|
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 ... |
1-469 |
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: 589.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1 MHHGTGPQNVQHQLQRSRACPGSEG---EEQPAHPNPPPSPAAPFAPSASPSAPQSPSYQIqqLMNRSPATGQNVNITLQ 77
Cdd:pfam15790 1 MHHGSGSQNVQRQLQRSKSVSGSEEqqqEQQPATVNHPQSPVTTFAPAASPSAPQSPNYQI--IMSRSPVTGQNVNITLQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 78 SVGPVVGGNQQITLAPLPLPSPTSPGFQFSAQPRRFEHGSPSYIQVTSPLSQQVQTQSPTQPSPGPGQALQnvRAGAPGP 157
Cdd:pfam15790 79 NVGQMVAGNQQITLTPLPLQSPASPGFQHSAPQWRFEHGSPSYIQVTSPLPQQVQPQSPTQHSPVPLQGVQ--RPGAPGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 158 GLGLCSSSPTGgFVDASVLVRQISL-SPSSGGHFVFQDGSGLTQIAQG-AQVQLQHPGTPITVRERRPSQPHTQSGGTIH 235
Cdd:pfam15790 157 GLGVCGQSPTR-FVDASMLVRQISLgSPSGGGHFVYQDGTGLAQIAPGaGQVQLASPGTPGSVRERRLSQPHSQTGGTIH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 236 HLGPQSPAAAGgAGLQPLASPSHITTANLPPQISSIIQGQlvqqqqvlqgppLPRPLGFERTPGVLLPGAGGAAGF-GMT 314
Cdd:pfam15790 236 HLGPQSPAAAG-AGLQTLGSPGHITTSNLPPQISSIIQGQ------------LARPLGFEKTAQVVVAGAGGPAASfGIP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 315 SPPPPTSPSRTAVPPGLSSLPLTSVGNTG-MKKVPKKLEEIPPASPEMAQMRKQCLDYHYQEMQALKEVFKEYLIELFFL 393
Cdd:pfam15790 303 SSIPPTSPSRTSPPPGLSSNPLTSTGMSGsVKKVPKKLEEIAPATPEIAQLRKQCLDHHTKKMESLKEVFKEYLIELFFL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 394 QHFQGNMMDFLAFKKKHYAPLQAYLRQNDLDIeeeeEEEEEEEEKSEVINDEQ--------------------------- 446
Cdd:pfam15790 383 QHLQGNMMDFLAFKKKHCVPLYTYLRQNDLDL----EEEEEEEEQSEVINDEVkvvtgkdgqtgtpvaiatqlppnvsaa 458
|
490 500 510
....*....|....*....|....*....|.
gi 152012891 447 --------QALAGSLVAGAGSTVETDLFKRQ 469
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 ... |
1055-1271 |
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 152012891 1055 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1134
Cdd:cd18003 1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1135 YIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSP 1214
Cdd:cd18003 81 YYGSAKERKLKRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 152012891 1215 LHNTFLELWTMVHFLVPGI------SRPYLSSPLRAPSEESQDYYHKVVIRLHRVTQPFILRR 1271
Cdd:cd18003 161 LQNSLMELWSLMHFLMPHIfqshqeFKEWFSNPLTAMSEGSQEENEELVRRLHKVLRPFLLRR 223
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
1029-1350 |
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 152012891 1029 EAILPKGSARVTTSvkfnaPSLLYGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHL 1108
Cdd:PLN03142 149 DGLGGSGGTRLLVQ-----PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHM 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1109 VVVRSCNILKWELELKRWCPGLKILSYIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRV 1188
Cdd:PLN03142 224 VVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1189 KGMTERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPGI--SRPYLSSPLRAPSEESQdyyHKVVIRLHRVTQP 1266
Cdd:PLN03142 304 KNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIfsSAETFDEWFQISGENDQ---QEVVQQLHKVLRP 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1267 FILRRTKRDVEKQLTKKYEHVLKCRLSNRQKALYEdVILQPGTQEALKSGHFVNVLSILVRLQRICNHPGLVEPRHPGSS 1346
Cdd:PLN03142 381 FLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYK-ALLQKDLDVVNAGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPP 459
|
....
gi 152012891 1347 YVAG 1350
Cdd:PLN03142 460 YTTG 463
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
849-1338 |
7.50e-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: 7.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 849 EQVVEIKLRVELEEKRKKALNLQKVSRRGKELRPKGFDALQESSLDSGMSGRKRKASISLTDDEVDDEEETIEEEEANEG 928
Cdd:COG0553 35 LARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLRLLLALLLLALLLLLAGLLALALLLLALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 929 VVDHQTELSNLAKEAELPLLDLMKLYEGAFLPSSQWPRPKPDGEDTSGEEDADDCPGDRESRKDLVLIDSLFIMDQFKAA 1008
Cdd:COG0553 115 GLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELAL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1009 ERMNIGK-PNAKDIADVTAVAEAILPKGSARVTTSVKFNAPSLLYGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKT 1087
Cdd:COG0553 195 LAAEAELlLLLELLLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1088 VQIIAFFAHLAcNEGNWGPHLVVV-RSCnILKWELELKRWCPGLKILSYIGShrelkAKRQEWAEP-NSFHVCITSYTQF 1165
Cdd:COG0553 275 IQALALLLELK-ERGLARPVLIVApTSL-VGNWQRELAKFAPGLRVLVLDGT-----RERAKGANPfEDADLVITSYGLL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1166 FRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPGisrpYLSSPlrap 1245
Cdd:COG0553 348 RRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPG----LLGSL---- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1246 sEESQDYYHKVVI--------RLHRVTQPFILRRTKRDVEKQLTKKYEHVLKCRLSNRQKALYEDVI--LQPGTQEALKS 1315
Cdd:COG0553 420 -KAFRERFARPIEkgdeealeRLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLeyLRRELEGAEGI 498
|
490 500
....*....|....*....|...
gi 152012891 1316 GHFVNVLSILVRLQRICNHPGLV 1338
Cdd:COG0553 499 RRRGLILAALTRLRQICSHPALL 521
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
1058-1338 |
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 152012891 1058 YQKIGLDWLAKLYRK-NLNGILADEAGLGKTVQIIAFFAHLACNEGNWG-PHLVVVRSCNILKWELELKRWC--PGLKIL 1133
Cdd:pfam00176 1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1134 SYIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDS 1213
Cdd:pfam00176 81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1214 PLHNTFLELWTMVHFLVPGI--SRPYLSSPLRAPSEESQDYyhKVVIRLHRVTQPFILRRTKRDVEKQLTKKYEHVLKCR 1291
Cdd:pfam00176 161 PLQNNLEELWALLNFLRPGPfgSLSTFRNWFDRPIERGGGK--KGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCR 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 152012891 1292 LSNRQKALYEDVILQPGTQEALKS--GHFVN--VLSILVRLQRICNHPGLV 1338
Cdd:pfam00176 239 LSKLQRKLYQTFLLKKDLNAIKTGegGREIKasLLNILMRLRKICNHPGLI 289
|
|
| DEXHc_SMARCA1_SMARCA5 |
cd17997 |
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ... |
1053-1273 |
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 152012891 1053 GALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKI 1132
Cdd:cd17997 2 GTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1133 LSYIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLID 1212
Cdd:cd17997 82 VVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 152012891 1213 SPLHNTFLELWTMVHFLVPGIsrpYLSSPLRAP---SEESQDYYHKVVIRLHRVTQPFILRRTK 1273
Cdd:cd17997 162 TPLQNNLHELWALLNFLLPDV---FTSSEDFDEwfnVNNCDDDNQEVVQRLHKVLRPFLLRRIK 222
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
1055-1231 |
6.26e-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: 6.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1055 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1134
Cdd:cd17919 1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1135 YIGShRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSP 1214
Cdd:cd17919 81 YHGS-QRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTP 159
|
170
....*....|....*..
