|
Name |
Accession |
Description |
Interval |
E-value |
| NCKAP5 |
pfam15246 |
Nck-associated protein 5, Peripheral clock protein; NCKAP5 is short for Nck-associated protein ... |
1465-1773 |
3.74e-151 |
|
Nck-associated protein 5, Peripheral clock protein; NCKAP5 is short for Nck-associated protein 5, which is also known as the Peripheral clock protein. NCKAP5 is a protein family, which interacts with the SH3-containing region of the adaptor protein Nck. Nck is a protein that interacts with receptor tyrosine kinases and guanine nucleotide exchange factor Sos. The role of Nck can be thought of as similar to Grb2. The role of NCKAP5 is to assist Nck with its adaptor protein role.
Pssm-ID: 464586 Cd Length: 309 Bit Score: 466.55 E-value: 3.74e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1465 LSPTIEEKVMLCIQENVEKGQVQTKSTSVDAKPKPGPSFASWFGFRRSRLPALSSRKMDVSKTKAEKKDAKGLGFGNKQL 1544
Cdd:pfam15246 1 LQSTIEEKVMLGIQENVLKGQVQDKSQSVETKQKTGPSIASWFGFRKSKLPALSSRKMDVSKGKEEKKEWKGSGFGGKQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1545 KSERKKEKKKPELQCEMENELNRDIELADGPDSGLQNRNNLKTPPDIYDQVKFVSRNRPSPVPCATKDTFMTELLNRVDK 1624
Cdd:pfam15246 81 KSEKKKEKKKEELQCALEEELAYKNEVGLDRDGRGHSKKLLKIPQDCEVQMGQEQSQLSSPYTCMTKDTFMQELLNRVDK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1625 KAAQQTESGSNNVSCRSVLKGSSQGSCVTGSSIGTQGTHKKNVKTKADTEIPKGSLIKEANEHLQEDEEDTVADSAFQSH 1704
Cdd:pfam15246 161 KAAQQTESGSNNVSCRSVSKGSSQGSCLPSNSISTQGNHKKNSKTKADMEIPRESLIKEVAENVQEDEEDTLADSACQDH 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246200473 1705 TIETNCQMRTLDSGIGTFPLPDSGNRSAGRHLCQADSPDDTEPLLSLQPALCAASSIRAQTLEREVPSS 1773
Cdd:pfam15246 241 FIGSGCQMRTLDSGIGTFPLPDSGNRSTGRHIPKPESSEETEPLLSLQPALPTAVPRRARTLEREVPSS 309
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
826-1103 |
6.88e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 61.49 E-value: 6.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 826 PSAGP--VTLERSPAPGKLSRFKKSEGPEPLFALPPDSHIPKPSTqlphGSKMFSRRDWVQYSRSQIPASQLLPRPPAEP 903
Cdd:PHA03247 2614 PSPLPpdTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAP----GRVSRPRRARRLGRAAQASSPPQRPRRRAAR 2689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 904 ------SDDGEPPTRDKHCDPGPEAGVrsPSLPSPPGRSVSLLARPSYDyLSPPSWAKPESGVPSEAARTVLKSPPLKGS 977
Cdd:PHA03247 2690 ptvgslTSLADPPPPPPTPEPAPHALV--SATPLPPGPAAARQASPALP-AAPAPPAVPAGPATPGGPARPARPPTTAGP 2766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 978 SAPiiyfnqTVTEVQGKKPSVAFKKPVFTPPPPSTETAIQTRCPAHSPSSSFAGMAPGPPKVSPKRSVPktPPhqtlgTT 1057
Cdd:PHA03247 2767 PAP------APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLP--PP-----TS 2833
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1246200473 1058 QTDIGLRTPKNCPSTREPLEIPSPKGVSPARKGQLNDSVSTPPKPS 1103
Cdd:PHA03247 2834 AQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPA 2879
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-248 |
1.39e-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: 60.07 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 2 EGKRQLEKrdfgkrLSLDSSLVEymdsnKYIEhLLTQLEEQHRSLWreklaVARLQREVAQRrsegamhEKLIHELEEER 81
Cdd:TIGR02168 197 ELERQLKS------LERQAEKAE-----RYKE-LKAELRELELALL-----VLRLEELREEL-------EELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 82 HLRLQSEKRLQEVTLESERNRIQMRGLQQQFSRMEETVRNLLQSQgppeQKKEdtVNIMVYQEKLSEEERKHKEALEDRh 161
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI----SRLE--QQKQILRERLANLERQLEELEAQL- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 162 mvvdedsrsegssaDEGKEKTKLLLERLKALEAENSALALENENQREQyercLDEVANQVVQALLTQKDLREECVKLKTR 241
Cdd:TIGR02168 326 --------------EELESKLDELAEELAELEEKLEELKEELESLEAE----LEELEAELEELESRLEELEEQLETLRSK 387
|
....*..
gi 1246200473 242 VFDLEQQ 248
Cdd:TIGR02168 388 VAQLELQ 394
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
804-1109 |
6.99e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.03 E-value: 6.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 804 PTRGKSSPQKSRimePEAslMVPSAGPVT-LERSPAPGKlsrfkkseGPEPlfalPPdsHIPKPSTQLPHGSKMFSRRDW 882
Cdd:PHA03247 2673 AAQASSPPQRPR---RRA--ARPTVGSLTsLADPPPPPP--------TPEP----AP--HALVSATPLPPGPAAARQASP 2733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 883 VQYSRSQIPASQLLPRPPAEPSDDGEPPTRDKHCDPGPEAGVRSPSLPSPPGRSVSLLARPSYDYLSPPSWAKPESGVPS 962
Cdd:PHA03247 2734 ALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLA 2813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 963 EAARTVLKSPPLKGSSAPiiyfnQTVTEVQGKKPSVAFKKPV-----------FTPPPPSTETAIQTRCPAHSPSSSFAg 1031
Cdd:PHA03247 2814 PAAALPPAASPAGPLPPP-----TSAQPTAPPPPPGPPPPSLplggsvapggdVRRRPPSRSPAAKPAAPARPPVRRLA- 2887
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246200473 1032 mAPGPPKVSPKRSVPKTPPHQtlgttqtdigLRTPKNCPSTREPLEIPSPKGVSPARKGQLNDSVSTPPKPSFLGVNE 1109
Cdd:PHA03247 2888 -RPAVSRSTESFALPPDQPER----------PPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGE 2954
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
14-293 |
3.11e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 14 KRLSLDSSLVEYMDSNKYIEHLLTQLEEQHRSLWREKLAVARLQREVAQRRSEgamHEKLIHELEEERHLRLQSEKRLQE 93
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE---LEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 94 VTLESERNRIQMRGLQQQFSRMEETVRNLLqsqgppEQKKEDTVNIMVYQEKLSEEERKHKEALEDRHMVVDEDSRSEGS 173
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELE------EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 174 SADEGKEKTKLLLERLKALEAENSALALENENQREQyERCLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTLS 253
