|
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 ... |
1-505 |
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: 646.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1 MHHGTGPQNVQHQLQRSRACPGSEG---EEQPAHPNPPPSPAAPFAPSASPSAPQSPSYQIqqLMNRSPATGQNVNITLQ 77
Cdd:pfam15790 1 MHHGSGSQNVQRQLQRSKSVSGSEEqqqEQQPATVNHPQSPVTTFAPAASPSAPQSPNYQI--IMSRSPVTGQNVNITLQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 78 SVGPVVGGNQQITLAPLPLPSPTSPGFQFSAQPRRFEHGSPSYIQVTSPLSQQVQTQSPTQPSPGPGQALQnvRAGAPGP 157
Cdd:pfam15790 79 NVGQMVAGNQQITLTPLPLQSPASPGFQHSAPQWRFEHGSPSYIQVTSPLPQQVQPQSPTQHSPVPLQGVQ--RPGAPGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 158 GLGLCSSSPTGgFVDASVLVRQISL-SPSSGGHFVFQDGSGLTQIAQG-AQVQLQHPGTPITVRERRPSQPHTQSGGTIH 235
Cdd:pfam15790 157 GLGVCGQSPTR-FVDASMLVRQISLgSPSGGGHFVYQDGTGLAQIAPGaGQVQLASPGTPGSVRERRLSQPHSQTGGTIH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 236 HLGPQSPAAAGgAGLQPLASPSHITTANLPPQISSIIQGQlvqqqqvlqgppLPRPLGFERTPGVLLPGAGGAAGF-GMT 314
Cdd:pfam15790 236 HLGPQSPAAAG-AGLQTLGSPGHITTSNLPPQISSIIQGQ------------LARPLGFEKTAQVVVAGAGGPAASfGIP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 315 SPPPPTSPSRTAVPPGLSSLPLTSVGNTG-MKKVPKKLEEIPPASPEMAQMRKQCLDYHYQEMQALKEVFKEYLIELFFL 393
Cdd:pfam15790 303 SSIPPTSPSRTSPPPGLSSNPLTSTGMSGsVKKVPKKLEEIAPATPEIAQLRKQCLDHHTKKMESLKEVFKEYLIELFFL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 394 QHFQGNMMDFLAFKKKHYAPLQAYLRQNDLDIeeeeEEEEEEEEKSEVINDEVKVVTGKDGQTGTPVAIATQLPPKVSAA 473
Cdd:pfam15790 383 QHLQGNMMDFLAFKKKHCVPLYTYLRQNDLDL----EEEEEEEEQSEVINDEVKVVTGKDGQTGTPVAIATQLPPNVSAA 458
|
490 500 510
....*....|....*....|....*....|..
9C62_G 474 fSSQQQPFQQALAGSLVAGAGSTVETDLFKRQ 505
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 ... |
1091-1307 |
1.98e-134 |
|
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: 1.98e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1170
Cdd:cd18003 1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1171 YIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSP 1250
Cdd:cd18003 81 YYGSAKERKLKRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
9C62_G 1251 LHNTFLELWTMVHFLVPGI------SRPYLSSPLRAPSEESQDYYHKVVIRLHRVTQPFILRR 1307
Cdd:cd18003 161 LQNSLMELWSLMHFLMPHIfqshqeFKEWFSNPLTAMSEGSQEENEELVRRLHKVLRPFLLRR 223
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
885-1374 |
2.00e-59 |
|
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: 2.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 885 EQVVEIKLRVELEEKRKKALNLQKVSRRGKELRPKGFDALQESSLDSGMSGRKRKASISLTDDEVDDEEETIEEEEANEG 964
Cdd:COG0553 35 LARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLRLLLALLLLALLLLLAGLLALALLLLALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 965 VVDHQTELSNLAKEAELPLLDLMKLYEGAFLPSSQWPRPKPDGEDTSGEEDADDCPGDRESRKDLVLIDSLFIMDQFKAA 1044
Cdd:COG0553 115 GLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELAL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1045 ERMNIGK-PNAKDIADVTAVAEAILPKGSARVTTSVKFNAPSLLYGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKT 1123
Cdd:COG0553 195 LAAEAELlLLLELLLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1124 VQIIAFFAHLAcNEGNWGPHLVVV-RSCnILKWELELKRWCPGLKILSYIGShrelkAKRQEWAEP-NSFHVCITSYTQF 1201
Cdd:COG0553 275 IQALALLLELK-ERGLARPVLIVApTSL-VGNWQRELAKFAPGLRVLVLDGT-----RERAKGANPfEDADLVITSYGLL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1202 FRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPGisrpYLSSPlrap 1281
Cdd:COG0553 348 RRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPG----LLGSL---- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1282 sEESQDYYHKVVI--------RLHRVTQPFILRRTKRDVEKQLTKKYEHVLKCRLSNRQKALYEDVI--LQPGTQEALKS 1351
Cdd:COG0553 420 -KAFRERFARPIEkgdeealeRLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLeyLRRELEGAEGI 498
|
490 500
....*....|....*....|...
9C62_G 1352 GHFVNVLSILVRLQRICNHPGLV 1374
Cdd:COG0553 499 RRRGLILAALTRLRQICSHPALL 521
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
1094-1374 |
2.02e-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: 2.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1094 YQKIGLDWLAKLYRK-NLNGILADEAGLGKTVQIIAFFAHLACNEGNWG-PHLVVVRSCNILKWELELKRWC--PGLKIL 1169
Cdd:pfam00176 1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1170 SYIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDS 1249
Cdd:pfam00176 81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1250 PLHNTFLELWTMVHFLVPGI--SRPYLSSPLRAPSEESQDYyhKVVIRLHRVTQPFILRRTKRDVEKQLTKKYEHVLKCR 1327
Cdd:pfam00176 161 PLQNNLEELWALLNFLRPGPfgSLSTFRNWFDRPIERGGGK--KGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCR 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
9C62_G 1328 LSNRQKALYEDVILQPGTQEALKS--GHFVN--VLSILVRLQRICNHPGLV 1374
Cdd:pfam00176 239 LSKLQRKLYQTFLLKKDLNAIKTGegGREIKasLLNILMRLRKICNHPGLI 289
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
1065-1386 |
2.70e-59 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 225.06 E-value: 2.70e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1065 EAILPKGSARVTTSvkfnaPSLLYGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHL 1144
Cdd:PLN03142 149 DGLGGSGGTRLLVQ-----PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHM 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1145 VVVRSCNILKWELELKRWCPGLKILSYIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRV 1224
Cdd:PLN03142 224 VVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1225 KGMTERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPGI--SRPYLSSPLRAPSEESQdyyHKVVIRLHRVTQP 1302
Cdd:PLN03142 304 KNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIfsSAETFDEWFQISGENDQ---QEVVQQLHKVLRP 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1303 FILRRTKRDVEKQLTKKYEHVLKCRLSNRQKALYEdVILQPGTQEALKSGHFVNVLSILVRLQRICNHPGLVEPRHPGSS 1382
Cdd:PLN03142 381 FLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYK-ALLQKDLDVVNAGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPP 459
|
....
