|
Name |
Accession |
Description |
Interval |
E-value |
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
226-456 |
1.28e-24 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 107.84 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 226 QLKESFQQLQLERDECAEHIEGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVP-- 303
Cdd:pfam15070 1 QLMESLKQLQTERDQYAENLKEEGAVWQQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEQPPAgp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 304 SEVE------LQHLRKELERVAGELQSQVKNNQHISLLNrrqeERIREQEERLRKQEERLQEQHEKLR------------ 365
Cdd:pfam15070 81 SEEEqrlqeeAEQLQKELEALAGQLQAQVQDNEQLSRLN----QEQEQRLLELERAAERWGEQAEDRKqiledmqsdrat 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 366 -------------QLAKPQSVF--------------------------------EEL----------------------- 377
Cdd:pfam15070 157 isralsqnrelkeQLAELQNGFvkltnenmeltsalqseqhvkkelakklgqlqEELgelketlelksqeaqslqeqrdq 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 378 ----------------------------------------------------------EHLEAASQQNQQLTAQLSLMAL 399
Cdd:pfam15070 237 ylahlqqyvaayqqlasekeelhkqyllqtqlmdrlqheevqgkvaaemarqelqetqERLEALTQQNQQLQAQLSLLAN 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767985209 400 PGEGHGGEHlDSEGEEAPRPMPSVPEDPESREAMSSFMDHL-----KEKADLSELVKKQELR 456
Cdd:pfam15070 317 PGEGDGLES-EEEEEEAPRPSLSIPEDFESREAMVAFFNSAlaqaeEERAELRRQLKEQKRR 377
|
|
| GM130_C |
pfam19046 |
GM130 C-terminal binding motif; This entry represents the C-terminal motif from the GM130 ... |
570-609 |
3.89e-15 |
|
GM130 C-terminal binding motif; This entry represents the C-terminal motif from the GM130 protein that is bound by the GRASP65 PDZ domain pfam04495.
Pssm-ID: 465957 Cd Length: 46 Bit Score: 69.72 E-value: 3.89e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767985209 570 PLLDKPTAQPIV------QDHQEHPGLGSNCCVPLFCWAWLPRRRR 609
Cdd:pfam19046 1 SPPENPTAQQIMqllpeiQNPQEHPGLGSNPCIPFFYRADENDEVK 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
80-376 |
4.79e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 80 QERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYF 159
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 160 EEESKDLAVRLQHSLQckgELESALSAVIATEKKKANQLSscskahtewELEQSLQDQALLKAQLTQLKESFQQLQLERd 239
Cdd:COG1196 308 EERRRELEERLEELEE---ELAELEEELEELEEELEELEE---------ELEEAEEELEEAEAELAEAEEALLEAEAEL- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 240 ecAEHIEGERARWHQRMSKMSQEIcTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELQHLRKELERVA 319
Cdd:COG1196 375 --AEAEEELEELAEELLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 767985209 320 GELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVFEE 376
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
80-374 |
2.71e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.54 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 80 QERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYF 159
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 160 EEESKDLAVRLQHSLQCKGELEsalsAVIATEKKKANQLSScSKAHTEWELEQSLQDQALLKAQLTQLKESFQQLQLERD 239
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELE----AQLEELESKLDELAE-ELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 240 ECAEHIEGERARWHQRMSKMSQ---EICTLKKEKQQDMRRVEELERSLSKL-----KNQMAEPLPPEPPAVPSEVELQHL 311
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASlnnEIERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEE 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767985209 312 RKELERVAGELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVF 374
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL 518
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
86-290 |
4.33e-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: 55.54 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 86 LDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKD 165
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 166 LAVRLQHSLQcKGELESALSAVIATEKKKA----NQLSSCSKAHTEwELEQSLQDQALLKAQLTQLKESFQQLQLERDEC 241
Cdd:COG4942 109 LLRALYRLGR-QPPLALLLSPEDFLDAVRRlqylKYLAPARREQAE-ELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767985209 242 AEHIEGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQ 290
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
92-327 |
8.47e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 8.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 92 KISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEE-------ESK 164
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQeienvksELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 165 DLAVRLQHSLQCKGELESALSAVIATE-----KKKANQLSSCSKAHTEWE-----LEQSLQDQALLKAQLTQLKesfQQL 234
Cdd:TIGR02169 762 ELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEarlreIEQKLNRLTLEKEYLEKEI---QEL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 235 QLERDECAEHIEGERARWHQ---RMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELQHL 311
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENlngKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
250
....*....|....*.