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAE-EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1246200473 254 ILFQQRVRPTSDLLLQKLHSRILDLSTGDLLSDVERSRSL 293
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
754-1102 |
8.44e-07 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 54.39 E-value: 8.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 754 TPTESFHPRTVTQSTQRQRLTKPTHATSCQSHSRSSVATGIYQKKS----LTKIPTRGKSSPQKSRIMEPEASLMVPSAG 829
Cdd:pfam03154 178 SGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQStaapHTLIQQTPTLHPQRLPSPHPPLQPMTQPPP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 830 PVTLERSPAPGKLSRFKKSEGPEPLFALPPdsHIPKPSTQLPHGSKMFSRRDWVQYSRSQ---IPASQLLPRPPAEPSDD 906
Cdd:pfam03154 258 PSQVSPQPLPQPSLHGQMPPMPHSLQTGPS--HMQHPVPPQPFPLTPQSSQSQVPPGPSPaapGQSQQRIHTPPSQSQLQ 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 907 GEPPTRDKhcdPGPEAGVRSPSLPSPPGRSVSLLARPSYD----YLSPPSWAKPESGVPSEAARTVLKSPPlkgssapii 982
Cdd:pfam03154 336 SQQPPREQ---PLPPAPLSMPHIKPPPTTPIPQLPNPQSHkhppHLSGPSPFQMNSNLPPPPALKPLSSLS--------- 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 983 yfnqTVTEVQGKKPSVAFKKPVFTPPPPSTETAIQTRCPAHSPSSSfagMAPGPPKVSPKRSVPKTPPHQTLGTTQTDIg 1062
Cdd:pfam03154 404 ----THHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAA---SHPPTSGLHQVPSQSPFPQHPFVPGGPPPI- 475
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1246200473 1063 lrTPKNCPSTREPLEIPS---PKGVSPARKGQLNDSVSTPPKP 1102
Cdd:pfam03154 476 --TPPSGPPTSTSSAMPGiqpPSSASVSSSGPVPAAVSCPLPP 516
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
18-239 |
2.22e-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: 52.75 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 18 LDSSLVEYMDSNKYIEHLLTQLEEQHRSLWREKLAVARLQREVAQRRSEGAMHEKLIHELEEErHLRLQSEKRLQEVTLE 97
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE-LTLLNEEAANLRERLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 98 SERNRI-----QMRGLQQQFSRMEETVRNL---LQSQGPPEQKKEDTVNImVYQEKLSEEERKHkeALEDRHMVVDEDSR 169
Cdd:TIGR02168 828 SLERRIaaterRLEDLEEQIEELSEDIESLaaeIEELEELIEELESELEA-LLNERASLEEALA--LLRSELEELSEELR 904
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246200473 170 SEGSSADEGKEKTKLLLERLKALEAENSALALENENQ----REQYERCLDEVANQVVQALLTQKDLREECVKLK 239
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLqerlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
32-261 |
2.86e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 32 IEHLLTQLEEQHRSLWREKLAVARLQREVAQRRSEGAMHEKLIHELEEERHLRLQSEKRLQEVTLESERNRIQMRGLQQQ 111
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 112 FSR-----------MEETVRNLLQSQGPPEQKKEDTVNIMVYQEKLSEEERKHKEALEDRHMVVDEDSRSEGSSADEGKE 180
Cdd:TIGR02168 794 LKEelkalrealdeLRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 181 KTKLLLERLKALEAENSALALENENQREQyercLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTLsilfQQRV 260
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEE----LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL----QERL 945
|
.
gi 1246200473 261 R 261
Cdd:TIGR02168 946 S 946
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
36-234 |
3.00e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 36 LTQLEEQHRSLwREKL--AVARLQREVAQRRSEGAMHEKLIHELEEERHLRLQSEKRLQEVTLESERNRIQMRGLQQQFS 113
Cdd:COG1196 297 LARLEQDIARL-EERRreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 114 RMEETVRNLLQSQGPPEQKKEDTVNIMVYQEKLSEEERKHKEALEDRhmVVDEDSRSEGSSADEGKEKTKLLLERLKALE 193
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE--LEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1246200473 194 AENSALALENENQREQYERCLDEVANQVVQALLTQKDLREE 234
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
5-278 |
4.24e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 5 RQLEKRDFGKRLSLDSSLVEYMDSNKYIEHLLTQLEEQHRSLWREKLAVARLQREVAQRRSEGAMHEKLIHELEEERhLR 84
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL-EE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 85 LQSEKRLQEVTLESERNRiqmrgLQQQFSRMEETVRNLLQSQgppEQKKEDTVNIMVYQEKLSEEERKHKEALEDRhmvv 164
Cdd:COG1196 349 AEEELEEAEAELAEAEEA-----LLEAEAELAEAEEELEELA---EELLEALRAAAELAAQLEELEEAEEALLERL---- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 165 dEDSRSEGSSADEGKEKTKLLLERLKALEAENSALALENENQREQYERCLDEVANQVVQALLTQKDLREECVKLKTRVFD 244
Cdd:COG1196 417 -ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
250 260 270
....*....|....*....|....*....|....
gi 1246200473 245 LEQQNRTLSiLFQQRVRPTSDLLLQKLHSRILDL 278
Cdd:COG1196 496 LLEAEADYE-GFLEGVKAALLLAGLRGLAGAVAV 528
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
33-304 |
6.34e-06 |
|
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: 51.28 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 33 EHLLTQLEEQHRSL-WREKLAVARLQREVAQRRSEGAMHEKLIHELEEERHL-RLQSEKRlqevtlESERNRIQMRGLQQ 110
Cdd:pfam17380 299 ERLRQEKEEKAREVeRRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELeRIRQEER------KRELERIRQEEIAM 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 111 QFSRMEETVRNLLQSQGPPEQKKEDTVniMVYQEKLSEEERKHKEALEDRHMvvdEDSRSEgssADEGKEKTKLLLERLK 190
Cdd:pfam17380 373 EISRMRELERLQMERQQKNERVRQELE--AARKVKILEEERQRKIQQQKVEM---EQIRAE---QEEARQREVRRLEEER 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 191 ALEAENsaLALENENQREQYERCLDEVANQVVQALLTQKDLRE--ECVKLKTRVFDLEQQNRTLSILFQQRVRptsdlll 268
Cdd:pfam17380 445 AREMER--VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDrkRAEEQRRKILEKELEERKQAMIEEERKR------- 515
|
250 260 270
....*....|....*....|....*....|....*.