9C62_G 1383 YVAG 1386
Cdd:PLN03142 460 YTTG 463
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
1897-2022 |
1.82e-38 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 141.46 E-value: 1.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1897 SGKLEALAILLQKLKSEGRRVLILSQMILMLDILEMFLNFHYLTYVRIDENASSEQRQELMRSFNRDRRIFCAILSTHSR 1976
Cdd:cd18793 10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
9C62_G 1977 TTGINLVEADTVVFYDNDLNPVMDAKAQEWCDRIGRCKDIHIYRLV 2022
Cdd:cd18793 90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
1896-2039 |
4.68e-31 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 134.54 E-value: 4.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1896 DSGKLEALAILLQKLKSEGRRVLILSQMILMLDILEMFLNFHYLTYVRIDENASSEQRQELMRSFNRD-RRIFCAILSTH 1974
Cdd:PLN03142 469 NSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTR 548
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
9C62_G 1975 SRTTGINLVEADTVVFYDNDLNPVMDAKAQEWCDRIGRCKDIHIYRLVSGNSIEEKLLKNGTKDL 2039
Cdd:PLN03142 549 AGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKL 613
|
|
| HSA |
smart00573 |
domain in helicases and associated with SANT domains; |
800-871 |
7.95e-27 |
|
domain in helicases and associated with SANT domains;
Pssm-ID: 214727 [Multi-domain] Cd Length: 73 Bit Score: 105.56 E-value: 7.95e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
9C62_G 800 PKLQEAPRPKSHWDYLLEEMQWMATDFAQERRWKVAAAKKLVRTVVRHHEEKQLREERG-KKEEQSRLRRIAA 871
Cdd:smart00573 1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERReEKNEKRRLRKLAA 73
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
1876-2033 |
8.14e-25 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 113.01 E-value: 8.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1876 LRQ-TTAPRLLqFPELRLVQFDSGKLEALAILLQKLKSEGRRVLILSQMILMLDILEMFLNFHYLTYVRIDENASSEQRQ 1954
Cdd:COG0553 511 LRQiCSHPALL-LEEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERD 589
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
9C62_G 1955 ELMRSFNRDRRIFCAILSTHSRTTGINLVEADTVVFYDNDLNPVMDAKAQEWCDRIGRCKDIHIYRLVSGNSIEEKLLK 2033
Cdd:COG0553 590 ELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILE 668
|
|
| HSA |
pfam07529 |
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ... |
802-868 |
3.13e-21 |
|
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. This region does not form a compact domain in the known structures.
Pssm-ID: 462194 [Multi-domain] Cd Length: 67 Bit Score: 89.55 E-value: 3.13e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
9C62_G 802 LQEAPR-PKSHWDYLLEEMQWMATDFAQERRWKVAAAKKLVRTVVRHHEEKQLREERgKKEEQSRLRR 868
Cdd:pfam07529 1 RDEPERrEKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHKNIEKEEQK-RIEREEKQRL 67
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1084-1272 |
9.49e-17 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 81.38 E-value: 9.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1084 PSLLYGALRDYQKIGLDWLAKLYRknlNGILADEAGLGKTVQIIAfFAHLACNEGNWGPHLVVV--RScniLK--WELEL 1159
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALL-PALEALKRGKGGRVLVLVptRE---LAeqWAEEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1160 KRWCP--GLKILSYIGSHRELKAKRQEWAEPnsFHVCITSYTQFFRGLT--AFTRVRWKCLVIDEMQRVKGMTER-HWEA 1234
Cdd:smart00487 75 KKLGPslGLKVVGLYGGDSKREQLRKLESGK--TDILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGGFGdQLEK 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
9C62_G 1235 VFTL--QSQQRLLL---IDSPLHNTFLELWTMVHFLVPGISRP 1272
Cdd:smart00487 153 LLKLlpKNVQLLLLsatPPEEIENLLELFLNDPVFIDVGFTPL 195
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1898-2013 |
6.01e-14 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 70.32 E-value: 6.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1898 GKLEALAILLQKlkSEGRRVLILSQMILMLDIlEMFLNFHYLTYVRIDENASSEQRQELMRSFNRDRRIFcaILSTHSRT 1977
Cdd:pfam00271 1 EKLEALLELLKK--ERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDV--LVATDVAE 75
|
90 100 110
....*....|....*....|....*....|....*.
9C62_G 1978 TGINLVEADTVVFYDNDLNPVMDakAQewcdRIGRC 2013
Cdd:pfam00271 76 RGLDLPDVDLVINYDLPWNPASY--IQ----RIGRA 105
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1928-2013 |
4.90e-10 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 58.38 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1928 DILEMFLNFHYLTYVRIDENASSEQRQELMRSFNRDRRIFcaILSTHSRTTGINLVEADTVVFYDNDLNPVMDakAQewc 2007
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKV--LVATDVAERGLDLPGVDLVIIYDLPWSPASY--IQ--- 73
|
....*.
9C62_G 2008 dRIGRC 2013
Cdd:smart00490 74 -RIGRA 78
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
554-816 |
1.74e-07 |
|
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: 57.35 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 554 PPTPQAAQLAGQRQSQQQYDPSTGPPVQNAASLHT---------PLPQL-----------PGRLPPAGVPTAALSSALQF 613
Cdd:pfam09770 108 AARAAQSSAQPPASSLPQYQYASQQSQQPSKPVRTgyekykepePIPDLqvdaslwgvapKKAAAPAPAPQPAAQPASLP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 614 AQQPQV-----VEAQTQLQIPVKTQQPNVPIPAPPSSqlpiPPSQPAQLALHVPTPGKVQVQASQLSSLPQMVASTRLPV 688
Cdd:pfam09770 188 APSRKMmsleeVEAAMRAQAKKPAQQPAPAPAQPPAA----PPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPV 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 689 DPAPPCPRPLPTSSTSSLAPVS-GSGPGPSPARSSPV------NRPSSAtnkalspvtsRTPGVVASAPTKPQSPAQNAT 761
Cdd:pfam09770 264 TILQRPQSPQPDPAQPSIQPQAqQFHQQPPPVPVQPTqilqnpNRLSAA----------RVGYPQNPQPGVQPAPAHQAH 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
9C62_G 762 SSQdSSQDTLTEQITLENQVHQRIAELRKAGLwsqrrlpkLQEAPRPK-SHWDYLL 816
Cdd:pfam09770 334 RQQ-GSFGRQAPIITHPQQLAQLSEEEKAAYL--------DEEAKRAKrNHKIFLL 380
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
3040-3159 |
2.96e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 49.77 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 3040 TQIQVAKLPQVVQQQTPVASIQQVASA--SQQAS-PQTVALTQATAAGQQVQMIPAVTATAQVVQQKLIQQQVVT--TAS 3114
Cdd:PRK14971 355 TLIQLAQLTQKGDDASGGRGPKQHIKPvfTQPAAaPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVSVdpPAA 434
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
9C62_G 3115 APLQTPGAPNPAQVPASSDSPSQQPKLQMRVPAVRLKTPTKPPCQ 3159
Cdd:PRK14971 435 VPVNPPSTAPQAVRPAQFKEEKKIPVSKVSSLGPSTLRPIQEKAE 479
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
574-762 |
6.10e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.17 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 574 PSTGPPVQNAASLHTPLPQLPgrlPPAGVPTAALSSalqfaqqpqvveaqtqLQIPVKTQQPNVPIPAPPSSqlPIPPSQ 653
Cdd:PHA03247 2686 RAARPTVGSLTSLADPPPPPP---TPEPAPHALVSA----------------TPLPPGPAAARQASPALPAA--PAPPAV 2744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 654 PAQLAlhvpTPGKVQVQAS-QLSSLPQMVASTRLPVDPAPPCPRPLPTSSTSSLAPVSGSGPGPSPArSSPVNRPSSATN 732
Cdd:PHA03247 2745 PAGPA----TPGGPARPARpPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADP-PAAVLAPAAALP 2819
|
170 180 190
....*....|....*....|....*....|..
9C62_G 733 KALSPVTSRTP--GVVASAPTKPQSPAQNATS 762
Cdd:PHA03247 2820 PAASPAGPLPPptSAQPTAPPPPPGPPPPSLP 2851
|
|
| SP1-4_arthropods_N |
cd22553 |
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ... |
3010-3142 |
2.12e-04 |
|
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. One SP is clade SP1-4, which is expressed ubiquitously throughout development. SP1-4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. This model represents the N-terminal domain of SP1-4 from arthropods.
Pssm-ID: 411778 [Multi-domain] Cd Length: 384 Bit Score: 46.56 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 3010 AYAAQPALKTQFLTtPISQAQKLAGAQ--QVQTQIQVAKLPQVVQQQTPVAsIQQVASASQQASPQTvaltqATAAGQQV 3087
Cdd:cd22553 188 AGGGNQALQAQVIP-QLAQAAQLQPQQlaQVSSQGYIQQIPANASQQQPQM-VQQGPNQSGQIIGQV-----ASASSIQA 260
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
9C62_G 3088 QMIPAVT-ATAQVVQQKLIQQQVVTTASAPLQTPGAPNPAQVPASSDSPSQQPKLQ 3142
Cdd:cd22553 261 AAIPLTVyTGALAGQNGSNQQQVGQIVTSPIQGMTQGLTAPASSSIPTVVQQQAIQ 316
|
|
| SP1-4_arthropods_N |
cd22553 |
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ... |
2876-3101 |
2.80e-04 |
|
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. One SP is clade SP1-4, which is expressed ubiquitously throughout development. SP1-4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. This model represents the N-terminal domain of SP1-4 from arthropods.