gi 767985209 312 RKELERVAGELQSQVK 327
Cdd:TIGR02169 919 LSELKAKLEALEEELS 934
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
70-318 |
3.04e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 70 ATLKDLESPCQERAVVLDST---SVKISRLKNTIKSLKQQKKQVE-HQLEEEKKANNERQKAERE---LEVQIQTL---I 139
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVlkkESELIKLKELAEQLKELEEKLKkYNLEELEKKAEEYEKLKEKlikLKGEIKSLkkeL 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 140 IQKEELNTDLYHMERSLRYFEEESKDLAVRLQH-SLQCKGELESALSAViatEK--KKANQLSSCSK---------AHTE 207
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEElGFESVEELEERLKEL---EPfyNEYLELKDAEKelereekelKKLE 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 208 WELEQSLQDQALLKAQLTQLKESFQQLQLERDEcaehieGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKL 287
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSE------EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
250 260 270
....*....|....*....|....*....|.
gi 767985209 288 KNQMAEPLPPEPpavpsevELQHLRKELERV 318
Cdd:PRK03918 700 KEELEEREKAKK-------ELEKLEKALERV 723
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
92-320 |
3.46e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.58 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 92 KISRLKNTIKSLKQQKKQVEhqlEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKDLAVRLQ 171
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQME---LEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 172 HSLQCKGELESALSAVIATEKKkANQLSSCSK-----------------AHTEWELEQSLQDQALLKAQLTQLKESFQQL 234
Cdd:pfam05557 80 LKKKYLEALNKKLNEKESQLAD-AREVISCLKnelselrrqiqraelelQSTNSELEELQERLDLLKAKASEAEQLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 235 QLERDECAEHIegerarwhQRMSKMSQEICT------LKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVEL 308
Cdd:pfam05557 159 EKQQSSLAEAE--------QRIKELEFEIQSqeqdseIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEV 230
|
250
....*....|..
gi 767985209 309 QHLRKELERVAG 320
Cdd:pfam05557 231 EDLKRKLEREEK 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
92-459 |
1.58e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 92 KISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAErelEVQIQTLIIQK-EELNTDLYHMERSlryfeEESKDLAVRL 170
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD---ELKKAAAAKKKaDEAKKKAEEKKKA-----DEAKKKAEEA 1443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 171 QHSLQCKGELESALSA----VIATEKKKANQLSSCSKAHTEWELEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIE 246
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAeeakKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 247 GERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELqhLRKELERVAGELQSQV 326
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE--AKKAEEARIEEVMKLY 1601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 327 KNNQHISLLNRRQEERIREQEERLRKQEErlqEQHEKLRQLAKPQSVFEELEHLEAASQQNQQLTAQLSLMALPGEGHGG 406
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEE---EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE 1678
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 767985209 407 EHLDSEGEEAPRPMPSVPEDPESREAMSSFMDHLKEKADLSELVKKQELRFIQ 459
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIK 1731
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
226-456 |
1.28e-24 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 107.84 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 226 QLKESFQQLQLERDECAEHIEGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVP-- 303
Cdd:pfam15070 1 QLMESLKQLQTERDQYAENLKEEGAVWQQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEQPPAgp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 304 SEVE------LQHLRKELERVAGELQSQVKNNQHISLLNrrqeERIREQEERLRKQEERLQEQHEKLR------------ 365
Cdd:pfam15070 81 SEEEqrlqeeAEQLQKELEALAGQLQAQVQDNEQLSRLN----QEQEQRLLELERAAERWGEQAEDRKqiledmqsdrat 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 366 -------------QLAKPQSVF--------------------------------EEL----------------------- 377
Cdd:pfam15070 157 isralsqnrelkeQLAELQNGFvkltnenmeltsalqseqhvkkelakklgqlqEELgelketlelksqeaqslqeqrdq 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 378 ----------------------------------------------------------EHLEAASQQNQQLTAQLSLMAL 399
Cdd:pfam15070 237 ylahlqqyvaayqqlasekeelhkqyllqtqlmdrlqheevqgkvaaemarqelqetqERLEALTQQNQQLQAQLSLLAN 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767985209 400 PGEGHGGEHlDSEGEEAPRPMPSVPEDPESREAMSSFMDHL-----KEKADLSELVKKQELR 456
Cdd:pfam15070 317 PGEGDGLES-EEEEEEAPRPSLSIPEDFESREAMVAFFNSAlaqaeEERAELRRQLKEQKRR 377
|
|
| GM130_C |
pfam19046 |
GM130 C-terminal binding motif; This entry represents the C-terminal motif from the GM130 ... |
570-609 |
3.89e-15 |
|
GM130 C-terminal binding motif; This entry represents the C-terminal motif from the GM130 protein that is bound by the GRASP65 PDZ domain pfam04495.