gi 152012891 1215 LHNTFLELWTMVHFLVP 1231
Cdd:cd17919 160 LQNNLEELWALLDFLDP 176
|
|
| DEXQc_INO80 |
cd18002 |
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ... |
1055-1271 |
4.21e-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: 4.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1055 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1134
Cdd:cd18002 1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1135 YIGSHRELKAKRQEWAEPN------SFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRL 1208
Cdd:cd18002 81 YWGNPKDRKVLRKFWDRKNlytrdaPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 152012891 1209 LLIDSPLHNTFLELWTMVHFLVPGI------SRPYLSSPLRAPSEESQDYYHKVVIRLHRVTQPFILRR 1271
Cdd:cd18002 161 LLTGTPIQNSMAELWALLHFIMPTLfdshdeFNEWFSKDIESHAENKTGLNEHQLKRLHMILKPFMLRR 229
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
1053-1273 |
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 152012891 1053 GALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLAcNEGNWGPHLVVVRSCNILKWELELKRWCPGLKI 1132
Cdd:cd18012 3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRK-EEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1133 LSYIGShrelKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLID 1212
Cdd:cd18012 82 LVIHGT----KRKREKLRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 152012891 1213 SPLHNTFLELWTMVHFLVPGisrpYLSSP------LRAPSEESQDyyHKVVIRLHRVTQPFILRRTK 1273
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 ... |
1053-1273 |
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 152012891 1053 GALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKI 1132
Cdd:cd17996 2 GTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1133 LSYIGShRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKgmtERHWEAVFTL----QSQQRL 1208
Cdd:cd17996 82 IVYKGT-PDVRKKLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMK---NAQSKLTQTLntyyHARYRL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 152012891 1209 LLIDSPLHNTFLELWTMVHFLVPGI--SRP----YLSSPLRAPSEESQDYYHK-----VVIRLHRVTQPFILRRTK 1273
Cdd:cd17996 158 LLTGTPLQNNLPELWALLNFLLPKIfkSCKtfeqWFNTPFANTGEQVKIELNEeetllIIRRLHKVLRPFLLRRLK 233
|
|
| DEXHc_HELLS_SMARCA6 |
cd18009 |
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ... |
1053-1273 |
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 152012891 1053 GALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNeGNWGPHLVVVRSCNILKWELELKRWCPGLKI 1132
Cdd:cd18009 2 GVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRER-GVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1133 LSYIGSHRE-LKAKRQEWAEPNS---FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRL 1208
Cdd:cd18009 81 LLYHGTKEErERLRKKIMKREGTlqdFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 152012891 1209 LLIDSPLHNTFLELWTMVHFLVPGISRPY-----------LSSPLRAPSEESQDYYHKVVIRLHRVTQPFILRRTK 1273
Cdd:cd18009 161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLssfeswfdfssLSDNAADISNLSEEREQNIVHMLHAILKPFLLRRLK 236
|
|
| DEXHc_SMARCA5 |
cd18064 |
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ... |
1046-1283 |
2.33e-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: 2.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1046 NAPSLL-YGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELK 1124
Cdd:cd18064 6 DSPSYVkWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1125 RWCPGLKILSYIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQS 1204
Cdd:cd18064 86 RWVPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1205 QQRLLLIDSPLHNTFLELWTMVHFLVPGISRpylssplrapSEESQDYY---------HKVVIRLHRVTQPFILRRTKRD 1275
Cdd:cd18064 166 TNRLLLTGTPLQNNLHELWALLNFLLPDVFN----------SAEDFDSWfdtnnclgdQKLVERLHMVLRPFLLRRIKAD 235
|
....*...
gi 152012891 1276 VEKQLTKK 1283
Cdd:cd18064 236 VEKSLPPK 243
|
|
| DEXHc_SMARCAD1 |
cd17998 |
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ... |
1055-1231 |
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 152012891 1055 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLAcNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1134
Cdd:cd17998 1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLK-EIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1135 YIGSHRELKAKRQEwAEPN--SFHVCITSYT---------QFFRgltaftRVRWKCLVIDEMQRVKGMTERHWEAVFTLQ 1203
Cdd:cd17998 80 YYGSQEERKHLRYD-ILKGleDFDVIVTTYNlatsnpddrSFFK------RLKLNYVVYDEGHMLKNMTSERYRHLMTIN 152
|
170 180
....*....|....*....|....*...
gi 152012891 1204 SQQRLLLIDSPLHNTFLELWTMVHFLVP 1231
Cdd:cd17998 153 ANFRLLLTGTPLQNNLLELMSLLNFIMP 180
|
|
| DEXHc_CHD1_2 |
cd17993 |
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ... |
1055-1271 |
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 152012891 1055 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1134
Cdd:cd17993 2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1135 YIGSHRELKAKRQ-EWAEPNS----FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLL 1209
Cdd:cd17993 82 YLGDIKSRDTIREyEFYFSQTkklkFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 152012891 1210 LIDSPLHNTFLELWTMVHFLVPGisRPYLSSPLR-APSEESQDYYHkvviRLHRVTQPFILRR 1271
Cdd:cd17993 162 ITGTPLQNSLKELWALLHFLMPG--KFDIWEEFEeEHDEEQEKGIA----DLHKELEPFILRR 218
|
|
| DEXHc_SMARCA1 |
cd18065 |
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ... |
1053-1273 |
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 152012891 1053 GALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKI 1132
Cdd:cd18065 14 GTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1133 LSYIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLID 1212
Cdd:cd18065 94 VCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTG 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1213 SPLHNTFLELWTMVHFLVPGISRpylssplrapSEESQDYY---------HKVVIRLHRVTQPFILRRTK 1273
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; ... |
1055-1271 |
9.93e-40 |
|
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: 9.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1055 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPgLKILS 1134
Cdd:cd17995 1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1135 YIGSH--RELKAKRQ-----EWAEPNS----FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQ 1203
Cdd:cd17995 80 YHGSGesRQIIQQYEmyfkdAQGRKKKgvykFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 152012891 1204 SQQRLLLIDSPLHNTFLELWTMVHFLVPGisrpylssplRAPSEES--QDY----YHKVVIRLHRVTQPFILRR 1271
Cdd:cd17995 160 LEHKLLLTGTPLQNNTEELWSLLNFLEPE----------KFPSSEEflEEFgdlkTAEQVEKLQALLKPYMLRR 223
|
|
| DEXHc_CHD2 |
cd18054 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ... |
1048-1271 |
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 152012891 1048 PSLLYGA---LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELK 1124
Cdd:cd18054 11 PSYIGGEnleLRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1125 RWCPGLKILSYIGSHRELKAKRQ-EWAEPNS----FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAV 1199
Cdd:cd18054 91 IWAPEINVVVYIGDLMSRNTIREyEWIHSQTkrlkFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 152012891 1200 FTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPGISRPYlssplrapsEESQDYYHKV----VIRLHRVTQPFILRR 1271
Cdd:cd18054 171 IDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFW---------EDFEEDHGKGrengYQSLHKVLEPFLLRR 237
|
|
| DEXHc_SMARCA4 |
cd18062 |
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ... |
1039-1273 |
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 152012891 1039 VTTSVKFNAPSLLYGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILK 1118
Cdd:cd18062 8 VTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1119 WELELKRWCPGLKILSYIGShrelKAKRQEWA---EPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKgmtERH 1195
Cdd:cd18062 88 WVYEFDKWAPSVVKVSYKGS----PAARRAFVpqlRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMK---NHH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1196 WEAVFTLQSQ----QRLLLIDSPLHNTFLELWTMVHFLVPGISRP------YLSSPLRAPSEE---SQDYYHKVVIRLHR 1262
Cdd:cd18062 161 CKLTQVLNTHyvapRRLLLTGTPLQNKLPELWALLNFLLPTIFKScstfeqWFNAPFAMTGEKvdlNEEETILIIRRLHK 240
|
250
....*....|.
gi 152012891 1263 VTQPFILRRTK 1273
Cdd:cd18062 241 VLRPFLLRRLK 251
|
|
| DEXHc_SMARCA2 |
cd18063 |
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ... |
1039-1273 |
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 152012891 1039 VTTSVKFNAPSLLYGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILK 1118
Cdd:cd18063 8 ITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1119 WELELKRWCPGLKILSYIGS---HRELKAKRQEwaepNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKgmtERH 1195
Cdd:cd18063 88 WTYEFDKWAPSVVKISYKGTpamRRSLVPQLRS----GKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMK---NHH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1196 WEAVFTLQSQ----QRLLLIDSPLHNTFLELWTMVHFLVPGISRP------YLSSPLRAPSEE---SQDYYHKVVIRLHR 1262
Cdd:cd18063 161 CKLTQVLNTHyvapRRILLTGTPLQNKLPELWALLNFLLPTIFKScstfeqWFNAPFAMTGERvdlNEEETILIIRRLHK 240
|
250
....*....|.