Pssm-ID: 411778 [Multi-domain] Cd Length: 384 Bit Score: 46.17 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 2876 GTTVANLQVARLTRVPTSQLQAQGQMQTQAPQPAQVALAKPPVVSVPAAVVSSPGVTTLPMNVAGiSVAIGQPQKAA-GQ 2954
Cdd:cd22553 92 LLQTNNQQAIQLAPGGTQAILANQQTLIRPNTVQGQANASNVLQNIAQIASGGNAVQLPLNNMTQ-TIPVQVPVSTAnGQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 2955 TV---VAQPVHMQQLLKLKQQAVQQQKAIQPQAAQ-GPAAVQQKITA------QQITTPGAQQK-------------VAY 3011
Cdd:cd22553 171 TVyqtIQVPIQAIQSGNAGGGNQALQAQVIPQLAQaAQLQPQQLAQVssqgyiQQIPANASQQQpqmvqqgpnqsgqIIG 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 3012 AAQPALKTQFLTTPISQAQKLAGAQQVQTQIQVAKLP----QVVQQQTPVASIQQVASASQQASPQTVAL---TQATAAG 3084
Cdd:cd22553 251 QVASASSIQAAAIPLTVYTGALAGQNGSNQQQVGQIVtspiQGMTQGLTAPASSSIPTVVQQQAIQGNPLppgTQIIAAG 330
|
250
....*....|....*..
9C62_G 3085 QQVQMIPAVTATAQVVQ 3101
Cdd:cd22553 331 QQLQQDPNDPTKWQVVA 347
|
|
| PABP-1234 |
TIGR01628 |
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ... |
504-619 |
2.47e-03 |
|
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: 43.64 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 504 RQQAMPSTGMAEQSKRPRLEVGHQG---VVFQHPGAD-AGVPL----QQLMPTAQG------GMPPTPQAAQLAGQRQSQ 569
Cdd:TIGR01628 372 QDQFMQLQPRMRQLPMGSPMGGAMGqppYYGQGPQQQfNGQPLgwprMSMMPTPMGpggplrPNGLAPMNAVRAPSRNAQ 451
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
9C62_G 570 QQYDPSTGPPVQ-----NAASLHTPLPQlPGRLPPAGVPTAALSSALQFA---QQPQV 619
Cdd:TIGR01628 452 NAAQKPPMQPVMyppnyQSLPLSQDLPQ-PQSTASQGGQNKKLAQVLASAtpqMQKQV 508
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
2894-3146 |
3.95e-03 |
|
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: 43.07 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 2894 QLQAQGQMQTQAPQPAQVALAKPPVVSVPAAVVSSPGVTTLPMNVAGISVAIGQPQKAAGQTVvaqPVHMQQllklKQQA 2973
Cdd:pfam09606 222 QAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPM---GPPGQQ----PGAM 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 2974 VQQQKAIQPQAAQGPAAVQQKITAQQITTPGAQQKVAYAAQPAlktqflttpiSQAQKLAGAQQVQTQIQVAKLPQVVQQ 3053
Cdd:pfam09606 295 PNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQG----------GQVVALGGLNHLETWNPGNFGGLGANP 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 3054 QtpvasiqqvasasQQASPQTVALTQATAAGQQVQMipavtATAQVVQQKliQQQVVTTASAPLQTPGA-------PNPA 3126
Cdd:pfam09606 365 M-------------QRGQPGMMSSPSPVPGQQVRQV-----TPNQFMRQS--PQPSVPSPQGPGSQPPQshpggmiPSPA 424
|
250 260
....*....|....*....|
9C62_G 3127 QVPASSDSPSQQPKLQMRVP 3146
Cdd:pfam09606 425 LIPSPSPQMSQQPAQQRTIG 444
|
|
| |
|
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 ... |
1-505 |
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: 646.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1 MHHGTGPQNVQHQLQRSRACPGSEG---EEQPAHPNPPPSPAAPFAPSASPSAPQSPSYQIqqLMNRSPATGQNVNITLQ 77
Cdd:pfam15790 1 MHHGSGSQNVQRQLQRSKSVSGSEEqqqEQQPATVNHPQSPVTTFAPAASPSAPQSPNYQI--IMSRSPVTGQNVNITLQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 78 SVGPVVGGNQQITLAPLPLPSPTSPGFQFSAQPRRFEHGSPSYIQVTSPLSQQVQTQSPTQPSPGPGQALQnvRAGAPGP 157
Cdd:pfam15790 79 NVGQMVAGNQQITLTPLPLQSPASPGFQHSAPQWRFEHGSPSYIQVTSPLPQQVQPQSPTQHSPVPLQGVQ--RPGAPGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 158 GLGLCSSSPTGgFVDASVLVRQISL-SPSSGGHFVFQDGSGLTQIAQG-AQVQLQHPGTPITVRERRPSQPHTQSGGTIH 235
Cdd:pfam15790 157 GLGVCGQSPTR-FVDASMLVRQISLgSPSGGGHFVYQDGTGLAQIAPGaGQVQLASPGTPGSVRERRLSQPHSQTGGTIH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 236 HLGPQSPAAAGgAGLQPLASPSHITTANLPPQISSIIQGQlvqqqqvlqgppLPRPLGFERTPGVLLPGAGGAAGF-GMT 314
Cdd:pfam15790 236 HLGPQSPAAAG-AGLQTLGSPGHITTSNLPPQISSIIQGQ------------LARPLGFEKTAQVVVAGAGGPAASfGIP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 315 SPPPPTSPSRTAVPPGLSSLPLTSVGNTG-MKKVPKKLEEIPPASPEMAQMRKQCLDYHYQEMQALKEVFKEYLIELFFL 393
Cdd:pfam15790 303 SSIPPTSPSRTSPPPGLSSNPLTSTGMSGsVKKVPKKLEEIAPATPEIAQLRKQCLDHHTKKMESLKEVFKEYLIELFFL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 394 QHFQGNMMDFLAFKKKHYAPLQAYLRQNDLDIeeeeEEEEEEEEKSEVINDEVKVVTGKDGQTGTPVAIATQLPPKVSAA 473
Cdd:pfam15790 383 QHLQGNMMDFLAFKKKHCVPLYTYLRQNDLDL----EEEEEEEEQSEVINDEVKVVTGKDGQTGTPVAIATQLPPNVSAA 458
|
490 500 510
....*....|....*....|....*....|..
9C62_G 474 fSSQQQPFQQALAGSLVAGAGSTVETDLFKRQ 505
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 ... |
1091-1307 |
1.98e-134 |
|
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: 1.98e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1170
Cdd:cd18003 1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1171 YIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSP 1250
Cdd:cd18003 81 YYGSAKERKLKRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
9C62_G 1251 LHNTFLELWTMVHFLVPGI------SRPYLSSPLRAPSEESQDYYHKVVIRLHRVTQPFILRR 1307
Cdd:cd18003 161 LQNSLMELWSLMHFLMPHIfqshqeFKEWFSNPLTAMSEGSQEENEELVRRLHKVLRPFLLRR 223
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
885-1374 |
2.00e-59 |
|
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: 2.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 885 EQVVEIKLRVELEEKRKKALNLQKVSRRGKELRPKGFDALQESSLDSGMSGRKRKASISLTDDEVDDEEETIEEEEANEG 964
Cdd:COG0553 35 LARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLRLLLALLLLALLLLLAGLLALALLLLALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 965 VVDHQTELSNLAKEAELPLLDLMKLYEGAFLPSSQWPRPKPDGEDTSGEEDADDCPGDRESRKDLVLIDSLFIMDQFKAA 1044
Cdd:COG0553 115 GLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELAL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1045 ERMNIGK-PNAKDIADVTAVAEAILPKGSARVTTSVKFNAPSLLYGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKT 1123
Cdd:COG0553 195 LAAEAELlLLLELLLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1124 VQIIAFFAHLAcNEGNWGPHLVVV-RSCnILKWELELKRWCPGLKILSYIGShrelkAKRQEWAEP-NSFHVCITSYTQF 1201
Cdd:COG0553 275 IQALALLLELK-ERGLARPVLIVApTSL-VGNWQRELAKFAPGLRVLVLDGT-----RERAKGANPfEDADLVITSYGLL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1202 FRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPGisrpYLSSPlrap 1281
Cdd:COG0553 348 RRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPG----LLGSL---- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1282 sEESQDYYHKVVI--------RLHRVTQPFILRRTKRDVEKQLTKKYEHVLKCRLSNRQKALYEDVI--LQPGTQEALKS 1351
Cdd:COG0553 420 -KAFRERFARPIEkgdeealeRLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLeyLRRELEGAEGI 498
|
490 500
....*....|....*....|...