gi 1246200473 269 qKLHSRILDLSTGDLLSDVERSRSLTHSRTDVEMHE 304
Cdd:pfam17380 516 -KLLEKEMEERQKAIYEEERRREAEEERRKQQEMEE 550
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
826-1081 |
1.67e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 50.07 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 826 PSAGPVTLERSP-APGKLSRFKKSEGPEPLFALPPDSHIPKPSTQLPHGSKMFSRRdwvQYSRSQIPASQLLPRPPAEPS 904
Cdd:PTZ00449 510 PPEGPEASGLPPkAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAK---EHKPSKIPTLSKKPEFPKDPK 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 905 DDGEPPTRDKHCDP-GPEAGVRSPS--------LPSPPGRSVSLLArPSydylSPPSWAKPESGVPSEAARTVLKSPPLK 975
Cdd:PTZ00449 587 HPKDPEEPKKPKRPrSAQRPTRPKSpklpelldIPKSPKRPESPKS-PK----RPPPPQRPSSPERPEGPKIIKSPKPPK 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 976 GSSAPI-IYFNQTVTEVQGKKPSVAfKKPVFTPPPPSTETAIQTRCPAHSPSSSFAGMAPGPPKVSPKRSVPKTPPHQTL 1054
Cdd:PTZ00449 662 SPKPPFdPKFKEKFYDDYLDAAAKS-KETKTTVVLDESFESILKETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPD 740
|
250 260 270
....*....|....*....|....*....|
gi 1246200473 1055 GTTQTDIGLRTPKNCPSTR---EPLEIPSP 1081
Cdd:PTZ00449 741 AEQPDDIEFFTPPEEERTFfheTPADTPLP 770
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
720-1103 |
1.73e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 50.32 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 720 LQPGAAARDYPFLKRSEEETERNIPRQEVDDVAVTPTESFHPRTVTQSTQRQRLTKPTHATScqshsrssvatgiyqkks 799
Cdd:PHA03247 2617 LPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASS------------------ 2678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 800 ltkiPTRGKSSPQKSRIMEPEASLMVPSAGPVTLERSPAPgKLSRFKKSEGPEP---LFALPPDSHIPKPSTQLPHGSKM 876
Cdd:PHA03247 2679 ----PPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHA-LVSATPLPPGPAAarqASPALPAAPAPPAVPAGPATPGG 2753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 877 FSRRdwvqySRSQIPASQLLPRPPAEPSddgEPPTRDKHCDPGPEAGVRSPSLPSPPGRSVSLLARPSYDYLSPPSwAKP 956
Cdd:PHA03247 2754 PARP-----ARPPTTAGPPAPAPPAAPA---AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPA-ASP 2824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 957 ESGVPSEAARTVLKSPPLKGSSAPIIYFNQTV-----------TEVQGKKPSVAFKKPV--------------FTPPPPS 1011
Cdd:PHA03247 2825 AGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVapggdvrrrppSRSPAAKPAAPARPPVrrlarpavsrstesFALPPDQ 2904
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1012 TETAIQTRCPAHSPSSSFAGMAPGP---PKVSPKRSVPKTPPHQTLGTTQTDIGLRTPKNCPSTREPLEIPSPKGVSPAr 1088
Cdd:PHA03247 2905 PERPPQPQAPPPPQPQPQPPPPPQPqppPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPA- 2983
|
410
....*....|....*
gi 1246200473 1089 kgqlnDSVSTPPKPS 1103
Cdd:PHA03247 2984 -----PSREAPASST 2993
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-258 |
2.32e-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: 49.68 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1 MEGKRQLEKRDFGKRLSLDsslveymDSNKYIEHL---LTQLEEQHRSLwREKLAVAR-----LQREVAQRRSEGAMHEK 72
Cdd:TIGR02169 694 QSELRRIENRLDELSQELS-------DASRKIGEIekeIEQLEQEEEKL-KERLEELEedlssLEQEIENVKSELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 73 LIHELEEERHlrlqsEKRLQEVTLESERNRIQMRGLQQQFSRMEETVRNLLQSQGPPEQKKEDTVNIMVYQEKLSEEERK 152
Cdd:TIGR02169 766 RIEELEEDLH-----KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 153 HKEALEDRhmvvdEDSRSEGSSADEGKektkllLERLKALEAENSALALENENQREQYERCLDEVANQVVQALLTQKDLR 232
Cdd:TIGR02169 841 QRIDLKEQ-----IKSIEKEIENLNGK------KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
250 260
....*....|....*....|....*.
gi 1246200473 233 EECVKLKTRvfdLEQQNRTLSILFQQ 258
Cdd:TIGR02169 910 AQIEKKRKR---LSELKAKLEALEEE 932
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1007-1461 |
2.34e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.55 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1007 PPPPSTETAIQTRCPAHSPSSsfagmapgpPKVSPKRSVPKTPPHQTLGTTQTDIGLRTPKNCPSTREPLEIPSPKGVSP 1086
Cdd:PHA03247 2559 APPAAPDRSVPPPRPAPRPSE---------PAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPP 2629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1087 ARKGQLNDSVSTPPKPSFLGVNESPSSQVSSPSSSAPSKSHSTPQGCQNPQERGLKTRLPvglkvfmkspqllrksstvp 1166
Cdd:PHA03247 2630 SPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAAR-------------------- 2689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1167 gkhekdslneASKSSAAVSKDKPGTSRNASSLETTGGERNVSPLGLRAQESLAEGLPLETATPeslesSTPGADGEDAVE 1246
Cdd:PHA03247 2690 ----------PTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP-----AVPAGPATPGGP 2754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1247 NKSVKRSLSSNKPLLKPALGMNGAKARSQSFSAHSGDKPPTASVEGPGKVRTQIITNTAeRGNSLTRQSSSTEGSPSKTA 1326
Cdd:PHA03247 2755 ARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLA-PAAALPPAASPAGPLPPPTS 2833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1327 SAPVSDGLP----------GAGRPLGHPSSRQGSLGSTGSSSSQHG--SPSKLPLRILPKSEGPLA--PPGTEEQPAYAQ 1392
Cdd:PHA03247 2834 AQPTAPPPPpgppppslplGGSVAPGGDVRRRPPSRSPAAKPAAPArpPVRRLARPAVSRSTESFAlpPDQPERPPQPQA 2913
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246200473 1393 GEGVRVTAPEEAgsdhgrcPSTPKDglgAPQSPGRTRHPSSFETSRTSKLETSGRYPDtstTRTGAVSP 1461
Cdd:PHA03247 2914 PPPPQPQPQPPP-------PPQPQP---PPPPPPRPQPPLAPTTDPAGAGEPSGAVPQ---PWLGALVP 2969
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
32-292 |
2.92e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 32 IEHLLTQLEEQHRSLwreklavaRLQREVAQRrsegamHEKLIHELEE-ERHLRLqseKRLQEVTLESERNRIQMRGLQQ 110
Cdd:COG1196 191 LEDILGELERQLEPL--------ERQAEKAER------YRELKEELKElEAELLL---LKLRELEAELEELEAELEELEA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 111 QFSRMEETVRNLlqsqgppEQKKEDTvnimvyQEKLSEEERKHKEALEDRHMVVDEDSRSEGSSAdegkektkLLLERLK 190
Cdd:COG1196 254 ELEELEAELAEL-------EAELEEL------RLELEELELELEEAQAEEYELLAELARLEQDIA--------RLEERRR 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 191 ALEAENSALALENENQREQYERCLDEVANQVVQALLTQKDLREECVKLKT-------RVFDLEQQNRTLSILFQQRVRPT 263
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEaeealleAEAELAEAEEELEELAEELLEAL 392
|
250 260
....*....|....*....|....*....