Pssm-ID: 465957 Cd Length: 46 Bit Score: 69.72 E-value: 3.89e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 767985209 570 PLLDKPTAQPIV------QDHQEHPGLGSNCCVPLFCWAWLPRRRR 609
Cdd:pfam19046 1 SPPENPTAQQIMqllpeiQNPQEHPGLGSNPCIPFFYRADENDEVK 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
80-376 |
4.79e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 80 QERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYF 159
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 160 EEESKDLAVRLQHSLQckgELESALSAVIATEKKKANQLSscskahtewELEQSLQDQALLKAQLTQLKESFQQLQLERd 239
Cdd:COG1196 308 EERRRELEERLEELEE---ELAELEEELEELEEELEELEE---------ELEEAEEELEEAEAELAEAEEALLEAEAEL- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 240 ecAEHIEGERARWHQRMSKMSQEIcTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELQHLRKELERVA 319
Cdd:COG1196 375 --AEAEEELEELAEELLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 767985209 320 GELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVFEE 376
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
80-374 |
2.71e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.54 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 80 QERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYF 159
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 160 EEESKDLAVRLQHSLQCKGELEsalsAVIATEKKKANQLSScSKAHTEWELEQSLQDQALLKAQLTQLKESFQQLQLERD 239
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELE----AQLEELESKLDELAE-ELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 240 ECAEHIEGERARWHQRMSKMSQ---EICTLKKEKQQDMRRVEELERSLSKL-----KNQMAEPLPPEPPAVPSEVELQHL 311
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASlnnEIERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEE 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767985209 312 RKELERVAGELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVF 374
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
96-418 |
4.67e-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: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 96 LKNTIKSLKQQKKQ----VEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFE---EESKDLAV 168
Cdd:COG1196 198 LERQLEPLERQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEaelEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 169 RLQHSLQCKGELESALSAVIAT-------EKKKANQLSScSKAHTEWELEQSLQDQALLKAQLTQLKESFQQLQLERDEC 241
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARleqdiarLEERRRELEE-RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 242 AEHIEGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELQHLRKELERVAGE 321
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 322 L----QSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVFEELEHLEAASQQNQQLTAQLSLM 397
Cdd:COG1196 437 EeeeeEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
330 340
....*....|....*....|.
gi 767985209 398 ALPGEGHGGEHLDSEGEEAPR 418
Cdd:COG1196 517 AGLRGLAGAVAVLIGVEAAYE 537
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
86-290 |
4.33e-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: 55.54 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 86 LDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKD 165
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 166 LAVRLQHSLQcKGELESALSAVIATEKKKA----NQLSSCSKAHTEwELEQSLQDQALLKAQLTQLKESFQQLQLERDEC 241
Cdd:COG4942 109 LLRALYRLGR-QPPLALLLSPEDFLDAVRRlqylKYLAPARREQAE-ELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767985209 242 AEHIEGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQ 290
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
92-327 |
8.47e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 8.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 92 KISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEE-------ESK 164
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQeienvksELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 165 DLAVRLQHSLQCKGELESALSAVIATE-----KKKANQLSSCSKAHTEWE-----LEQSLQDQALLKAQLTQLKesfQQL 234
Cdd:TIGR02169 762 ELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEarlreIEQKLNRLTLEKEYLEKEI---QEL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 235 QLERDECAEHIEGERARWHQ---RMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELQHL 311
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENlngKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
250
....*....|....*.
gi 767985209 312 RKELERVAGELQSQVK 327
Cdd:TIGR02169 919 LSELKAKLEALEEELS 934
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
92-432 |
2.56e-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: 53.91 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 92 KISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKDLAVRLQ 171
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 172 HSLQCKGELESALSAV---IATEKKKANQLSScskahtewELEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIEGE 248
Cdd:TIGR02168 765 ELEERLEEAEEELAEAeaeIEELEAQIEQLKE--------ELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 249 RARW---HQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEplppeppavpSEVELQHLRKELERVAGELQSq 325
Cdd:TIGR02168 837 ERRLedlEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS----------LEEALALLRSELEELSEELRE- 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 326 vknnqhisllnrrqeerireQEERLRKQEERLQEQHEKLRQLAkpqsvfeelEHLEAASQQNQQLTAQLSlmalpgeghg 405
Cdd:TIGR02168 906 --------------------LESKRSELRRELEELREKLAQLE---------LRLEGLEVRIDNLQERLS---------- 946
|
330 340
....*....|....*....|....*..
