEEAKAKKEELERLKKRLTGLTpeklekelEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 301 KEDHVNRNR----EHNENL----NAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELsSSLHQKLCSFQEEMVKEK 372
Cdd:PRK03918 435 KGKCPVCGRelteEHRKELleeyTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEL-IKLKELAEQLKELEEKLK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 373 NLFEEELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQEKYDSMVQS 452
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 453 LEDVTAQFESYKAL--TASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEI 530
Cdd:PRK03918 594 LKELEPFYNEYLELkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSR 673
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 217272802 531 TVSFLQKITDlqnQLKQQEEDFRKQLEDEEGRKAEKENTTAELtEEINKWRLLYEELYNKTKPFQ 595
Cdd:PRK03918 674 ELAGLRAELE---ELEKRREEIKKTLEKLKEELEEREKAKKEL-EKLEKALERVEELREKVKKYK 734
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
193-577 |
4.34e-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: 50.44 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 193 EMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEeiscasdQVEKYKLDIAQLEENLKEKNDEILSL 272
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE-------QLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 273 KQSLEENIVILSKQVEDLNVKCQLLEKEKEDhvnrNREHNENLNAEMQNLKQKFileQQEREKLQQKELQIDSLLQQEKE 352
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEE----AEEELAEAEAEIEELEAQI---EQLKEELKALREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 353 LSSSLHQKLcSFQEEMVKEKNLFEEELKQTLDELDKLqqkEEQAERLVKQLEEEAKSRAeelklleeKLKGKEAELEKSS 432
Cdd:TIGR02168 815 LNEEAANLR-ERLESLERRIAATERRLEDLEEQIEEL---SEDIESLAAEIEELEELIE--------ELESELEALLNER 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 433 AAHTQATLLLQEKYDSMVQSLEDVTAQF----ESYKALTAS------EIEDLKLENSSLQEKAAKAGK-NAEDVQHQILA 501
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRselrRELEELREKlaqlelRLEGLEVRIDNLQERLSEEYSlTLEEAEALENK 962
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217272802 502 TESSNQEyvrmlldLQTKSALKETEIKEITVSFLQKITDLQnQLKQQEEDFRKQLEDEEGRKAEKENTTAELTEEI 577
Cdd:TIGR02168 963 IEDDEEE-------ARRRLKRLENKIKELGPVNLAAIEEYE-ELKERYDFLTAQKEDLTEAKETLEEAIEEIDREA 1030
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
246-679 |
5.72e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 246 DQVEKYKLDIAQLEENLKEKNDEILSLKQsLEENIVILSKQVEDLNVKCQLLEKEKEDHvnrnrehneNLNAEMQNLKQK 325
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE-LEEELEELEAELEELREELEKLEKLLQLL---------PLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 326 FILEQQEREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLEE 405
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 406 EAKSRAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQEKYDSMVQSLEDVtaqFESYKALTASEIEDLKLENSSLQEKA 485
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSL---ILTIAGVLFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 486 AKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEitvsFLQKITDLQnQLKQQEEDFRKQLEDEEGRKAE 565
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLE----LLDRIEELQ-ELLREAEELEEELQLEELEQEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 566 KENTTAELTEEINKWRLLYEELynktkpfqlqldafeVEKQALLNEHGAAQEQLNKIRDSYAKLLGHQNLKQkikhvvkL 645
Cdd:COG4717 373 AALLAEAGVEDEEELRAALEQA---------------EEYQELKEELEELEEQLEELLGELEELLEALDEEE-------L 430
|
410 420 430
....*....|....*....|....*....|....
gi 217272802 646 KDENSQLKSEVSKLRCQLAKKKQSETKLQEELNK 679
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELEAELEQ 464
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
326-494 |
5.92e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 326 FILEQQEREKLQQKELQIDSLLQQ-EKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLE 404
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEaKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 405 EEAKSRAEELKLLEEKLKGKEAELEKssaahtqatllLQEKYDSMVQSLEDvtaQFESYKALTASEIEDLKLEN--SSLQ 482
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEK-----------KEEELEELIEEQLQ---ELERISGLTAEEAKEILLEKveEEAR 168
|
170
....*....|..