gi 1246200473 264 SDLLLQKLHSRILDLSTGDLLSDVERSRS 292
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEE 421
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
851-1103 |
3.11e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.17 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 851 PEPLFALP--PDSHIPKPS-TQLPHGSKMFSRRdwvqySRSQIPASQLLPRPPAEPSDD-------GEPPTRDKHCDPGP 920
Cdd:PHA03247 2554 PLPPAAPPaaPDRSVPPPRpAPRPSEPAVTSRA-----RRPDAPPQSARPRAPVDDRGDprgpappSPLPPDTHAPDPPP 2628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 921 EAGVRSPSLPSPPG----------------------RSVSLLARPSYDYlSPPSWAKPESGVPSEAARTVLKSPPLKG-- 976
Cdd:PHA03247 2629 PSPSPAANEPDPHPpptvppperprddpapgrvsrpRRARRLGRAAQAS-SPPQRPRRRAARPTVGSLTSLADPPPPPpt 2707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 977 -SSAPIIYFNQTVTEVQGKKPSVAFKKPVFTPPPPSTETAIQT----RCPAHSPSSSfagmapGPPKVSPKRSVPKTPPH 1051
Cdd:PHA03247 2708 pEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATpggpARPARPPTTA------GPPAPAPPAAPAAGPPR 2781
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1246200473 1052 QTLGTTQTDIGLRTPkNCPSTREPLEIPSP-KGVSPARKGQLNDSVSTPPKPS 1103
Cdd:PHA03247 2782 RLTRPAVASLSESRE-SLPSPWDPADPPAAvLAPAAALPPAASPAGPLPPPTS 2833
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
8-269 |
5.51e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.18 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 8 EKRDFGKRLSLDSSLVE--YMDSNKYIEHLLTQLEEQHRSLWREKLAVARLQREVAqrrsegaMHEKLIHELEEERHLRL 85
Cdd:pfam05483 265 ESRDKANQLEEKTKLQDenLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQ-------IATKTICQLTEEKEAQM 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 86 QsekrlqevtlESERNRIQMRGLQQQFSRMEETVRNLLQSQGPPEQKKEDTVNI--MVYQEKLSEEE-----RKHKEA-L 157
Cdd:pfam05483 338 E----------ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIitMELQKKSSELEemtkfKNNKEVeL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 158 EDRHMVVDEDSRSegssADEGKEKTKLLlERLKALEAENSALALENENQREQYERCLDEVANQVVQALLTQKDLREECVK 237
Cdd:pfam05483 408 EELKKILAEDEKL----LDEKKQFEKIA-EELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK 482
|
250 260 270
....*....|....*....|....*....|..
gi 1246200473 238 LKTRVFDLEQQNRTLSILFQQRVRPTSDLLLQ 269
Cdd:pfam05483 483 EKLKNIELTAHCDKLLLENKELTQEASDMTLE 514
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
53-261 |
8.95e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 8.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 53 VARLQREVAQ------RRSEGAMHEklIHELEEERHLRLQSEKRLQEVTLESERNRIQMRGLQQQFSRMEETVRNL--LQ 124
Cdd:COG4717 48 LERLEKEADElfkpqgRKPELNLKE--LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 125 SQGPPEQKKEDTvnimvyQEKLSEEERKhKEALEDRHMVVDEDSRSEgssadegKEKTKLLLERLKALEAENSALALENE 204
Cdd:COG4717 126 QLLPLYQELEAL------EAELAELPER-LEELEERLEELRELEEEL-------EELEAELAELQEELEELLEQLSLATE 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1246200473 205 NQREQYERCLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTLSIlfQQRVR 261
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL--EERLK 246
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1208-1466 |
1.04e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 47.47 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1208 SPLGLRAQESLAEGLPLETATP-----ESLESSTPGADGEDAVENKSVKRSLSSNKPLLKPALGMNGAKARSQSFSAHSG 1282
Cdd:PHA03307 164 SDAASSRQAALPLSSPEETARApssppAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1283 DKPPTASVEG--PGKVRTQIITNTAERGNSLTRQSSSTEGSPSKTASAPVSDGLPGAGRPLGHPSSRQGSLGSTGSSSSQ 1360
Cdd:PHA03307 244 SSGCGWGPENecPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1361 HGSPSklPLRILPKSEGPLAPPGTEEQPAyaqgegvrvtAPEEAGSDHGRCPSTPKDGLGAPQSPGRTRHPSSFETSRTS 1440
Cdd:PHA03307 324 SSSSS--TSSSSESSRGAAVSPGPSPSRS----------PSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRAR 391
|
250 260
....*....|....*....|....*..
gi 1246200473 1441 KLET-SGRYPDTSTTRTGAVSPEAPLS 1466
Cdd:PHA03307 392 AAVAgRARRRDATGRFPAGRPRPSPLD 418
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
819-1034 |
1.36e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 47.00 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 819 PEASLMVPSAGPvTLERSPAPGklsrfkkSEGPEPLFALPPDSHIPKPSTQLPHGSKmfsRRDWVQ-YSRSQIPASQLLP 897
Cdd:PRK10263 345 PVASVDVPPAQP-TVAWQPVPG-------PQTGEPVIAPAPEGYPQQSQYAQPAVQY---NEPLQQpVQPQQPYYAPAAE 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 898 RPPAEPSDDGEPPTRDKHCDPGP---EAGVRSPSLPSPPGRSVS--LLARPSYDYLSP----PSWAKPESGVPSEAARTV 968
Cdd:PRK10263 414 QPAQQPYYAPAPEQPAQQPYYAPapeQPVAGNAWQAEEQQSTFApqSTYQTEQTYQQPaaqePLYQQPQPVEQQPVVEPE 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246200473 969 LKSPPLKGSSAPIIYFNQtVTEVQGKKPS--VAFKKPVFTP---PPPSTETAIQTRCPAHSPSSSFAGMAP 1034
Cdd:PRK10263 494 PVVEETKPARPPLYYFEE-VEEKRAREREqlAAWYQPIPEPvkePEPIKSSLKAPSVAAVPPVEAAAAVSP 563
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
35-228 |
1.88e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 35 LLTQLEEQHRSLWRE-----KLAVARLQREVAQRRSEGAMHEKLiHELEEERHlrlQSEKRLQEV-----TLESERNRI- 103
Cdd:COG4717 47 LLERLEKEADELFKPqgrkpELNLKELKELEEELKEAEEKEEEY-AELQEELE---ELEEELEELeaeleELREELEKLe 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 104 QMRGLQQQFSRMEETVRNLlqSQGPP-----EQKKEDTVNIMVYQEKLSEEERKHKEALEDRHMVVDEDSRSEGSSADEG 178
Cdd:COG4717 123 KLLQLLPLYQELEALEAEL--AELPErleelEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1246200473 179 KEKtklLLERLKALEAENSALALENENQREQYERCLDEVANQVVQALLTQ 228
Cdd:COG4717 201 LEE---LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
43-209 |
3.19e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 43 HRSLWREKLAVARLQREV----AQRRSEGAMHEKLIHELEEERHLRLQSEKRLQEVTLESER--NRIQMRglQQQFSRME 116
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRileeAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKleKRLLQK--EENLDRKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 117 ETV---RNLLQSQGPPEQKKEDTVNIMvyQEKLSEEERKHKEALEdrhmvvdedsRSEGSSADEGKEktkLLLERLKA-L 192
Cdd:PRK12704 103 ELLekrEEELEKKEKELEQKQQELEKK--EEELEELIEEQLQELE----------RISGLTAEEAKE---ILLEKVEEeA 167
|
170
....*....|....*..