gi 767985209 406 gEHLDSEGEEAPRPMPSVPEDPESREA 432
Cdd:TIGR02168 947 -EEYSLTLEEAEALENKIEDDEEEARR 972
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
86-290 |
4.38e-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: 4.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 86 LDSTSVKISRLKNTIKSLKQQKKQVEhqlEEEKKANNERQKAERE---LEVQIQTLIIQKEELNTDLYH----MERSLRY 158
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAE---ERLAKLEAEIDKLLAEieeLEREIEEERKRRDKLTEEYAElkeeLEDLRAE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 159 FEEESKDLAVRLQHSLQCKGELESAlsaviateKKKANQLSSCSKAHTEwELEQSLQDQALLKAQLTQLKESFQQLQLER 238
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKL--------KREINELKRELDRLQE-ELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767985209 239 DECAEHI---EGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQ 290
Cdd:TIGR02169 444 EDKALEIkkqEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
98-291 |
1.37e-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: 50.92 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 98 NTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKDLAVRLQHSLQCK 177
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 178 GELESALSAVIATEKKKANQ------LSSCSKAHTEWELE------QSLQDQAL-LKAQLTQLKESFQQLQLERDECAEH 244
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQpplallLSPEDFLDAVRRLQylkylaPARREQAEeLRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767985209 245 I---EGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQM 291
Cdd:COG4942 180 LaelEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
86-395 |
2.06e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 86 LDSTSVKISRLKNTIKSLKqqkKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKD 165
Cdd:TIGR02168 181 LERTRENLDRLEDILNELE---RQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 166 LAVRL------------------------QHSLQCKGELESALSAVIATEKKKANQLSScSKAHTEWELEQSLQDQALLK 221
Cdd:TIGR02168 258 LTAELqeleekleelrlevseleeeieelQKELYALANEISRLEQQKQILRERLANLER-QLEELEAQLEELESKLDELA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 222 AQLTQLKESFQQLQLERDECAEHIEGERARWHQRMSKMSqeicTLKKEKQQDMRRVEELERSLSKLKNQmaeplppeppa 301
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLE----ELEEQLETLRSKVAQLELQIASLNNE----------- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 302 vpseveLQHLRKELERVAGELQSQVKNN-QHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSvfEELEHL 380
Cdd:TIGR02168 402 ------IERLEARLERLEDRRERLQQEIeELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR--EELEEA 473
|
330
....*....|....*
gi 767985209 381 EAASQQNQQLTAQLS 395
Cdd:TIGR02168 474 EQALDAAERELAQLQ 488
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
70-318 |
3.04e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 70 ATLKDLESPCQERAVVLDST---SVKISRLKNTIKSLKQQKKQVE-HQLEEEKKANNERQKAERE---LEVQIQTL---I 139
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVlkkESELIKLKELAEQLKELEEKLKkYNLEELEKKAEEYEKLKEKlikLKGEIKSLkkeL 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 140 IQKEELNTDLYHMERSLRYFEEESKDLAVRLQH-SLQCKGELESALSAViatEK--KKANQLSSCSK---------AHTE 207
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEElGFESVEELEERLKEL---EPfyNEYLELKDAEKelereekelKKLE 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 208 WELEQSLQDQALLKAQLTQLKESFQQLQLERDEcaehieGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKL 287
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSE------EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
250 260 270
....*....|....*....|....*....|.
gi 767985209 288 KNQMAEPLPPEPpavpsevELQHLRKELERV 318
Cdd:PRK03918 700 KEELEEREKAKK-------ELEKLEKALERV 723
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
67-394 |
5.27e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 67 TSSATLKDLESPCQERAVvldstsvKISRLKNTIKSLKQQKKQVEHQLEEEK----KANNERQKAERE----------LE 132
Cdd:TIGR04523 51 NKEKELKNLDKNLNKDEE-------KINNSNNKIKILEQQIKDLNDKLKKNKdkinKLNSDLSKINSEikndkeqknkLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 133 VQIQTLIIQKEELNTDLYHMERSLRYFEEESKDLAVRLQHSLQCKGELESALSAVIATEKKKANQLSSCSKAHTEWE--- 209
Cdd:TIGR04523 124 VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElll 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 210 --LEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIEGERArwhqRMSKMSQEICTLK----------KEKQQDM--- 274
Cdd:TIGR04523 204 snLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT----EISNTQTQLNQLKdeqnkikkqlSEKQKELeqn 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 275 -RRVEELERSLSKLKNQMAEPLPPEPPAVPSEV--ELQHLRKELErvagELQSQV-KNNQHISLLNRR----QEERIREQ 346
Cdd:TIGR04523 280 nKKIKELEKQLNQLKSEISDLNNQKEQDWNKELksELKNQEKKLE----EIQNQIsQNNKIISQLNEQisqlKKELTNSE 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 767985209 347 EERLRKQEErLQEQHEKLRQLAKP-QSVFEELEHLEAAS-------QQNQQLTAQL 394
Cdd:TIGR04523 356 SENSEKQRE-LEEKQNEIEKLKKEnQSYKQEIKNLESQIndleskiQNQEKLNQQK 410
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
85-336 |
1.31e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 85 VLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESK 164
Cdd:TIGR04523 205 NLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIK 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 165 DLAVRLQhslqckgELESALSAViatEKKKANQLSSCSKAhtewELEQSLQDQALLKAQLTQLKESFQQL-----QLERD 239
Cdd:TIGR04523 285 ELEKQLN-------QLKSEISDL---NNQKEQDWNKELKS----ELKNQEKKLEEIQNQISQNNKIISQLneqisQLKKE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 240 ecAEHIEGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSL----SKLKNQMAEPLPPEPPAVPSEVELQHLRKEL 315
Cdd:TIGR04523 351 --LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIndleSKIQNQEKLNQQKDEQIKKLQQEKELLEKEI 428
|
250 260
....*....|....*....|.
