|
Name |
Accession |
Description |
Interval |
E-value |
| EP400_N |
pfam15790 |
E1A-binding protein p400, N-terminal; EP400_N is a family of eukaryote proteins. the exact ... |
2-470 |
0e+00 |
|
E1A-binding protein p400, N-terminal; EP400_N is a family of eukaryote proteins. the exact function of this domain is not known. This family is largely low-complexity residues.
Pssm-ID: 434938 [Multi-domain] Cd Length: 489 Bit Score: 589.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 2 MHHGTGPQNVQHQLQRSRACPGSEG---EEQPAHPNPPPSPAAPFAPSASPSAPQSPSYQIqqLMNRSPATGQNVNITLQ 78
Cdd:pfam15790 1 MHHGSGSQNVQRQLQRSKSVSGSEEqqqEQQPATVNHPQSPVTTFAPAASPSAPQSPNYQI--IMSRSPVTGQNVNITLQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 79 SVGPVVGGNQQITLAPLPLPSPTSPGFQFSAQPRRFEHGSPSYIQVTSPLSQQVQTQSPTQPSPGPGQALQnvRAGAPGP 158
Cdd:pfam15790 79 NVGQMVAGNQQITLTPLPLQSPASPGFQHSAPQWRFEHGSPSYIQVTSPLPQQVQPQSPTQHSPVPLQGVQ--RPGAPGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 159 GLGLCSSSPTGgFVDASVLVRQISL-SPSSGGHFVFQDGSGLTQIAQG-AQVQLQHPGTPITVRERRPSQPHTQSGGTIH 236
Cdd:pfam15790 157 GLGVCGQSPTR-FVDASMLVRQISLgSPSGGGHFVYQDGTGLAQIAPGaGQVQLASPGTPGSVRERRLSQPHSQTGGTIH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 237 HLGPQSPAAAGgAGLQPLASPSHITTANLPPQISSIIQGQlvqqqqvlqgppLPRPLGFERTPGVLLPGAGGAAGF-GMT 315
Cdd:pfam15790 236 HLGPQSPAAAG-AGLQTLGSPGHITTSNLPPQISSIIQGQ------------LARPLGFEKTAQVVVAGAGGPAASfGIP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 316 SPPPPTSPSRTAVPPGLSSLPLTSVGNTG-MKKVPKKLEEIPPASPEMAQMRKQCLDYHYQEMQALKEVFKEYLIELFFL 394
Cdd:pfam15790 303 SSIPPTSPSRTSPPPGLSSNPLTSTGMSGsVKKVPKKLEEIAPATPEIAQLRKQCLDHHTKKMESLKEVFKEYLIELFFL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 395 QHFQGNMMDFLAFKKKHYAPLQAYLRQNDLDIeeeeEEEEEEEEKSEVINDEQ--------------------------- 447
Cdd:pfam15790 383 QHLQGNMMDFLAFKKKHCVPLYTYLRQNDLDL----EEEEEEEEQSEVINDEVkvvtgkdgqtgtpvaiatqlppnvsaa 458
|
490 500 510
....*....|....*....|....*....|.
gi 7959257 448 --------QALAGSLVAGAGSTVETDLFKRQ 470
Cdd:pfam15790 459 fstqqqpfQAHQGTASAGITNTVEMDAFKRQ 489
|
|
| DEXQc_SRCAP |
cd18003 |
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ... |
1056-1272 |
1.08e-135 |
|
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or DOMO1) is the core catalytic component of the multiprotein chromatin-remodeling SRCAP complex, that is necessary for the incorporation of the histone variant H2A.Z into nucleosomes. SRCAP is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350761 [Multi-domain] Cd Length: 223 Bit Score: 419.83 E-value: 1.08e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1135
Cdd:cd18003 1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1136 YIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSP 1215
Cdd:cd18003 81 YYGSAKERKLKRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7959257 1216 LHNTFLELWTMVHFLVPGI------SRPYLSSPLRAPSEESQDYYHKVVIRLHRVTQPFILRR 1272
Cdd:cd18003 161 LQNSLMELWSLMHFLMPHIfqshqeFKEWFSNPLTAMSEGSQEENEELVRRLHKVLRPFLLRR 223
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
1030-1351 |
6.33e-60 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 225.84 E-value: 6.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1030 EAILPKGSARVTTSvkfnaPSLLYGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHL 1109
Cdd:PLN03142 149 DGLGGSGGTRLLVQ-----PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHM 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1110 VVVRSCNILKWELELKRWCPGLKILSYIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRV 1189
Cdd:PLN03142 224 VVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1190 KGMTERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPGI--SRPYLSSPLRAPSEESQdyyHKVVIRLHRVTQP 1267
Cdd:PLN03142 304 KNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIfsSAETFDEWFQISGENDQ---QEVVQQLHKVLRP 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1268 FILRRTKRDVEKQLTKKYEHVLKCRLSNRQKALYEdVILQPGTQEALKSGHFVNVLSILVRLQRICNHPGLVEPRHPGSS 1347
Cdd:PLN03142 381 FLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYK-ALLQKDLDVVNAGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPP 459
|
....
gi 7959257 1348 YVAG 1351
Cdd:PLN03142 460 YTTG 463
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
850-1339 |
7.71e-60 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 219.71 E-value: 7.71e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 850 EQVVEIKLRVELEEKRKKALNLQKVSRRGKELRPKGFDALQESSLDSGMSGRKRKASISLTDDEVDDEEETIEEEEANEG 929
Cdd:COG0553 35 LARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLRLLLALLLLALLLLLAGLLALALLLLALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 930 VVDHQTELSNLAKEAELPLLDLMKLYEGAFLPSSQWPRPKPDGEDTSGEEDADDCPGDRESRKDLVLIDSLFIMDQFKAA 1009
Cdd:COG0553 115 GLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELAL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1010 ERMNIGK-PNAKDIADVTAVAEAILPKGSARVTTSVKFNAPSLLYGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKT 1088
Cdd:COG0553 195 LAAEAELlLLLELLLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1089 VQIIAFFAHLAcNEGNWGPHLVVV-RSCnILKWELELKRWCPGLKILSYIGShrelkAKRQEWAEP-NSFHVCITSYTQF 1166
Cdd:COG0553 275 IQALALLLELK-ERGLARPVLIVApTSL-VGNWQRELAKFAPGLRVLVLDGT-----RERAKGANPfEDADLVITSYGLL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1167 FRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPGisrpYLSSPlrap 1246
Cdd:COG0553 348 RRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPG----LLGSL---- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1247 sEESQDYYHKVVI--------RLHRVTQPFILRRTKRDVEKQLTKKYEHVLKCRLSNRQKALYEDVI--LQPGTQEALKS 1316
Cdd:COG0553 420 -KAFRERFARPIEkgdeealeRLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLeyLRRELEGAEGI 498
|
490 500
....*....|....*....|...
gi 7959257 1317 GHFVNVLSILVRLQRICNHPGLV 1339
Cdd:COG0553 499 RRRGLILAALTRLRQICSHPALL 521
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
1059-1339 |
1.04e-59 |
|
SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.
Pssm-ID: 425504 [Multi-domain] Cd Length: 289 Bit Score: 207.54 E-value: 1.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1059 YQKIGLDWLAKLYRK-NLNGILADEAGLGKTVQIIAFFAHLACNEGNWG-PHLVVVRSCNILKWELELKRWC--PGLKIL 1134
Cdd:pfam00176 1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1135 SYIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDS 1214
Cdd:pfam00176 81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1215 PLHNTFLELWTMVHFLVPGI--SRPYLSSPLRAPSEESQDYyhKVVIRLHRVTQPFILRRTKRDVEKQLTKKYEHVLKCR 1292
Cdd:pfam00176 161 PLQNNLEELWALLNFLRPGPfgSLSTFRNWFDRPIERGGGK--KGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCR 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 7959257 1293 LSNRQKALYEDVILQPGTQEALKS--GHFVN--VLSILVRLQRICNHPGLV 1339
Cdd:pfam00176 239 LSKLQRKLYQTFLLKKDLNAIKTGegGREIKasLLNILMRLRKICNHPGLI 289
|
|
| DEXHc_SMARCA1_SMARCA5 |
cd17997 |
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ... |
1054-1274 |
3.25e-56 |
|
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 and 5 (SMARCA1 and SMARCA5) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350755 [Multi-domain] Cd Length: 222 Bit Score: 194.85 E-value: 3.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1054 GALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKI 1133
Cdd:cd17997 2 GTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1134 LSYIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLID 1213
Cdd:cd17997 82 VVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7959257 1214 SPLHNTFLELWTMVHFLVPGIsrpYLSSPLRAP---SEESQDYYHKVVIRLHRVTQPFILRRTK 1274
Cdd:cd17997 162 TPLQNNLHELWALLNFLLPDV---FTSSEDFDEwfnVNNCDDDNQEVVQRLHKVLRPFLLRRIK 222
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
1056-1232 |
6.51e-53 |
|
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350677 [Multi-domain] Cd Length: 182 Bit Score: 183.92 E-value: 6.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1135
Cdd:cd17919 1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1136 YIGShRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSP 1215
Cdd:cd17919 81 YHGS-QRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTP 159
|
170
....*....|....*..