9C62_G 1352 GHFVNVLSILVRLQRICNHPGLV 1374
Cdd:COG0553 499 RRRGLILAALTRLRQICSHPALL 521
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
1094-1374 |
2.02e-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: 2.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1094 YQKIGLDWLAKLYRK-NLNGILADEAGLGKTVQIIAFFAHLACNEGNWG-PHLVVVRSCNILKWELELKRWC--PGLKIL 1169
Cdd:pfam00176 1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1170 SYIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDS 1249
Cdd:pfam00176 81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1250 PLHNTFLELWTMVHFLVPGI--SRPYLSSPLRAPSEESQDYyhKVVIRLHRVTQPFILRRTKRDVEKQLTKKYEHVLKCR 1327
Cdd:pfam00176 161 PLQNNLEELWALLNFLRPGPfgSLSTFRNWFDRPIERGGGK--KGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCR 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
9C62_G 1328 LSNRQKALYEDVILQPGTQEALKS--GHFVN--VLSILVRLQRICNHPGLV 1374
Cdd:pfam00176 239 LSKLQRKLYQTFLLKKDLNAIKTGegGREIKasLLNILMRLRKICNHPGLI 289
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
1065-1386 |
2.70e-59 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 225.06 E-value: 2.70e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1065 EAILPKGSARVTTSvkfnaPSLLYGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHL 1144
Cdd:PLN03142 149 DGLGGSGGTRLLVQ-----PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHM 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1145 VVVRSCNILKWELELKRWCPGLKILSYIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRV 1224
Cdd:PLN03142 224 VVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1225 KGMTERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPGI--SRPYLSSPLRAPSEESQdyyHKVVIRLHRVTQP 1302
Cdd:PLN03142 304 KNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIfsSAETFDEWFQISGENDQ---QEVVQQLHKVLRP 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1303 FILRRTKRDVEKQLTKKYEHVLKCRLSNRQKALYEdVILQPGTQEALKSGHFVNVLSILVRLQRICNHPGLVEPRHPGSS 1382
Cdd:PLN03142 381 FLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYK-ALLQKDLDVVNAGGERKRLLNIAMQLRKCCNHPYLFQGAEPGPP 459
|
....
9C62_G 1383 YVAG 1386
Cdd:PLN03142 460 YTTG 463
|
|
| DEXHc_SMARCA1_SMARCA5 |
cd17997 |
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ... |
1089-1309 |
6.19e-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: 6.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1089 GALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKI 1168
Cdd:cd17997 2 GTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1169 LSYIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLID 1248
Cdd:cd17997 82 VVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
9C62_G 1249 SPLHNTFLELWTMVHFLVPGIsrpYLSSPLRAP---SEESQDYYHKVVIRLHRVTQPFILRRTK 1309
Cdd:cd17997 162 TPLQNNLHELWALLNFLLPDV---FTSSEDFDEwfnVNNCDDDNQEVVQRLHKVLRPFLLRRIK 222
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
1091-1267 |
5.77e-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: 184.69 E-value: 5.77e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1170
Cdd:cd17919 1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1171 YIGShRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSP 1250
Cdd:cd17919 81 YHGS-QRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTP 159
|
170
....*....|....*..
9C62_G 1251 LHNTFLELWTMVHFLVP 1267
Cdd:cd17919 160 LQNNLEELWALLDFLDP 176
|
|
| DEXQc_INO80 |
cd18002 |
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ... |
1091-1307 |
4.01e-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: 184.25 E-value: 4.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1170
Cdd:cd18002 1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1171 YIGSHRELKAKRQEWAEPN------SFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRL 1244
Cdd:cd18002 81 YWGNPKDRKVLRKFWDRKNlytrdaPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
9C62_G 1245 LLIDSPLHNTFLELWTMVHFLVPGI------SRPYLSSPLRAPSEESQDYYHKVVIRLHRVTQPFILRR 1307
Cdd:cd18002 161 LLTGTPIQNSMAELWALLHFIMPTLfdshdeFNEWFSKDIESHAENKTGLNEHQLKRLHMILKPFMLRR 229
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
1089-1309 |
3.34e-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: 3.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1089 GALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLAcNEGNWGPHLVVVRSCNILKWELELKRWCPGLKI 1168
Cdd:cd18012 3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRK-EEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1169 LSYIGShrelKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLID 1248
Cdd:cd18012 82 LVIHGT----KRKREKLRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
9C62_G 1249 SPLHNTFLELWTMVHFLVPGisrpYLSSP------LRAPSEESQDyyHKVVIRLHRVTQPFILRRTK 1309
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 ... |
1089-1309 |
3.25e-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: 3.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1089 GALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKI 1168
Cdd:cd17996 2 GTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1169 LSYIGShRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKgmtERHWEAVFTL----QSQQRL 1244
Cdd:cd17996 82 IVYKGT-PDVRKKLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMK---NAQSKLTQTLntyyHARYRL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
9C62_G 1245 LLIDSPLHNTFLELWTMVHFLVPGI--SRP----YLSSPLRAPSEESQDYYHK-----VVIRLHRVTQPFILRRTK 1309
Cdd:cd17996 158 LLTGTPLQNNLPELWALLNFLLPKIfkSCKtfeqWFNTPFANTGEQVKIELNEeetllIIRRLHKVLRPFLLRRLK 233
|
|
| DEXHc_HELLS_SMARCA6 |
cd18009 |
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ... |
1089-1309 |
1.76e-47 |
|
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: 1.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1089 GALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNeGNWGPHLVVVRSCNILKWELELKRWCPGLKI 1168
Cdd:cd18009 2 GVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRER-GVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1169 LSYIGSHRE-LKAKRQEWAEPNS---FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRL 1244
Cdd:cd18009 81 LLYHGTKEErERLRKKIMKREGTlqdFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
9C62_G 1245 LLIDSPLHNTFLELWTMVHFLVPGISRPY-----------LSSPLRAPSEESQDYYHKVVIRLHRVTQPFILRRTK 1309
Cdd:cd18009 161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLssfeswfdfssLSDNAADISNLSEEREQNIVHMLHAILKPFLLRRLK 236
|
|
| DEXHc_SMARCA5 |
cd18064 |
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ... |
1082-1319 |
2.27e-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: 171.00 E-value: 2.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1082 NAPSLL-YGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELK 1160
Cdd:cd18064 6 DSPSYVkWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1161 RWCPGLKILSYIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQS 1240
Cdd:cd18064 86 RWVPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1241 QQRLLLIDSPLHNTFLELWTMVHFLVPGISRpylssplrapSEESQDYY---------HKVVIRLHRVTQPFILRRTKRD 1311
Cdd:cd18064 166 TNRLLLTGTPLQNNLHELWALLNFLLPDVFN----------SAEDFDSWfdtnnclgdQKLVERLHMVLRPFLLRRIKAD 235
|
....*...