gi 767985209 316 ERVageLQSQVKNNQHISLLN 336
Cdd:TIGR04523 429 ERL---KETIIKNNSEIKDLT 446
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
91-395 |
1.34e-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: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 91 VKISRLKNTIKSLKQQKKQVEhQLEEEKKANNERQKAERE------------LEVQIQTLIIQKEELNTDLYHMERSLRY 158
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLD-LIIDEKRQQLERLRREREkaeryqallkekREYEGYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 159 FEEESKDLAVRLQHSLQCKGELESALSAVIATEKKKANQLSSCSK---AHTEWELEQSLQDQALLKAQLTQLKESFQQLQ 235
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKekiGELEAEIASLERSIAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 236 LERDECAEHIEgerarwhqrmsKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMaepLPPEPPAVPSEVELQHLRKEL 315
Cdd:TIGR02169 329 AEIDKLLAEIE-----------ELEREIEEERKRRDKLTEEYAELKEELEDLRAEL---EEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 316 ERVAGELQSQVKNnqhisllnrrqeerIREQEERLRKQEERLQEQHEKLR----QLAKPQSVFEEL-EHLEAASQQNQQL 390
Cdd:TIGR02169 395 EKLKREINELKRE--------------LDRLQEELQRLSEELADLNAAIAgieaKINELEEEKEDKaLEIKKQEWKLEQL 460
|
....*
gi 767985209 391 TAQLS 395
Cdd:TIGR02169 461 AADLS 465
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
93-305 |
2.19e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 93 ISRLKNTIKSL-KQQKKQVEHQLEEEKKANNERQKAERELEvQIQTLIIQKEELNTDLYHMERSLRYFEEESKDLAVRLQ 171
Cdd:COG4717 48 LERLEKEADELfKPQGRKPELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 172 hslqckgelesaLSAVIATEKKKANQLSSCSKahtewELEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIEGERAR 251
Cdd:COG4717 127 ------------LLPLYQELEALEAELAELPE-----RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767985209 252 WHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSE 305
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
161-372 |
2.34e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 161 EESKDLAVRLQHSLQCKGELESALSAVIATEKKKANQLSSCSK--AHTEWELEQSLQDQALLKAQLTQLKESFQQLQLER 238
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERriAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 239 DECAEHIeGERARWHQRMSKMSQEICTLKKEKQQDMRR--------VEELERSLSKLKNQMAEPLPPEPPAVPSEVELQH 310
Cdd:COG4942 100 EAQKEEL-AELLRALYRLGRQPPLALLLSPEDFLDAVRrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767985209 311 LRKELERVAGELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQS 372
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
92-320 |
3.46e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.58 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 92 KISRLKNTIKSLKQQKKQVEhqlEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKDLAVRLQ 171
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQME---LEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 172 HSLQCKGELESALSAVIATEKKkANQLSSCSK-----------------AHTEWELEQSLQDQALLKAQLTQLKESFQQL 234
Cdd:pfam05557 80 LKKKYLEALNKKLNEKESQLAD-AREVISCLKnelselrrqiqraelelQSTNSELEELQERLDLLKAKASEAEQLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 235 QLERDECAEHIegerarwhQRMSKMSQEICT------LKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVEL 308
Cdd:pfam05557 159 EKQQSSLAEAE--------QRIKELEFEIQSqeqdseIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEV 230
|
250
....*....|..