gi 217272802 483 EKAAKAGKNAED 494
Cdd:PRK12704 169 HEAAVLIKEIEE 180
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
366-680 |
6.14e-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: 49.68 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 366 EEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLEE-EAKSRAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQE 444
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREyEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 445 KYDSMVQSLEDVTAQFESYKALTASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKE 524
Cdd:TIGR02169 263 LEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 525 TEIKEITVSFLQKITDLQNqLKQQEEDFRKQLEDEEGRKAEKENTTAELTEEInkwrllyEELYNKTKPFQLQLDAFEVE 604
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAE-LKEELEDLRAELEEVDKEFAETRDELKDYREKL-------EKLKREINELKRELDRLQEE 414
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217272802 605 KQALLNEHGAAQEQLNKIRDSYAKLlgHQNLKQKIKHVVKLKDENSQLKSEVSKLRCQLAKKKQSETKLQEELNKV 680
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAKINEL--EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
108-624 |
9.68e-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: 49.35 E-value: 9.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 108 DLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSkfsengnqknlriLSLELMKLRNKRETKMRGMMA 187
Cdd:pfam15921 114 DLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKC-------------LKEDMLEDSNTQIEQLRKMML 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 188 KQEGMEMKLQVTQRSLEESQGK------------------------------IAQLEGKLVSIEKEKIDEKSETEKLLEY 237
Cdd:pfam15921 181 SHEGVLQEIRSILVDFEEASGKkiyehdsmstmhfrslgsaiskilreldteISYLKGRIFPVEDQLEALKSESQNKIEL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 238 IeeISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVK--CQLLEKEKEDHVNRN--REHNE 313
Cdd:pfam15921 261 L--LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMymRQLSDLESTVSQLRSelREAKR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 314 NLNAEMQNLKQKFILE-------QQEREKLQQKELQIDSLLQQekeLSSSLHQKLCSFQEEMVKEKNLFEEELKQTLD-- 384
Cdd:pfam15921 339 MYEDKIEELEKQLVLAnselteaRTERDQFSQESGNLDDQLQK---LLADLHKREKELSLEKEQNKRLWDRDTGNSITid 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 385 ----ELDKLQQKEEQAERLVKQLEEEAKsraeelklleeklkgkeAELEKSSAAhtqatllLQEKYDSMvQSLEDVTAQF 460
Cdd:pfam15921 416 hlrrELDDRNMEVQRLEALLKAMKSECQ-----------------GQMERQMAA-------IQGKNESL-EKVSSLTAQL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 461 ESYKALTASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYV----RMLLDLQTKSALK---------ETEI 527
Cdd:pfam15921 471 ESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITklrsRVDLKLQELQHLKnegdhlrnvQTEC 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 528 KEITVSFLQKITDLQnQLKQQEEDFrKQLEDEEGRKA-EKENTTAELTEEINKWRLLYEELY-------NKTKPFQLQLD 599
Cdd:pfam15921 551 EALKLQMAEKDKVIE-ILRQQIENM-TQLVGQHGRTAgAMQVEKAQLEKEINDRRLELQEFKilkdkkdAKIRELEARVS 628
|
570 580
....*....|....*....|....*
gi 217272802 600 AFEVEKQALLNehgAAQEQLNKIRD 624
Cdd:pfam15921 629 DLELEKVKLVN---AGSERLRAVKD 650
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
376-682 |
1.56e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 376 EEELKQTLDELDKLQQKEEQAERLVKQLEEEAKS-------RAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQEKYDS 448
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLEPLERQAEKaeryrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 449 MVQSLEDVTAQFESYKAltasEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIK 528
Cdd:COG1196 258 LEAELAELEAELEELRL----ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 529 EITVSfLQKITDLQNQLKQQEEDFRKQLEDEEGRKAEKENTTAELTEEINKWRLLYEELYNKTKPFQLQLDAFEVEKQAL 608
Cdd:COG1196 334 ELEEE-LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 217272802 609 LNEHGAAQEQLNKIRDSYAKLLghQNLKQKIKHVVKLKDENSQLKSEVSKLRCQLAKKKQSETKLQEELNKVLG 682
Cdd:COG1196 413 LERLERLEEELEELEEALAELE--EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
29-303 |
2.09e-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: 48.14 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 29 LEVLKGPVSFQKSQRFKQQKESKQNLNVDKDTTLPASARKVKSSESKKESQKNDKDLKILEKEIRVLLQERGAQDRRIQD 108
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 109 LETE--------------LEKMEARLNAAL-----REKTSLSANNATLEKQLIEL-TRTNELLKSKFSENGNQKNLRILS 168
Cdd:TIGR02169 763 LEARieeleedlhkleeaLNDLEARLSHSRipeiqAELSKLEEEVSRIEARLREIeQKLNRLTLEKEYLEKEIQELQEQR 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 169 LELMKLRNKREtkmrgmmAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEISCASDQV 248
Cdd:TIGR02169 843 IDLKEQIKSIE-------KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 217272802 249 EKYKLDIAQLEENLKEKNDEILSLKQSLEEnIVILSKQVEDLNVKCQLLEKEKED 303
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGEDEE-IPEEELSLEDVQAELQRVEEEIRA 969
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
164-488 |
2.09e-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: 48.14 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 164 LRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEIsc 243
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI-- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 244 asdqvekyKLDIAQLEENLKEK-NDEILSLKQSLEEniviLSKQVEdlnvKCQLLEKEKEDHVNRNREHNENLNAEMQNL 322
Cdd:TIGR02169 271 --------EQLLEELNKKIKDLgEEEQLRVKEKIGE----LEAEIA----SLERSIAEKERELEDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 323 KQKfiLEQQEREkLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEeLKQTLDELDKLQQKEEQAERLVKQ 402
Cdd:TIGR02169 335 LAE--IEELERE-IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE-LKDYREKLEKLKREINELKRELDR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 403 LEEEAKSRAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQEKYDSMVQSLEDVTAQFESYKALTAsEIEDLKLENSSLQ 482
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE-EYDRVEKELSKLQ 489
|
....*.