gi 1246200473 193 EAENSALALENENQREQ 209
Cdd:PRK12704 168 RHEAAVLIKEIEEEAKE 184
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
849-1103 |
3.43e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.55 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 849 EGPEPLFALPPDSHIPKPSTQLPHGSKMFSRRDWVQYSRSQIPASQLLPRPPAEPSDDGePPTRDKhcDPGPEAGVRSPS 928
Cdd:PHA03307 49 ELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPT-PPGPSS--PDPPPPTPPPAS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 929 LPSPPGRSVSLLARPSYDYLSPPSWAKPESGVPSEAARTVLKSPPLKGSSAPIIyfNQTVTEVQGKKPSVAFKKPVF--- 1005
Cdd:PHA03307 126 PPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSP--EETARAPSSPPAEPPPSTPPAaas 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1006 -TPPPPSTETAIQTRCPAHSP--------SSSFAGMAPGPPKVSPKRSVPKTP-PHQTLGTTQTDIGLRTPKNCPSTREP 1075
Cdd:PHA03307 204 pRPPRRSSPISASASSPAPAPgrsaaddaGASSSDSSSSESSGCGWGPENECPlPRPAPITLPTRIWEASGWNGPSSRPG 283
|
250 260
....*....|....*....|....*...
gi 1246200473 1076 LEipSPKGVSPARkgqlnDSVSTPPKPS 1103
Cdd:PHA03307 284 PA--SSSSSPRER-----SPSPSPSSPG 304
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
30-220 |
3.49e-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: 45.14 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 30 KYIEHLLTQLEEQHRSLWREklaVARLQREVAQRrsegamhEKLIHELEEERHlrlQSEKRLQEVTLESERNRIQMRGLQ 109
Cdd:COG4942 37 AELEKELAALKKEEKALLKQ---LAALERRIAAL-------ARRIRALEQELA---ALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 110 QQFSRM---------EETVRNLLQSQGPpeqkkEDTVNIMVYQEKLSEEERKHKEALEDRhmvVDEDSRSEGSSADEGKE 180
Cdd:COG4942 104 EELAELlralyrlgrQPPLALLLSPEDF-----LDAVRRLQYLKYLAPARREQAEELRAD---LAELAALRAELEAERAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1246200473 181 KTKLLLE------RLKALEAENSALALENENQREQYERCLDEVANQ 220
Cdd:COG4942 176 LEALLAEleeeraALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
24-289 |
3.72e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 24 EYMDSNKYIEHLLTQLEEQHRSLWREKLAVARLQREVAQRRSegamhekLIHELEEERHLRLQSEKRLQEVTLESERNRI 103
Cdd:TIGR00618 536 TYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQ-------CDNRSKEDIPNLQNITVRLQDLTEKLSEAED 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 104 QMRGLQQqfsrmeetvRNLLQSQgpPEQKKEDtvnIMVYQEKLSEEERKHKEALEDRHMVVDEDSRSEGSSADegKEKTK 183
Cdd:TIGR00618 609 MLACEQH---------ALLRKLQ--PEQDLQD---VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSI--RVLPK 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 184 LLLERLKALEAENSALALENENQREQYERClDEVANQVVQALLTQKDLREE-CVKLKTRVFDLEQQNRTLSILFQ--QRV 260
Cdd:TIGR00618 673 ELLASRQLALQKMQSEKEQLTYWKEMLAQC-QTLLRELETHIEEYDREFNEiENASSSLGSDLAAREDALNQSLKelMHQ 751
|
250 260 270
....*....|....*....|....*....|....
gi 1246200473 261 RPTSDLLLQKLHSR-----ILDLSTGDLLSDVER 289
Cdd:TIGR00618 752 ARTVLKARTEAHFNnneevTAALQTGAELSHLAA 785
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
891-1442 |
4.04e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.70 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 891 PASQLLPRPPAEPSDDGEPPTRDKHCDPGPEAGVRS--PSLPSPPGRSVSllarPSYDYLSPPSWAKPESGVPSEAArtv 968
Cdd:PHA03247 2551 PPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRArrPDAPPQSARPRA----PVDDRGDPRGPAPPSPLPPDTHA--- 2623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 969 LKSPPLKGSSAPiiyfnqTVTEVQGKKPSVAFKKPVFTPPPPSTETAIQTRCPAHSPSSSFAGMAP----GPPKVSPKRS 1044
Cdd:PHA03247 2624 PDPPPPSPSPAA------NEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPrrraARPTVGSLTS 2697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1045 VPKTPPHQtlgttqtdiglRTPKNCPSTREPlEIPSPKGVSPARKGQLNDSVSTPPKPSFLGVNESPSSQVSSPSSSAPS 1124
Cdd:PHA03247 2698 LADPPPPP-----------PTPEPAPHALVS-ATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAG 2765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1125 KSHSTPqgcqnpqerglkTRLPVGlkvfmkSPQllRKSSTVPGKHEKDSLNEASKSSAAVSKDKPGTSRNASslettgge 1204
Cdd:PHA03247 2766 PPAPAP------------PAAPAA------GPP--RRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAA-------- 2817
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1205 rnvsplgLRAQESLAEGLPLETATPESLESSTPGAdgedavenksvkrslssnkplLKPALGMNGAKARSQSFSAHSGDK 1284
Cdd:PHA03247 2818 -------LPPAASPAGPLPPPTSAQPTAPPPPPGP---------------------PPPSLPLGGSVAPGGDVRRRPPSR 2869
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1285 PPTASVEGPGKVRTQIITNTAergnsLTRQSSSTEGSPSKTASAPVSDGLPgagRPLGHPSSRQGSLGSTgssssqhgsp 1364
Cdd:PHA03247 2870 SPAAKPAAPARPPVRRLARPA-----VSRSTESFALPPDQPERPPQPQAPP---PPQPQPQPPPPPQPQP---------- 2931
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1365 sklPLRILPKSEGPLAPpgtEEQPAYAQGEGVRVTAPEEAGSDHGRCP------STPKDGLGAPQS--PGRTRHPSSFET 1436
Cdd:PHA03247 2932 ---PPPPPPRPQPPLAP---TTDPAGAGEPSGAVPQPWLGALVPGRVAvprfrvPQPAPSREAPASstPPLTGHSLSRVS 3005
|
....*.
gi 1246200473 1437 SRTSKL 1442
Cdd:PHA03247 3006 SWASSL 3011
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
44-293 |
4.69e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 44 RSLWREKLAVARLQREVAQRRSEgamhekliheLEEerhlrLQSEKRLQEVTLESERNRiqmrgLQQQFSRMEETVRNLL 123
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREE----------LEQ-----AREELEQLEEELEQARSE-----LEQLEEELEELNEQLQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 124 QSQGPPEQKKEdtvNIMVYQEKLSEEERKHKEALEDRHMVVDEDSRSEgSSADEGKEKTKLLLERLKALEAENSALALEN 203
Cdd:COG4372 91 AAQAELAQAQE---ELESLQEEAEELQEELEELQKERQDLEQQRKQLE-AQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 204 ENQREQYERCLDEVANQVVQALLTQKDLREECVKLKTRVFDL-EQQNRTLSILFQQRVRPTSDLLLQKLHSRILDLSTGD 282
Cdd:COG4372 167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLiESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
250
....*....|.