gi 152012891 1263 VTQPFILRRTK 1273
Cdd:cd18063 241 VLRPFLLRRLK 251
|
|
| DEXHc_CHD1L |
cd18006 |
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ... |
1055-1271 |
3.56e-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: 3.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1055 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1134
Cdd:cd18006 1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1135 YIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSP 1214
Cdd:cd18006 81 YMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 152012891 1215 LHNTFLELWTMVHFLvpgisrpylsSPLRAPSEESQDYYHK---------VVIRLHRVTQPFILRR 1271
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 ... |
1055-1271 |
4.26e-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: 4.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1055 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQ---IIAFFAHLACNEGNWG--PHLVVVRSCNILKWELELKRWCP- 1128
Cdd:cd17999 1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQtlcILASDHHKRANSFNSEnlPSLVVCPPTLVGHWVAEIKKYFPn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1129 -GLKILSYIGSHRElkaKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQR 1207
Cdd:cd17999 81 aFLKPLAYVGPPQE---RRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 152012891 1208 LLLIDSPLHNTFLELWTMVHFLVPG-----------ISRPYLSSPLRAPSEESQDYYHKVVIRLHRVTQPFILRR 1271
Cdd:cd17999 158 LILSGTPIQNNVLELWSLFDFLMPGylgtekqfqrrFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
|
|
| DEXHc_CHD1 |
cd18053 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ... |
1055-1271 |
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 152012891 1055 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1134
Cdd:cd18053 21 LRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1135 YIGSHRELKAKR-QEWAEPNS----FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLL 1209
Cdd:cd18053 101 YLGDINSRNMIRtHEWMHPQTkrlkFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 152012891 1210 LIDSPLHNTFLELWTMVHFLVPGISRPYlsSPLRAPSEESQDYYHKvviRLHRVTQPFILRR 1271
Cdd:cd18053 181 ITGTPLQNSLKELWSLLHFIMPEKFSSW--EDFEEEHGKGREYGYA---SLHKELEPFLLRR 237
|
|
| DEXHc_ERCC6 |
cd18000 |
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ... |
1055-1238 |
1.90e-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: 117.04 E-value: 1.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1055 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKIL- 1133
Cdd:cd18000 1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1134 -----------SYIGSHRELKAKRQEWAEPNsfHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTL 1202
Cdd:cd18000 81 lhssgsgtgseEKLGSIERKSQLIRKVVGDG--GILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQL 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 152012891 1203 QSQQRLLLIDSPLHNTFLELWTMVHFLVPgisrPYL 1238
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; ... |
1055-1271 |
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 152012891 1055 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLAcNEGNW-GPHLVVVRSCNILKWELELKRWCPGLKIL 1133
Cdd:cd17994 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLY-KEGHSkGPFLVSAPLSTIINWEREFEMWAPDFYVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1134 SYIGShrelkakrqewaepnsfHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDS 1213
Cdd:cd17994 80 TYVGD-----------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGT 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 152012891 1214 PLHNTFLELWTMVHFLVPGisrpyLSSPLRAPSEESQDYYHKVVI-RLHRVTQPFILRR 1271
Cdd:cd17994 143 PLQNNLEELFHLLNFLTPE-----RFNNLQGFLEEFADISKEDQIkKLHDLLGPHMLRR 196
|
|
| HSA |
smart00573 |
domain in helicases and associated with SANT domains; |
764-835 |
1.42e-27 |
|
domain in helicases and associated with SANT domains;
Pssm-ID: 214727 [Multi-domain] Cd Length: 73 Bit Score: 107.10 E-value: 1.42e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 152012891 764 PKLQEAPRPKSHWDYLLEEMQWMATDFAQERRWKVAAAKKLVRTVVRHHEEKQLREERG-KKEEQSRLRRIAA 835
Cdd:smart00573 1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERReEKNEKRRLRKLAA 73
|
|
| DEXHc_ERCC6L |
cd18001 |
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ... |
1055-1271 |
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 152012891 1055 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLAcNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1134
Cdd:cd18001 1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMF-DSGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1135 YIGSHRELKAKRQEWAEpNSFHVCITSYTQFFRG---LTAFTR--VRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLL 1209
Cdd:cd18001 80 FHGTSKKERERNLERIQ-RGGGVLLTTYGMVLSNteqLSADDHdeFKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRII 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 152012891 1210 LIDSPLHNTFLELWTMVHFLVPG--------ISRPYLSSPLRAPSEES----QDYYHKVVIRLHRVTQPFILRR 1271
Cdd:cd18001 159 LTGTPIQNNLKELWALFDFACNGsllgtrktFKMEFENPITRGRDKDAtqgeKALGSEVAENLRQIIKPYFLRR 232
|
|
| DEXHc_ERCC6L2 |
cd18005 |
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ... |
1055-1271 |
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 152012891 1055 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHL---------ACN-----------EGNWGPHLVVVRSC 1114
Cdd:cd18005 1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVlgktgtrrdRENnrprfkkkppaSSAKKPVLIVAPLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1115 NILKWELELKRWcpG-LKILSYIGSHRE------LKAKRQEwaepnsfhVCITSYTQFFRGLTAFTRVRWKCLVIDEMQR 1187
Cdd:cd18005 81 VLYNWKDELDTW--GhFEVGVYHGSRKDdelegrLKAGRLE--------VVVTTYDTLRRCIDSLNSINWSAVIADEAHR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1188 VKGMTERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPG-----------ISRPYLSSPLRAPSEESQDYYHKV 1256
Cdd:cd18005 151 IKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGalgsrsqfkkhFSEPIKRGQRHTATARELRLGRKR 230
|
250
....*....|....*
gi 152012891 1257 VIRLHRVTQPFILRR 1271
Cdd:cd18005 231 KQELAVKLSKFFLRR 245
|
|
| DEXHc_CHD7 |
cd18059 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ... |
1055-1271 |
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 152012891 1055 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACnEGNWGPHLVVVRSCNILKWELELKRWCPgLKILS 1134
Cdd:cd18059 1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYL-KGIHGPFLVIAPLSTIPNWEREFRTWTE-LNVVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1135 YIGSH---RELKAKRQEWAEPN--------SFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQ 1203
Cdd:cd18059 79 YHGSQasrRTIQLYEMYFKDPQgrvikgsyKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 152012891 1204 SQQRLLLIDSPLHNTFLELWTMVHFLVPGisrpylssplRAPSEES--QDY----YHKVVIRLHRVTQPFILRR 1271
Cdd:cd18059 159 LEHKVLLTGTPLQNTVEELFSLLHFLEPS----------RFPSETTfmQEFgdlkTEEQVQKLQAILKPMMLRR 222
|
|
| DEXHc_RAD54 |
cd18004 |
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ... |
1055-1271 |
4.76e-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: 4.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1055 LRDYQKIGLDWLAK--LYRKNLNG---ILADEAGLGKTVQIIAFFAHLACNEGNWGPHL---VVVRSCNILK-WELELKR 1125
Cdd:cd18004 1 LRPHQREGVQFLYDclTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKPTAkkaLIVCPSSLVGnWKAEFDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1126 WCPG--LKILSYIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTR-VRWKCLVIDEMQRVKGMTERHWEAVFTL 1202
Cdd:cd18004 81 WLGLrrIKVVTADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKkISIDLLICDEGHRLKNSESKTTKALNSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1203 QSQQRLLLIDSPLHNTFLELWTMVHFLVPGI-----------SRPYLSSPLRAPSEESQDYYHKVVIRLHRVTQPFILRR 1271
Cdd:cd18004 161 PCRRRLLLTGTPIQNDLDEFFALVDFVNPGIlgslasfrkvfEEPILRSRDPDASEEDKELGAERSQELSELTSRFILRR 240
|
|
| DEXHc_CHD3 |
cd18055 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ... |
1055-1271 |
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 152012891 1055 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1134
Cdd:cd18055 1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1135 YIGS----------------------HRELKAKRQewaEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMT 1192
Cdd:cd18055 81 YTGDkdsraiirenefsfddnavkggKKAFKMKRE---AQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1193 ERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPGisrpyLSSPLRAPSEESQDYYHKVVI-RLHRVTQPFILRR 1271
Cdd:cd18055 158 SKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPE-----RFNNLEGFLEEFADISKEDQIkKLHDLLGPHMLRR 232
|
|
| DEXHc_CHD4 |
cd18056 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ... |
1055-1271 |
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 152012891 1055 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1134
Cdd:cd18056 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1135 YIGSH------RE-------------LKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERH 1195
Cdd:cd18056 81 YVGDKdsraiiREnefsfednairggKKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 152012891 1196 WEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPgiSRPYlssPLRAPSEESQDYYHKVVI-RLHRVTQPFILRR 1271
Cdd:cd18056 161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTP--ERFH---NLEGFLEEFADIAKEDQIkKLHDMLGPHMLRR 232
|
|
| DEXHc_CHD6 |
cd18058 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ... |
1055-1271 |
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 152012891 1055 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACnEGNWGPHLVVVRSCNILKWELELKRWCPgLKILS 1134
Cdd:cd18058 1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFL-MGIRGPFLIIAPLSTITNWEREFRTWTE-MNAIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1135 YIGSH--RELKAK-----RQEWAEPNS----FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQ 1203
Cdd:cd18058 79 YHGSQisRQMIQQyemyyRDEQGNPLSgifkFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 152012891 1204 SQQRLLLIDSPLHNTFLELWTMVHFLVPgISRPYLSSPLrapsEESQDY-YHKVVIRLHRVTQPFILRR 1271
Cdd:cd18058 159 LEHKVLLTGTPLQNSVEELFSLLNFLEP-SQFPSETTFL----EEFGDLkTEEQVKKLQSILKPMMLRR 222
|
|
| DEXHc_CHD5 |
cd18057 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ... |
1055-1271 |
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 152012891 1055 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1134
Cdd:cd18057 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1135 YIGSHRELKAKRQ-EWA-EPNS-----------------FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERH 1195
Cdd:cd18057 81 YTGDKESRSVIREnEFSfEDNAirsgkkvfrmkkeaqikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 152012891 1196 WEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVpgisrPYLSSPLRAPSEESQDYYHKVVI-RLHRVTQPFILRR 1271
Cdd:cd18057 161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLT-----PERFNNLEGFLEEFADISKEDQIkKLHDLLGPHMLRR 232
|
|
| DEXHc_CHD9 |
cd18061 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ... |
1055-1271 |
3.27e-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: 105.86 E-value: 3.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1055 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNeGNWGPHLVVVRSCNILKWELELKRWCpGLKILS 1134
Cdd:cd18061 1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLT-GIRGPFLIIAPLSTIANWEREFRTWT-DLNVVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1135 YIGS--HRELKAKRQEWAEPNS---------FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQ 1203
Cdd:cd18061 79 YHGSliSRQMIQQYEMYFRDSQgriirgayrFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 152012891 1204 SQQRLLLIDSPLHNTFLELWTMVHFLvpgisrpylsSPLRAPSEES--QDY----YHKVVIRLHRVTQPFILRR 1271
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 ... |
1055-1271 |
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 152012891 1055 LRDYQKIGLDWLakLYRknlNGILADEAGLGKTVQIIA---------------FFAHLACNEGNWGPH--LVVVRScNIL 1117
Cdd:cd18008 1 LLPYQKQGLAWM--LPR---GGILADEMGLGKTIQALAlilatrpqdpkipeeLEENSSDPKKLYLSKttLIVVPL-SLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1118 K-WELELKR--WCPGLKILSYIGSHRELKAKrqewaEPNSFHVCITSYT----------QFFRGLTAFT------RVRWK 1178
Cdd:cd18008 75 SqWKDEIEKhtKPGSLKVYVYHGSKRIKSIE-----ELSDYDIVITTYGtlasefpknkKGGGRDSKEKeasplhRIRWY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1179 CLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFL------VPGISRPYLSSPLRAPSEESQDy 1252
Cdd:cd18008 150 RVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLrvepfgDYPWFNSDISKPFSKNDRKALE- 228
|
250
....*....|....*....