gi 217272802 483 EKAAKA 488
Cdd:TIGR02169 490 RELAEA 495
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
307-558 |
2.20e-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: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 307 RNREHNENLNAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELSS---------SLHQKLCSFQEEMvkeknlfeE 377
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvaSAEREIAELEAEL--------E 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 378 ELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQekydsmVQSLEDVT 457
Cdd:COG4913 679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR------LELRALLE 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 458 AQFESY--KALTASEIEDLKLENSSLQEKAAKAGKNAEDVQHQIL-----------ATESSNQEYVRMLLDLQT------ 518
Cdd:COG4913 753 ERFAAAlgDAVERELRENLEERIDALRARLNRAEEELERAMRAFNrewpaetadldADLESLPEYLALLDRLEEdglpey 832
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 217272802 519 ----KSALKETEIkeitvsflQKITDLQNQLKQQEEDFRKQLED 558
Cdd:COG4913 833 eerfKELLNENSI--------EFVADLLSKLRRAIREIKERIDP 868
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
197-568 |
3.43e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 197 QVTQRSLEESQGKIAQLEGKLVSIEK--EKIDEKSE-TEKLLEYIEEISCAsdQVEKYKLDIAQLEENLKEKNDEILSLK 273
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERqlKSLERQAEkAERYKELKAELREL--ELALLVLRLEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 274 Q---SLEENIVILSKQVEDLNVKCQLLEKEKEDhvnrnrehnenLNAEMQNLKQKfileqqereklqqkelqIDSLLQQE 350
Cdd:TIGR02168 253 EeleELTAELQELEEKLEELRLEVSELEEEIEE-----------LQKELYALANE-----------------ISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 351 KELSSSLHQklcsfqeemvkeknlFEEELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEA---E 427
Cdd:TIGR02168 305 QILRERLAN---------------LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAeleE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 428 LEKSSAAHTQATLLLQEKYDSMVQSLEDVTAQFESYKAltasEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQ 507
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA----RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 217272802 508 EyvRMLLDLQTKSALKETEIKEITVSFLQKITDLQnQLKQQEEDFRKQLEDEEGRKAEKEN 568
Cdd:TIGR02168 446 E--EELEELQEELERLEEALEELREELEEAEQALD-AAERELAQLQARLDSLERLQENLEG 503
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
76-680 |
7.03e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 7.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 76 KESQKNDKDLKILEKEIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLkskf 155
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI---- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 156 sengNQKNLRILSLElmklrnkretkmrgmmAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKsETEKLL 235
Cdd:PRK03918 241 ----EELEKELESLE----------------GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE-EYIKLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 236 EYIEEISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEE---NIVILSKQVEDLNVKCQLLEKEKEDHVNRNR--- 309
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEElkkKLKELEKRLEELEERHELYEEAKAKKEELERlkk 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 310 ----EHNENLNAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELSSSLHQK-----LCSFQEEMVKEKNLFEE--- 377
Cdd:PRK03918 380 rltgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEEyta 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 378 ELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEAE-------LEKSSAAHTQATLLLQE--KYDS 448
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEeklkkynLEELEKKAEEYEKLKEKliKLKG 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 449 MVQSLED---VTAQFESYKALTASEIEDLKLENSSLQEKAAKAG-KNAEDVQHQILATESSNQEYVRM------LLDLQT 518
Cdd:PRK03918 540 EIKSLKKeleKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELkdaekeLEREEK 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 519 KSALKETEIKEITVSFLQKITDLQnQLKQQEEDFRKQLEDEEGRKAEKENTtaELTEEINKWRLLYEELYNKTKPFQLQL 598
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLE-ELRKELEELEKKYSEEEYEELREEYL--ELSRELAGLRAELEELEKRREEIKKTL 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 599 DAFEVEKQallnEHGAAQEQLNKIRDSYAKLlghQNLKQKIKHVVKLKDENSQLKSE--VSKLRCQLAKKKQSETKLQEE 676
Cdd:PRK03918 697 EKLKEELE----EREKAKKELEKLEKALERV---EELREKVKKYKALLKERALSKVGeiASEIFEELTEGKYSGVRVKAE 769
|
....