gi 1246200473 283 LLSDVERSRSL 293
Cdd:COG4372 247 DKEELLEEVIL 257
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
18-227 |
6.34e-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: 44.66 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 18 LDSSLVEYMDSNKYIEHLLTQLEEQHRSLwREKLAVARLQREVAQRRSEGAmhEKLIHELEEERHLRLQSEKRLQEvtlE 97
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEELESL-EAELEELEAELEELESRLEEL--EEQLETLRSKVAQLELQIASLNN---E 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 98 SERNRIQMRGLQQQFSRMEETVRNLLQSqgPPEQKKEDTVNIMVYQEKLSEEERKHKEALEDRHMVVDEDSRSEGSSADE 177
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELLKK--LEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246200473 178 GKEKTKLLLERLKALEA---------ENSALALENENQ--------------REQYERCLDEVANQVVQALLT 227
Cdd:TIGR02168 480 AERELAQLQARLDSLERlqenlegfsEGVKALLKNQSGlsgilgvlselisvDEGYEAAIEAALGGRLQAVVV 552
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
19-199 |
7.54e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 19 DSSLVEYMDSNKYIEHLLTQLEEQHRSLWREKLAVA-RLQRE-------------VAQRRSEgamHEKLIHELE------ 78
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQeQLQAEtelcaeaeemrarLAARKQE---LEEILHELEsrleee 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 79 EERHLRLQSE-KRLQ------EVTLESE---RNRIQMR--GLQQQFSRMEETVrNLLQSQGPPEQKK----EDTVNIMVY 142
Cdd:pfam01576 88 EERSQQLQNEkKKMQqhiqdlEEQLDEEeaaRQKLQLEkvTTEAKIKKLEEDI-LLLEDQNSKLSKErkllEERISEFTS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246200473 143 QekLSEEERKHK--EALEDRH--MVVDEDSRSegssadEGKEKTKLLLERLK-ALEAENSAL 199
Cdd:pfam01576 167 N--LAEEEEKAKslSKLKNKHeaMISDLEERL------KKEEKGRQELEKAKrKLEGESTDL 220
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1176-1467 |
7.98e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.39 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1176 EASKSSAAVSKDKPGTSRNASSLETTGGERNVSPLGLRAQESLAEGLPLETATPESLESSTPGADGEDAVENKSVKRSLS 1255
Cdd:PHA03307 47 SAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1256 SNKP------LLKPALGMNGAKARSQSFSAHSGDKPPTASVEGPGKVRTQIITNTAER----------GNSLTRQSSSTE 1319
Cdd:PHA03307 127 PPSPapdlseMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARapssppaeppPSTPPAAASPRP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1320 GSPSKTASAPVSDGLPGAGRPLGHPSSRQGSLGSTGSSSSQHGSPSKLPLRILPkseGPLAPPGTEEQPAYAQGEGVRVT 1399
Cdd:PHA03307 207 PRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRP---APITLPTRIWEASGWNGPSSRPG 283
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246200473 1400 APEEAGSDHGRCPSTPKDGLGAPQSPGRTRHPSSFETSRTSKLETSGRYPDTSttRTGAVSPEAPLSP 1467
Cdd:PHA03307 284 PASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESS--RGAAVSPGPSPSR 349
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
176-277 |
9.82e-04 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 41.53 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 176 DEGKEKTKLLLERLKALEAENSALALENE---NQREQYERCLDEVANQVVQAlltQKDLREECVKLKTrvfDLEQQNRTL 252
Cdd:pfam11559 48 DRDLEFRESLNETIRTLEAEIERLQSKIErlkTQLEDLERELALLQAKERQL---EKKLKTLEQKLKN---EKEELQRLK 121
|
90 100 110
....*....|....*....|....*....|
gi 1246200473 253 SILFQQRVRPT-----SDLLLQKLHSRILD 277
Cdd:pfam11559 122 NALQQIKTQFAhevkkRDREIEKLKERLAQ 151
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
40-211 |
1.46e-03 |
|
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: 43.57 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 40 EEQHRSLWREKLAVA--RLQREVAQRRSEGAMHEKLIHELE---EERHLRLQSEKRLQEVTLESERNRIQMRGLQQQFSR 114
Cdd:pfam17380 409 EERQRKIQQQKVEMEqiRAEQEEARQREVRRLEEERAREMErvrLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKR 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 115 MEETVRNLLQSQGPP---------------EQKKEDTVNIMVYQE--KLSEEERKHKEALEDRHMVVDEDSR-SEGSSAD 176
Cdd:pfam17380 489 AEEQRRKILEKELEErkqamieeerkrkllEKEMEERQKAIYEEErrREAEEERRKQQEMEERRRIQEQMRKaTEERSRL 568
|
170 180 190
....*....|....*....|....*....|....*
gi 1246200473 177 EGKEKTKLLLERLKaleaensalalENENQREQYE 211
Cdd:pfam17380 569 EAMEREREMMRQIV-----------ESEKARAEYE 592
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
5-234 |
1.47e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 5 RQLEKRDFGKRLSLDSSLveymdSNKYIEHLLTQLEEQHRSLWREKLAVARLQREVAQRRSEGAMHEKLIHELEEERHLR 84
Cdd:COG4717 317 EEEELEELLAALGLPPDL-----SPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAAL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 85 LQSEKRLQevtLESERNRiqmrgLQQQFSRMEETVRNLLQSQGPPEQKKEdtvnIMVYQEKLSEEERKHKEALEDRhmvv 164
Cdd:COG4717 392 EQAEEYQE---LKEELEE-----LEEQLEELLGELEELLEALDEEELEEE----LEELEEELEELEEELEELREEL---- 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246200473 165 dedsrsegssadegkektKLLLERLKALEAEN--SALALENENQREQYERCLDEVA-NQVVQALL--TQKDLREE 234
Cdd:COG4717 456 ------------------AELEAELEQLEEDGelAELLQELEELKAELRELAEEWAaLKLALELLeeAREEYREE 512
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1-234 |
2.38e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1 MEGKRQLEKRDFGKRL-SLDSSLVEYMDSNKYIEHLLTQLEEQhrslwreklaVARLQREVaqrRSEGAMHEKLIHELEE 79
Cdd:pfam01576 286 ARNKAEKQRRDLGEELeALKTELEDTLDTTAAQQELRSKREQE----------VTELKKAL---EEETRSHEAQLQEMRQ 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 80 eRHLrlQSEKRLQEVTLESERNRIQM----RGLQQQFSRMEETVRNLLQSQGPPEQK-KEDTVNIMVYQEKLSEEERKHK 154
Cdd:pfam01576 353 -KHT--QALEELTEQLEQAKRNKANLekakQALESENAELQAELRTLQQAKQDSEHKrKKLEGQLQELQARLSESERQRA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 155 EALEDRHMVVDE-DSRSEGSSADEGK-----------------------EKT--KL-LLERLKALEAENSALALENENQR 207
Cdd:pfam01576 430 ELAEKLSKLQSElESVSSLLNEAEGKniklskdvsslesqlqdtqellqEETrqKLnLSTRLRQLEDERNSLQEQLEEEE 509
|
250 260
....*....|....*....|....*..