gi 152012891 1253 yhkvviRLHRVTQPFILRR 1271
Cdd:cd18008 229 ------RLQALLKPILLRR 241
|
|
| DEXHc_CHD8 |
cd18060 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ... |
1055-1271 |
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 152012891 1055 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLAcNEGNWGPHLVVVRSCNILKWELELKRWCPgLKILS 1134
Cdd:cd18060 1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVY-NVGIHGPFLVIAPLSTITNWEREFNTWTE-MNTIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1135 YIGS--HRELKAKRQEWAEPNS---------FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQ 1203
Cdd:cd18060 79 YHGSlaSRQMIQQYEMYCKDSRgrlipgaykFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 152012891 1204 SQQRLLLIDSPLHNTFLELWTMVHFLVPGisrpYLSSPLRAPSEESQDYYHKVVIRLHRVTQPFILRR 1271
Cdd:cd18060 159 LEHKVLLTGTPLQNTVEELFSLLHFLEPS----QFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 222
|
|
| HSA |
pfam07529 |
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ... |
766-832 |
1.04e-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: 90.32 E-value: 1.04e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 152012891 766 LQEAPR-PKSHWDYLLEEMQWMATDFAQERRWKVAAAKKLVRTVVRHHEEKQLREERgKKEEQSRLRR 832
Cdd:pfam07529 1 RDEPERrEKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHKNIEKEEQK-RIEREEKQRL 67
|
|
| DEXHc_RAD54B |
cd18066 |
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ... |
1055-1271 |
2.41e-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: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1055 LRDYQKIGLDWL-----AKLYRKNLNGILADEAGLGKTVQIIAFFAHLACnEGNWGPH------LVVVRSCNILKWELEL 1123
Cdd:cd18066 1 LRPHQREGIEFLyecvmGMRVNERFGAILADEMGLGKTLQCISLIWTLLR-QGPYGGKpvikraLIVTPGSLVKNWKKEF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1124 KRWcpglkilsyIGSHR------ELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWE 1197
Cdd:cd18066 80 QKW---------LGSERikvftvDQDHKVEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1198 AVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPGI-----------SRPYLSSPLRAPSEESQDYYHKVVIRLHRVTQP 1266
Cdd:cd18066 151 ALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGIlgslstyrkvyEEPIVRSREPTATPEEKKLGEARAAELTRLTGL 230
|
....*
gi 152012891 1267 FILRR 1271
Cdd:cd18066 231 FILRR 235
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1048-1236 |
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 152012891 1048 PSLLYGALRDYQKIGLDWLAKLYRknlNGILADEAGLGKTVQIIAfFAHLACNEGNWGPHLVVV--RScniLK--WELEL 1123
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALL-PALEALKRGKGGRVLVLVptRE---LAeqWAEEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1124 KRWCP--GLKILSYIGSHRELKAKRQEWAEPnsFHVCITSYTQFFRGLT--AFTRVRWKCLVIDEMQRVKGMTER-HWEA 1198
Cdd:smart00487 75 KKLGPslGLKVVGLYGGDSKREQLRKLESGK--TDILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGGFGdQLEK 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 152012891 1199 VFTL--QSQQRLLL---IDSPLHNTFLELWTMVHFLVPGISRP 1236
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 ... |
1077-1243 |
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 152012891 1077 ILADEAGLGKTVQIIAFF-AHLACNEGNWGPHLVVVRSCnILKWELELKRWCPGLKILSYIGSH--RELKAKR-----QE 1148
Cdd:cd18007 30 ILAHTMGLGKTLQVITFLhTYLAAAPRRSRPLVLCPAST-LYNWEDEFKKWLPPDLRPLLVLVSlsASKRADArlrkiNK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1149 WAEPNSfhVCITSYTQFfRGLTA---------FTRVRWKC------LVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDS 1213
Cdd:cd18007 109 WHKEGG--VLLIGYELF-RNLASnattdprlkQEFIAALLdpgpdlLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGT 185
|
170 180 190
....*....|....*....|....*....|
gi 152012891 1214 PLHNTFLELWTMVHFLVPGisrpYLSSPLR 1243
Cdd:cd18007 186 PLQNNLKEYWTMVDFARPK----YLGTLKE 211
|
|
| DEXHc_HARP_SMARCAL1 |
cd18010 |
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ... |
1071-1233 |
1.90e-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: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1071 RKNLNGILADEAGLGKTVQIIAFFAHLacnEGNWgPHLVVVRSCNILKWELELKRWCPGLKILSYIgshreLKAKRQEWA 1150
Cdd:cd18010 14 RRGGRVLIADEMGLGKTVQAIAIAAYY---REEW-PLLIVCPSSLRLTWADEIERWLPSLPPDDIQ-----VIVKSKDGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1151 EPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVK-GMTERHWEAVFTLQSQQR-LLLIDSPLHNTFLELWTMVHF 1228
Cdd:cd18010 85 RDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKnSKAKRTKAALPLLKRAKRvILLSGTPALSRPIELFTQLDA 164
|
....*
gi 152012891 1229 LVPGI 1233
Cdd:cd18010 165 LDPKL 169
|
|
| DEXHc_RAD54A |
cd18067 |
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ... |
1055-1233 |
1.16e-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: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1055 LRDYQKIGLDWLAK----LYRKNLNG-ILADEAGLGKTVQIIAFFAHLACNEGNWGPHL----VVVRSCNILKWELELKR 1125
Cdd:cd18067 1 LRPHQREGVKFLYRcvtgRRIRGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaiVVSPSSLVKNWANELGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1126 WCpGLKILSYI---GSHRELKAKRQEWAEPNSFH----VCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEA 1198
Cdd:cd18067 81 WL-GGRLQPLAidgGSKKEIDRKLVQWASQQGRRvstpVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQA 159
|
170 180 190
....*....|....*....|....*....|....*
gi 152012891 1199 VFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPGI 1233
Cdd:cd18067 160 LDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGI 194
|
|
| DEXHc_ARIP4 |
cd18069 |
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ... |
1077-1250 |
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 152012891 1077 ILADEAGLGKTVQIIAF----FAHLACNEGnwgphLVVVRSCNILKWELELKRWCP-----------GLKILSYIGSHRE 1141
Cdd:cd18069 32 ILAHSMGLGKTLQVISFldvlLRHTGAKTV-----LAIVPVNTLQNWLSEFNKWLPppealpnvrprPFKVFILNDEHKT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1142 LKAKRQ---EWAEPNSfhVCITSYTQFfrgltaftRVR--WKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSPLH 1216
Cdd:cd18069 107 TAARAKvieDWVKDGG--VLLMGYEMF--------RLRpgPDVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQ 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 152012891 1217 NTFLELWTMVHFLVPGI--SRPYLSSPLRAPSEESQ 1250
Cdd:cd18069 177 NNLIEYWCMVDFVRPDFlgTRQEFSNMFERPILNGQ 212
|
|
| DEXHc_ATRX |
cd18068 |
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ... |
1076-1233 |
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 152012891 1076 GILADEAGLGKTVQIIAFFAHLACNE--GNWGPHLVVVRSCNILKWELELKRWCPGLKI--------LSYIGSHRELKAK 1145
Cdd:cd18068 31 CILAHCMGLGKTLQVVTFLHTVLLCEklENFSRVLVVCPLNTVLNWLNEFEKWQEGLKDeekievneLATYKRPQERSYK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1146 RQEWAEPNSfhVCITSYtQFFRGLTAFTRVRWKC-----------------LVIDEMQRVKGMTERHWEAVFTLQSQQRL 1208
Cdd:cd18068 111 LQRWQEEGG--VMIIGY-DMYRILAQERNVKSREklkeifnkalvdpgpdfVVCDEGHILKNEASAVSKAMNSIRTKRRI 187
|
170 180
....*....|....*....|....*
gi 152012891 1209 LLIDSPLHNTFLELWTMVHFLVPGI 1233
Cdd:cd18068 188 VLTGTPLQNNLIEYHCMVNFVKPNL 212
|
|
| DEXHc_TTF2 |
cd18072 |
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ... |
1055-1229 |
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 152012891 1055 LRDYQKIGLDWLakLYRKNLN---GILADEAGLGKTVQIIAFFahLACNEG-------------NWGPHL--VVVRSCNI 1116
Cdd:cd18072 1 LLLHQKQALAWL--LWRERQKprgGILADDMGLGKTLTMIALI--LAQKNTqnrkeeekekaltEWESKKdsTLVPSAGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1117 L---------KWELELKRWCPG--LKILSYIGSHRELKAKRQEwaepnSFHVCITSYTQFFRGL---------TAFTRVR 1176
Cdd:cd18072 77 LvvcpaslvhQWKNEVESRVASnkLRVCLYHGPNRERIGEVLR-----DYDIVITTYSLVAKEIptykeesrsSPLFRIA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 152012891 1177 WKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFL 1229
Cdd:cd18072 152 WARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFL 204
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
518-780 |
4.69e-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: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 518 PPTPQAAQLAGQRQSQQQYDPSTGPPVQNAASLHT---------PLPQL-----------PGRLPPAGVPTAALSSALQF 577
Cdd:pfam09770 108 AARAAQSSAQPPASSLPQYQYASQQSQQPSKPVRTgyekykepePIPDLqvdaslwgvapKKAAAPAPAPQPAAQPASLP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 578 AQQPQV-----VEAQTQLQIPVKTQQPNVPIPAPPSSqlpiPPSQPAQLALHVPTPGKVQVQASQLSSLPQMVASTRLPV 652
Cdd:pfam09770 188 APSRKMmsleeVEAAMRAQAKKPAQQPAPAPAQPPAA----PPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPV 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 653 DPAPPCPRPLPTSSTSSLAPVS-GSGPGPSPARSSPV------NRPSSAtnkalspvtsRTPGVVASAPTKPQSPAQNAT 725
Cdd:pfam09770 264 TILQRPQSPQPDPAQPSIQPQAqQFHQQPPPVPVQPTqilqnpNRLSAA----------RVGYPQNPQPGVQPAPAHQAH 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 152012891 726 SSQdSSQDTLTEQITLENQVHQRIAELRKAGLwsqrrlpkLQEAPRPK-SHWDYLL 780
Cdd:pfam09770 334 RQQ-GSFGRQAPIITHPQQLAQLSEEEKAAYL--------DEEAKRAKrNHKIFLL 380
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
496-733 |
8.23e-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: 8.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 496 QHPGADAGVPLQQLMptAQGGMPPTPQaAQLAGQRQSQQQYDPSTGPPVQNAASLHTPLPQLPGRL----PPAGVPTAAL 571
Cdd:pfam03154 290 QHPVPPQPFPLTPQS--SQSQVPPGPS-PAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMphikPPPTTPIPQL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 572 SSAlQFAQQPQVVEAQTQLQIPVKTQQP-------NVPIPAPPSS------------QLPIPPSQPaqlalhvPTPGKVQ 632
Cdd:pfam03154 367 PNP-QSHKHPPHLSGPSPFQMNSNLPPPpalkplsSLSTHHPPSAhppplqlmpqsqQLPPPPAQP-------PVLTQSQ 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 633 VQASQLSSLPQMVASTRLPVDPAPPCPRPLPTSSTSSLAPvsgSGPGPSPARSSPVNRPSSATNKALSpvtsrtpGVVAS 712
Cdd:pfam03154 439 SLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPP---SGPPTSTSSAMPGIQPPSSASVSSS-------GPVPA 508
|
250 260
....*....|....*....|.