gi 217272802 677 LNKV 680
Cdd:PRK03918 770 ENKV 773
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
73-407 |
7.09e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 73 ESKKESQKNDKDLKILEKEIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLK 152
Cdd:PRK02224 248 ERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 153 SKFSE--------NGNQKNLRILSLELmklrnkrETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEK 224
Cdd:PRK02224 328 DRLEEcrvaaqahNEEAESLREDADDL-------EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 225 IDEKSETEKLLEYIEEISCASDQVEKyklDIAQLEENLKEKNDEILSLKQSLEENivilskqvedlnvKCQLLEKEKED- 303
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREERDELRE---REAELEATLRTARERVEEAEALLEAG-------------KCPECGQPVEGs 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 304 -HVNR---NREHNENLNAEMQNLKqkfileqQEREKLQQKELQIDSLLQQEKELSSSLHQ-----KLCSFQEEMVKEKNL 374
Cdd:PRK02224 465 pHVETieeDRERVEELEAELEDLE-------EEVEEVEERLERAEDLVEAEDRIERLEERredleELIAERRETIEEKRE 537
|
330 340 350
....*....|....*....|....*....|....
gi 217272802 375 FEEELKQTLDELD-KLQQKEEQAERLVKQLEEEA 407
Cdd:PRK02224 538 RAEELRERAAELEaEAEEKREAAAEAEEEAEEAR 571
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
106-301 |
1.27e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 106 IQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELtrtnELLKSkfsengnqknlriLSLELMKLRNKRETKMR-G 184
Cdd:PRK05771 88 IKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERL----EPWGN-------------FDLDLSLLLGFKYVSVFvG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 185 MMAKQEGMEMKLQVTQRSLEEsqgkIAQLEGK---LVSIEKEKIDEKSETEKLLEY----IEEISCASDQVEKYKLDIAQ 257
Cdd:PRK05771 151 TVPEDKLEELKLESDVENVEY----ISTDKGYvyvVVVVLKELSDEVEEELKKLGFerleLEEEGTPSELIREIKEELEE 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 217272802 258 LEENLKEKNDEILSLKQSLEENIV----ILSKQVEDLNVKCQLLEKEK 301
Cdd:PRK05771 227 IEKERESLLEELKELAKKYLEELLalyeYLEIELERAEALSKFLKTDK 274
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
68-406 |
1.53e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 68 KVKSSESKKESQKNDKDLKILEKEIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRT 147
Cdd:PRK02224 334 RVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 148 NELLKSKFSE-NGNQKNLRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEkekiD 226
Cdd:PRK02224 414 LEELREERDElREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLE----E 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 227 EKSETEKLLEYIEEISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEEniviLSKQVEDLNVKCQllekEKEDHVN 306
Cdd:PRK02224 490 EVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE----LRERAAELEAEAE----EKREAAA 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 307 RNREHNENLNAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELSSsLHQKLCSFQE------EMVKEKNLFEEELK 380
Cdd:PRK02224 562 EAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIER-LREKREALAElnderrERLAEKRERKRELE 640
|
330 340
....*....|....*....|....*...
gi 217272802 381 QTLDE--LDKLQQKEEQAERLVKQLEEE 406
Cdd:PRK02224 641 AEFDEarIEEAREDKERAEEYLEQVEEK 668
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
222-572 |
1.61e-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: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 222 KEKIDEKSETEKLLE-YIEEISCASDQVEKYKLDIAQLEENLKEKND----EILSLKQSLEENIVILSKQVEDLNVKCQL 296
Cdd:TIGR02169 176 LEELEEVEENIERLDlIIDEKRQQLERLRREREKAERYQALLKEKREyegyELLKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 297 LEKEKEDHVNRNREHNENLNAEMQNLKQKFILEQQE-REKLQQKELQIDSLLQQEKELSSSlhqklcsfQEEMVKEKNLF 375
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEIASLERSIAEKERE--------LEDAEERLAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 376 EEELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRAEELKLLEEKLkgkeAELEKSSAAhtqatllLQEKYDSMVQSLED 455
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL----EEVDKEFAE-------TRDELKDYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 456 VTaqfesykaltaSEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITvsfl 535
Cdd:TIGR02169 397 LK-----------REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA---- 461
|
330 340 350
....*....|....*....|....*....|....*..