9C62_G 1312 VEKQLTKK 1319
Cdd:cd18064 236 VEKSLPPK 243
|
|
| DEXHc_SMARCAD1 |
cd17998 |
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ... |
1091-1267 |
8.95e-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: 8.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLAcNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1170
Cdd:cd17998 1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLK-EIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1171 YIGSHRELKAKRQEwAEPN--SFHVCITSYT---------QFFRgltaftRVRWKCLVIDEMQRVKGMTERHWEAVFTLQ 1239
Cdd:cd17998 80 YYGSQEERKHLRYD-ILKGleDFDVIVTTYNlatsnpddrSFFK------RLKLNYVVYDEGHMLKNMTSERYRHLMTIN 152
|
170 180
....*....|....*....|....*...
9C62_G 1240 SQQRLLLIDSPLHNTFLELWTMVHFLVP 1267
Cdd:cd17998 153 ANFRLLLTGTPLQNNLLELMSLLNFIMP 180
|
|
| DEXHc_CHD1_2 |
cd17993 |
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ... |
1091-1307 |
1.11e-44 |
|
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: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1170
Cdd:cd17993 2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1171 YIGSHRELKAKRQ-EWAEPNS----FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLL 1245
Cdd:cd17993 82 YLGDIKSRDTIREyEFYFSQTkklkFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
9C62_G 1246 LIDSPLHNTFLELWTMVHFLVPGisRPYLSSPLR-APSEESQDYYHkvviRLHRVTQPFILRR 1307
Cdd:cd17993 162 ITGTPLQNSLKELWALLHFLMPG--KFDIWEEFEeEHDEEQEKGIA----DLHKELEPFILRR 218
|
|
| DEXHc_SMARCA1 |
cd18065 |
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ... |
1083-1309 |
1.38e-43 |
|
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: 159.80 E-value: 1.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1083 APSLLYGA-LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKR 1161
Cdd:cd18065 7 SPSYVKGGtLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1162 WCPGLKILSYIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQ 1241
Cdd:cd18065 87 WVPSLRAVCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTT 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
9C62_G 1242 QRLLLIDSPLHNTFLELWTMVHFLVPGISRpylssplrapSEESQDYY---------HKVVIRLHRVTQPFILRRTK 1309
Cdd:cd18065 167 NRLLLTGTPLQNNLHELWALLNFLLPDVFN----------SADDFDSWfdtknclgdQKLVERLHAVLKPFLLRRIK 233
|
|
| DEXHc_CHD6_7_8_9 |
cd17995 |
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ... |
1091-1307 |
1.77e-39 |
|
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; Chromodomain-helicase-DNA-binding protein 6-9 (CHD6, CHD7, CHD8, and CHD9) are members of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350753 [Multi-domain] Cd Length: 223 Bit Score: 147.78 E-value: 1.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPgLKILS 1170
Cdd:cd17995 1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1171 YIGSH--RELKAKRQ-----EWAEPNS----FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQ 1239
Cdd:cd17995 80 YHGSGesRQIIQQYEmyfkdAQGRKKKgvykFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9C62_G 1240 SQQRLLLIDSPLHNTFLELWTMVHFLVPGisrpylssplRAPSEES--QDY----YHKVVIRLHRVTQPFILRR 1307
Cdd:cd17995 160 LEHKLLLTGTPLQNNTEELWSLLNFLEPE----------KFPSSEEflEEFgdlkTAEQVEKLQALLKPYMLRR 223
|
|
| DEXHc_CHD2 |
cd18054 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ... |
1084-1307 |
1.59e-38 |
|
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: 1.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1084 PSLLYGA---LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELK 1160
Cdd:cd18054 11 PSYIGGEnleLRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1161 RWCPGLKILSYIGSHRELKAKRQ-EWAEPNS----FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAV 1235
Cdd:cd18054 91 IWAPEINVVVYIGDLMSRNTIREyEWIHSQTkrlkFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
9C62_G 1236 FTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPGISRPYlssplrapsEESQDYYHKV----VIRLHRVTQPFILRR 1307
Cdd:cd18054 171 IDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFW---------EDFEEDHGKGrengYQSLHKVLEPFLLRR 237
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
1897-2022 |
1.82e-38 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 141.46 E-value: 1.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1897 SGKLEALAILLQKLKSEGRRVLILSQMILMLDILEMFLNFHYLTYVRIDENASSEQRQELMRSFNRDRRIFCAILSTHSR 1976
Cdd:cd18793 10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
9C62_G 1977 TTGINLVEADTVVFYDNDLNPVMDAKAQEWCDRIGRCKDIHIYRLV 2022
Cdd:cd18793 90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
|
|
| DEXHc_SMARCA4 |
cd18062 |
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ... |
1075-1309 |
2.49e-35 |
|
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: 136.71 E-value: 2.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1075 VTTSVKFNAPSLLYGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILK 1154
Cdd:cd18062 8 VTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1155 WELELKRWCPGLKILSYIGShrelKAKRQEWA---EPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKgmtERH 1231
Cdd:cd18062 88 WVYEFDKWAPSVVKVSYKGS----PAARRAFVpqlRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMK---NHH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1232 WEAVFTLQSQ----QRLLLIDSPLHNTFLELWTMVHFLVPGISRP------YLSSPLRAPSEE---SQDYYHKVVIRLHR 1298
Cdd:cd18062 161 CKLTQVLNTHyvapRRLLLTGTPLQNKLPELWALLNFLLPTIFKScstfeqWFNAPFAMTGEKvdlNEEETILIIRRLHK 240
|
250
....*....|.
9C62_G 1299 VTQPFILRRTK 1309
Cdd:cd18062 241 VLRPFLLRRLK 251
|
|
| DEXHc_CHD1L |
cd18006 |
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ... |
1091-1307 |
3.76e-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: 134.87 E-value: 3.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1170
Cdd:cd18006 1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1171 YIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSP 1250
Cdd:cd18006 81 YMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
9C62_G 1251 LHNTFLELWTMVHFLvpgisrpylsSPLRAPSEESQDYYHK---------VVIRLHRVTQPFILRR 1307
Cdd:cd18006 161 IQNSLQELYALLSFI----------EPNVFPKDKLDDFIKAysetddeseTVEELHLLLQPFLLRR 216
|
|
| DEXHc_SMARCA2 |
cd18063 |
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ... |
1075-1309 |
4.12e-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: 135.96 E-value: 4.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1075 VTTSVKFNAPSLLYGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILK 1154
Cdd:cd18063 8 ITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1155 WELELKRWCPGLKILSYIGShRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKgmtERHWEA 1234
Cdd:cd18063 88 WTYEFDKWAPSVVKISYKGT-PAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMK---NHHCKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1235 VFTLQSQ----QRLLLIDSPLHNTFLELWTMVHFLVPGISRP------YLSSPLRAPSEE---SQDYYHKVVIRLHRVTQ 1301
Cdd:cd18063 164 TQVLNTHyvapRRILLTGTPLQNKLPELWALLNFLLPTIFKScstfeqWFNAPFAMTGERvdlNEEETILIIRRLHKVLR 243
|
....*...