gi 152012891 713 APTKPQSPAQNATSSQDSSQD 733
Cdd:pfam03154 509 AVSCPLPPVQIKEEALDEAEE 529
|
|
| DEXHc_HLTF1_SMARC3 |
cd18071 |
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ... |
1076-1271 |
5.42e-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: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1076 GILADEAGLGKTVQIIAFFAHlacnegnwGPHLVVVRSCNILKWELELKRWC-PG-LKILSYIGSHRELKAKrqewaEPN 1153
Cdd:cd18071 51 GILADDMGLGKTLTTISLILA--------NFTLIVCPLSVLSNWETQFEEHVkPGqLKVYTYHGGERNRDPK-----LLS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1154 SFHVCITSYTQF-----FRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHF 1228
Cdd:cd18071 118 KYDIVLTTYNTLasdfgAKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSF 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 152012891 1229 L--VPGISRPYLSSPLRAPSEESQDyyhKVVIRLHRVTQPFILRR 1271
Cdd:cd18071 198 LhlKPFSNPEYWRRLIQRPLTMGDP---TGLKRLQVLMKQITLRR 239
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
1077-1232 |
6.63e-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: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1077 ILADEAGLGKTVQIIAfFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCpGLKILSYIGSHRElKAKRQEWAEPNSFH 1156
Cdd:cd18011 21 LLADEVGLGKTIEAGL-IIKELLLRGDAKRVLILCPASLVEQWQDELQDKF-GLPFLILDRETAA-QLRRLIGNPFEEFP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1157 VCITSYTQFFRG---LTAFTRVRWKCLVIDEMQRVKGM-----TERhWEAVFTLQSQQR--LLLIDSPLHNTFLELWTMV 1226
Cdd:cd18011 98 IVIVSLDLLKRSeerRGLLLSEEWDLVVVDEAHKLRNSgggkeTKR-YKLGRLLAKRARhvLLLTATPHNGKEEDFRALL 176
|
....*.
gi 152012891 1227 HFLVPG 1232
Cdd:cd18011 177 SLLDPG 182
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
477-643 |
1.87e-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: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 477 MAEQSKRPRlevghQGVVFQHPGADAGVPLQQLMPTAQGgmPPTPQAAQLAGQRQSQQQYDPSTGPPVQnaaslhtPLPQ 556
Cdd:pfam09770 203 MRAQAKKPA-----QQPAPAPAQPPAAPPAQQAQQQQQF--PPQIQQQQQPQQQPQQPQQHPGQGHPVT-------ILQR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 557 LPGRLPPAGVPTAALSSALQFAQQPQVVEAQTQ-LQIPVKTQQPNVPIPAPPSSQLPIPPSQPAQLALHV-PTPGKVQVQ 634
Cdd:pfam09770 269 PQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQiLQNPNRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSfGRQAPIITH 348
|
....*....
gi 152012891 635 ASQLSSLPQ 643
Cdd:pfam09770 349 PQQLAQLSE 357
|
|
| DEXQc_SHPRH |
cd18070 |
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ... |
1055-1192 |
3.31e-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: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1055 LRDYQKIGLDWLaklyrKNLNGILADEAGLGKTVQIIAF-FAH-----------LACNEGNWGPHLVV---VRSCN---- 1115
Cdd:cd18070 1 LLPYQRRAVNWM-----LVPGGILADEMGLGKTVEVLALiLLHprpdndldaadDDSDEMVCCPDCLVaetPVSSKatli 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1116 -----ILK-WELELKRWCP-GLKILSYIGSHRELKAKRQEWAEPNSFHVCITSYT-------------------QFFRGL 1169
Cdd:cd18070 76 vcpsaILAqWLDEINRHVPsSLKVLTYQGVKKDGALASPAPEILAEYDIVVTTYDvlrtelhyaeanrsnrrrrRQKRYE 155
|
170 180
....*....|....*....|....*.
gi 152012891 1170 ---TAFTRVRWKCLVIDEMQRVKGMT 1192
Cdd:cd18070 156 appSPLVLVEWWRVCLDEAQMVESST 181
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
511-734 |
5.42e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.86 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 511 PTAQGGMPPTPQAAQLAGQRQSQQQYDPSTGP--PVQNAASLHTPLPQLPgrlPPAGVPTAALSSALQFAQQPQVVEAQT 588
Cdd:PHA03247 2735 LPAAPAPPAVPAGPATPGGPARPARPPTTAGPpaPAPPAAPAAGPPRRLT---RPAVASLSESRESLPSPWDPADPPAAV 2811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 589 QLQIPV--KTQQPNVPIPAPPSSQLPIPPSQPAQLALHVPTPGKV------QVQASQLSSLPQMVASTRLPVDPAPPCPR 660
Cdd:PHA03247 2812 LAPAAAlpPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVapggdvRRRPPSRSPAAKPAAPARPPVRRLARPAV 2891
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 152012891 661 PLPTSSTSSlapvsgsgPGPSPARSSPVNRPSSATNKALSPVTSRtPGVVASAPTKPQSPAQNATSSQDSSQDT 734
Cdd:PHA03247 2892 SRSTESFAL--------PPDQPERPPQPQAPPPPQPQPQPPPPPQ-PQPPPPPPPRPQPPLAPTTDPAGAGEPS 2956
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
495-772 |
1.42e-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: 49.91 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 495 FQHPGADAGVPLQQLMPT---AQGGMPPTPQAAQL-----AGQRQSQQQYDPSTGP----PVQNAASLHTPLPQLPGRLP 562
Cdd:pfam05109 439 FAAPNTTTGLPSSTHVPTnltAPASTGPTVSTADVtsptpAGTTSGASPVTPSPSPrdngTESKAPDMTSPTSAVTTPTP 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 563 PAGVPTAALSSALQFAQQPQVveAQTQLQIPVKTQQPNVPIPAPPSSQlPIPPSQpaqlalhVPTPGKVQVQASQLSSLP 642
Cdd:pfam05109 519 NATSPTPAVTTPTPNATSPTL--GKTSPTSAVTTPTPNATSPTPAVTT-PTPNAT-------IPTLGKTSPTSAVTTPTP 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 643 QMVASTrlpvdpappcprPLPTSSTSSLAPVSGSGPGPSPARSSPVNRPSSATNKALSPVTSRTpgvVASAPTKPQSPAQ 722
Cdd:pfam05109 589 NATSPT------------VGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSS---TSSMSLRPSSISE 653
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 152012891 723 NATSsqdSSQDTLTEQITLENQVH----QRIAELRKAGLwSQRRLPKLQEAPRP 772
Cdd:pfam05109 654 TLSP---STSDNSTSHMPLLTSAHptggENITQVTPAST-STHHVSTSSPAPRP 703
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
469-722 |
3.03e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.17 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 469 QQAMPSTGMAEQSKRPRLEVGHQGVVFQHPGADAGVPLQQLMPTAQGGMPPTPQAAQLAGQRQSQQQYDPSTGPPVQNAA 548
Cdd:PHA03247 2572 RPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPER 2651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 549 SLHTPLP---QLPGRLPPAGVPTAAlSSALQFAQQPQV---VEAQTQLQIPVKTQQPNVPIPAPPSSQLPIPPSQPAQLA 622
Cdd:PHA03247 2652 PRDDPAPgrvSRPRRARRLGRAAQA-SSPPQRPRRRAArptVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQ 2730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 623 LHVPTPGKvqvqasqlSSLPQMVASTRLPVDPAPPCPRPLPTSSTSSLAPVSGSGPGPSPARSSPVNRPSSATNKALSPV 702
Cdd:PHA03247 2731 ASPALPAA--------PAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPW 2802
|
250 260
....*....|....*....|
gi 152012891 703 TSRTPGVVASAPTKPQSPAQ 722
Cdd:PHA03247 2803 DPADPPAAVLAPAAALPPAA 2822
|
|
| PHA03269 |
PHA03269 |
envelope glycoprotein C; Provisional |
588-721 |
6.07e-05 |
|
envelope glycoprotein C; Provisional
Pssm-ID: 165527 [Multi-domain] Cd Length: 566 Bit Score: 47.80 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 588 TQLQIPVKTQQPNVPIP---APPSSQLPIPPSQPAQLALHVPTPGKVQVQAS----QLSSLPQMVASTRLpvDPAPPCPR 660