gi 217272802 536 QKITDLQNQLKQQEEDFRKqLEDEEgRKAEKENTTAE 572
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDR-VEKEL-SKLQRELAEAE 496
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
313-578 |
1.93e-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: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 313 ENLNAEMQNLKQKFILEQQEREKLQQKELQID---SLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTLDELDKL 389
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSrqiSALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 390 QQKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEAEL-----------------EKSSAAHTQATLLLQEKYDSMVQS 452
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaanlrerleslERRIAATERRLEDLEEQIEELSED 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 453 LEDVTAQFESYKALTA---SEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKE 529
Cdd:TIGR02168 854 IESLAAEIEELEELIEeleSELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 217272802 530 ITVSFLQKITDLQNQLKQQEEDFRKQLEDEEGRKAEKENTTAELTEEIN 578
Cdd:TIGR02168 934 LEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
228-459 |
2.16e-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: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 228 KSETEKLLEYIEEiscasdQVEKYKLDIAQLEENL---KEKNDEIlslkqSLEENIVILSKQVEDLNVKCQLLEKEKEDH 304
Cdd:COG3206 170 REEARKALEFLEE------QLPELRKELEEAEAALeefRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 305 VNRNREHNENLNAEMQNLKQkfILEQQEREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTLD 384
Cdd:COG3206 239 EARLAALRAQLGSGPDALPE--LLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 217272802 385 ELDKLQQKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEAELEkssaahtqatlLLQEKYDSMVQSLEDVTAQ 459
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE-----------VARELYESLLQRLEEARLA 380
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
330-577 |
2.45e-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: 44.67 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 330 QQEREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQ---EEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLEEE 406
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEkeiEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 407 AKSRAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQEKY----DSMVQSLEDVTAQFESYKALTASEIEDLKLENSSLQ 482
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEvsriEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 483 EKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITvSFLQKITDLQNQLKQQEEDFRKQLEDEEGR 562
Cdd:TIGR02169 847 EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE-AQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
250
....*....|....*
gi 217272802 563 KAEKENTTAELTEEI 577
Cdd:TIGR02169 926 LEALEEELSEIEDPK 940
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
66-708 |
2.88e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 66 ARKVKSSESKKESQKNDkDLKILEKEIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELT 145
Cdd:PTZ00121 1157 ARKAEDARKAEEARKAE-DAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEA 1235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 146 RTNELLKSKFSENGNQKNLRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQGKiaqlEGKLVSIEKEKI 225
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE----EKKKADEAKKKA 1311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 226 DEKSETEKLLEYIEEiscasdqvEKYKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLEKEKEDHV 305
Cdd:PTZ00121 1312 EEAKKADEAKKKAEE--------AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA 1383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 306 NRNREHNEnlnaEMQNLKQKFILEQQEREKLQQKElqidsllqQEKELSSSLHQKlcsfQEEMVKEKNLFEE-ELKQTLD 384
Cdd:PTZ00121 1384 KKKAEEKK----KADEAKKKAEEDKKKADELKKAA--------AAKKKADEAKKK----AEEKKKADEAKKKaEEAKKAD 1447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 385 ELDKLQQKEEQAERLVKQLEEEAKS---RAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQEKYDSMVQSLEDVTAQfE 461
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKAdeaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD-E 1526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 462 SYKALTASEIEDLKlenSSLQEKAAKAGKNAEDVQ--HQILATESSNQEYVRMLLDLQTKSALKETE---IKEITVSFLQ 536
Cdd:PTZ00121 1527 AKKAEEAKKADEAK---KAEEKKKADELKKAEELKkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEearIEEVMKLYEE 1603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 537 KITDLQNQLKQQEEDFRK--QLEDEEGRKAEKENTTAELTEEINKW-RLLYEELYNKTKPFQLQLDAFEVEKQA-----L 608
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKaeELKKAEEEKKKVEQLKKKEAEEKKKAeELKKAEEENKIKAAEEAKKAEEDKKKAeeakkA 1683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 609 LNEHGAAQEQLNKIRDSYAK---LLGHQNLKQKIKHVVKLKDENSQLKSEVSKLRCQLAKKKQSETKLQE-ELNKVLGIK 684
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKaeeLKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEeEKKKIAHLK 1763
|
650 660
....*....|....*....|....