gi 767985209 309 QHLRKELERVAG 320
Cdd:pfam05557 231 EDLKRKLEREEK 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
94-399 |
3.53e-04 |
|
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: 43.56 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 94 SRLKNTIKsLKQQKKQVEHQLEEEKKANNERQKaerelevQIQTLIIQKEELNTDLyhmeRSLRYFEEESKDLAVRLQHS 173
Cdd:pfam05483 209 ARLEMHFK-LKEDHEKIQHLEEEYKKEINDKEK-------QVSLLLIQITEKENKM----KDLTFLLEESRDKANQLEEK 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 174 LQCKGElesALSAVIATEKKKANQLSSCSKAhteweLEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIEGERARWH 253
Cdd:pfam05483 277 TKLQDE---NLKELIEKKDHLTKELEDIKMS-----LQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHS 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 254 QRMSKMSQEICTLKKEKQQDMRRVEELERSLS----KLKNQMAEPLPPEPPAVPSEVELQhlrkELERVAGELQSQVKNN 329
Cdd:pfam05483 349 FVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEEMTKFKNNKEVELE----ELKKILAEDEKLLDEK 424
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767985209 330 QHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVF----EELE-HLEAASQQNQQLTAQLSLMAL 399
Cdd:pfam05483 425 KQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYlkevEDLKtELEKEKLKNIELTAHCDKLLL 499
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
86-289 |
6.73e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 86 LDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKD 165
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 166 LAVRLQHSLQCKGELESALSAVIATEKKKANQLSSCSKAHTEWELEqslqdqallkaqLTQLKESFQQLQLERDECAEHI 245
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI------------IKNLDNTRESLETQLKVLSRSI 477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767985209 246 EGERARWH---QRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKN 289
Cdd:TIGR04523 478 NKIKQNLEqkqKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE 524
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
87-316 |
7.49e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 87 DSTSVKISRLKNTIKSLKQQKKQVEHQLEE-EKKANNERQKAE-RELEVQIQTLIIQKEELNTDLyhmerslryfeeesk 164
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEaEAALEEFRQKNGlVDLSEEAKLLLQQLSELESQL--------------- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 165 dLAVRLQHSlqckgELESALSAVIATEKKKANQLSSCSKAHTEWELEQSLQDqalLKAQLTQLKESF-------QQLQLE 237
Cdd:COG3206 229 -AEARAELA-----EAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAE---LEAELAELSARYtpnhpdvIALRAQ 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767985209 238 RDECAEHIEGERARwhqrmskmsqEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPeppavpsEVELQHLRKELE 316
Cdd:COG3206 300 IAALRAQLQQEAQR----------ILASLEAELEALQAREASLQAQLAQLEARLAELPEL-------EAELRRLEREVE 361
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
68-367 |
7.66e-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: 42.74 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 68 SSATLKDLESPCQERAVVLDstsvKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELnt 147
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEE----RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL-- 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 148 dlyhmERSLRYFEEESKDLAVRLQHSLQCKGELESALSAviatekkkanqlsscskahTEWELEQSLQDQALLKAQLTQL 227
Cdd:TIGR02168 802 -----REALDELRAELTLLNEEAANLRERLESLERRIAA-------------------TERRLEDLEEQIEELSEDIESL 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 228 KESFQQLQLERDEcaehIEGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAeplppeppavpsevE 307
Cdd:TIGR02168 858 AAEIEELEELIEE----LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--------------E 919
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 308 LQHLRKELERVAGELQSQVKNNQhiSLLNRRQEERIREQEERLRKQEERLQEQHEKLRQL 367
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQ--ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
72-272 |
1.38e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 72 LKDLESPCQERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYH 151
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 152 MERS-------LRYFEEESKDLAVRLQHSLQCKGELESALSaviatekKKANQLSSCSKAHTEWELEQSLQDQALLKAQL 224
Cdd:TIGR02168 391 LELQiaslnneIERLEARLERLEDRRERLQQEIEELLKKLE-------EAELKELQAELEELEEELEELQEELERLEEAL 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767985209 225 TQLKESFQQLQLERDECAEHIEGERARWH------QRMSKMSQEICTLKKEKQQ 272
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQARLDslerlqENLEGFSEGVKALLKNQSG 517
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
92-459 |
1.58e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 92 KISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAErelEVQIQTLIIQK-EELNTDLYHMERSlryfeEESKDLAVRL 170
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD---ELKKAAAAKKKaDEAKKKAEEKKKA-----DEAKKKAEEA 1443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 171 QHSLQCKGELESALSA----VIATEKKKANQLSSCSKAHTEWELEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIE 246
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAeeakKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 247 GERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELqhLRKELERVAGELQSQV 326
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE--AKKAEEARIEEVMKLY 1601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 327 KNNQHISLLNRRQEERIREQEERLRKQEErlqEQHEKLRQLAKPQSVFEELEHLEAASQQNQQLTAQLSLMALPGEGHGG 406
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEE---EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE 1678
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 767985209 407 EHLDSEGEEAPRPMPSVPEDPESREAMSSFMDHLKEKADLSELVKKQELRFIQ 459
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIK 1731
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
73-282 |
1.71e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 73 KDLESPCQERAVVLDSTSVKISRLKNTIKSLKQ--QKKQVEHQLEEEKKANNERQKaeRELEVQIQTLIIQKEELNTDLY 150
Cdd:TIGR02169 787 RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQklNRLTLEKEYLEKEIQELQEQR--IDLKEQIKSIEKEIENLNGKKE 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 151 HMERSLRYFEEESKDLAVRLQHSLQCKGELESALSAViateKKKANQLsscskahtEWELEQSLQDQALLKAQLTQLKE- 229
Cdd:TIGR02169 865 ELEEELEELEAALRDLESRLGDLKKERDELEAQLREL----ERKIEEL--------EAQIEKKRKRLSELKAKLEALEEe 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 230 -------------------SFQQLQLERDECAEHIEG----------ERARWHQRMSKMSQEICTLKKEKQQDMRRVEEL 280
Cdd:TIGR02169 933 lseiedpkgedeeipeeelSLEDVQAELQRVEEEIRAlepvnmlaiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
..