gi 1246200473 208 EQYERCLDEVANQVVQALLTQKDLREE 234
Cdd:pfam01576 510 EAKRNVERQLSTLQAQLSDMKKKLEED 536
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
48-248 |
2.45e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 48 REKLAvaRLQREVAQRRSEGAMHEKLIHELEEERHlRLQSEKRLQEVTLESERNRIQMRGLQQQFSRMEETVRNLLQSQg 127
Cdd:COG4913 609 RAKLA--ALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASS- 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 128 ppeqkkeDTVnimvyqEKLSEEERKHKEALEDrhmVVDEDSRSEGSSADEGKEKTKLLLERLKALEAENSALALENENQR 207
Cdd:COG4913 685 -------DDL------AALEEQLEELEAELEE---LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1246200473 208 EQYERCLDEVANQVVQALLtQKDLREECVKLKTRVFDLEQQ 248
Cdd:COG4913 749 ALLEERFAAALGDAVEREL-RENLEERIDALRARLNRAEEE 788
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
38-223 |
2.94e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.83 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 38 QLEEQHRSLWREKLaVARLQREVAQRRSEGAMHEKLIHELEEERHLRLQSEKRLQEVtlesERNRIQMRGLQQQFSRMEE 117
Cdd:pfam13868 172 EAEREEIEEEKERE-IARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEA----EKKARQRQELQQAREEQIE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 118 TVRNLLQSQGppEQKKEDTVNIMvyqEKLSEEERKHKEALEDRHMVVDEdsrsegssadEGKEKTKLLLERLKALEAENS 197
Cdd:pfam13868 247 LKERRLAEEA--EREEEEFERML---RKQAEDEEIEQEEAEKRRMKRLE----------HRRELEKQIEEREEQRAAERE 311
|
170 180
....*....|....*....|....*....
gi 1246200473 198 ALALENENQRE---QYERCLDEVANQVVQ 223
Cdd:pfam13868 312 EELEEGERLREeeaERRERIEEERQKKLK 340
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
1299-1507 |
3.74e-03 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1299 QIITNTAERGNSLTRQSSSTEGSPSKtasAPVSDGLPGAGRplGHPSSRQGSLGSTGSSSSQHGSpsKLPLRILPKSEGP 1378
Cdd:PTZ00449 487 KLIKKSKKKLAPIEEEDSDKHDEPPE---GPEASGLPPKAP--GDKEGEEGEHEDSKESDEPKEG--GKPGETKEGEVGK 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 1379 LAPPGTEEQPAYAQGEGVRVTAPEEagSDHGRCPSTPKDGlGAPQSPGRTRHPSSFETSRTSKLETSGRYPDTSTTRTGA 1458
Cdd:PTZ00449 560 KPGPAKEHKPSKIPTLSKKPEFPKD--PKHPKDPEEPKKP-KRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRP 636
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1246200473 1459 VSPEAPLSPTIEEkvmlciqenvekGQVQTKSTSVDAKPKP--GPSFASWF 1507
Cdd:PTZ00449 637 PPPQRPSSPERPE------------GPKIIKSPKPPKSPKPpfDPKFKEKF 675
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
49-311 |
3.76e-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: 42.27 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 49 EKLAVARLQREVAQRRSEGAMHEKLIHELEEERHLRLQSEKRLQEVTLEserNRIQMRGLQQQFSRMEEtvrnlLQSQGP 128
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE---YLLYLDYLKLNEERIDL-----LQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 129 PEQKKEdtvnimvyqEKLSEEERKHKEALEDRHMVVDEDSRSEgssadegkektKLLLERLKALEAENsalaLENENQRE 208
Cdd:pfam02463 248 DEQEEI---------ESSKQEIEKEEEKLAQVLKENKEEEKEK-----------KLQEEELKLLAKEE----EELKSELL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 209 QYERCLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTLSILFQQRVRPTSDLLLQKLHSRiLDLSTGDLLSDVE 288
Cdd:pfam02463 304 KLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLE-QLEEELLAKKKLE 382
|
250 260
....*....|....*....|...
gi 1246200473 289 RSRSLTHSRTDVEMHECQLNTKS 311
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEEEK 405
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
35-245 |
3.83e-03 |
|
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.
Pssm-ID: 405365 [Multi-domain] Cd Length: 191 Bit Score: 40.55 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 35 LLTQLEEQHRSLWREKLAVARLQREVAqrrsegAMHEKLIHELEEerhlrlqsekrlqevtleSERNRIQMRGLQQ--QF 112
Cdd:pfam14662 6 LLTCVEDLQANNQKLLQENSKLKATVE------TREETNAKLLEE------------------NLNLRKQAKSQQQavQK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 113 SRM-EETVRNLLQSqgppEQKKEDTVNIMVYQEKLSEEERKHKEALEDRHMVVDEDSRSEgssADEGKEKTKLLLER--- 188
Cdd:pfam14662 62 EKLlEEELEDLKLI----VNSLEEARRSLLAQNKQLEKENQSLLQEIESLQEENKKNQAE---RDKLQKKKKELLKSkac 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1246200473 189 LKALEAENSALALENENQREQYERCLDEVANQVVQALLTQKDLREECVKLKTRVFDL 245
Cdd:pfam14662 135 LKEQLHSCEDLACNRETILIEKTTQIEELKSTVEEYSSIEEELRAEKSRLESQLPDM 191
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
36-252 |
4.09e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 36 LTQLEEqhrslWREKLAVARLQREVAQRRSEGAMH--EKLIHELEE-ERHLRLQS-EKRLQEVTLESER---NRIQMRGL 108
Cdd:PRK02224 161 LGKLEE-----YRERASDARLGVERVLSDQRGSLDqlKAQIEEKEEkDLHERLNGlESELAELDEEIERyeeQREQARET 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 109 QQQFSRMEETVRNLLQSQGPPEQKKEDTvnimvyQEKLSEEERK---HKEALEDRHMVVDE-DSRSEGSSADEGKEktkl 184
Cdd:PRK02224 236 RDEADEVLEEHEERREELETLEAEIEDL------RETIAETEREreeLAEEVRDLRERLEElEEERDDLLAEAGLD---- 305
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246200473 185 llerlkalEAENSALALenenQREQYERCLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTL 252
Cdd:PRK02224 306 --------DADAEAVEA----RREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEEL 361
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
108-293 |
4.37e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 108 LQQQFSRMEETVRNLLQSQGPPEQKKEDTVnimvyQEKLSEEERKHKEALEDRHMVVDEDSRSEGSSADEGK------EK 181
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAAL-----LEAKELLLRERNQQRQEARREREELQREEERLVQKEEqldaraEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 182 TKLLLERLKALEAENSALALENENQREQYERCLDEV-------ANQVVQALLtQKDLREEC---VKLKTRVFDLEQQNRT 251
Cdd:PRK12705 100 LDNLENQLEEREKALSARELELEELEKQLDNELYRVagltpeqARKLLLKLL-DAELEEEKaqrVKKIEEEADLEAERKA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1246200473 252 LSILFQQRVRPTSDLllqklhSRILDLSTGDLLSDVERSRSL 293
Cdd:PRK12705 179 QNILAQAMQRIASET------ASDLSVSVVPIPSDAMKGRII 214
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
20-247 |
4.89e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 20 SSLVEYMDSNKYIEHLLTQLEEQHRSLWREklaVARLQREVAQRRSEGAMHEKLIHELEEER----HLRLQSEKRLQEVT 95
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLRE---INEISSELPELREELEKLEKEVKELEELKeeieELEKELESLEGSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 96 LESER---NRIQMRGLQQQFSRMEETVRNLLQSQGppeqKKEDTVNIMVYQEKLSEEER---KHKEALEDRHMVVDE--- 166
Cdd:PRK03918 256 KLEEKireLEERIEELKKEIEELEEKVKELKELKE----KAEEYIKLSEFYEEYLDELReieKRLSRLEEEINGIEErik 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 167 DSRSEGSSADEGKEKTKLLLERLKALE----AENSALALENENQR---EQYERCLDEVANQVVQALLTQKDLREECVKLK 239
Cdd:PRK03918 332 ELEEKEERLEELKKKLKELEKRLEELEerheLYEEAKAKKEELERlkkRLTGLTPEKLEKELEELEKAKEEIEEEISKIT 411
|
....*...