gi 217272802 685 HFDPSKAFHHESKENFALKTPLKE 708
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEELDE 1787
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
85-580 |
2.91e-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: 44.19 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 85 LKILEKEIRVLLQERGAQDRRIQ---DLETELEKMEARLNAALREKTSL---SANNATLEKQ-LIELTRTNELLKSKFSE 157
Cdd:TIGR00618 395 LQSLCKELDILQREQATIDTRTSafrDLQGQLAHAKKQQELQQRYAELCaaaITCTAQCEKLeKIHLQESAQSLKEREQQ 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 158 NGNQKNLRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQRSLEESQG---KIAQLEGKLVSIEKEKIDEKSETEKL 234
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPltrRMQRGEQTYAQLETSEEDVYHQLTSE 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 235 LEYIEEISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNEN 314
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHL 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 315 LNAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEE 394
Cdd:TIGR00618 635 QQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIE 714
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 395 QAERLVKQLEEEAKSRaeelklleeklkgkEAELEKSSAAHTQATLLLQEKYDSMVQSLEDvtAQFESYKALTASEIEDL 474
Cdd:TIGR00618 715 EYDREFNEIENASSSL--------------GSDLAAREDALNQSLKELMHQARTVLKARTE--AHFNNNEEVTAALQTGA 778
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 475 KLENssLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITVSFLQKITDLQNQLKQQEEdfrk 554
Cdd:TIGR00618 779 ELSH--LAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLL---- 852
|
490 500
....*....|....*....|....*.
gi 217272802 555 QLEDEEGRKAEKENTTAELTEEINKW 580
Cdd:TIGR00618 853 KYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
39-494 |
3.29e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 39 QKSQRFKQQKESKQNLNVDKDTTLPASAR-KVKSSESKKESQKNDKDLKILEKEIRVLLQERGAQDRRIQDLETELEKME 117
Cdd:PTZ00121 1284 KKAEEKKKADEAKKAEEKKKADEAKKKAEeAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAE 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 118 ARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSENGNQKNLRILSLELMK---LRNKRETKMRGMMAKQEGMEM 194
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKadeAKKKAEEKKKADEAKKKAEEA 1443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 195 KLQVTQRSLEESQGKIAQL-----EGKLVSIEKEKIDEKSETEKLLEYIEEISCASDQVEKYKLDIAQLEENLK-EKNDE 268
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEEAkkkaeEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKaEEAKK 1523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 269 ILSLKQSLEENIVILSKQVEDLNVKCQLLEKEKEDHVNRNREHNENLNAEmqnlKQKFILEQQEREKLQQKELQIDSLLQ 348
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE----EDKNMALRKAEEAKKAEEARIEEVMK 1599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 349 QEKELSSSLHQKLCSFQEEMVKEKNLF-EEELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEAE 427
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 217272802 428 LEKSSAAHTQATLLLQEKYDSMVQSledvtAQFESYKALTASEIEDLKLENSSLQEKAAKAGKNAED 494
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKA-----EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
239-406 |
3.34e-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: 44.07 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 239 EEISCASDQVEKYKLDIAQL-----EENLKEKNDEILSLKQSLEENIviLSKQVEDLNVKcqllekEKEDHVNRNREHNE 313
Cdd:pfam06160 237 KEIQQLEEQLEENLALLENLeldeaEEALEEIEERIDQLYDLLEKEV--DAKKYVEKNLP------EIEDYLEHAEEQNK 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 314 NLNAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELSSSLHQK------LCSFQEEMVKEKNLFEEELKQTLDELD 387
Cdd:pfam06160 309 ELKEELERVQQSYTLNENELERVRGLEKQLEELEKRYDEIVERLEEKevayseLQEELEEILEQLEEIEEEQEEFKESLQ 388
|
170
....*....|....*....
gi 217272802 388 KLQQKEEQAERLVKQLEEE 406
Cdd:pfam06160 389 SLRKDELEAREKLDEFKLE 407
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
232-475 |
5.79e-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: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 232 EKLLEYIEEISCASDQVEKYKLDIAQLEEnLKEKNDEILSLKQSLEENIVILSK-QVEDLNVKCQLLEKEKEdhvnRNRE 310
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEYLRAAlRLWFAQRRLELLEAELE----ELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 311 HNENLNAEMQNLKQKFILEQQEREKLQQKELQIDslLQQEKELssslhqklcsfqeemvkeknlfEEELKQTLDELDKLQ 390
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNG--GDRLEQL----------------------EREIERLERELEERE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 391 QKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEAELEKSSAAhtqatllLQEKYDSMVQSLEDVTAQFESykalTASE 470
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA-------LEEALAEAEAALRDLRRELRE----LEAE 427
|
....*
gi 217272802 471 IEDLK 475
Cdd:COG4913 428 IASLE 432
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
79-262 |
9.01e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 79 QKNDKDLKILEKEIRVLLQERGAQDRRIQDLETELEKMEARLNA--ALREKTSLSANNATLEKQLIELTRTNELLkskfs 156
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAEREIAELEAELERL----- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 157 ENGNQKnLRILSLELMKLRNKRET---KMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEK 233
Cdd:COG4913 681 DASSDD-LAALEEQLEELEAELEEleeELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
170 180 190
....*....|....*....|....*....|
gi 217272802 234 LLEYIEEISCA-SDQVEKYKLDIAQLEENL 262
Cdd:COG4913 760 GDAVERELRENlEERIDALRARLNRAEEEL 789
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
464-675 |
1.37e-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: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 464 KALTASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITvsflQKITDLQN 543
Cdd:TIGR02168 227 LALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA----NEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 544 Q---LKQQEEDFRKQLEDEEGRKAEKENTTAELTEEINKWRLLYEELYNKTKPFQLQLDAFEVEKQALLNEHGAAQEQLN 620
Cdd:TIGR02168 303 QkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 217272802 621 KIRDSYAKLLghQNLKQKIKHVVKLKDENSQLKSEVSKLRCQLAK--KKQSETKLQE 675
Cdd:TIGR02168 383 TLRSKVAQLE--LQIASLNNEIERLEARLERLEDRRERLQQEIEEllKKLEEAELKE 437
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
84-241 |
1.44e-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: 41.06 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 84 DLKILEKEIRVLLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIELTRTNELLKSKFSENGNQKN 163
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 164 LRILSLELMKLRNKR---ETKMRGMMAKQEGMEMKLQVTQRSLEESQGKIAQLEGKLvsiEKEKIDEKSETEKLLEYIEE 240
Cdd:COG1579 91 YEALQKEIESLKRRIsdlEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAELEELEAEREE 167
|
.