Cdd:PHA03269 13 ACINLIIANLNTNIPIPelhTSAATQKPDPAPAPHQAASRAPDPAVAPTSAAsrkpDLAQAPTPAASEKF--DPAPAPHQ 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 152012891 661 PLPTSSTSSLAPVSGSGPGPSPArSSPVNRPSSATNKALSPVT--SRTPGVVASAPTKPQSPA 721
Cdd:PHA03269 91 AASRAPDPAVAPQLAAAPKPDAA-EAFTSAAQAHEAPADAGTSaaSKKPDPAAHTQHSPPPFA 152
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
469-730 |
8.81e-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: 47.31 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 469 QQAMPSTGMAEQSKRPRLEVGHQGVVFQHPGADAGVPLQQLMPTAQGGMP--------PTPQAAQLAGQRQSQQQYDPST 540
Cdd:pfam09606 171 PNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGqqaqanggMNPQQMGGAPNQVAMQQQQPQQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 541 GPPVQNAASLHTPLPQLPGRLP---PAGVPTAALSSAlqfAQQPQVVEAQTQLQIP-VKTQQPNVpiPAPPSSQLPIPPS 616
Cdd:pfam09606 251 QGQQSQLGMGINQMQQMPQGVGggaGQGGPGQPMGPP---GQQPGAMPNVMSIGDQnNYQQQQTR--QQQQQQGGNHPAA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 617 QPAQLALHVptpgkvqVQASQLSSLP-QMVASTRLPVDPAPPCPRPL--------------PTSSTSSLAPVSGSGPGPS 681
Cdd:pfam09606 326 HQQQMNQSV-------GQGGQVVALGgLNHLETWNPGNFGGLGANPMqrgqpgmmsspspvPGQQVRQVTPNQFMRQSPQ 398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 152012891 682 PARSSPVNrPSSATNKALSPVTSRTPGVVAS-APTKPQSPAQNATSSQDS 730
Cdd:pfam09606 399 PSVPSPQG-PGSQPPQSHPGGMIPSPALIPSpSPQMSQQPAQQRTIGQDS 447
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
480-726 |
9.89e-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: 47.22 E-value: 9.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 480 QSKRPRLEVGHQGVVFQHPGADAGVPlqqlmptaqGGMPPTPQAAQLAGQRQSQQQydpSTGPPVQNAAS----LHTPLP 555
Cdd:pfam05109 500 ESKAPDMTSPTSAVTTPTPNATSPTP---------AVTTPTPNATSPTLGKTSPTS---AVTTPTPNATSptpaVTTPTP 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 556 QlpGRLPPAG--VPTAALSSALQFAQQPQVVEAQTQLQI-----------PVKTQQPNVPIPAPPSSQLPIPPSQPAQLA 622
Cdd:pfam05109 568 N--ATIPTLGktSPTSAVTTPTPNATSPTVGETSPQANTtnhtlggtsstPVVTSPPKNATSAVTTGQHNITSSSTSSMS 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 623 LHVPTPGKVQVQASQLSSLPQMVASTRlpVDPAPPCPRPLPTSSTSSLAPVSGSGPGPSPARSSPVNRPSSATNKALSPV 702
Cdd:pfam05109 646 LRPSSISETLSPSTSDNSTSHMPLLTS--AHPTGGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTSTKPGE 723
|
250 260
....*....|....*....|....
gi 152012891 703 TSRTPGVVASAPTKPQSPAQNATS 726
Cdd:pfam05109 724 VNVTKGTPPKNATSPQAPSGQKTA 747
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
586-770 |
1.21e-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: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 586 AQTQLQipvKTQQPNVPIPAPPSSQLPIPPSQPAQLALHVPTPGKVQVQ---ASQLSSLPQMVASTRLPVDPAPPCPRPL 662
Cdd:pfam03154 162 AQQQIL---QTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPpqgSPATSQPPNQTQSTAAPHTLIQQTPTLH 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 663 PTSSTSSLAPVSGSGPGPSPARSSPVNRPSSATNKALSPVtsrtPGVVASAPTKPQSPAQ----NATSSQDSSQDTLTEQ 738
Cdd:pfam03154 239 PQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPM----PHSLQTGPSHMQHPVPpqpfPLTPQSSQSQVPPGPS 314
|
170 180 190
....*....|....*....|....*....|..
gi 152012891 739 ITLENQVHQRIAELRKAGLWSQRRLPKLQEAP 770
Cdd:pfam03154 315 PAAPGQSQQRIHTPPSQSQLQSQQPPREQPLP 346
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
1055-1184 |
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 152012891 1055 LRDYQKIGLD-WLAKLYRKNLNGILADEAGLGKTvqIIAFFAHLACNEGNWGPH-LVVVRSCNILK-WELELKRWCPGLK 1131
Cdd:pfam04851 4 LRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKT--LTAAKLIARLFKKGPIKKvLFLVPRKDLLEqALEEFKKFLPNYV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 152012891 1132 ILSYIGSHRELKAKRQEWaepnsfHVCITSYTQFFRGLTAFTRV----RWKCLVIDE 1184
Cdd:pfam04851 82 EIGEIISGDKKDESVDDN------KIVVTTIQSLYKALELASLEllpdFFDVIIIDE 132
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
499-736 |
2.15e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 46.02 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 499 GADAGVPLQQLMPTAQggMPPTPQAAQLAGQRQSQQQYDPSTGPPVQNAASlhtPLPQLPGRLPPAGVPTAALSSALQFA 578
Cdd:PRK12323 369 GGGAGPATAAAAPVAQ--PAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAAR---AVAAAPARRSPAPEALAAARQASARG 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 579 QQPQVVEAQTQLQIPVKTQQPNVPIPAPPSSQLPIPPSQPAQLALHVPTPGKVqvqaSQLSSLPQMVAStrlpvdpappc 658
Cdd:PRK12323 444 PGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDP----PPWEELPPEFAS----------- 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 659 prplptsstsslAPVSGSGPGPSPARSSPVNRPS----SATNKALSPVTSRTPGVVASAPTKPQSPAQNATSSQDSSQDT 734
Cdd:PRK12323 509 ------------PAPAQPDAAPAGWVAESIPDPAtadpDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDM 576
|
..
gi 152012891 735 LT 736
Cdd:PRK12323 577 FD 578
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
480-728 |
2.56e-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: 45.91 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 480 QSKRPRLEVGHQGVVFQHPGADAGVPLQQLMPTAQG------GMPPT---PQAAQLAGQRQSQQQYDPSTGPpvQNAASL 550
Cdd:pfam03154 168 QTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSApsvppqGSPATsqpPNQTQSTAAPHTLIQQTPTLHP--QRLPSP 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 551 HTPLPQLPGRLPPAGVPTAALSSALQFAQQPQvveaqtqLQIPVKTQQPNVPIPAPP----------SSQLPIPPSQ--- 617
Cdd:pfam03154 246 HPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPP-------MPHSLQTGPSHMQHPVPPqpfpltpqssQSQVPPGPSPaap 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 618 ----------PAQLALHVPTPGKVQVQASQLSSLPQMVASTRLPVDPAPPCPRPLPTSSTSSLAPVSGSG-----PGPSP 682
Cdd:pfam03154 319 gqsqqrihtpPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSnlpppPALKP 398
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 152012891 683 ARSSPVNRPSSATNKALS--PVTSRTPGVVASAPTKPQSPAQNATSSQ 728
Cdd:pfam03154 399 LSSLSTHHPPSAHPPPLQlmPQSQQLPPPPAQPPVLTQSQSLPPPAAS 446
|
|
| DEXQc_bact_SNF2 |
cd18013 |
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ... |
1055-1229 |
2.59e-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: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1055 LRDYQKIGLDWLAKLYRknlNGILADeAGLGKTVQIIAFFAHLACnEGNWGPHLV-----VVRScnilKWELELKRW--C 1127
Cdd:cd18013 1 PHPYQKVAINFIIEHPY---CGLFLD-MGLGKTVTTLTALSDLQL-DDFTRRVLViaplrVARS----TWPDEVEKWnhL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 1128 PGLKILSYIGSHREL-KAKRQEWaepnsfHVCITSYtQFFRGLTAFTRVRW--KCLVIDEMQRVKGMTERHWEAVFTLQS 1204
Cdd:cd18013 72 RNLTVSVAVGTERQRsKAANTPA------DLYVINR-ENLKWLVNKSGDPWpfDMVVIDELSSFKSPRSKRFKALRKVRP 144
|
170 180
....*....|....*....|....*..