gi 1246200473 240 TRVFDLEQ 247
Cdd:PRK03918 412 ARIGELKK 419
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
32-234 |
5.51e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 32 IEHLLTQLEEQHRSLWREKLAVARLQREVAQRRSEGAMHEKLIHELEEERHLRLQSEKRLQEVTLESERNRIQMRGLQQQ 111
Cdd:COG1196 619 GDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 112 FSRMEETVRNLLQSQGPPEQKKEDTVNimvyQEKLSEEERKHKEALEDRHMVVDEDS----RSEGSSADEGKEKTKLLLE 187
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEA----LEEQLEAEREELLEELLEEEELLEEEaleeLPEPPDLEELERELERLER 774
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1246200473 188 RLKALEAENsALAL-ENENQREQYErcldevanqvvqALLTQK-DLREE 234
Cdd:COG1196 775 EIEALGPVN-LLAIeEYEELEERYD------------FLSEQReDLEEA 810
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
4-252 |
5.74e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 4 KRQLEKRDfgkrlSLDSSLVEYMDSNKYIEHLLTQLEEQHRSLWREKLAVARLQRevAQRRSEGAMHEKLIHELEEerhl 83
Cdd:PRK03918 327 EERIKELE-----EKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELER--LKKRLTGLTPEKLEKELEE---- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 84 rlqSEKRLQEVTLESERNRIQMRGLQQQFSRMEETVRNLLQSQGP-P----EQKKEDTVNIMV-YQEKLSEEERKHKEAL 157
Cdd:PRK03918 396 ---LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcPvcgrELTEEHRKELLEeYTAELKRIEKELKEIE 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 158 EDRHMVVDEDSRSEGSSADEGK-EKTKLLLERLKALEAENSALALEN-ENQREQYERcLDEVANQVVQALLTQKDLREEC 235
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESElIKLKELAEQLKELEEKLKKYNLEElEKKAEEYEK-LKEKLIKLKGEIKSLKKELEKL 551
|
250
....*....|....*..
gi 1246200473 236 VKLKTRVFDLEQQNRTL 252
Cdd:PRK03918 552 EELKKKLAELEKKLDEL 568
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
20-256 |
8.04e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 20 SSLVEYMDSNKYIEHLLTQLEEQHRSLwreKLAVARLQREVAQRRSE-GAMHEKLIHELEEERHLRlqseKRLQEVTLES 98
Cdd:TIGR04523 204 SNLKKKIQKNKSLESQISELKKQNNQL---KDNIEKKQQEINEKTTEiSNTQTQLNQLKDEQNKIK----KQLSEKQKEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 99 ERNRIQMRGLQQQFSRMEETVRNLLQsqgppeQKKEDTVNimvyqeKLSEEERKHKEALEDRHMVVDE------------ 166
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNN------QKEQDWNK------ELKSELKNQEKKLEEIQNQISQnnkiisqlneqi 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 167 --------DSRSEGSSAD-EGKEKTKLL----------LERLKALEAENSALALENENQREQyERCLDE---VANQVVQA 224
Cdd:TIGR04523 345 sqlkkeltNSESENSEKQrELEEKQNEIeklkkenqsyKQEIKNLESQINDLESKIQNQEKL-NQQKDEqikKLQQEKEL 423
|
250 260 270
....*....|....*....|....*....|...
gi 1246200473 225 LLTQ-KDLREECVKLKTRVFDLEQQNRTLSILF 256
Cdd:TIGR04523 424 LEKEiERLKETIIKNNSEIKDLTNQDSVKELII 456
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
32-252 |
8.68e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 32 IEHLLTQLEEQHRSLWREKLAVARLQREVAQRRSEGAMHEKLIHELEEERHLRLQSEKRLQEVTLESERNRI----QMRG 107
Cdd:COG4372 75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAereeELKE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 108 LQQQFSRMEETVRNLLQS-QGPPEQKKEDTVNIMVYQEKLSEEERKHKEALEDRHMVVDEDSRSEGSSADEGKEKTKLLL 186
Cdd:COG4372 155 LEEQLESLQEELAALEQElQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246200473 187 ERLKALEAENSALALENENQREQYERCLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTL 252
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLAL 300
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
826-1034 |
8.75e-03 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 40.96 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 826 PSAGPVtlerSPAPGKLSRFKKSEGPEPLfALPPDSHIPKPSTQLPHGSkmfSRRDWVQYSRSQIPASQLLPRP---PAE 902
Cdd:PRK14086 90 PSAGEP----APPPPHARRTSEPELPRPG-RRPYEGYGGPRADDRPPGL---PRQDQLPTARPAYPAYQQRPEPgawPRA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 903 PSDDGEPPTRDKHCDPGPEAGVRSPSLPSPPGRSVSLLARPSYDYLS-PPSWAKPESGVPSEAARTVLKSPPlkGSSAPi 981
Cdd:PRK14086 162 ADDYGWQQQRLGFPPRAPYASPASYAPEQERDREPYDAGRPEYDQRRrDYDHPRPDWDRPRRDRTDRPEPPP--GAGHV- 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1246200473 982 iyfnqtVTEVQGKKPSVAFKKPVFTPPPPSTETAIQTrcPAHSPSSSFAGMAP 1034
Cdd:PRK14086 239 ------HRGGPGPPERDDAPVVPIRPSAPGPLAAQPA--PAPGPGEPTARLNP 283
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
883-1051 |
9.53e-03 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 40.91 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 883 VQYSRSQIPASQLLPRPPAEPSDDGEPPTRDKHCDPGPEAGVRSPSLPSPPGRSVSL------LARPSYDYLSPPSWAKP 956
Cdd:pfam03154 174 LQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLiqqtptLHPQRLPSPHPPLQPMT 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246200473 957 ESGVPSEAARTVLKSPPLKGSSAPIIYFNQT-VTEVQGKKPSVAFKKPVFT-----PPPPSTETAIQTRCPAHSPSSSFA 1030
Cdd:pfam03154 254 QPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTgPSHMQHPVPPQPFPLTPQSsqsqvPPGPSPAAPGQSQQRIHTPPSQSQ 333
|
170 180
....*....|....*....|.
gi 1246200473 1031 GMAPGPPKVSPKRSVPKTPPH 1051
Cdd:pfam03154 334 LQSQQPPREQPLPPAPLSMPH 354
|
|
| |