gi 217272802 241 I 241
Cdd:COG1579 168 L 168
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
95-395 |
1.46e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 95 LLQERGAQDRRIQDLETELEKMEARLNAALREKTSLSANNATLEKQLIElTRTNELLKSKFSENGN-----QKNLRILSL 169
Cdd:PRK11281 71 LLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLS-TLSLRQLESRLAQTLDqlqnaQNDLAEYNS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 170 ELMKLRNKRETkmrgmmakqegmemklqvTQRSLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLeyieeiscasdQVE 249
Cdd:PRK11281 150 QLVSLQTQPER------------------AQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLL-----------QAE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 250 KYKLDiAQLEENlkekndeilslKQSLEEN---IVILSKQVEDLNVKCQLLEKEKEDhvnrnreHNENLNAEMQNLKQKF 326
Cdd:PRK11281 201 QALLN-AQNDLQ-----------RKSLEGNtqlQDLLQKQRDYLTARIQRLEHQLQL-------LQEAINSKRLTLSEKT 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 217272802 327 ILEQQEREKLQQkeLQIDSLLQQEKELSSSLHQKLCSFQEEMvkeKNLFEEEL--KQTLDELDKLQQK-EEQ 395
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 ... |
44-576 |
2.41e-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: 41.25 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 44 FKQQKESKQNLNVDKDTTLPASARKVKSSESKKESQKNDKdlkilEKEIRVLLQERGAQDRRIQDLETELEKMEARLNAa 123
Cdd:pfam05483 199 FEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDK-----EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQ- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 124 LREKTSLSANN-ATLEKQLIELTRTNE-----LLKSKFSENGNQKNLRILSLELMKLRNKRETKMRGMMAKQEG------ 191
Cdd:pfam05483 273 LEEKTKLQDENlKELIEKKDHLTKELEdikmsLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAhsfvvt 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 192 --------MEMKLQVTQRSLE--ESQGKIAQLEGKLVSIEKEKIDE-KSETEKLLEYIEEISCASDQVEKYKLDIAQLEE 260
Cdd:pfam05483 353 efeattcsLEELLRTEQQRLEknEDQLKIITMELQKKSSELEEMTKfKNNKEVELEELKKILAEDEKLLDEKKQFEKIAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 261 NLKEKNDEILSLKQSLEENIVIL--------------SKQVEDLNVKCQ---LLEKEKEDHVNRNREHNENLNAEMQNLK 323
Cdd:pfam05483 433 ELKGKEQELIFLLQAREKEIHDLeiqltaiktseehyLKEVEDLKTELEkekLKNIELTAHCDKLLLENKELTQEASDMT 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 324 QKFILEQQEREKLQQKELQIDSLLQQEKELSSSLHQKLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQL 403
Cdd:pfam05483 513 LELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 404 EEEA---KSRAEELKLLEEKLKGKEAELEKSSAAHTQATLLLQEKYDSMVQSLEDVTAQFESYKALTASEIEDLKLENSS 480
Cdd:pfam05483 593 ENKCnnlKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEK 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 481 LQEKAAKAGKNAEDV-----------QHQILA----TESSNQEYVRMLLDLQTKSAL---KETEIKEITVSFLQKITDLQ 542
Cdd:pfam05483 673 LLEEVEKAKAIADEAvklqkeidkrcQHKIAEmvalMEKHKHQYDKIIEERDSELGLyknKEQEQSSAKAALEIELSNIK 752
|
570 580 590
....*....|....*....|....*....|....