gi 152012891 1205 Q-QRLL-LIDSPLHNTFLELWTMVHFL 1229
Cdd:cd18013 145 ViKRLIgLTGTPSPNGLMDLWAQIALL 171
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
472-653 |
2.85e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 45.75 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 472 MPSTGMAEQSKRPRLEvghqgvvfqhpgadagvPLQQLMPTAQGGMPPTPQAAqlagqrqSQQQYDPSTGPPvqnaaslh 551
Cdd:PRK07764 364 LPSASDDERGLLARLE-----------------RLERRLGVAGGAGAPAAAAP-------SAAAAAPAAAPA-------- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 552 tplpqlPGRLPPAGVPTAALSSALQFAQQPQVVEAQTQLQIPVKTQQPNVPIPAPPSSQLPIPPSQPAQLALHVPTPGKV 631
Cdd:PRK07764 412 ------PAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPP 485
|
170 180
....*....|....*....|..
gi 152012891 632 QVQASQLSSLPQMVASTRLPVD 653
Cdd:PRK07764 486 AAPAPAAAPAAPAAPAAPAGAD 507
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
538-774 |
4.94e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.31 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 538 PSTGPPVQNAASLHTPLPQ--LPGRLPPAGVPTAALSSALQFAQQ--PQVVEAQTQLQIPVKTQQPNVPIPaPPSSQL-- 611
Cdd:PHA03247 2686 RAARPTVGSLTSLADPPPPppTPEPAPHALVSATPLPPGPAAARQasPALPAAPAPPAVPAGPATPGGPAR-PARPPTta 2764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 612 ----PIPPSQPAQLALHVPTPGKVQVQASQLSSLPQMVASTRLPVDPAPPCPRPLPTSSTSSLAPVSGSGPGPSPARSSP 687
Cdd:PHA03247 2765 gppaPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPG 2844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 688 VNRPSSATNKALSP-------VTSRTPGVVASAPTKP------QSPAQNATSSQDSSQDTLTEQITLENQVHQRIAELRK 754
Cdd:PHA03247 2845 PPPPSLPLGGSVAPggdvrrrPPSRSPAAKPAAPARPpvrrlaRPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPP 2924
|
250 260
....*....|....*....|
gi 152012891 755 AglwSQRRLPKLQEAPRPKS 774
Cdd:PHA03247 2925 P---PPQPQPPPPPPPRPQP 2941
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
498-648 |
8.89e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 43.93 E-value: 8.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 498 PGADAGVPlqqlmPTAQGGMPPTPQAAQLAGQRQSQQQYDPSTGPPV----QNAASLHTPLPQLPGRLPPAGVPTAALSS 573
Cdd:PRK14951 366 PAAAAEAA-----APAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPaaaaSAPAAPPAAAPPAPVAAPAAAAPAAAPAA 440
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 152012891 574 ALQFAQQPQVVEAQTQ---LQIPVKTQqpnvPIPAPPSSQlPIPPSQPAQLALHVPTPGKVQVQAsqlssLPQMVAST 648
Cdd:PRK14951 441 APAAVALAPAPPAQAApetVAIPVRVA----PEPAVASAA-PAPAAAPAAARLTPTEEGDVWHAT-----VQQLAAAE 508
|
|
| PABP-1234 |
TIGR01628 |
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ... |
468-583 |
9.43e-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: 9.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 468 RQQAMPSTGMAEQSKRPRLEVGHQG---VVFQHPGAD-AGVPL----QQLMPTAQG------GMPPTPQAAQLAGQRQSQ 533
Cdd:TIGR01628 372 QDQFMQLQPRMRQLPMGSPMGGAMGqppYYGQGPQQQfNGQPLgwprMSMMPTPMGpggplrPNGLAPMNAVRAPSRNAQ 451
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 152012891 534 QQYDPSTGPPVQ-----NAASLHTPLPQlPGRLPPAGVPTAALSSALQFA---QQPQV 583
Cdd:TIGR01628 452 NAAQKPPMQPVMyppnyQSLPLSQDLPQ-PQSTASQGGQNKKLAQVLASAtpqMQKQV 508
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
470-751 |
1.06e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 43.92 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 470 QAMPSTGMAEQSKRPRLEVGHQGVVFQHPGADAGVPLQQLMPtaqggmPPTPQAAQLAGQRQSQQQYDPSTGPPVQNAAs 549
Cdd:PRK10263 361 QPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQ------PQQPYYAPAAEQPAQQPYYAPAPEQPAQQPY- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 550 lHTPLPQLPGRLPPAGVPTAALSSALQFAQQPQVVEAQTQLQIPVKTQQPNVPipaPPSSQLPIP------PSQPA---- 619
Cdd:PRK10263 434 -YAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVE---QQPVVEPEPvveetkPARPPlyyf 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 620 ------------QLA---------LHVPTPGKVQVQASQLSSLPQM-VASTRLPVDPAPPCPRPLPTSSTSSLAPV---- 673
Cdd:PRK10263 510 eeveekrarereQLAawyqpipepVKEPEPIKSSLKAPSVAAVPPVeAAAAVSPLASGVKKATLATGAAATVAAPVfsla 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 674 SGSGPGPS------PARSSPvNRPSSATNKALSPVTSRTPGV-VASAPTKPQSPAQNATSSQDSS-------QDTLTEQI 739
Cdd:PRK10263 590 NSGGPRPQvkegigPQLPRP-KRIRVPTRRELASYGIKLPSQrAAEEKAREAQRNQYDSGDQYNDdeidamqQDELARQF 668
|
330
....*....|..
gi 152012891 740 TleNQVHQRIAE 751
Cdd:PRK10263 669 A--QTQQQRYGE 678
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
498-731 |
1.69e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.24 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 498 PGADAGVPLQQLMPTAQGGMPPTPQAAQLAGQRQSQ--QQYDPSTGPPVQNAASLHTPLPQLPGRLPPAG--VPTAALSS 573
Cdd:PHA03307 73 PGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPpgPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGspGPPPAASP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 574 ALQFAQQPQVVEAQT---QLQIPVKTQQPNVPIPAPPSSQLPI------------PPSQPAQLALHVPTPGKVQVQASQL 638
Cdd:PHA03307 153 PAAGASPAAVASDAAssrQAALPLSSPEETARAPSSPPAEPPPstppaaasprppRRSSPISASASSPAPAPGRSAADDA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 639 SSLPQMVASTRLPV---DPAPPCPRPLPTSSTSSLAPVSGSGPGPSPARSSPVnRPSSATNKALSPVTSRTPGVVASAPT 715
Cdd:PHA03307 233 GASSSDSSSSESSGcgwGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPA-SSSSSPRERSPSPSPSSPGSGPAPSS 311
|
250
....*....|....*.
gi 152012891 716 KPQSPAQNATSSQDSS 731
Cdd:PHA03307 312 PRASSSSSSSRESSSS 327
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
483-721 |
1.74e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 43.33 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 483 RPRLEVGHQGVVFQHPGADAGVPLQQLMPTAQGGMPPTPQAAqlagqrqsqqqydPSTGPPVQNAASlhtPLPQLPGRLP 562
Cdd:PRK12323 364 RPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAA-------------PAAAPAAAAAAR---AVAAAPARRS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 563 PAGVPTAALSSALQFAQQPQVVEAQTQLQIPVKTQQPNVPIPAPPSSQLPIPPSQPAQLALHVPTPGKVqvqaSQLSSLP 642
Cdd:PRK12323 428 PAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDP----PPWEELP 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 152012891 643 QMVASTRLPVDPAPPCPRPLPTSSTSSLAPVSGSGPGPSPARSSPvnrPSSATNKALSPVTSRTPGVVASAPTKPQSPA 721
Cdd:PRK12323 504 PEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAA---PAPRAAAATEPVVAPRPPRASASGLPDMFDG 579
|
|
| PRK10905 |
PRK10905 |
cell division protein DamX; Validated |
518-719 |
1.95e-03 |
|
cell division protein DamX; Validated
Pssm-ID: 236792 [Multi-domain] Cd Length: 328 Bit Score: 42.23 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 518 PPTPQAAQLAGQRQSQQQYDPSTGPPVQNAASlhtPLPQLPGRLPPAGvptaALSSALQFAQQP-QVVEAQTQLQIPVkt 596
Cdd:PRK10905 55 PGTTSAEQTAGNTQQDVSLPPISSTPTQGQTP---VATDGQQRVEVQG----DLNNALTQPQNQqQLNNVAVNSTLPT-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 597 qQPNVPIPAPPSSQLPIPPSQPAQLALHVPTPGKVQVQASqlSSLPQMVASTRLPVDPAPPCPRPLPTSSTSSLAPVSGS 676
Cdd:PRK10905 126 -EPATVAPVRNGNASRQTAKTQTAERPATTRPARKQAVIE--PKKPQATAKTEPKPVAQTPKRTEPAAPVASTKAPAATS 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 152012891 677 GPGPSP-ARSSPVNRPSSATNKALSPVTSRTPGVVASAPTKPQS 719
Cdd:PRK10905 203 TPAPKEtATTAPVQTASPAQTTATPAAGGKTAGNVGSLKSAPSS 246
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
500-725 |
2.52e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.67 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 500 ADAGVPLQQLMPTAQGGMPPTPQAAQLAGQRQSQQQYDPSTGPPvqNAASLHTPLPQLPGRLPPAGVPTAALSSALQFAQ 579
Cdd:PRK07764 589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGA--AAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGG 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 580 QPQVVEAQTqlqiPVKTQQPNVPIPAPPSSQLPIPPSQPAQLALHVPTPGKVQVQASQlsslPQMVASTRLPVDPAPPCP 659
Cdd:PRK07764 667 DGWPAKAGG----AAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQ----PPQAAQGASAPSPAADDP 738