gi 7959257 1216 LHNTFLELWTMVHFLVP 1232
Cdd:cd17919 160 LQNNLEELWALLDFLDP 176
|
|
| DEXQc_INO80 |
cd18002 |
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ... |
1056-1272 |
4.17e-52 |
|
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 chromatin remodeling complex. INO80 removes histone H3-containing nucleosomes from associated chromatin, promotes CENP-ACnp1 chromatin assembly at the centromere in a redundant manner with another chromatin-remodeling factor Chd1Hrp1. INO80 mutants have severe defects in oxygen consumption and promiscuous cell division that is no longer coupled with metabolic status. INO80 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350760 [Multi-domain] Cd Length: 229 Bit Score: 183.47 E-value: 4.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1135
Cdd:cd18002 1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1136 YIGSHRELKAKRQEWAEPN------SFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRL 1209
Cdd:cd18002 81 YWGNPKDRKVLRKFWDRKNlytrdaPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7959257 1210 LLIDSPLHNTFLELWTMVHFLVPGI------SRPYLSSPLRAPSEESQDYYHKVVIRLHRVTQPFILRR 1272
Cdd:cd18002 161 LLTGTPIQNSMAELWALLHFIMPTLfdshdeFNEWFSKDIESHAENKTGLNEHQLKRLHMILKPFMLRR 229
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
1054-1274 |
1.75e-49 |
|
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350770 [Multi-domain] Cd Length: 218 Bit Score: 175.45 E-value: 1.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1054 GALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLAcNEGNWGPHLVVVRSCNILKWELELKRWCPGLKI 1133
Cdd:cd18012 3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRK-EEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1134 LSYIGShrelKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLID 1213
Cdd:cd18012 82 LVIHGT----KRKREKLRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7959257 1214 SPLHNTFLELWTMVHFLVPGisrpYLSSP------LRAPSEESQDyyHKVVIRLHRVTQPFILRRTK 1274
Cdd:cd18012 158 TPIENHLGELWSIFDFLNPG----LLGSYkrfkkrFAKPIEKDGD--EEALEELKKLISPFILRRLK 218
|
|
| DEXHc_SMARCA2_SMARCA4 |
cd17996 |
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ... |
1054-1274 |
1.70e-48 |
|
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, members 2 and 4 (SMARCA2 and SMARCA4) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350754 [Multi-domain] Cd Length: 233 Bit Score: 172.94 E-value: 1.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1054 GALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKI 1133
Cdd:cd17996 2 GTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1134 LSYIGShRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKgmtERHWEAVFTL----QSQQRL 1209
Cdd:cd17996 82 IVYKGT-PDVRKKLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMK---NAQSKLTQTLntyyHARYRL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7959257 1210 LLIDSPLHNTFLELWTMVHFLVPGI--SRP----YLSSPLRAPSEESQDYYHK-----VVIRLHRVTQPFILRRTK 1274
Cdd:cd17996 158 LLTGTPLQNNLPELWALLNFLLPKIfkSCKtfeqWFNTPFANTGEQVKIELNEeetllIIRRLHKVLRPFLLRRLK 233
|
|
| DEXHc_HELLS_SMARCA6 |
cd18009 |
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ... |
1054-1274 |
9.20e-48 |
|
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or SMARCA6) is a major epigenetic regulator crucial for normal heterochromatin structure and function. HELLS is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350767 [Multi-domain] Cd Length: 236 Bit Score: 171.03 E-value: 9.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1054 GALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNeGNWGPHLVVVRSCNILKWELELKRWCPGLKI 1133
Cdd:cd18009 2 GVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRER-GVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1134 LSYIGSHRE-LKAKRQEWAEPNS---FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRL 1209
Cdd:cd18009 81 LLYHGTKEErERLRKKIMKREGTlqdFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7959257 1210 LLIDSPLHNTFLELWTMVHFLVPGISRPY-----------LSSPLRAPSEESQDYYHKVVIRLHRVTQPFILRRTK 1274
Cdd:cd18009 161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLssfeswfdfssLSDNAADISNLSEEREQNIVHMLHAILKPFLLRRLK 236
|
|
| DEXHc_SMARCA5 |
cd18064 |
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ... |
1047-1284 |
2.35e-47 |
|
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 (SMARCA5, also called SNF2H) is the catalytic subunit of the four known chromatin-remodeling complexes: CHRAC, RSF, ACF/WCRF, and WICH. SMARCA5 plays a major role organising arrays of nucleosomes adjacent to the binding sites for the architectural transcription factor CTCF sites and acts to promote CTCF binding SMARCA5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350822 [Multi-domain] Cd Length: 244 Bit Score: 170.23 E-value: 2.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1047 NAPSLL-YGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELK 1125
Cdd:cd18064 6 DSPSYVkWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1126 RWCPGLKILSYIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQS 1205
Cdd:cd18064 86 RWVPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1206 QQRLLLIDSPLHNTFLELWTMVHFLVPGISRpylssplrapSEESQDYY---------HKVVIRLHRVTQPFILRRTKRD 1276
Cdd:cd18064 166 TNRLLLTGTPLQNNLHELWALLNFLLPDVFN----------SAEDFDSWfdtnnclgdQKLVERLHMVLRPFLLRRIKAD 235
|
....*...
gi 7959257 1277 VEKQLTKK 1284
Cdd:cd18064 236 VEKSLPPK 243
|
|
| DEXHc_SMARCAD1 |
cd17998 |
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ... |
1056-1232 |
4.74e-45 |
|
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 (SMARCAD1, also known as ATP-dependent helicase 1 or Hel1) possesses intrinsic ATP-dependent nucleosome-remodeling activity and is required for both DNA repair and heterochromatin organization. SMARCAD1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350756 [Multi-domain] Cd Length: 187 Bit Score: 161.40 E-value: 4.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLAcNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1135
Cdd:cd17998 1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLK-EIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1136 YIGSHRELKAKRQEwAEPN--SFHVCITSYT---------QFFRgltaftRVRWKCLVIDEMQRVKGMTERHWEAVFTLQ 1204
Cdd:cd17998 80 YYGSQEERKHLRYD-ILKGleDFDVIVTTYNlatsnpddrSFFK------RLKLNYVVYDEGHMLKNMTSERYRHLMTIN 152
|
170 180
....*....|....*....|....*...
gi 7959257 1205 SQQRLLLIDSPLHNTFLELWTMVHFLVP 1232
Cdd:cd17998 153 ANFRLLLTGTPLQNNLLELMSLLNFIMP 180
|
|
| DEXHc_CHD1_2 |
cd17993 |
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ... |
1056-1272 |
5.82e-45 |
|
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and similar proteins; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as the substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but is also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. Both are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350751 [Multi-domain] Cd Length: 218 Bit Score: 162.53 E-value: 5.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1135
Cdd:cd17993 2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1136 YIGSHRELKAKRQ-EWAEPNS----FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLL 1210
Cdd:cd17993 82 YLGDIKSRDTIREyEFYFSQTkklkFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7959257 1211 LIDSPLHNTFLELWTMVHFLVPGisRPYLSSPLR-APSEESQDYYHkvviRLHRVTQPFILRR 1272
Cdd:cd17993 162 ITGTPLQNSLKELWALLHFLMPG--KFDIWEEFEeEHDEEQEKGIA----DLHKELEPFILRR 218
|
|
| DEXHc_SMARCA1 |
cd18065 |
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ... |
1054-1274 |
9.19e-44 |
|
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 (SMARCA1, also called SNF2L) is a component of NURF (nucleosome-remodeling factor) and CERF (CECR2-containing-remodeling factor) complexes which promote the perturbation of chromatin structure in an ATP-dependent manner. SMARCA1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350823 [Multi-domain] Cd Length: 233 Bit Score: 159.41 E-value: 9.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1054 GALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKI 1133
Cdd:cd18065 14 GTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1134 LSYIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLID 1213
Cdd:cd18065 94 VCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTG 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1214 SPLHNTFLELWTMVHFLVPGISRpylssplrapSEESQDYY---------HKVVIRLHRVTQPFILRRTK 1274
Cdd:cd18065 174 TPLQNNLHELWALLNFLLPDVFN----------SADDFDSWfdtknclgdQKLVERLHAVLKPFLLRRIK 233
|
|
| DEXHc_CHD6_7_8_9 |
cd17995 |
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ... |
1056-1272 |
1.00e-39 |
|
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; Chromodomain-helicase-DNA-binding protein 6-9 (CHD6, CHD7, CHD8, and CHD9) are members of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350753 [Multi-domain] Cd Length: 223 Bit Score: 147.39 E-value: 1.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPgLKILS 1135
Cdd:cd17995 1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1136 YIGSH--RELKAKRQ-----EWAEPNS----FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQ 1204
Cdd:cd17995 80 YHGSGesRQIIQQYEmyfkdAQGRKKKgvykFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7959257 1205 SQQRLLLIDSPLHNTFLELWTMVHFLVPGisrpylssplRAPSEES--QDY----YHKVVIRLHRVTQPFILRR 1272
Cdd:cd17995 160 LEHKLLLTGTPLQNNTEELWSLLNFLEPE----------KFPSSEEflEEFgdlkTAEQVEKLQALLKPYMLRR 223
|
|
| DEXHc_CHD2 |
cd18054 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ... |
1049-1272 |
8.31e-39 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. CHD2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350812 [Multi-domain] Cd Length: 237 Bit Score: 145.53 E-value: 8.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1049 PSLLYGA---LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELK 1125
Cdd:cd18054 11 PSYIGGEnleLRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1126 RWCPGLKILSYIGSHRELKAKRQ-EWAEPNS----FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAV 1200
Cdd:cd18054 91 IWAPEINVVVYIGDLMSRNTIREyEWIHSQTkrlkFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7959257 1201 FTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPGISRPYlssplrapsEESQDYYHKV----VIRLHRVTQPFILRR 1272
Cdd:cd18054 171 IDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFW---------EDFEEDHGKGrengYQSLHKVLEPFLLRR 237
|
|
| DEXHc_SMARCA4 |
cd18062 |
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ... |
1040-1274 |
8.73e-36 |
|
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4, also known as transcription activator BRG1) is a component of the CREST-BRG1 complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. Mutation of SMARCA4 (BRG1), the ATPase of BAF (mSWI/SNF) and PBAF complexes, contributes to a range of malignancies and neurologic disorders. SMARCA4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350820 [Multi-domain] Cd Length: 251 Bit Score: 137.10 E-value: 8.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1040 VTTSVKFNAPSLLYGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILK 1119
Cdd:cd18062 8 VTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1120 WELELKRWCPGLKILSYIGShrelKAKRQEWA---EPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKgmtERH 1196
Cdd:cd18062 88 WVYEFDKWAPSVVKVSYKGS----PAARRAFVpqlRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMK---NHH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1197 WEAVFTLQSQ----QRLLLIDSPLHNTFLELWTMVHFLVPGISRP------YLSSPLRAPSEE---SQDYYHKVVIRLHR 1263
Cdd:cd18062 161 CKLTQVLNTHyvapRRLLLTGTPLQNKLPELWALLNFLLPTIFKScstfeqWFNAPFAMTGEKvdlNEEETILIIRRLHK 240
|
250
....*....|.
gi 7959257 1264 VTQPFILRRTK 1274
Cdd:cd18062 241 VLRPFLLRRLK 251
|
|
| DEXHc_SMARCA2 |
cd18063 |
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ... |
1040-1274 |
1.33e-35 |
|
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (SMARCA2, also known as brahma homolog) is a component of the BAF complex. SMARCA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350821 [Multi-domain] Cd Length: 251 Bit Score: 136.73 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1040 VTTSVKFNAPSLLYGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILK 1119
Cdd:cd18063 8 ITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1120 WELELKRWCPGLKILSYIGS---HRELKAKRQEwaepNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKgmtERH 1196
Cdd:cd18063 88 WTYEFDKWAPSVVKISYKGTpamRRSLVPQLRS----GKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMK---NHH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1197 WEAVFTLQSQ----QRLLLIDSPLHNTFLELWTMVHFLVPGISRP------YLSSPLRAPSEE---SQDYYHKVVIRLHR 1263
Cdd:cd18063 161 CKLTQVLNTHyvapRRILLTGTPLQNKLPELWALLNFLLPTIFKScstfeqWFNAPFAMTGERvdlNEEETILIIRRLHK 240
|
250
....*....|.