gi 217272802 543 NQLKQQEEDFRKQLEDEEGRKAEKENTTAELTEE 576
Cdd:pfam05483 753 AELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
467-680 |
3.99e-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: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 467 TASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEITvsflQKITDLQNQLK 546
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE----KEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 547 QQEEDFRKQLedeegRKAEKENTTAELTEEINK------------WRLLYEELYNKTKPFQLQLDAFEVEKQALLNEHGA 614
Cdd:COG4942 101 AQKEELAELL-----RALYRLGRQPPLALLLSPedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217272802 615 AQEQLNKIRDSYAKLLGHQNLKQKIkhvvklkdeNSQLKSEVSKLRCQLAKKKQSETKLQEELNKV 680
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKL---------LARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
334-555 |
4.25e-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: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 334 EKLQQKELQIDSLLQQEKELSSSLhQKLCSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRAEE 413
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKEL-AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 414 LKLLEEKLKGKEAELEKSSAAHTQATLLLQEKYDSMVQSLEDVTAQFESYKALTA---SEIEDLKLENSSLQEKAAKAGK 490
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEelrADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 217272802 491 NAEDVQHQILATESSNQEYVRMLLDLQTKSALKETEIKEItvsfLQKITDLQNQLKQQEEDFRKQ 555
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL----QQEAEELEALIARLEAEAAAA 239
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
209-677 |
7.74e-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: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 209 KIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEENIVILSKQVE 288
Cdd:TIGR04523 195 KLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 289 DLNVKCQLLeKEKEDHVNRNREHNENLNAEMQNLKQKFILEQ--QEREKLQQKELQIDSLLQQEKELSSSLhQKLCSFQE 366
Cdd:TIGR04523 275 ELEQNNKKI-KELEKQLNQLKSEISDLNNQKEQDWNKELKSElkNQEKKLEEIQNQISQNNKIISQLNEQI-SQLKKELT 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 367 EMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEAELEKssaahtqatllLQEKY 446
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK-----------LQQEK 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 447 DSMVQSLEDVTAQFESYKaltaSEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSALKETE 526
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNN----SEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 527 IKEITvsflQKITDLQNQ---LKQQEEDFRKQLEDEEGRKAEKENTTAELTEEINK--WRLLYEELYNKTKPFQLQLDAF 601
Cdd:TIGR04523 498 LKKLN----EEKKELEEKvkdLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEEL 573
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217272802 602 EVEKQALLNEHGAAQEQLNKIRDSYAKLLghQNLKQKIKHVVKLKDENSQLKSEVSKLRCQLAKKKQSETKLQEEL 677
Cdd:TIGR04523 574 KQTQKSLKKKQEEKQELIDQKEKEKKDLI--KEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
45-587 |
9.44e-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: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 45 KQQKESKQNLNVDKDTTLPASARKVKSSESKKESQKNDKDLKILEKEIRVLLQERGAQDRRIQDLETELEKMEARLNAAL 124
Cdd:pfam02463 495 LEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELP 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 125 REKTSLSANN---ATLEKQLIELTRTNELLKSKFSENGNQKNLRILSLELMKLRNKRETKMRGMMAKQEGMEMKLQVTQR 201
Cdd:pfam02463 575 LGARKLRLLIpklKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSL 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 202 SLEESQGKIAQLEGKLVSIEKEKIDEKSETEKLLEYIEEISCASDQVEKYKLDIAQLEENLKEKNDEILSLKQSLEENIV 281
Cdd:pfam02463 655 EEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKI 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 282 ILSKQVEDLNVKCQLLEKEKEDHVNRNREHNENLNAEMQNLKQKFILEQQEREKLQQKELQIDSLLQQEKELSSSLHQKL 361
Cdd:pfam02463 735 NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEA 814
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 362 CSFQEEMVKEKNLFEEELKQTLDELDKLQQKEEQAERLVKQLEEEAKSRAEELKLLEEKLKGKEAELEKSSAAHTQATLL 441
Cdd:pfam02463 815 ELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEK 894
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217272802 442 LQEKYDSMVQSLEDVTAQFESYKALTASEIEDLKLENSSLQEKAAKAGKNAEDVQHQILATESSNQEYVRMLLDLQTKSA 521
Cdd:pfam02463 895 EKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGK 974
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 217272802 522 LKETEIKEITVSFLQKITDLQNQLKQQEEDFRKQLEDEEGRKAEKENTTAELTEEINKWRLLYEEL 587
Cdd:pfam02463 975 VNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYL 1040
|
|
| |