9C62_G 1302 PFILRRTK 1309
Cdd:cd18063 244 PFLLRRLK 251
|
|
| DEXHc_Mot1 |
cd17999 |
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ... |
1091-1307 |
6.34e-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: 126.31 E-value: 6.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQ---IIAFFAHLACNEGNWG--PHLVVVRSCNILKWELELKRWCP- 1164
Cdd:cd17999 1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQtlcILASDHHKRANSFNSEnlPSLVVCPPTLVGHWVAEIKKYFPn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1165 -GLKILSYIGSHRElkaKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQR 1243
Cdd:cd17999 81 aFLKPLAYVGPPQE---RRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
9C62_G 1244 LLLIDSPLHNTFLELWTMVHFLVPG-----------ISRPYLSSPLRAPSEESQDYYHKVVIRLHRVTQPFILRR 1307
Cdd:cd17999 158 LILSGTPIQNNVLELWSLFDFLMPGylgtekqfqrrFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
|
|
| DEXHc_CHD1 |
cd18053 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ... |
1091-1307 |
2.38e-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: 124.78 E-value: 2.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1170
Cdd:cd18053 21 LRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1171 YIGSHRELKAKR-QEWAEPNS----FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLL 1245
Cdd:cd18053 101 YLGDINSRNMIRtHEWMHPQTkrlkFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
9C62_G 1246 LIDSPLHNTFLELWTMVHFLVPGISRPYlsSPLRAPSEESQDYYHKvviRLHRVTQPFILRR 1307
Cdd:cd18053 181 ITGTPLQNSLKELWSLLHFIMPEKFSSW--EDFEEEHGKGREYGYA---SLHKELEPFLLRR 237
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
1896-2039 |
4.68e-31 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 134.54 E-value: 4.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1896 DSGKLEALAILLQKLKSEGRRVLILSQMILMLDILEMFLNFHYLTYVRIDENASSEQRQELMRSFNRD-RRIFCAILSTH 1974
Cdd:PLN03142 469 NSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTR 548
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
9C62_G 1975 SRTTGINLVEADTVVFYDNDLNPVMDAKAQEWCDRIGRCKDIHIYRLVSGNSIEEKLLKNGTKDL 2039
Cdd:PLN03142 549 AGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKL 613
|
|
| DEXHc_ERCC6 |
cd18000 |
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ... |
1091-1274 |
1.36e-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: 118.20 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKIL- 1169
Cdd:cd18000 1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1170 -----------SYIGSHRELKAKRQEWAEPNsfHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTL 1238
Cdd:cd18000 81 lhssgsgtgseEKLGSIERKSQLIRKVVGDG--GILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQL 158
|
170 180 190
....*....|....*....|....*....|....*.
9C62_G 1239 QSQQRLLLIDSPLHNTFLELWTMVHFLVPgisrPYL 1274
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; ... |
1091-1307 |
3.23e-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: 3.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLAcNEGNW-GPHLVVVRSCNILKWELELKRWCPGLKIL 1169
Cdd:cd17994 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLY-KEGHSkGPFLVSAPLSTIINWEREFEMWAPDFYVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1170 SYIGShrelkakrqewaepnsfHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDS 1249
Cdd:cd17994 80 TYVGD-----------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGT 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
9C62_G 1250 PLHNTFLELWTMVHFLVPGisrpyLSSPLRAPSEESQDYYHKVVI-RLHRVTQPFILRR 1307
Cdd:cd17994 143 PLQNNLEELFHLLNFLTPE-----RFNNLQGFLEEFADISKEDQIkKLHDLLGPHMLRR 196
|
|
| DEXHc_ERCC6L |
cd18001 |
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ... |
1091-1307 |
6.22e-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: 6.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLAcNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1170
Cdd:cd18001 1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMF-DSGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1171 YIGSHRELKAKRQEWAEpNSFHVCITSYTQFFRG---LTAFTR--VRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLL 1245
Cdd:cd18001 80 FHGTSKKERERNLERIQ-RGGGVLLTTYGMVLSNteqLSADDHdeFKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRII 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9C62_G 1246 LIDSPLHNTFLELWTMVHFLVPG--------ISRPYLSSPLRAPSEES----QDYYHKVVIRLHRVTQPFILRR 1307
Cdd:cd18001 159 LTGTPIQNNLKELWALFDFACNGsllgtrktFKMEFENPITRGRDKDAtqgeKALGSEVAENLRQIIKPYFLRR 232
|
|
| HSA |
smart00573 |
domain in helicases and associated with SANT domains; |
800-871 |
7.95e-27 |
|
domain in helicases and associated with SANT domains;
Pssm-ID: 214727 [Multi-domain] Cd Length: 73 Bit Score: 105.56 E-value: 7.95e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
9C62_G 800 PKLQEAPRPKSHWDYLLEEMQWMATDFAQERRWKVAAAKKLVRTVVRHHEEKQLREERG-KKEEQSRLRRIAA 871
Cdd:smart00573 1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERReEKNEKRRLRKLAA 73
|
|
| DEXHc_ERCC6L2 |
cd18005 |
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ... |
1091-1307 |
1.25e-26 |
|
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: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHL---------ACN-----------EGNWGPHLVVVRSC 1150
Cdd:cd18005 1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVlgktgtrrdRENnrprfkkkppaSSAKKPVLIVAPLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1151 NILKWELELKRWcpG-LKILSYIGSHRE------LKAKRQEwaepnsfhVCITSYTQFFRGLTAFTRVRWKCLVIDEMQR 1223
Cdd:cd18005 81 VLYNWKDELDTW--GhFEVGVYHGSRKDdelegrLKAGRLE--------VVVTTYDTLRRCIDSLNSINWSAVIADEAHR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1224 VKGMTERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPG-----------ISRPYLSSPLRAPSEESQDYYHKV 1292
Cdd:cd18005 151 IKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGalgsrsqfkkhFSEPIKRGQRHTATARELRLGRKR 230
|
250
....*....|....*
9C62_G 1293 VIRLHRVTQPFILRR 1307
Cdd:cd18005 231 KQELAVKLSKFFLRR 245
|
|
| DEXHc_CHD7 |
cd18059 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ... |
1091-1307 |
2.87e-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: 109.74 E-value: 2.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACnEGNWGPHLVVVRSCNILKWELELKRWCPgLKILS 1170
Cdd:cd18059 1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYL-KGIHGPFLVIAPLSTIPNWEREFRTWTE-LNVVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1171 YIGSH---RELKAKRQEWAEPN--------SFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQ 1239
Cdd:cd18059 79 YHGSQasrRTIQLYEMYFKDPQgrvikgsyKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9C62_G 1240 SQQRLLLIDSPLHNTFLELWTMVHFLVPGisrpylssplRAPSEES--QDY----YHKVVIRLHRVTQPFILRR 1307
Cdd:cd18059 159 LEHKVLLTGTPLQNTVEELFSLLHFLEPS----------RFPSETTfmQEFgdlkTEEQVQKLQAILKPMMLRR 222
|
|
| DEXHc_RAD54 |
cd18004 |
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ... |
1091-1307 |
5.49e-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: 109.30 E-value: 5.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAK--LYRKNLNG---ILADEAGLGKTVQIIAFFAHLACNEGNWGPHL---VVVRSCNILK-WELELKR 1161
Cdd:cd18004 1 LRPHQREGVQFLYDclTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKPTAkkaLIVCPSSLVGnWKAEFDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1162 WCPG--LKILSYIGSHRELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTR-VRWKCLVIDEMQRVKGMTERHWEAVFTL 1238
Cdd:cd18004 81 WLGLrrIKVVTADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKkISIDLLICDEGHRLKNSESKTTKALNSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1239 QSQQRLLLIDSPLHNTFLELWTMVHFLVPGI-----------SRPYLSSPLRAPSEESQDYYHKVVIRLHRVTQPFILRR 1307
Cdd:cd18004 161 PCRRRLLLTGTPIQNDLDEFFALVDFVNPGIlgslasfrkvfEEPILRSRDPDASEEDKELGAERSQELSELTSRFILRR 240
|
|
| DEXHc_CHD3 |
cd18055 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ... |
1091-1307 |
9.72e-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: 9.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1170
Cdd:cd18055 1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1171 YIGS----------------------HRELKAKRQewaEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMT 1228
Cdd:cd18055 81 YTGDkdsraiirenefsfddnavkggKKAFKMKRE---AQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1229 ERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPGisrpyLSSPLRAPSEESQDYYHKVVI-RLHRVTQPFILRR 1307
Cdd:cd18055 158 SKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPE-----RFNNLEGFLEEFADISKEDQIkKLHDLLGPHMLRR 232
|
|
| DEXHc_CHD4 |
cd18056 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ... |
1091-1307 |
1.13e-25 |
|
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: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1170
Cdd:cd18056 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1171 YIGSH------RE-------------LKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERH 1231