gi 7959257 1264 VTQPFILRRTK 1274
Cdd:cd18063 241 VLRPFLLRRLK 251
|
|
| DEXHc_CHD1L |
cd18006 |
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ... |
1056-1272 |
3.60e-35 |
|
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, also known as ALC1) is involved in DNA repair by regulating chromatin relaxation following DNA damage. CHD1L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350764 [Multi-domain] Cd Length: 216 Bit Score: 134.10 E-value: 3.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1135
Cdd:cd18006 1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1136 YIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSP 1215
Cdd:cd18006 81 YMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7959257 1216 LHNTFLELWTMVHFLvpgisrpylsSPLRAPSEESQDYYHK---------VVIRLHRVTQPFILRR 1272
Cdd:cd18006 161 IQNSLQELYALLSFI----------EPNVFPKDKLDDFIKAysetddeseTVEELHLLLQPFLLRR 216
|
|
| DEXHc_Mot1 |
cd17999 |
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ... |
1056-1272 |
4.38e-32 |
|
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in eukaryotes) regulates transcription in association with TATA binding protein (TBP). Mot1, Ino80C, and NC2 function coordinately to regulate pervasive transcription in yeast and mammals. Mot1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350757 [Multi-domain] Cd Length: 232 Bit Score: 125.93 E-value: 4.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQ---IIAFFAHLACNEGNWG--PHLVVVRSCNILKWELELKRWCP- 1129
Cdd:cd17999 1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQtlcILASDHHKRANSFNSEnlPSLVVCPPTLVGHWVAEIKKYFPn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1130 -GLKILSYIGSHRElkaKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQR 1208
Cdd:cd17999 81 aFLKPLAYVGPPQE---RRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7959257 1209 LLLIDSPLHNTFLELWTMVHFLVPG-----------ISRPYLSSPLRAPSEESQDYYHKVVIRLHRVTQPFILRR 1272
Cdd:cd17999 158 LILSGTPIQNNVLELWSLFDFLMPGylgtekqfqrrFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
|
|
| DEXHc_CHD1 |
cd18053 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ... |
1056-1272 |
4.10e-31 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350811 [Multi-domain] Cd Length: 237 Bit Score: 123.24 E-value: 4.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1135
Cdd:cd18053 21 LRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1136 YIGSHRELKAKR-QEWAEPNS----FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLL 1210
Cdd:cd18053 101 YLGDINSRNMIRtHEWMHPQTkrlkFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7959257 1211 LIDSPLHNTFLELWTMVHFLVPGISRPYlsSPLRAPSEESQDYYHKvviRLHRVTQPFILRR 1272
Cdd:cd18053 181 ITGTPLQNSLKELWSLLHFIMPEKFSSW--EDFEEEHGKGREYGYA---SLHKELEPFLLRR 237
|
|
| DEXHc_ERCC6 |
cd18000 |
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ... |
1056-1239 |
1.98e-29 |
|
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, also known Cockayne syndrome group B (CSB), Rad26 in Saccharomyces cerevisiae, and Rhp26 in Schizosaccharomyces pombe) is a DNA-binding protein that is important in transcription-coupled excision repair. ERCC6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350758 [Multi-domain] Cd Length: 193 Bit Score: 116.65 E-value: 1.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKIL- 1134
Cdd:cd18000 1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1135 -----------SYIGSHRELKAKRQEWAEPNsfHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTL 1203
Cdd:cd18000 81 lhssgsgtgseEKLGSIERKSQLIRKVVGDG--GILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQL 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 7959257 1204 QSQQRLLLIDSPLHNTFLELWTMVHFLVPgisrPYL 1239
Cdd:cd18000 159 RTPHRLILSGTPIQNNLKELWSLFDFVFP----PYL 190
|
|
| DEXHc_CHD3_4_5 |
cd17994 |
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ... |
1056-1272 |
1.71e-28 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD3, CHD4, and CHD5 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350752 [Multi-domain] Cd Length: 196 Bit Score: 114.46 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLAcNEGNW-GPHLVVVRSCNILKWELELKRWCPGLKIL 1134
Cdd:cd17994 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLY-KEGHSkGPFLVSAPLSTIINWEREFEMWAPDFYVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1135 SYIGShrelkakrqewaepnsfHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDS 1214
Cdd:cd17994 80 TYVGD-----------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGT 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 7959257 1215 PLHNTFLELWTMVHFLVPGisrpyLSSPLRAPSEESQDYYHKVVI-RLHRVTQPFILRR 1272
Cdd:cd17994 143 PLQNNLEELFHLLNFLTPE-----RFNNLQGFLEEFADISKEDQIkKLHDLLGPHMLRR 196
|
|
| HSA |
smart00573 |
domain in helicases and associated with SANT domains; |
765-836 |
1.43e-27 |
|
domain in helicases and associated with SANT domains;
Pssm-ID: 214727 [Multi-domain] Cd Length: 73 Bit Score: 107.10 E-value: 1.43e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7959257 765 PKLQEAPRPKSHWDYLLEEMQWMATDFAQERRWKVAAAKKLVRTVVRHHEEKQLREERG-KKEEQSRLRRIAA 836
Cdd:smart00573 1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERReEKNEKRRLRKLAA 73
|
|
| DEXHc_ERCC6L |
cd18001 |
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ... |
1056-1272 |
3.25e-27 |
|
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint helicase (ERCC6L, also known as RAD26L) is an essential component of the mitotic spindle assembly checkpoint, by acting as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. ERCC6L is proposed to stimulate cancer cell proliferation by promoting cell cycle through a way of RAB31-MAPK-CDK2. ERCC6L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350759 [Multi-domain] Cd Length: 232 Bit Score: 111.69 E-value: 3.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLAcNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1135
Cdd:cd18001 1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMF-DSGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1136 YIGSHRELKAKRQEWAEpNSFHVCITSYTQFFRG---LTAFTR--VRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLL 1210
Cdd:cd18001 80 FHGTSKKERERNLERIQ-RGGGVLLTTYGMVLSNteqLSADDHdeFKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRII 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7959257 1211 LIDSPLHNTFLELWTMVHFLVPG--------ISRPYLSSPLRAPSEES----QDYYHKVVIRLHRVTQPFILRR 1272
Cdd:cd18001 159 LTGTPIQNNLKELWALFDFACNGsllgtrktFKMEFENPITRGRDKDAtqgeKALGSEVAENLRQIIKPYFLRR 232
|
|
| DEXHc_ERCC6L2 |
cd18005 |
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ... |
1056-1272 |
6.51e-27 |
|
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as RAD26L) may play a role in DNA repair and mitochondrial function. In humans, mutations in the ERCC6L2 gene are associated with bone marrow failure syndrome 2. ERCC6L2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350763 [Multi-domain] Cd Length: 245 Bit Score: 111.32 E-value: 6.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHL---------ACN-----------EGNWGPHLVVVRSC 1115
Cdd:cd18005 1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVlgktgtrrdRENnrprfkkkppaSSAKKPVLIVAPLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1116 NILKWELELKRWcpG-LKILSYIGSHRE------LKAKRQEwaepnsfhVCITSYTQFFRGLTAFTRVRWKCLVIDEMQR 1188
Cdd:cd18005 81 VLYNWKDELDTW--GhFEVGVYHGSRKDdelegrLKAGRLE--------VVVTTYDTLRRCIDSLNSINWSAVIADEAHR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1189 VKGMTERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPG-----------ISRPYLSSPLRAPSEESQDYYHKV 1257
Cdd:cd18005 151 IKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGalgsrsqfkkhFSEPIKRGQRHTATARELRLGRKR 230
|
250
....*....|....*
gi 7959257 1258 VIRLHRVTQPFILRR 1272
Cdd:cd18005 231 KQELAVKLSKFFLRR 245
|
|
| DEXHc_CHD7 |
cd18059 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ... |
1056-1272 |
1.95e-26 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; Chromodomain-helicase-DNA-binding protein 7 (CHD7) is a probable transcription regulator. It may be involved in the 45S precursor rRNA production. CHD7 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350817 [Multi-domain] Cd Length: 222 Bit Score: 109.35 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACnEGNWGPHLVVVRSCNILKWELELKRWCPgLKILS 1135
Cdd:cd18059 1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYL-KGIHGPFLVIAPLSTIPNWEREFRTWTE-LNVVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1136 YIGSH---RELKAKRQEWAEPN--------SFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQ 1204
Cdd:cd18059 79 YHGSQasrRTIQLYEMYFKDPQgrvikgsyKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7959257 1205 SQQRLLLIDSPLHNTFLELWTMVHFLVPGisrpylssplRAPSEES--QDY----YHKVVIRLHRVTQPFILRR 1272
Cdd:cd18059 159 LEHKVLLTGTPLQNTVEELFSLLHFLEPS----------RFPSETTfmQEFgdlkTEEQVQKLQAILKPMMLRR 222
|
|
| DEXHc_RAD54 |
cd18004 |
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ... |
1056-1272 |
4.80e-26 |
|
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350762 [Multi-domain] Cd Length: 240 Bit Score: 108.53 E-value: 4.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAK--LYRKNLNG---ILADEAGLGKTVQIIAFFAHLACNEGNWGPHL---VVVRSCNILK-WELELKR 1126
Cdd:cd18004 1 LRPHQREGVQFLYDclTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKPTAkkaLIVCPSSLVGnWKAEFDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1127 WCPG--LKILSYIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTR-VRWKCLVIDEMQRVKGMTERHWEAVFTL 1203
Cdd:cd18004 81 WLGLrrIKVVTADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKkISIDLLICDEGHRLKNSESKTTKALNSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1204 QSQQRLLLIDSPLHNTFLELWTMVHFLVPGI-----------SRPYLSSPLRAPSEESQDYYHKVVIRLHRVTQPFILRR 1272
Cdd:cd18004 161 PCRRRLLLTGTPIQNDLDEFFALVDFVNPGIlgslasfrkvfEEPILRSRDPDASEEDKELGAERSQELSELTSRFILRR 240
|
|
| DEXHc_CHD3 |
cd18055 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ... |
1056-1272 |
5.09e-26 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. CHD3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350813 [Multi-domain] Cd Length: 232 Bit Score: 108.17 E-value: 5.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1135
Cdd:cd18055 1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1136 YIGS----------------------HRELKAKRQewaEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMT 1193
Cdd:cd18055 81 YTGDkdsraiirenefsfddnavkggKKAFKMKRE---AQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1194 ERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPGisrpyLSSPLRAPSEESQDYYHKVVI-RLHRVTQPFILRR 1272