gi 767985209 281 ER 282
Cdd:TIGR02169 1013 EK 1014
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
81-378 |
2.29e-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: 41.11 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 81 ERAVVLDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQKEELNTDLYHMERSLRYFE 160
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 161 EESKDLAVRLQHSLQCKGELESALSAVIATEKKKaNQLSSCSKAHTEWELEQSLQDQALLKAQLTQLKesfqQLQLERDE 240
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKE-NKEEEKEKKLQEEELKLLAKEEEELKSELLKLE----RRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 241 CAEHIEGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELQHLRKELERVAG 320
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 767985209 321 ELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVFEELE 378
Cdd:pfam02463 395 EELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEE 452
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
95-393 |
2.45e-03 |
|
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: 41.11 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 95 RLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQTLIIQ----KEELNTDLYHMERSLRYFEEESK--DLAV 168
Cdd:TIGR00618 532 RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCdnrsKEDIPNLQNITVRLQDLTEKLSEaeDMLA 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 169 RLQHSLQCKGELESALSAVIATEKKKAN--QLSSCSKAHTEWELEQSLQDQALL-----------------------KAQ 223
Cdd:TIGR00618 612 CEQHALLRKLQPEQDLQDVRLHLQQCSQelALKLTALHALQLTLTQERVREHALsirvlpkellasrqlalqkmqseKEQ 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 224 LTQLKESFQQLQLERDECAEHIEGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERslsKLKNQMAEPLPPEPPAVP 303
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH---QARTVLKARTEAHFNNNE 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 304 SEVELQHLRKELERVAGELQSQVK----NNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQL-----AKPQSVF 374
Cdd:TIGR00618 769 EVTAALQTGAELSHLAAEIQFFNRlreeDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRleeksATLGEIT 848
|
330
....*....|....*....
gi 767985209 375 EELEHLEAASQQNQQLTAQ 393
Cdd:TIGR00618 849 HQLLKYEECSKQLAQLTQE 867
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
65-240 |
4.65e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 39.36 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 65 GPTSSATLKDLESPCQERavvlDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQkaeRELEVQIQTLIIQKEE 144
Cdd:pfam09787 39 LDSSTALTLELEELRQER----DLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQL---QELEEQLATERSARRE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 145 LNTDLYHMERSLRYFEEESKDLAVRLQHSLQckgELESALSaviatekKKANQLSSCSKAHT-EWELEQSL--------Q 215
Cdd:pfam09787 112 AEAELERLQEELRYLEEELRRSKATLQSRIK---DREAEIE-------KLRNQLTSKSQSSSsQSELENRLhqltetliQ 181
|
170 180
....*....|....*....|....*
gi 767985209 216 DQALLKAqLTQLKESFqQLQLERDE 240
Cdd:pfam09787 182 KQTMLEA-LSTEKNSL-VLQLERME 204
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
180-289 |
4.98e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 180 LESALSAVIATEKKKANQLSSCSKAHTEWELEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIE------------- 246
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIErlerelsearsee 457
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 767985209 247 GERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLKN 289
Cdd:COG2433 458 RREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
86-269 |
5.06e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 86 LDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNerqkaerELEVQIQTLIIQKEELNTDLYHMERSLRYFEEESKD 165
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-------ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 166 LAVRLQHSLQCKGELE---------------SALSAVIATEKKKANQLSSCSK--AHTEWELEQSLQDQALLKAQLTQLK 228
Cdd:COG3883 91 RARALYRSGGSVSYLDvllgsesfsdfldrlSALSKIADADADLLEELKADKAelEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767985209 229 ESFQQLQLERDECAEHIEGERARWHQRMSKMSQEICTLKKE 269
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
188-382 |
5.22e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 188 IATEKKKANQLSSCSKAHTEWELEQSLQdqaLLKAQLTQLKESFQQLQLERDECAEHIEGERAR----WHQRMSKMSQEI 263
Cdd:COG4913 264 YAAARERLAELEYLRAALRLWFAQRRLE---LLEAELEELRAELARLEAELERLEARLDALREEldelEAQIRGNGGDRL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 264 CTLKKEKQQDMRRVEELERSLSKLKNQMAEPLPPEPPAVPSEVELQHLRKELERVAGELQSQVKNNQHisllnrrqeeri 343
Cdd:COG4913 341 EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA------------ 408
|
170 180 190
....*....|....*....|....*....|....*....