Cdd:cd18056 81 YVGDKdsraiiREnefsfednairggKKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
9C62_G 1232 WEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPgiSRPYlssPLRAPSEESQDYYHKVVI-RLHRVTQPFILRR 1307
Cdd:cd18056 161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTP--ERFH---NLEGFLEEFADIAKEDQIkKLHDMLGPHMLRR 232
|
|
| DEXHc_CHD6 |
cd18058 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ... |
1091-1307 |
2.04e-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: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACnEGNWGPHLVVVRSCNILKWELELKRWCPgLKILS 1170
Cdd:cd18058 1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFL-MGIRGPFLIIAPLSTITNWEREFRTWTE-MNAIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1171 YIGSH--RELKAK-----RQEWAEPNS----FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQ 1239
Cdd:cd18058 79 YHGSQisRQMIQQyemyyRDEQGNPLSgifkFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
9C62_G 1240 SQQRLLLIDSPLHNTFLELWTMVHFLVPgISRPYLSSPLrapsEESQDY-YHKVVIRLHRVTQPFILRR 1307
Cdd:cd18058 159 LEHKVLLTGTPLQNSVEELFSLLNFLEP-SQFPSETTFL----EEFGDLkTEEQVKKLQSILKPMMLRR 222
|
|
| DEXHc_CHD5 |
cd18057 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ... |
1091-1307 |
4.17e-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: 4.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCPGLKILS 1170
Cdd:cd18057 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1171 YIGSHRELKAKRQ-EWA-EPNS-----------------FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERH 1231
Cdd:cd18057 81 YTGDKESRSVIREnEFSfEDNAirsgkkvfrmkkeaqikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
9C62_G 1232 WEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVpgisrPYLSSPLRAPSEESQDYYHKVVI-RLHRVTQPFILRR 1307
Cdd:cd18057 161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLT-----PERFNNLEGFLEEFADISKEDQIkKLHDLLGPHMLRR 232
|
|
| DEXHc_CHD9 |
cd18061 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ... |
1091-1307 |
4.67e-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: 106.24 E-value: 4.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNeGNWGPHLVVVRSCNILKWELELKRWCpGLKILS 1170
Cdd:cd18061 1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLT-GIRGPFLIIAPLSTIANWEREFRTWT-DLNVVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1171 YIGS--HRELKAKRQEWAEPNS---------FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQ 1239
Cdd:cd18061 79 YHGSliSRQMIQQYEMYFRDSQgriirgayrFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
9C62_G 1240 SQQRLLLIDSPLHNTFLELWTMVHFLvpgisrpylsSPLRAPSEES--QDY----YHKVVIRLHRVTQPFILRR 1307
Cdd:cd18061 159 LEHKVLLTGTPLQNTVEELFSLLHFL----------EPLRFPSESTfmQEFgdlkTEEQVQKLQAILKPMMLRR 222
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
1876-2033 |
8.14e-25 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 113.01 E-value: 8.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1876 LRQ-TTAPRLLqFPELRLVQFDSGKLEALAILLQKLKSEGRRVLILSQMILMLDILEMFLNFHYLTYVRIDENASSEQRQ 1954
Cdd:COG0553 511 LRQiCSHPALL-LEEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERD 589
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
9C62_G 1955 ELMRSFNRDRRIFCAILSTHSRTTGINLVEADTVVFYDNDLNPVMDAKAQEWCDRIGRCKDIHIYRLVSGNSIEEKLLK 2033
Cdd:COG0553 590 ELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILE 668
|
|
| DEXDc_SHPRH-like |
cd18008 |
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ... |
1091-1307 |
1.23e-24 |
|
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: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLakLYRknlNGILADEAGLGKTVQIIA---------------FFAHLACNEGNWGPH--LVVVRScNIL 1153
Cdd:cd18008 1 LLPYQKQGLAWM--LPR---GGILADEMGLGKTIQALAlilatrpqdpkipeeLEENSSDPKKLYLSKttLIVVPL-SLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1154 K-WELELKR--WCPGLKILSYIGSHRELKAKrqewaEPNSFHVCITSYT----------QFFRGLTAFT------RVRWK 1214
Cdd:cd18008 75 SqWKDEIEKhtKPGSLKVYVYHGSKRIKSIE-----ELSDYDIVITTYGtlasefpknkKGGGRDSKEKeasplhRIRWY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1215 CLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFL------VPGISRPYLSSPLRAPSEESQDy 1288
Cdd:cd18008 150 RVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLrvepfgDYPWFNSDISKPFSKNDRKALE- 228
|
250
....*....|....*....
9C62_G 1289 yhkvviRLHRVTQPFILRR 1307
Cdd:cd18008 229 ------RLQALLKPILLRR 241
|
|
| DEXHc_CHD8 |
cd18060 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ... |
1091-1307 |
3.29e-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: 3.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLAcNEGNWGPHLVVVRSCNILKWELELKRWCPgLKILS 1170
Cdd:cd18060 1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVY-NVGIHGPFLVIAPLSTITNWEREFNTWTE-MNTIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1171 YIGS--HRELKAKRQEWAEPNS---------FHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQ 1239
Cdd:cd18060 79 YHGSlaSRQMIQQYEMYCKDSRgrlipgaykFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
9C62_G 1240 SQQRLLLIDSPLHNTFLELWTMVHFLVPGisrpYLSSPLRAPSEESQDYYHKVVIRLHRVTQPFILRR 1307
Cdd:cd18060 159 LEHKVLLTGTPLQNTVEELFSLLHFLEPS----QFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 222
|
|
| HSA |
pfam07529 |
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ... |
802-868 |
3.13e-21 |
|
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. This region does not form a compact domain in the known structures.
Pssm-ID: 462194 [Multi-domain] Cd Length: 67 Bit Score: 89.55 E-value: 3.13e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
9C62_G 802 LQEAPR-PKSHWDYLLEEMQWMATDFAQERRWKVAAAKKLVRTVVRHHEEKQLREERgKKEEQSRLRR 868
Cdd:pfam07529 1 RDEPERrEKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHKNIEKEEQK-RIEREEKQRL 67
|
|
| DEXHc_RAD54B |
cd18066 |
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ... |
1091-1307 |
3.50e-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: 83.74 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWL-----AKLYRKNLNGILADEAGLGKTVQIIAFFAHLACnEGNWGPH------LVVVRSCNILKWELEL 1159
Cdd:cd18066 1 LRPHQREGIEFLyecvmGMRVNERFGAILADEMGLGKTLQCISLIWTLLR-QGPYGGKpvikraLIVTPGSLVKNWKKEF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1160 KRWcpglkilsyIGSHR------ELKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWE 1233
Cdd:cd18066 80 QKW---------LGSERikvftvDQDHKVEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1234 AVFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPGI-----------SRPYLSSPLRAPSEESQDYYHKVVIRLHRVTQP 1302
Cdd:cd18066 151 ALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGIlgslstyrkvyEEPIVRSREPTATPEEKKLGEARAAELTRLTGL 230
|
....*
9C62_G 1303 FILRR 1307
Cdd:cd18066 231 FILRR 235
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1084-1272 |
9.49e-17 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 81.38 E-value: 9.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1084 PSLLYGALRDYQKIGLDWLAKLYRknlNGILADEAGLGKTVQIIAfFAHLACNEGNWGPHLVVV--RScniLK--WELEL 1159
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALL-PALEALKRGKGGRVLVLVptRE---LAeqWAEEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1160 KRWCP--GLKILSYIGSHRELKAKRQEWAEPnsFHVCITSYTQFFRGLT--AFTRVRWKCLVIDEMQRVKGMTER-HWEA 1234
Cdd:smart00487 75 KKLGPslGLKVVGLYGGDSKREQLRKLESGK--TDILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGGFGdQLEK 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
9C62_G 1235 VFTL--QSQQRLLL---IDSPLHNTFLELWTMVHFLVPGISRP 1272
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 ... |
1113-1279 |
4.40e-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: 4.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1113 ILADEAGLGKTVQIIAFF-AHLACNEGNWGPHLVVVRSCnILKWELELKRWCPGLKILSYIGSH--RELKAKR-----QE 1184
Cdd:cd18007 30 ILAHTMGLGKTLQVITFLhTYLAAAPRRSRPLVLCPAST-LYNWEDEFKKWLPPDLRPLLVLVSlsASKRADArlrkiNK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1185 WAEPNSfhVCITSYTQFfRGLTA---------FTRVRWKC------LVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDS 1249
Cdd:cd18007 109 WHKEGG--VLLIGYELF-RNLASnattdprlkQEFIAALLdpgpdlLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGT 185
|
170 180 190
....*....|....*....|....*....|
9C62_G 1250 PLHNTFLELWTMVHFLVPGisrpYLSSPLR 1279
Cdd:cd18007 186 PLQNNLKEYWTMVDFARPK----YLGTLKE 211
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1898-2013 |
6.01e-14 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 70.32 E-value: 6.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1898 GKLEALAILLQKlkSEGRRVLILSQMILMLDIlEMFLNFHYLTYVRIDENASSEQRQELMRSFNRDRRIFcaILSTHSRT 1977
Cdd:pfam00271 1 EKLEALLELLKK--ERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDV--LVATDVAE 75
|
90 100 110
....*....|....*....|....*....|....*.