Cdd:cd18055 158 SKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPE-----RFNNLEGFLEEFADISKEDQIkKLHDLLGPHMLRR 232
|
|
| DEXHc_CHD4 |
cd18056 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ... |
1056-1272 |
5.93e-26 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. CHD4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350814 [Multi-domain] Cd Length: 232 Bit Score: 108.23 E-value: 5.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1135
Cdd:cd18056 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1136 YIGSH------RE-------------LKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERH 1196
Cdd:cd18056 81 YVGDKdsraiiREnefsfednairggKKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7959257 1197 WEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPgiSRPYlssPLRAPSEESQDYYHKVVI-RLHRVTQPFILRR 1272
Cdd:cd18056 161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTP--ERFH---NLEGFLEEFADIAKEDQIkKLHDMLGPHMLRR 232
|
|
| DEXHc_CHD6 |
cd18058 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ... |
1056-1272 |
1.07e-25 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; Chromodomain-helicase-DNA-binding protein 6 (CHD6) is a DNA-dependent ATPase that plays a role in chromatin remodeling. It regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. It activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2.2 and acts as a transcriptional repressor of different viruses including influenza virus or papillomavirus. During influenza virus infection, the viral polymerase complex localizes CHD6 to inactive chromatin where it gets degraded in a proteasome independent-manner. CHD6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350816 [Multi-domain] Cd Length: 222 Bit Score: 107.05 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACnEGNWGPHLVVVRSCNILKWELELKRWCPgLKILS 1135
Cdd:cd18058 1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFL-MGIRGPFLIIAPLSTITNWEREFRTWTE-MNAIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1136 YIGSH--RELKAK-----RQEWAEPNS----FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQ 1204
Cdd:cd18058 79 YHGSQisRQMIQQyemyyRDEQGNPLSgifkFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7959257 1205 SQQRLLLIDSPLHNTFLELWTMVHFLVPgISRPYLSSPLrapsEESQDY-YHKVVIRLHRVTQPFILRR 1272
Cdd:cd18058 159 LEHKVLLTGTPLQNSVEELFSLLNFLEP-SQFPSETTFL----EEFGDLkTEEQVKKLQSILKPMMLRR 222
|
|
| DEXHc_CHD5 |
cd18057 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ... |
1056-1272 |
2.18e-25 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350815 [Multi-domain] Cd Length: 232 Bit Score: 106.69 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1135
Cdd:cd18057 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1136 YIGSHRELKAKRQ-EWA-EPNS-----------------FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERH 1196
Cdd:cd18057 81 YTGDKESRSVIREnEFSfEDNAirsgkkvfrmkkeaqikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7959257 1197 WEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVpgisrPYLSSPLRAPSEESQDYYHKVVI-RLHRVTQPFILRR 1272
Cdd:cd18057 161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLT-----PERFNNLEGFLEEFADISKEDQIkKLHDLLGPHMLRR 232
|
|
| DEXHc_CHD9 |
cd18061 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ... |
1056-1272 |
3.53e-25 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; Chromodomain-helicase-DNA-binding protein 9 (CHD9) acts as a transcriptional coactivator for PPARA and possibly other nuclear receptors. It is proposed to be a ATP-dependent chromatin remodeling protein. CHD9 has DNA-dependent ATPase activity and binds to A/T-rich DNA. It also associates with A/T-rich regulatory regions in promoters of genes that participate in the differentiation of progenitors during osteogenesis. CHD9 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350819 [Multi-domain] Cd Length: 222 Bit Score: 105.47 E-value: 3.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNeGNWGPHLVVVRSCNILKWELELKRWCpGLKILS 1135
Cdd:cd18061 1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLT-GIRGPFLIIAPLSTIANWEREFRTWT-DLNVVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1136 YIGS--HRELKAKRQEWAEPNS---------FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQ 1204
Cdd:cd18061 79 YHGSliSRQMIQQYEMYFRDSQgriirgayrFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7959257 1205 SQQRLLLIDSPLHNTFLELWTMVHFLvpgisrpylsSPLRAPSEES--QDY----YHKVVIRLHRVTQPFILRR 1272
Cdd:cd18061 159 LEHKVLLTGTPLQNTVEELFSLLHFL----------EPLRFPSESTfmQEFgdlkTEEQVQKLQAILKPMMLRR 222
|
|
| DEXDc_SHPRH-like |
cd18008 |
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ... |
1056-1272 |
6.44e-25 |
|
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350766 [Multi-domain] Cd Length: 241 Bit Score: 105.45 E-value: 6.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLakLYRknlNGILADEAGLGKTVQIIA---------------FFAHLACNEGNWGPH--LVVVRScNIL 1118
Cdd:cd18008 1 LLPYQKQGLAWM--LPR---GGILADEMGLGKTIQALAlilatrpqdpkipeeLEENSSDPKKLYLSKttLIVVPL-SLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1119 K-WELELKR--WCPGLKILSYIGSHRELKAKrqewaEPNSFHVCITSYT----------QFFRGLTAFT------RVRWK 1179
Cdd:cd18008 75 SqWKDEIEKhtKPGSLKVYVYHGSKRIKSIE-----ELSDYDIVITTYGtlasefpknkKGGGRDSKEKeasplhRIRWY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1180 CLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFL------VPGISRPYLSSPLRAPSEESQDy 1253
Cdd:cd18008 150 RVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLrvepfgDYPWFNSDISKPFSKNDRKALE- 228
|
250
....*....|....*....
gi 7959257 1254 yhkvviRLHRVTQPFILRR 1272
Cdd:cd18008 229 ------RLQALLKPILLRR 241
|
|
| DEXHc_CHD8 |
cd18060 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ... |
1056-1272 |
1.71e-24 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; Chromodomain-helicase-DNA-binding protein 8 (CHD8) is a DNA helicase that acts as a chromatin remodeling factor and regulates transcription. It also acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. It suppresses p53/TP53-mediated apoptosis by recruiting histone H1 and preventing p53/TP53 transactivation activity and of STAT3 activity by suppressing the LIF-induced STAT3 transcriptional activity. It also acts as a negative regulator of Wnt signaling pathway and CTNNB1-targeted gene expression. CHD8 is also involved in both enhancer blocking and epigenetic remodeling at chromatin boundary via its interaction with CTCF. It also acts as a transcription activator via its interaction with ZNF143 by participating in efficient U6 RNA polymerase III transcription. CHD8 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350818 [Multi-domain] Cd Length: 222 Bit Score: 103.59 E-value: 1.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLAcNEGNWGPHLVVVRSCNILKWELELKRWCPgLKILS 1135
Cdd:cd18060 1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVY-NVGIHGPFLVIAPLSTITNWEREFNTWTE-MNTIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1136 YIGS--HRELKAKRQEWAEPNS---------FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQ 1204
Cdd:cd18060 79 YHGSlaSRQMIQQYEMYCKDSRgrlipgaykFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7959257 1205 SQQRLLLIDSPLHNTFLELWTMVHFLVPGisrpYLSSPLRAPSEESQDYYHKVVIRLHRVTQPFILRR 1272
Cdd:cd18060 159 LEHKVLLTGTPLQNTVEELFSLLHFLEPS----QFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 222
|
|
| HSA |
pfam07529 |
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ... |
767-833 |
1.08e-21 |
|
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. This region does not form a compact domain in the known structures.
Pssm-ID: 462194 [Multi-domain] Cd Length: 67 Bit Score: 89.94 E-value: 1.08e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7959257 767 LQEAPR-PKSHWDYLLEEMQWMATDFAQERRWKVAAAKKLVRTVVRHHEEKQLREERgKKEEQSRLRR 833
Cdd:pfam07529 1 RDEPERrEKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHKNIEKEEQK-RIEREEKQRL 67
|
|
| DEXHc_RAD54B |
cd18066 |
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ... |
1056-1272 |
2.46e-17 |
|
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as RDH54, binds to double-stranded DNA, displays ATPase activity in the presence of DNA, and may have a role in meiotic and mitotic recombination. RAD54B is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350824 [Multi-domain] Cd Length: 235 Bit Score: 83.36 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWL-----AKLYRKNLNGILADEAGLGKTVQIIAFFAHLACnEGNWGPH------LVVVRSCNILKWELEL 1124
Cdd:cd18066 1 LRPHQREGIEFLyecvmGMRVNERFGAILADEMGLGKTLQCISLIWTLLR-QGPYGGKpvikraLIVTPGSLVKNWKKEF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1125 KRWcpglkilsyIGSHR------ELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWE 1198
Cdd:cd18066 80 QKW---------LGSERikvftvDQDHKVEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1199 AVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPGI-----------SRPYLSSPLRAPSEESQDYYHKVVIRLHRVTQP 1267
Cdd:cd18066 151 ALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGIlgslstyrkvyEEPIVRSREPTATPEEKKLGEARAAELTRLTGL 230
|
....*
gi 7959257 1268 FILRR 1272
Cdd:cd18066 231 FILRR 235
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1049-1237 |
5.01e-17 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 81.38 E-value: 5.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1049 PSLLYGALRDYQKIGLDWLAKLYRknlNGILADEAGLGKTVQIIAfFAHLACNEGNWGPHLVVV--RScniLK--WELEL 1124
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALL-PALEALKRGKGGRVLVLVptRE---LAeqWAEEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1125 KRWCP--GLKILSYIGSHRELKAKRQEWAEPnsFHVCITSYTQFFRGLT--AFTRVRWKCLVIDEMQRVKGMTER-HWEA 1199
Cdd:smart00487 75 KKLGPslGLKVVGLYGGDSKREQLRKLESGK--TDILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGGFGdQLEK 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 7959257 1200 VFTL--QSQQRLLL---IDSPLHNTFLELWTMVHFLVPGISRP 1237
Cdd:smart00487 153 LLKLlpKNVQLLLLsatPPEEIENLLELFLNDPVFIDVGFTPL 195
|
|
| DEXHc_ATRX-like |
cd18007 |
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ... |
1078-1244 |
2.30e-15 |
|
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) which is involved in transcriptional regulation and chromatin remodeling, and ARIP4 (also called androgen receptor-interacting protein 4, RAD54 like 2 or RAD54L2) which modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350765 [Multi-domain] Cd Length: 239 Bit Score: 77.33 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1078 ILADEAGLGKTVQIIAFF-AHLACNEGNWGPHLVVVRSCnILKWELELKRWCPGLKILSYIGSH--RELKAKR-----QE 1149