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 152012891 660 RPLPtsSTSSLAPVSGSGPGPSPARSSPVNRPSSATNKALSPVTSRTPGVVASAPTKPQSPAQNAT 725
Cdd:PRK07764 739 VPLP--PEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAE 802
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
506-772 |
3.02e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 42.36 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 506 LQQLMPTAQGGMPPTPQAAQLAGQrQSQQQYDPSTGPPVQNAASLHtPLPQLPGRLPPAGVPTAALSSALQFAQQPQVVE 585
Cdd:PHA03378 585 LASSAPSYAQTPWPVPHPSQTPEP-PTTQSHIPETSAPRQWPMPLR-PIPMRPLRMQPITFNVLVFPTPHQPPQVEITPY 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 586 AQTQLQIPVKTQQPNvpiPAPPSSQLPI---------PPSQPAQLALHVPTPGKVQVQASQLSSLPQMVASTRLPVDPAP 656
Cdd:PHA03378 663 KPTWTQIGHIPYQPS---PTGANTMLPIqwapgtmqpPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAA 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 657 PCPRPLPTSSTSSLAPVSGSGPGPSPARSSPVNRPSSATNKALSPVTSRTPgvvASAPTKPQSPAQNATSSQDSSQDTLT 736
Cdd:PHA03378 740 APGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRP---RGAPTPQPPPQAGPTSMQLMPRAAPG 816
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 152012891 737 EQITLENQVHQRIAELRKAG---LWSQRRLPKLQEA-PRP 772
Cdd:PHA03378 817 QQGPTKQILRQLLTGGVKRGrpsLKKPAALERQAAAgPTP 856
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
505-717 |
4.55e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 41.99 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 505 PLQQLMPTAQGGMPPTPQAAQlagqrQSQQQYDPSTGPPVQNAASLHTPLPQlpgrlPPAGVPTAALSSALQFAQQPQVV 584
Cdd:PRK10263 755 PQQPVAPQQQYQQPQQPVAPQ-----PQYQQPQQPVAPQPQYQQPQQPVAPQ-----PQYQQPQQPVAPQPQYQQPQQPV 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 585 EAQTQLQIPvktQQPNVPIPAPP-----------SSQLPIPPSQPAQLALHVPTPGKVQ-VQASQLSSLPQMV----AST 648
Cdd:PRK10263 825 APQPQYQQP---QQPVAPQPQDTllhpllmrngdSRPLHKPTTPLPSLDLLTPPPSEVEpVDTFALEQMARLVearlADF 901
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 152012891 649 RLPVDPAPPCPRPLPTSSTSSLApvsgsgPGPSPARSSPVNRPSSatnKALSPVTSRtpgVVASAPTKP 717
Cdd:PRK10263 902 RIKADVVNYSPGPVITRFELNLA------PGVKAARISNLSRDLA---RSLSTVAVR---VVEVIPGKP 958
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
519-726 |
4.77e-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: 41.68 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 519 PTPQAAQL---AGQRQSQQQYDP-------------STGPPVQNAASLHTPLPQLPGRLPPAGVPTAALSSALQFAQQPQ 582
Cdd:pfam03154 149 PSPQDNESdsdSSAQQQILQTQPpvlqaqsgaasppSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPH 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 583 VVEAQTQLQIPVKTQQPNVPI-----PAPPSSQLPIPPSQPAQLALHVPTPGKVQVQASQL------SSLPQMVASTRLP 651
Cdd:pfam03154 229 TLIQQTPTLHPQRLPSPHPPLqpmtqPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMqhpvppQPFPLTPQSSQSQ 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 152012891 652 VDPAPPCPRPLPTSSTSSLAPVSGSGPGPSPARSSPvnrpssatnkaLSPVTSRTPGvVASAPTKPQSPAQNATS 726
Cdd:pfam03154 309 VPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQP-----------LPPAPLSMPH-IKPPPTTPIPQLPNPQS 371
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
492-759 |
5.32e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.85 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 492 GVVFQHPGADAGVPLQQLMPTAQGGMPPTPQAAQLAGQRQSQQQYDPSTGPP----VQNAASLHTPLPQLPGRLPPAGVP 567
Cdd:PHA03247 2729 RQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPrrltRPAVASLSESRESLPSPWDPADPP 2808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 568 TAAL--SSALQFAQQPQVVEAQTQLQIPVKTQQPNVPIPA-----------------PPSSQLPIPPSQPAQL-ALHVPT 627
Cdd:PHA03247 2809 AAVLapAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPslplggsvapggdvrrrPPSRSPAAKPAAPARPpVRRLAR 2888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 628 PGKVQVQAS------QLSSLPQMVASTR-LPVDPAPPCPRPLPTSST-----SSLAPVSGSGPGPSPARSSPVNRPSSAT 695
Cdd:PHA03247 2889 PAVSRSTESfalppdQPERPPQPQAPPPpQPQPQPPPPPQPQPPPPPpprpqPPLAPTTDPAGAGEPSGAVPQPWLGALV 2968
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 152012891 696 NKALSPVTSRTPGVVASAPTkPQSPAQNATSSQDSSQDTLTEQITLENQVHQRIAELRKAgLWS 759
Cdd:PHA03247 2969 PGRVAVPRFRVPQPAPSREA-PASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQT-LWP 3030
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
494-731 |
6.45e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.46 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 494 VFQHPGADAGVPLQQLMPTAQGGMPPTPQAAQLAGQRQSQQQYDPSTGPPV-----------QNAASLHT--PLPQLPGR 560
Cdd:PHA03247 2479 VYRRPAEARFPFAAGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVhprmltwirglEELASDDAgdPPPPLPPA 2558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 561 LPPAG----VPT----------AALSSALQFAQQPQVVEAQTQLQIPVKTQQPNVPIPAPPSSQLPIPP-SQPAQLALHV 625
Cdd:PHA03247 2559 APPAApdrsVPPprpaprpsepAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPpPSPSPAANEP 2638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 626 PTPGKVQVQASQLSSLPQMVASTRLPVDPAPPCPRPLPTSST---------SSLAPVSGSGPGPSPARSsPVNRPSSATN 696
Cdd:PHA03247 2639 DPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPqrprrraarPTVGSLTSLADPPPPPPT-PEPAPHALVS 2717
|
250 260 270
....*....|....*....|....*....|....*.
gi 152012891 697 KA-LSPVTSRTPGVVASAPTKPQSPAQNATSSQDSS 731
Cdd:PHA03247 2718 ATpLPPGPAAARQASPALPAAPAPPAVPAGPATPGG 2753
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
555-732 |
6.54e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 41.37 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 555 PQLPGRLP-PAGVPTAALSSALQFAQQPQVVEAQTQLQIPVKTQQPNVPIPAPPSSqlpippSQPAQLALHVPTPGKVQV 633
Cdd:PRK07003 374 ARVAGAVPaPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAA------PAPPATADRGDDAADGDA 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 634 QASQLSSLPQMVASTRLPVDPAPPCPRPLPTSSTSSLAPVSGSGPGPSPARSSPVNRPSSATNKALSpVTSRTPGVVASA 713
Cdd:PRK07003 448 PVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPA-AASREDAPAAAA 526
|
170
....*....|....*....
gi 152012891 714 PTKPQSPAQNATSSQDSSQ 732
Cdd:PRK07003 527 PPAPEARPPTPAAAAPAAR 545
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
538-722 |
7.34e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 41.21 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 538 PSTGPPVQNAASLHTPLPQLPGRL-PPAGVPTAALSSALQFAQQPQVVEAQTQLQIPVKTQQPNVPIPAPPSSQLPIPPS 616
Cdd:PHA03378 701 PTPMRPPAAPPGRAQRPAAATGRArPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPP 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 617 QPAQLALHVPTPGKVQVQASQLSSLPQMVASTRLPVDPAPPCPRPLPTSST------------SSLAPVSGSGPGPSPAR 684
Cdd:PHA03378 781 QAPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQLLTGgvkrgrpslkkpAALERQAAAGPTPSPGS 860
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 152012891 685 SS------------PVNRPSSATNKALSPVTsrtpgvvASAPTKPQSPAQ 722
Cdd:PHA03378 861 GTsdkivqapvfypPVLQPIQVMRQLGSVRA-------AAASTVTQAPTE 903
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
503-724 |
8.37e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 503 GVPLQQLMPTAQGgmPPTPQAAQlagqrqsqqqyDPSTGPPVQNAAslhtplPQLPGRLPPAGVPTAALSSALQfaqqPQ 582
Cdd:PHA03247 2476 GAPVYRRPAEARF--PFAAGAAP-----------DPGGGGPPDPDA------PPAPSRLAPAILPDEPVGEPVH----PR 2532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 583 VVEAQTQLQIPVKTQQPNVPIPAPPSSQLP-----IPPSQPAqlalhvPTPGKVQVQA-SQLSSLPQMVASTRLPVDPA- 655
Cdd:PHA03247 2533 MLTWIRGLEELASDDAGDPPPPLPPAAPPAapdrsVPPPRPA------PRPSEPAVTSrARRPDAPPQSARPRAPVDDRg 2606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152012891 656 ------------PPCPRPLPTSSTSSLAPVSGSGPGPSPARSSPVNRPSSATNKALSPVTSRTPGVVASAPTKPQSPAQN 723
Cdd:PHA03247 2607 dprgpappsplpPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRR 2686
|
.
gi 152012891 724 A 724
Cdd:PHA03247 2687 A 2687
|
|
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