gi 767985209 344 reqeeRLRKQEERLQEQHEKLRQlakpqsvfeELEHLEA 382
Cdd:COG4913 409 -----EAEAALRDLRRELRELEA---------EIASLER 433
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
86-381 |
7.02e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 86 LDSTSVKISRLKNTIKSLKQQKKQVEHQLEEEKKANNERQKAERELEVQIQ-------------TLIIQKEELNTDLYHM 152
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKelkelkekaeeyiKLSEFYEEYLDELREI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 153 ERSLRYFEEESKDLAVRLQhslqckgELESALSAVIATEKKKANQLSSCSKAHTEWELeqsLQDQALLKAQLTQLKESFQ 232
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIK-------ELEEKEERLEELKKKLKELEKRLEELEERHEL---YEEAKAKKEELERLKKRLT 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 233 QLQLER-DECAEHIEGERARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSK--LKNQMAEPLPPEPPAVPSEVELQ 309
Cdd:PRK03918 383 GLTPEKlEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELK 462
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767985209 310 HLRKELERVAGELqsqvknnqhisllnrrqeerireqeERLRKQEERLQEQHEKLRQLAKPQSVFEELEHLE 381
Cdd:PRK03918 463 RIEKELKEIEEKE-------------------------RKLRKELRELEKVLKKESELIKLKELAEQLKELE 509
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
209-399 |
8.06e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 209 ELEQSLQDQALLKAQLTQLKESFQQLQLERDECAEHIEgeRARWHQRMSKMSQEICTLKKEKQQDMRRVEELERSLSKLK 288
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELE--KLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 289 NQmaeplppeppavpsEVELQHLRKELERVAGELQSQVknnQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQ-L 367
Cdd:COG4717 160 EL--------------EEELEELEAELAELQEELEELL---EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEeL 222
|
170 180 190
....*....|....*....|....*....|..
gi 767985209 368 AKPQSVFEELEHLEAASQQNQQLTAQLSLMAL 399
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARLLLLI 254
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
63-389 |
8.76e-03 |
|
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: 39.18 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 63 REGPTSSATLKDLESPCQERAVVlDSTSVKISRLKNTIKSLKQQKkQVEHQLEEEKKANNERQKAERELevqiQTLIIQK 142
Cdd:TIGR00618 196 AELLTLRSQLLTLCTPCMPDTYH-ERKQVLEKELKHLREALQQTQ-QSHAYLTQKREAQEEQLKKQQLL----KQLRARI 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 143 EELNTDLYHME--RSLRYFEEESKDLAVRLQHSLQCKGELESALSAVIATEKKKANQLSSCSKAhteweleqsLQDQALL 220
Cdd:TIGR00618 270 EELRAQEAVLEetQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAH---------VKQQSSI 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 221 KAQLTQLKESFQQLQLERDEcaehiEGERARWHQRMSKMSQEICTLKKEkQQDMRRVEELERSLSKLKNQMAEPLPPEPP 300
Cdd:TIGR00618 341 EEQRRLLQTLHSQEIHIRDA-----HEVATSIREISCQQHTLTQHIHTL-QQQKTTLTQKLQSLCKELDILQREQATIDT 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767985209 301 AVPSEVELQhlrKELERVAGELQSQVKNNQHISLLNRRQEERIREQEERLRKQEERLQEQHEKLRQLAKPQSVFEELEHL 380
Cdd:TIGR00618 415 RTSAFRDLQ---GQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAV 491
|
....*....
gi 767985209 381 EAASQQNQQ 389
Cdd:TIGR00618 492 VLARLLELQ 500
|
|
| |