Cdd:cd18007 30 ILAHTMGLGKTLQVITFLhTYLAAAPRRSRPLVLCPAST-LYNWEDEFKKWLPPDLRPLLVLVSlsASKRADArlrkiNK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1150 WAEPNSfhVCITSYTQFfRGLTA---------FTRVRWKC------LVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDS 1214
Cdd:cd18007 109 WHKEGG--VLLIGYELF-RNLASnattdprlkQEFIAALLdpgpdlLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGT 185
|
170 180 190
....*....|....*....|....*....|
gi 7959257 1215 PLHNTFLELWTMVHFLVPGisrpYLSSPLR 1244
Cdd:cd18007 186 PLQNNLKEYWTMVDFARPK----YLGTLKE 211
|
|
| DEXHc_HARP_SMARCAL1 |
cd18010 |
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ... |
1072-1234 |
1.97e-13 |
|
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a like 1, also known as HARP) is recruited to stalled replication forks to promote repair and helps restart replication. It plays a role in DNA repair, telomere maintenance and replication fork stability in response to DNA replication stress. Mutations cause Schimke Immunoosseous Dysplasia. SMARCAL1 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350768 [Multi-domain] Cd Length: 213 Bit Score: 71.08 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1072 RKNLNGILADEAGLGKTVQIIAFFAHLacnEGNWgPHLVVVRSCNILKWELELKRWCPGLKILSYIgshreLKAKRQEWA 1151
Cdd:cd18010 14 RRGGRVLIADEMGLGKTVQAIAIAAYY---REEW-PLLIVCPSSLRLTWADEIERWLPSLPPDDIQ-----VIVKSKDGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1152 EPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVK-GMTERHWEAVFTLQSQQR-LLLIDSPLHNTFLELWTMVHF 1229
Cdd:cd18010 85 RDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKnSKAKRTKAALPLLKRAKRvILLSGTPALSRPIELFTQLDA 164
|
....*
gi 7959257 1230 LVPGI 1234
Cdd:cd18010 165 LDPKL 169
|
|
| DEXHc_RAD54A |
cd18067 |
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ... |
1056-1234 |
1.15e-10 |
|
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as RAD54L or RAD54, plays a role in homologous recombination related repair of DNA double-strand breaks. RAD54A is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350825 [Multi-domain] Cd Length: 243 Bit Score: 63.64 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAK----LYRKNLNG-ILADEAGLGKTVQIIAFFAHLACNEGNWGPHL----VVVRSCNILKWELELKR 1126
Cdd:cd18067 1 LRPHQREGVKFLYRcvtgRRIRGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaiVVSPSSLVKNWANELGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1127 WCpGLKILSYI---GSHRELKAKRQEWAEPNSFH----VCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEA 1199
Cdd:cd18067 81 WL-GGRLQPLAidgGSKKEIDRKLVQWASQQGRRvstpVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQA 159
|
170 180 190
....*....|....*....|....*....|....*
gi 7959257 1200 VFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPGI 1234
Cdd:cd18067 160 LDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGI 194
|
|
| DEXHc_ARIP4 |
cd18069 |
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ... |
1078-1251 |
1.90e-09 |
|
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called RAD54 like 2 or RAD54L2 ) modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. ARIP4 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350827 [Multi-domain] Cd Length: 227 Bit Score: 59.83 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1078 ILADEAGLGKTVQIIAF----FAHLACNEGnwgphLVVVRSCNILKWELELKRWCP-----------GLKILSYIGSHRE 1142
Cdd:cd18069 32 ILAHSMGLGKTLQVISFldvlLRHTGAKTV-----LAIVPVNTLQNWLSEFNKWLPppealpnvrprPFKVFILNDEHKT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1143 LKAKRQ---EWAEPNSfhVCITSYTQFfrgltaftRVR--WKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSPLH 1217
Cdd:cd18069 107 TAARAKvieDWVKDGG--VLLMGYEMF--------RLRpgPDVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQ 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 7959257 1218 NTFLELWTMVHFLVPGI--SRPYLSSPLRAPSEESQ 1251
Cdd:cd18069 177 NNLIEYWCMVDFVRPDFlgTRQEFSNMFERPILNGQ 212
|
|
| DEXHc_ATRX |
cd18068 |
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ... |
1077-1234 |
2.81e-09 |
|
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) is involved in transcriptional regulation and chromatin remodeling. Mutations in humans cause mental retardation, X-linked, syndromic, with hypotonic facies 1 (MRXSHF1) and alpha-thalassemia myelodysplasia syndrome (ATMDS). ATRX is part of the a DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350826 [Multi-domain] Cd Length: 246 Bit Score: 59.52 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1077 GILADEAGLGKTVQIIAFFAHLACNE--GNWGPHLVVVRSCNILKWELELKRWCPGLKI--------LSYIGSHRELKAK 1146
Cdd:cd18068 31 CILAHCMGLGKTLQVVTFLHTVLLCEklENFSRVLVVCPLNTVLNWLNEFEKWQEGLKDeekievneLATYKRPQERSYK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1147 RQEWAEPNSfhVCITSYtQFFRGLTAFTRVRWKC-----------------LVIDEMQRVKGMTERHWEAVFTLQSQQRL 1209
Cdd:cd18068 111 LQRWQEEGG--VMIIGY-DMYRILAQERNVKSREklkeifnkalvdpgpdfVVCDEGHILKNEASAVSKAMNSIRTKRRI 187
|
170 180
....*....|....*....|....*
gi 7959257 1210 LLIDSPLHNTFLELWTMVHFLVPGI 1234
Cdd:cd18068 188 VLTGTPLQNNLIEYHCMVNFVKPNL 212
|
|
| DEXHc_TTF2 |
cd18072 |
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ... |
1056-1230 |
9.32e-09 |
|
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called Forkhead-box E1/FOXE1 ) is a transcription termination factor that couples ATP hydrolysis with the removal of RNA polymerase II from the DNA template. Single nucleotide polymorphism (SNP) within the 5'-UTR of TTF2 is associated with thyroid cancer risk.TTF2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350830 [Multi-domain] Cd Length: 241 Bit Score: 57.88 E-value: 9.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLakLYRKNLN---GILADEAGLGKTVQIIAFFahLACNEG-------------NWGPHL--VVVRSCNI 1117
Cdd:cd18072 1 LLLHQKQALAWL--LWRERQKprgGILADDMGLGKTLTMIALI--LAQKNTqnrkeeekekaltEWESKKdsTLVPSAGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1118 L---------KWELELKRWCPG--LKILSYIGSHRELKAKRQEwaepnSFHVCITSYTQFFRGL---------TAFTRVR 1177
Cdd:cd18072 77 LvvcpaslvhQWKNEVESRVASnkLRVCLYHGPNRERIGEVLR-----DYDIVITTYSLVAKEIptykeesrsSPLFRIA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 7959257 1178 WKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFL 1230
Cdd:cd18072 152 WARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFL 204
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
519-781 |
4.61e-08 |
|
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.
Pssm-ID: 401645 [Multi-domain] Cd Length: 846 Bit Score: 58.12 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 519 PPTPQAAQLAGQRQSQQQYDPSTGPPVQNAASLHT---------PLPQL-----------PGRLPPAGVPTAALSSALQF 578
Cdd:pfam09770 108 AARAAQSSAQPPASSLPQYQYASQQSQQPSKPVRTgyekykepePIPDLqvdaslwgvapKKAAAPAPAPQPAAQPASLP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 579 AQQPQV-----VEAQTQLQIPVKTQQPNVPIPAPPSSqlpiPPSQPAQLALHVPTPGKVQVQASQLSSLPQMVASTRLPV 653
Cdd:pfam09770 188 APSRKMmsleeVEAAMRAQAKKPAQQPAPAPAQPPAA----PPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPV 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 654 DPAPPCPRPLPTSSTSSLAPVS-GSGPGPSPARSSPV------NRPSSAtnkalspvtsRTPGVVASAPTKPQSPAQNAT 726
Cdd:pfam09770 264 TILQRPQSPQPDPAQPSIQPQAqQFHQQPPPVPVQPTqilqnpNRLSAA----------RVGYPQNPQPGVQPAPAHQAH 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 7959257 727 SSQdSSQDTLTEQITLENQVHQRIAELRKAGLwsqrrlpkLQEAPRPK-SHWDYLL 781
Cdd:pfam09770 334 RQQ-GSFGRQAPIITHPQQLAQLSEEEKAAYL--------DEEAKRAKrNHKIFLL 380
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
497-734 |
7.76e-08 |
|
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: 57.47 E-value: 7.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 497 QHPGADAGVPLQQLMptAQGGMPPTPQaAQLAGQRQSQQQYDPSTGPPVQNAASLHTPLPQLPGRL----PPAGVPTAAL 572
Cdd:pfam03154 290 QHPVPPQPFPLTPQS--SQSQVPPGPS-PAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMphikPPPTTPIPQL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 573 SSAlQFAQQPQVVEAQTQLQIPVKTQQP-------NVPIPAPPSS------------QLPIPPSQPaqlalhvPTPGKVQ 633
Cdd:pfam03154 367 PNP-QSHKHPPHLSGPSPFQMNSNLPPPpalkplsSLSTHHPPSAhppplqlmpqsqQLPPPPAQP-------PVLTQSQ 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 634 VQASQLSSLPQMVASTRLPVDPAPPCPRPLPTSSTSSLAPvsgSGPGPSPARSSPVNRPSSATNKALSpvtsrtpGVVAS 713
Cdd:pfam03154 439 SLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPP---SGPPTSTSSAMPGIQPPSSASVSSS-------GPVPA 508
|
250 260
....*....|....*....|.
gi 7959257 714 APTKPQSPAQNATSSQDSSQD 734
Cdd:pfam03154 509 AVSCPLPPVQIKEEALDEAEE 529
|
|
| DEXHc_HLTF1_SMARC3 |
cd18071 |
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ... |
1077-1272 |
5.27e-07 |
|
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as HIP116 or SMARCA3) has both helicase and E3 ubiquitin ligase activities and ATP-dependent nucleosome-remodeling activity. HLTF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350829 [Multi-domain] Cd Length: 239 Bit Score: 52.86 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1077 GILADEAGLGKTVQIIAFFAHlacnegnwGPHLVVVRSCNILKWELELKRWC-PG-LKILSYIGSHRELKAKrqewaEPN 1154
Cdd:cd18071 51 GILADDMGLGKTLTTISLILA--------NFTLIVCPLSVLSNWETQFEEHVkPGqLKVYTYHGGERNRDPK-----LLS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1155 SFHVCITSYTQF-----FRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHF 1229
Cdd:cd18071 118 KYDIVLTTYNTLasdfgAKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSF 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 7959257 1230 L--VPGISRPYLSSPLRAPSEESQDyyhKVVIRLHRVTQPFILRR 1272
Cdd:cd18071 198 LhlKPFSNPEYWRRLIQRPLTMGDP---TGLKRLQVLMKQITLRR 239
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
1078-1233 |
6.76e-07 |
|
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350769 [Multi-domain] Cd Length: 207 Bit Score: 51.91 E-value: 6.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1078 ILADEAGLGKTVQIIAfFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCpGLKILSYIGSHRElKAKRQEWAEPNSFH 1157
Cdd:cd18011 21 LLADEVGLGKTIEAGL-IIKELLLRGDAKRVLILCPASLVEQWQDELQDKF-GLPFLILDRETAA-QLRRLIGNPFEEFP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1158 VCITSYTQFFRG---LTAFTRVRWKCLVIDEMQRVKGM-----TERhWEAVFTLQSQQR--LLLIDSPLHNTFLELWTMV 1227
Cdd:cd18011 98 IVIVSLDLLKRSeerRGLLLSEEWDLVVVDEAHKLRNSgggkeTKR-YKLGRLLAKRARhvLLLTATPHNGKEEDFRALL 176
|
....*.
gi 7959257 1228 HFLVPG 1233
Cdd:cd18011 177 SLLDPG 182
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
478-644 |
1.78e-06 |
|
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.
Pssm-ID: 401645 [Multi-domain] Cd Length: 846 Bit Score: 53.12 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 478 MAEQSKRPRlevghQGVVFQHPGADAGVPLQQLMPTAQGgmPPTPQAAQLAGQRQSQQQYDPSTGPPVQnaaslhtPLPQ 557
Cdd:pfam09770 203 MRAQAKKPA-----QQPAPAPAQPPAAPPAQQAQQQQQF--PPQIQQQQQPQQQPQQPQQHPGQGHPVT-------ILQR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 558 LPGRLPPAGVPTAALSSALQFAQQPQVVEAQTQ-LQIPVKTQQPNVPIPAPPSSQLPIPPSQPAQLALHV-PTPGKVQVQ 635
Cdd:pfam09770 269 PQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQiLQNPNRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSfGRQAPIITH 348
|
....*....
gi 7959257 636 ASQLSSLPQ 644
Cdd:pfam09770 349 PQQLAQLSE 357
|
|
| DEXQc_SHPRH |
cd18070 |
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ... |
1056-1193 |
3.28e-06 |
|
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously expressed protein that contains motifs characteristic of several DNA repair proteins, transcription factors, and helicases. SHPRH is a functional homolog of S. cerevisiae RAD5 and is involved in DNA repair. SHPRH is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350828 [Multi-domain] Cd Length: 257 Bit Score: 50.42 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLaklyrKNLNGILADEAGLGKTVQIIAF-FAH-----------LACNEGNWGPHLVV---VRSCN---- 1116
Cdd:cd18070 1 LLPYQRRAVNWM-----LVPGGILADEMGLGKTVEVLALiLLHprpdndldaadDDSDEMVCCPDCLVaetPVSSKatli 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1117 -----ILK-WELELKRWCP-GLKILSYIGSHRELKAKRQEWAEPNSFHVCITSYT-------------------QFFRGL 1170
Cdd:cd18070 76 vcpsaILAqWLDEINRHVPsSLKVLTYQGVKKDGALASPAPEILAEYDIVVTTYDvlrtelhyaeanrsnrrrrRQKRYE 155
|
170 180
....*....|....*....|....*.
gi 7959257 1171 ---TAFTRVRWKCLVIDEMQRVKGMT 1193
Cdd:cd18070 156 appSPLVLVEWWRVCLDEAQMVESST 181
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
512-735 |
5.11e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.86 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 512 PTAQGGMPPTPQAAQLAGQRQSQQQYDPSTGP--PVQNAASLHTPLPQLPgrlPPAGVPTAALSSALQFAQQPQVVEAQT 589
Cdd:PHA03247 2735 LPAAPAPPAVPAGPATPGGPARPARPPTTAGPpaPAPPAAPAAGPPRRLT---RPAVASLSESRESLPSPWDPADPPAAV 2811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 590 QLQIPV--KTQQPNVPIPAPPSSQLPIPPSQPAQLALHVPTPGKV------QVQASQLSSLPQMVASTRLPVDPAPPCPR 661
Cdd:PHA03247 2812 LAPAAAlpPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVapggdvRRRPPSRSPAAKPAAPARPPVRRLARPAV 2891
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7959257 662 PLPTSSTSSlapvsgsgPGPSPARSSPVNRPSSATNKALSPVTSRtPGVVASAPTKPQSPAQNATSSQDSSQDT 735
Cdd:PHA03247 2892 SRSTESFAL--------PPDQPERPPQPQAPPPPQPQPQPPPPPQ-PQPPPPPPPRPQPPLAPTTDPAGAGEPS 2956
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
496-773 |
1.16e-05 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 50.30 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 496 FQHPGADAGVPLQQLMPT---AQGGMPPTPQAAQL-----AGQRQSQQQYDPSTGP----PVQNAASLHTPLPQLPGRLP 563
Cdd:pfam05109 439 FAAPNTTTGLPSSTHVPTnltAPASTGPTVSTADVtsptpAGTTSGASPVTPSPSPrdngTESKAPDMTSPTSAVTTPTP 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 564 PAGVPTAALSSALQFAQQPQVveAQTQLQIPVKTQQPNVPIPAPPSSQlPIPPSQpaqlalhVPTPGKVQVQASQLSSLP 643
Cdd:pfam05109 519 NATSPTPAVTTPTPNATSPTL--GKTSPTSAVTTPTPNATSPTPAVTT-PTPNAT-------IPTLGKTSPTSAVTTPTP 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 644 QMVASTrlpvdpappcprPLPTSSTSSLAPVSGSGPGPSPARSSPVNRPSSATNKALSPVTSRTpgvVASAPTKPQSPAQ 723
Cdd:pfam05109 589 NATSPT------------VGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSS---TSSMSLRPSSISE 653
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 7959257 724 NATSsqdSSQDTLTEQITLENQVH----QRIAELRKAGLwSQRRLPKLQEAPRP 773
Cdd:pfam05109 654 TLSP---STSDNSTSHMPLLTSAHptggENITQVTPAST-STHHVSTSSPAPRP 703
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
470-723 |
2.70e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.55 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 470 QQAMPSTGMAEQSKRPRLEVGHQGVVFQHPGADAGVPLQQLMPTAQGGMPPTPQAAQLAGQRQSQQQYDPSTGPPVQNAA 549
Cdd:PHA03247 2572 RPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPER 2651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 550 SLHTPLP---QLPGRLPPAGVPTAAlSSALQFAQQPQV---VEAQTQLQIPVKTQQPNVPIPAPPSSQLPIPPSQPAQLA 623
Cdd:PHA03247 2652 PRDDPAPgrvSRPRRARRLGRAAQA-SSPPQRPRRRAArptVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQ 2730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 624 LHVPTPGKvqvqasqlSSLPQMVASTRLPVDPAPPCPRPLPTSSTSSLAPVSGSGPGPSPARSSPVNRPSSATNKALSPV 703
Cdd:PHA03247 2731 ASPALPAA--------PAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPW 2802
|
250 260
....*....|....*....|
gi 7959257 704 TSRTPGVVASAPTKPQSPAQ 723
Cdd:PHA03247 2803 DPADPPAAVLAPAAALPPAA 2822
|
|
| PHA03269 |
PHA03269 |
envelope glycoprotein C; Provisional |
589-722 |
6.23e-05 |
|
envelope glycoprotein C; Provisional
Pssm-ID: 165527 [Multi-domain] Cd Length: 566 Bit Score: 47.80 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 589 TQLQIPVKTQQPNVPIP---APPSSQLPIPPSQPAQLALHVPTPGKVQVQAS----QLSSLPQMVASTRLpvDPAPPCPR 661
Cdd:PHA03269 13 ACINLIIANLNTNIPIPelhTSAATQKPDPAPAPHQAASRAPDPAVAPTSAAsrkpDLAQAPTPAASEKF--DPAPAPHQ 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7959257 662 PLPTSSTSSLAPVSGSGPGPSPArSSPVNRPSSATNKALSPVT--SRTPGVVASAPTKPQSPA 722
Cdd:PHA03269 91 AASRAPDPAVAPQLAAAPKPDAA-EAFTSAAQAHEAPADAGTSaaSKKPDPAAHTQHSPPPFA 152
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
470-731 |
7.76e-05 |
|
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.
Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 47.70 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 470 QQAMPSTGMAEQSKRPRLEVGHQGVVFQHPGADAGVPLQQLMPTAQGGMP--------PTPQAAQLAGQRQSQQQYDPST 541
Cdd:pfam09606 171 PNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGqqaqanggMNPQQMGGAPNQVAMQQQQPQQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 542 GPPVQNAASLHTPLPQLPGRLP---PAGVPTAALSSAlqfAQQPQVVEAQTQLQIP-VKTQQPNVpiPAPPSSQLPIPPS 617
Cdd:pfam09606 251 QGQQSQLGMGINQMQQMPQGVGggaGQGGPGQPMGPP---GQQPGAMPNVMSIGDQnNYQQQQTR--QQQQQQGGNHPAA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 618 QPAQLALHVptpgkvqVQASQLSSLP-QMVASTRLPVDPAPPCPRPL--------------PTSSTSSLAPVSGSGPGPS 682
Cdd:pfam09606 326 HQQQMNQSV-------GQGGQVVALGgLNHLETWNPGNFGGLGANPMqrgqpgmmsspspvPGQQVRQVTPNQFMRQSPQ 398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 7959257 683 PARSSPVNrPSSATNKALSPVTSRTPGVVAS-APTKPQSPAQNATSSQDS 731
Cdd:pfam09606 399 PSVPSPQG-PGSQPPQSHPGGMIPSPALIPSpSPQMSQQPAQQRTIGQDS 447
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
481-727 |
8.50e-05 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 47.60 E-value: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 481 QSKRPRLEVGHQGVVFQHPGADAGVPlqqlmptaqGGMPPTPQAAQLAGQRQSQQQydpSTGPPVQNAAS----LHTPLP 556
Cdd:pfam05109 500 ESKAPDMTSPTSAVTTPTPNATSPTP---------AVTTPTPNATSPTLGKTSPTS---AVTTPTPNATSptpaVTTPTP 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 557 QlpGRLPPAG--VPTAALSSALQFAQQPQVVEAQTQLQI-----------PVKTQQPNVPIPAPPSSQLPIPPSQPAQLA 623
Cdd:pfam05109 568 N--ATIPTLGktSPTSAVTTPTPNATSPTVGETSPQANTtnhtlggtsstPVVTSPPKNATSAVTTGQHNITSSSTSSMS 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 624 LHVPTPGKVQVQASQLSSLPQMVASTRlpVDPAPPCPRPLPTSSTSSLAPVSGSGPGPSPARSSPVNRPSSATNKALSPV 703
Cdd:pfam05109 646 LRPSSISETLSPSTSDNSTSHMPLLTS--AHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGE 723
|
250 260
....*....|....*....|....
gi 7959257 704 TSRTPGVVASAPTKPQSPAQNATS 727
Cdd:pfam05109 724 VNVTKGTPPKNATSPQAPSGQKTA 747
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
587-771 |
1.16e-04 |
|
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: 47.07 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 587 AQTQLQipvKTQQPNVPIPAPPSSQLPIPPSQPAQLALHVPTPGKVQVQ---ASQLSSLPQMVASTRLPVDPAPPCPRPL 663
Cdd:pfam03154 162 AQQQIL---QTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPpqgSPATSQPPNQTQSTAAPHTLIQQTPTLH 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 664 PTSSTSSLAPVSGSGPGPSPARSSPVNRPSSATNKALSPVtsrtPGVVASAPTKPQSPAQ----NATSSQDSSQDTLTEQ 739
Cdd:pfam03154 239 PQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPM----PHSLQTGPSHMQHPVPpqpfPLTPQSSQSQVPPGPS 314
|
170 180 190
....*....|....*....|....*....|..
gi 7959257 740 ITLENQVHQRIAELRKAGLWSQRRLPKLQEAP 771
Cdd:pfam03154 315 PAAPGQSQQRIHTPPSQSQLQSQQPPREQPLP 346
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
1056-1185 |
1.94e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 43.81 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLD-WLAKLYRKNLNGILADEAGLGKTvqIIAFFAHLACNEGNWGPH-LVVVRSCNILK-WELELKRWCPGLK 1132
Cdd:pfam04851 4 LRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKT--LTAAKLIARLFKKGPIKKvLFLVPRKDLLEqALEEFKKFLPNYV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 7959257 1133 ILSYIGSHRELKAKRQEWaepnsfHVCITSYTQFFRGLTAFTRV----RWKCLVIDE 1185
Cdd:pfam04851 82 EIGEIISGDKKDESVDDN------KIVVTTIQSLYKALELASLEllpdFFDVIIIDE 132
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
500-737 |
2.03e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 46.02 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 500 GADAGVPLQQLMPTAQggMPPTPQAAQLAGQRQSQQQYDPSTGPPVQNAASlhtPLPQLPGRLPPAGVPTAALSSALQFA 579
Cdd:PRK12323 369 GGGAGPATAAAAPVAQ--PAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAAR---AVAAAPARRSPAPEALAAARQASARG 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 580 QQPQVVEAQTQLQIPVKTQQPNVPIPAPPSSQLPIPPSQPAQLALHVPTPGKVqvqaSQLSSLPQMVAStrlpvdpappc 659
Cdd:PRK12323 444 PGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDP----PPWEELPPEFAS----------- 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 660 prplptsstsslAPVSGSGPGPSPARSSPVNRPS----SATNKALSPVTSRTPGVVASAPTKPQSPAQNATSSQDSSQDT 735
Cdd:PRK12323 509 ------------PAPAQPDAAPAGWVAESIPDPAtadpDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDM 576
|
..
gi 7959257 736 LT 737
Cdd:PRK12323 577 FD 578
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
481-729 |
2.35e-04 |
|
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: 46.30 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 481 QSKRPRLEVGHQGVVFQHPGADAGVPLQQLMPTAQG------GMPPT---PQAAQLAGQRQSQQQYDPSTGPpvQNAASL 551
Cdd:pfam03154 168 QTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSApsvppqGSPATsqpPNQTQSTAAPHTLIQQTPTLHP--QRLPSP 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 552 HTPLPQLPGRLPPAGVPTAALSSALQFAQQPQvveaqtqLQIPVKTQQPNVPIPAPP----------SSQLPIPPSQ--- 618
Cdd:pfam03154 246 HPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPP-------MPHSLQTGPSHMQHPVPPqpfpltpqssQSQVPPGPSPaap 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 619 ----------PAQLALHVPTPGKVQVQASQLSSLPQMVASTRLPVDPAPPCPRPLPTSSTSSLAPVSGSG-----PGPSP 683
Cdd:pfam03154 319 gqsqqrihtpPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSnlpppPALKP 398
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 7959257 684 ARSSPVNRPSSATNKALS--PVTSRTPGVVASAPTKPQSPAQNATSSQ 729
Cdd:pfam03154 399 LSSLSTHHPPSAHPPPLQlmPQSQQLPPPPAQPPVLTQSQSLPPPAAS 446
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
473-654 |
2.64e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 45.75 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 473 MPSTGMAEQSKRPRLEvghqgvvfqhpgadagvPLQQLMPTAQGGMPPTPQAAqlagqrqSQQQYDPSTGPPvqnaaslh 552
Cdd:PRK07764 364 LPSASDDERGLLARLE-----------------RLERRLGVAGGAGAPAAAAP-------SAAAAAPAAAPA-------- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 553 tplpqlPGRLPPAGVPTAALSSALQFAQQPQVVEAQTQLQIPVKTQQPNVPIPAPPSSQLPIPPSQPAQLALHVPTPGKV 632
Cdd:PRK07764 412 ------PAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPP 485
|
170 180
....*....|....*....|..
gi 7959257 633 QVQASQLSSLPQMVASTRLPVD 654
Cdd:PRK07764 486 AAPAPAAAPAAPAAPAAPAGAD 507
|
|
| DEXQc_bact_SNF2 |
cd18013 |
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ... |
1056-1230 |
2.66e-04 |
|
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprise a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. The bacterial SNF2 present in this family are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350771 [Multi-domain] Cd Length: 218 Bit Score: 44.26 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1056 LRDYQKIGLDWLAKLYRknlNGILADeAGLGKTVQIIAFFAHLACnEGNWGPHLV-----VVRScnilKWELELKRW--C 1128
Cdd:cd18013 1 PHPYQKVAINFIIEHPY---CGLFLD-MGLGKTVTTLTALSDLQL-DDFTRRVLViaplrVARS----TWPDEVEKWnhL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 1129 PGLKILSYIGSHREL-KAKRQEWaepnsfHVCITSYtQFFRGLTAFTRVRW--KCLVIDEMQRVKGMTERHWEAVFTLQS 1205
Cdd:cd18013 72 RNLTVSVAVGTERQRsKAANTPA------DLYVINR-ENLKWLVNKSGDPWpfDMVVIDELSSFKSPRSKRFKALRKVRP 144
|
170 180
....*....|....*....|....*..
gi 7959257 1206 Q-QRLL-LIDSPLHNTFLELWTMVHFL 1230
Cdd:cd18013 145 ViKRLIgLTGTPSPNGLMDLWAQIALL 171
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
539-775 |
4.81e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.31 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 539 PSTGPPVQNAASLHTPLPQ--LPGRLPPAGVPTAALSSALQFAQQ--PQVVEAQTQLQIPVKTQQPNVPIPaPPSSQL-- 612
Cdd:PHA03247 2686 RAARPTVGSLTSLADPPPPppTPEPAPHALVSATPLPPGPAAARQasPALPAAPAPPAVPAGPATPGGPAR-PARPPTta 2764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 613 ----PIPPSQPAQLALHVPTPGKVQVQASQLSSLPQMVASTRLPVDPAPPCPRPLPTSSTSSLAPVSGSGPGPSPARSSP 688
Cdd:PHA03247 2765 gppaPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPG 2844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 689 VNRPSSATNKALSP-------VTSRTPGVVASAPTKP------QSPAQNATSSQDSSQDTLTEQITLENQVHQRIAELRK 755
Cdd:PHA03247 2845 PPPPSLPLGGSVAPggdvrrrPPSRSPAAKPAAPARPpvrrlaRPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPP 2924
|
250 260
....*....|....*....|
gi 7959257 756 AglwSQRRLPKLQEAPRPKS 775
Cdd:PHA03247 2925 P---PPQPQPPPPPPPRPQP 2941
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
499-649 |
8.81e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 43.93 E-value: 8.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 499 PGADAGVPlqqlmPTAQGGMPPTPQAAQLAGQRQSQQQYDPSTGPPV----QNAASLHTPLPQLPGRLPPAGVPTAALSS 574
Cdd:PRK14951 366 PAAAAEAA-----APAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPaaaaSAPAAPPAAAPPAPVAAPAAAAPAAAPAA 440
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7959257 575 ALQFAQQPQVVEAQTQ---LQIPVKTQqpnvPIPAPPSSQlPIPPSQPAQLALHVPTPGKVQVQAsqlssLPQMVAST 649
Cdd:PRK14951 441 APAAVALAPAPPAQAApetVAIPVRVA----PEPAVASAA-PAPAAAPAAARLTPTEEGDVWHAT-----VQQLAAAE 508
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
471-752 |
9.16e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 44.31 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 471 QAMPSTGMAEQSKRPRLEVGHQGVVFQHPGADAGVPLQQLMPtaqggmPPTPQAAQLAGQRQSQQQYDPSTGPPVQNAAs 550
Cdd:PRK10263 361 QPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQ------PQQPYYAPAAEQPAQQPYYAPAPEQPAQQPY- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 551 lHTPLPQLPGRLPPAGVPTAALSSALQFAQQPQVVEAQTQLQIPVKTQQPNVPipaPPSSQLPIP------PSQPA---- 620
Cdd:PRK10263 434 -YAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVE---QQPVVEPEPvveetkPARPPlyyf 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 621 ------------QLA---------LHVPTPGKVQVQASQLSSLPQM-VASTRLPVDPAPPCPRPLPTSSTSSLAPV---- 674
Cdd:PRK10263 510 eeveekrarereQLAawyqpipepVKEPEPIKSSLKAPSVAAVPPVeAAAAVSPLASGVKKATLATGAAATVAAPVfsla 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 675 SGSGPGPS------PARSSPvNRPSSATNKALSPVTSRTPGV-VASAPTKPQSPAQNATSSQDSS-------QDTLTEQI 740
Cdd:PRK10263 590 NSGGPRPQvkegigPQLPRP-KRIRVPTRRELASYGIKLPSQrAAEEKAREAQRNQYDSGDQYNDdeidamqQDELARQF 668
|
330
....*....|..
gi 7959257 741 TleNQVHQRIAE 752
Cdd:PRK10263 669 A--QTQQQRYGE 678
|
|
| PABP-1234 |
TIGR01628 |
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ... |
469-584 |
9.27e-04 |
|
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.
Pssm-ID: 130689 [Multi-domain] Cd Length: 562 Bit Score: 44.03 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 469 RQQAMPSTGMAEQSKRPRLEVGHQG---VVFQHPGAD-AGVPL----QQLMPTAQG------GMPPTPQAAQLAGQRQSQ 534
Cdd:TIGR01628 372 QDQFMQLQPRMRQLPMGSPMGGAMGqppYYGQGPQQQfNGQPLgwprMSMMPTPMGpggplrPNGLAPMNAVRAPSRNAQ 451
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 7959257 535 QQYDPSTGPPVQ-----NAASLHTPLPQlPGRLPPAGVPTAALSSALQFA---QQPQV 584
Cdd:TIGR01628 452 NAAQKPPMQPVMyppnyQSLPLSQDLPQ-PQSTASQGGQNKKLAQVLASAtpqMQKQV 508
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
499-732 |
1.57e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 499 PGADAGVPLQQLMPTAQGGMPPTPQAAQLAGQRQSQ--QQYDPSTGPPVQNAASLHTPLPQLPGRLPPAG--VPTAALSS 574
Cdd:PHA03307 73 PGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPpgPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGspGPPPAASP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 575 ALQFAQQPQVVEAQT---QLQIPVKTQQPNVPIPAPPSSQLPI------------PPSQPAQLALHVPTPGKVQVQASQL 639
Cdd:PHA03307 153 PAAGASPAAVASDAAssrQAALPLSSPEETARAPSSPPAEPPPstppaaasprppRRSSPISASASSPAPAPGRSAADDA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 640 SSLPQMVASTRLPV---DPAPPCPRPLPTSSTSSLAPVSGSGPGPSPARSSPVnRPSSATNKALSPVTSRTPGVVASAPT 716
Cdd:PHA03307 233 GASSSDSSSSESSGcgwGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPA-SSSSSPRERSPSPSPSSPGSGPAPSS 311
|
250
....*....|....*.
gi 7959257 717 KPQSPAQNATSSQDSS 732
Cdd:PHA03307 312 PRASSSSSSSRESSSS 327
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
484-722 |
1.66e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 43.33 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 484 RPRLEVGHQGVVFQHPGADAGVPLQQLMPTAQGGMPPTPQAAqlagqrqsqqqydPSTGPPVQNAASlhtPLPQLPGRLP 563
Cdd:PRK12323 364 RPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAA-------------PAAAPAAAAAAR---AVAAAPARRS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 564 PAGVPTAALSSALQFAQQPQVVEAQTQLQIPVKTQQPNVPIPAPPSSQLPIPPSQPAQLALHVPTPGKVqvqaSQLSSLP 643
Cdd:PRK12323 428 PAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDP----PPWEELP 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7959257 644 QMVASTRLPVDPAPPCPRPLPTSSTSSLAPVSGSGPGPSPARSSPvnrPSSATNKALSPVTSRTPGVVASAPTKPQSPA 722
Cdd:PRK12323 504 PEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAA---PAPRAAAATEPVVAPRPPRASASGLPDMFDG 579
|
|
| PRK10905 |
PRK10905 |
cell division protein DamX; Validated |
519-720 |
1.85e-03 |
|
cell division protein DamX; Validated
Pssm-ID: 236792 [Multi-domain] Cd Length: 328 Bit Score: 42.62 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 519 PPTPQAAQLAGQRQSQQQYDPSTGPPVQNAASlhtPLPQLPGRLPPAGvptaALSSALQFAQQP-QVVEAQTQLQIPVkt 597
Cdd:PRK10905 55 PGTTSAEQTAGNTQQDVSLPPISSTPTQGQTP---VATDGQQRVEVQG----DLNNALTQPQNQqQLNNVAVNSTLPT-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 598 qQPNVPIPAPPSSQLPIPPSQPAQLALHVPTPGKVQVQASqlSSLPQMVASTRLPVDPAPPCPRPLPTSSTSSLAPVSGS 677
Cdd:PRK10905 126 -EPATVAPVRNGNASRQTAKTQTAERPATTRPARKQAVIE--PKKPQATAKTEPKPVAQTPKRTEPAAPVASTKAPAATS 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 7959257 678 GPGPSP-ARSSPVNRPSSATNKALSPVTSRTPGVVASAPTKPQS 720
Cdd:PRK10905 203 TPAPKEtATTAPVQTASPAQTTATPAAGGKTAGNVGSLKSAPSS 246
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
501-726 |
2.31e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.67 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 501 ADAGVPLQQLMPTAQGGMPPTPQAAQLAGQRQSQQQYDPSTGPPvqNAASLHTPLPQLPGRLPPAGVPTAALSSALQFAQ 580
Cdd:PRK07764 589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGA--AAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGG 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 581 QPQVVEAQTqlqiPVKTQQPNVPIPAPPSSQLPIPPSQPAQLALHVPTPGKVQVQASQlsslPQMVASTRLPVDPAPPCP 660
Cdd:PRK07764 667 DGWPAKAGG----AAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQ----PPQAAQGASAPSPAADDP 738
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7959257 661 RPLPtsSTSSLAPVSGSGPGPSPARSSPVNRPSSATNKALSPVTSRTPGVVASAPTKPQSPAQNAT 726
Cdd:PRK07764 739 VPLP--PEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAE 802
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
507-773 |
2.53e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 42.75 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 507 LQQLMPTAQGGMPPTPQAAQLAGQrQSQQQYDPSTGPPVQNAASLHtPLPQLPGRLPPAGVPTAALSSALQFAQQPQVVE 586
Cdd:PHA03378 585 LASSAPSYAQTPWPVPHPSQTPEP-PTTQSHIPETSAPRQWPMPLR-PIPMRPLRMQPITFNVLVFPTPHQPPQVEITPY 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 587 AQTQLQIPVKTQQPNvpiPAPPSSQLPI---------PPSQPAQLALHVPTPGKVQVQASQLSSLPQMVASTRLPVDPAP 657
Cdd:PHA03378 663 KPTWTQIGHIPYQPS---PTGANTMLPIqwapgtmqpPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAA 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 658 PCPRPLPTSSTSSLAPVSGSGPGPSPARSSPVNRPSSATNKALSPVTSRTPgvvASAPTKPQSPAQNATSSQDSSQDTLT 737
Cdd:PHA03378 740 APGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRP---RGAPTPQPPPQAGPTSMQLMPRAAPG 816
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 7959257 738 EQITLENQVHQRIAELRKAG---LWSQRRLPKLQEA-PRP 773
Cdd:PHA03378 817 QQGPTKQILRQLLTGGVKRGrpsLKKPAALERQAAAgPTP 856
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
506-718 |
4.11e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 41.99 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 506 PLQQLMPTAQGGMPPTPQAAQlagqrQSQQQYDPSTGPPVQNAASLHTPLPQlpgrlPPAGVPTAALSSALQFAQQPQVV 585
Cdd:PRK10263 755 PQQPVAPQQQYQQPQQPVAPQ-----PQYQQPQQPVAPQPQYQQPQQPVAPQ-----PQYQQPQQPVAPQPQYQQPQQPV 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 586 EAQTQLQIPvktQQPNVPIPAPP-----------SSQLPIPPSQPAQLALHVPTPGKVQ-VQASQLSSLPQMV----AST 649
Cdd:PRK10263 825 APQPQYQQP---QQPVAPQPQDTllhpllmrngdSRPLHKPTTPLPSLDLLTPPPSEVEpVDTFALEQMARLVearlADF 901
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7959257 650 RLPVDPAPPCPRPLPTSSTSSLApvsgsgPGPSPARSSPVNRPSSatnKALSPVTSRtpgVVASAPTKP 718
Cdd:PRK10263 902 RIKADVVNYSPGPVITRFELNLA------PGVKAARISNLSRDLA---RSLSTVAVR---VVEVIPGKP 958
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
520-727 |
4.42e-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: 42.06 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 520 PTPQAAQL---AGQRQSQQQYDP-------------STGPPVQNAASLHTPLPQLPGRLPPAGVPTAALSSALQFAQQPQ 583
Cdd:pfam03154 149 PSPQDNESdsdSSAQQQILQTQPpvlqaqsgaasppSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPH 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 584 VVEAQTQLQIPVKTQQPNVPI-----PAPPSSQLPIPPSQPAQLALHVPTPGKVQVQASQL------SSLPQMVASTRLP 652
Cdd:pfam03154 229 TLIQQTPTLHPQRLPSPHPPLqpmtqPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMqhpvppQPFPLTPQSSQSQ 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7959257 653 VDPAPPCPRPLPTSSTSSLAPVSGSGPGPSPARSSPvnrpssatnkaLSPVTSRTPGvVASAPTKPQSPAQNATS 727
Cdd:pfam03154 309 VPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQP-----------LPPAPLSMPH-IKPPPTTPIPQLPNPQS 371
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
493-760 |
5.14e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.85 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 493 GVVFQHPGADAGVPLQQLMPTAQGGMPPTPQAAQLAGQRQSQQQYDPSTGPP----VQNAASLHTPLPQLPGRLPPAGVP 568
Cdd:PHA03247 2729 RQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPrrltRPAVASLSESRESLPSPWDPADPP 2808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 569 TAAL--SSALQFAQQPQVVEAQTQLQIPVKTQQPNVPIPA-----------------PPSSQLPIPPSQPAQL-ALHVPT 628
Cdd:PHA03247 2809 AAVLapAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPslplggsvapggdvrrrPPSRSPAAKPAAPARPpVRRLAR 2888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 629 PGKVQVQAS------QLSSLPQMVASTR-LPVDPAPPCPRPLPTSST-----SSLAPVSGSGPGPSPARSSPVNRPSSAT 696
Cdd:PHA03247 2889 PAVSRSTESfalppdQPERPPQPQAPPPpQPQPQPPPPPQPQPPPPPpprpqPPLAPTTDPAGAGEPSGAVPQPWLGALV 2968
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7959257 697 NKALSPVTSRTPGVVASAPTkPQSPAQNATSSQDSSQDTLTEQITLENQVHQRIAELRKAgLWS 760
Cdd:PHA03247 2969 PGRVAVPRFRVPQPAPSREA-PASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQT-LWP 3030
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
495-732 |
6.14e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.46 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 495 VFQHPGADAGVPLQQLMPTAQGGMPPTPQAAQLAGQRQSQQQYDPSTGPPV-----------QNAASLHT--PLPQLPGR 561
Cdd:PHA03247 2479 VYRRPAEARFPFAAGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVhprmltwirglEELASDDAgdPPPPLPPA 2558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 562 LPPAG----VPT----------AALSSALQFAQQPQVVEAQTQLQIPVKTQQPNVPIPAPPSSQLPIPP-SQPAQLALHV 626
Cdd:PHA03247 2559 APPAApdrsVPPprpaprpsepAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPpPSPSPAANEP 2638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 627 PTPGKVQVQASQLSSLPQMVASTRLPVDPAPPCPRPLPTSST---------SSLAPVSGSGPGPSPARSsPVNRPSSATN 697
Cdd:PHA03247 2639 DPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPqrprrraarPTVGSLTSLADPPPPPPT-PEPAPHALVS 2717
|
250 260 270
....*....|....*....|....*....|....*.
gi 7959257 698 KA-LSPVTSRTPGVVASAPTKPQSPAQNATSSQDSS 732
Cdd:PHA03247 2718 ATpLPPGPAAARQASPALPAAPAPPAVPAGPATPGG 2753
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
539-723 |
6.25e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 41.59 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 539 PSTGPPVQNAASLHTPLPQLPGRL-PPAGVPTAALSSALQFAQQPQVVEAQTQLQIPVKTQQPNVPIPAPPSSQLPIPPS 617
Cdd:PHA03378 701 PTPMRPPAAPPGRAQRPAAATGRArPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPP 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 618 QPAQLALHVPTPGKVQVQASQLSSLPQMVASTRLPVDPAPPCPRPLPTSST------------SSLAPVSGSGPGPSPAR 685
Cdd:PHA03378 781 QAPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQLLTGgvkrgrpslkkpAALERQAAAGPTPSPGS 860
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 7959257 686 SS------------PVNRPSSATNKALSPVTsrtpgvvASAPTKPQSPAQ 723
Cdd:PHA03378 861 GTsdkivqapvfypPVLQPIQVMRQLGSVRA-------AAASTVTQAPTE 903
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
556-733 |
6.33e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 41.37 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 556 PQLPGRLP-PAGVPTAALSSALQFAQQPQVVEAQTQLQIPVKTQQPNVPIPAPPSSqlpippSQPAQLALHVPTPGKVQV 634
Cdd:PRK07003 374 ARVAGAVPaPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAA------PAPPATADRGDDAADGDA 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 635 QASQLSSLPQMVASTRLPVDPAPPCPRPLPTSSTSSLAPVSGSGPGPSPARSSPVNRPSSATNKALSpVTSRTPGVVASA 714
Cdd:PRK07003 448 PVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPA-AASREDAPAAAA 526
|
170
....*....|....*....
gi 7959257 715 PTKPQSPAQNATSSQDSSQ 733
Cdd:PRK07003 527 PPAPEARPPTPAAAAPAAR 545
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
504-725 |
7.96e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.46 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 504 GVPLQQLMPTAQGgmPPTPQAAQlagqrqsqqqyDPSTGPPVQNAAslhtplPQLPGRLPPAGVPTAALSSALQfaqqPQ 583
Cdd:PHA03247 2476 GAPVYRRPAEARF--PFAAGAAP-----------DPGGGGPPDPDA------PPAPSRLAPAILPDEPVGEPVH----PR 2532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 584 VVEAQTQLQIPVKTQQPNVPIPAPPSSQLP-----IPPSQPAqlalhvPTPGKVQVQA-SQLSSLPQMVASTRLPVDPA- 656
Cdd:PHA03247 2533 MLTWIRGLEELASDDAGDPPPPLPPAAPPAapdrsVPPPRPA------PRPSEPAVTSrARRPDAPPQSARPRAPVDDRg 2606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959257 657 ------------PPCPRPLPTSSTSSLAPVSGSGPGPSPARSSPVNRPSSATNKALSPVTSRTPGVVASAPTKPQSPAQN 724
Cdd:PHA03247 2607 dprgpappsplpPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRR 2686
|
.
gi 7959257 725 A 725
Cdd:PHA03247 2687 A 2687
|
|
| |