9C62_G 1978 TGINLVEADTVVFYDNDLNPVMDakAQewcdRIGRC 2013
Cdd:pfam00271 76 RGLDLPDVDLVINYDLPWNPASY--IQ----RIGRA 105
|
|
| DEXHc_HARP_SMARCAL1 |
cd18010 |
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ... |
1091-1269 |
2.87e-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: 71.47 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAklyRKNLNGILADEAGLGKTVQIIAFFAHLacnEGNWgPHLVVVRSCNILKWELELKRWCPGLKILS 1170
Cdd:cd18010 1 LLPFQREGVCFAL---RRGGRVLIADEMGLGKTVQAIAIAAYY---REEW-PLLIVCPSSLRLTWADEIERWLPSLPPDD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1171 YIgshreLKAKRQEWAEPNSFHVCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVK-GMTERHWEAVFTLQSQQR-LLLID 1248
Cdd:cd18010 74 IQ-----VIVKSKDGLRDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKnSKAKRTKAALPLLKRAKRvILLSG 148
|
170 180
....*....|....*....|.
9C62_G 1249 SPLHNTFLELWTMVHFLVPGI 1269
Cdd:cd18010 149 TPALSRPIELFTQLDALDPKL 169
|
|
| DEXHc_RAD54A |
cd18067 |
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ... |
1091-1269 |
1.72e-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: 64.03 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAK----LYRKNLNG-ILADEAGLGKTVQIIAFFAHLACNEGNWGPHL----VVVRSCNILKWELELKR 1161
Cdd:cd18067 1 LRPHQREGVKFLYRcvtgRRIRGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaiVVSPSSLVKNWANELGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1162 WCpGLKILSYI---GSHRELKAKRQEWAEPNSFH----VCITSYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEA 1234
Cdd:cd18067 81 WL-GGRLQPLAidgGSKKEIDRKLVQWASQQGRRvstpVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQA 159
|
170 180 190
....*....|....*....|....*....|....*
9C62_G 1235 VFTLQSQQRLLLIDSPLHNTFLELWTMVHFLVPGI 1269
Cdd:cd18067 160 LDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGI 194
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1928-2013 |
4.90e-10 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 58.38 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1928 DILEMFLNFHYLTYVRIDENASSEQRQELMRSFNRDRRIFcaILSTHSRTTGINLVEADTVVFYDNDLNPVMDakAQewc 2007
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKV--LVATDVAERGLDLPGVDLVIIYDLPWSPASY--IQ--- 73
|
....*.
9C62_G 2008 dRIGRC 2013
Cdd:smart00490 74 -RIGRA 78
|
|
| DEXHc_ARIP4 |
cd18069 |
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ... |
1113-1286 |
3.60e-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: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1113 ILADEAGLGKTVQIIAF----FAHLACNEGnwgphLVVVRSCNILKWELELKRWCP-----------GLKILSYIGSHRE 1177
Cdd:cd18069 32 ILAHSMGLGKTLQVISFldvlLRHTGAKTV-----LAIVPVNTLQNWLSEFNKWLPppealpnvrprPFKVFILNDEHKT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1178 LKAKRQ---EWAEPNSfhVCITSYTQFfrgltaftRVR--WKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSPLH 1252
Cdd:cd18069 107 TAARAKvieDWVKDGG--VLLMGYEMF--------RLRpgPDVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQ 176
|
170 180 190
....*....|....*....|....*....|....*.
9C62_G 1253 NTFLELWTMVHFLVPGI--SRPYLSSPLRAPSEESQ 1286
Cdd:cd18069 177 NNLIEYWCMVDFVRPDFlgTRQEFSNMFERPILNGQ 212
|
|
| DEXHc_ATRX |
cd18068 |
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ... |
1112-1269 |
5.35e-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: 5.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1112 GILADEAGLGKTVQIIAFFAHLACNE--GNWGPHLVVVRSCNILKWELELKRWCPGLKI--------LSYIGSHRELKAK 1181
Cdd:cd18068 31 CILAHCMGLGKTLQVVTFLHTVLLCEklENFSRVLVVCPLNTVLNWLNEFEKWQEGLKDeekievneLATYKRPQERSYK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1182 RQEWAEPNSfhVCITSYtQFFRGLTAFTRVRWKC-----------------LVIDEMQRVKGMTERHWEAVFTLQSQQRL 1244
Cdd:cd18068 111 LQRWQEEGG--VMIIGY-DMYRILAQERNVKSREklkeifnkalvdpgpdfVVCDEGHILKNEASAVSKAMNSIRTKRRI 187
|
170 180
....*....|....*....|....*
9C62_G 1245 LLIDSPLHNTFLELWTMVHFLVPGI 1269
Cdd:cd18068 188 VLTGTPLQNNLIEYHCMVNFVKPNL 212
|
|
| DEXHc_TTF2 |
cd18072 |
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ... |
1091-1265 |
1.59e-08 |
|
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: 58.26 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLakLYRKNLN---GILADEAGLGKTVQIIAFFahLACNEG-------------NWGPHL--VVVRSCNI 1152
Cdd:cd18072 1 LLLHQKQALAWL--LWRERQKprgGILADDMGLGKTLTMIALI--LAQKNTqnrkeeekekaltEWESKKdsTLVPSAGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1153 L---------KWELELKRWCPG--LKILSYIGSHRELKAKRQEwaepnSFHVCITSYTQFFRGL---------TAFTRVR 1212
Cdd:cd18072 77 LvvcpaslvhQWKNEVESRVASnkLRVCLYHGPNRERIGEVLR-----DYDIVITTYSLVAKEIptykeesrsSPLFRIA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
9C62_G 1213 WKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHFL 1265
Cdd:cd18072 152 WARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFL 204
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
554-816 |
1.74e-07 |
|
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: 57.35 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 554 PPTPQAAQLAGQRQSQQQYDPSTGPPVQNAASLHT---------PLPQL-----------PGRLPPAGVPTAALSSALQF 613
Cdd:pfam09770 108 AARAAQSSAQPPASSLPQYQYASQQSQQPSKPVRTgyekykepePIPDLqvdaslwgvapKKAAAPAPAPQPAAQPASLP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 614 AQQPQV-----VEAQTQLQIPVKTQQPNVPIPAPPSSqlpiPPSQPAQLALHVPTPGKVQVQASQLSSLPQMVASTRLPV 688
Cdd:pfam09770 188 APSRKMmsleeVEAAMRAQAKKPAQQPAPAPAQPPAA----PPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPV 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 689 DPAPPCPRPLPTSSTSSLAPVS-GSGPGPSPARSSPV------NRPSSAtnkalspvtsRTPGVVASAPTKPQSPAQNAT 761
Cdd:pfam09770 264 TILQRPQSPQPDPAQPSIQPQAqQFHQQPPPVPVQPTqilqnpNRLSAA----------RVGYPQNPQPGVQPAPAHQAH 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
9C62_G 762 SSQdSSQDTLTEQITLENQVHQRIAELRKAGLwsqrrlpkLQEAPRPK-SHWDYLL 816
Cdd:pfam09770 334 RQQ-GSFGRQAPIITHPQQLAQLSEEEKAAYL--------DEEAKRAKrNHKIFLL 380
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
532-769 |
2.00e-07 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 57.08 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 532 QHPGADAGVPLQQLMptAQGGMPPTPQaAQLAGQRQSQQQYDPSTGPPVQNAASLHTPLPQLPGRL----PPAGVPTAAL 607
Cdd:pfam03154 290 QHPVPPQPFPLTPQS--SQSQVPPGPS-PAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMphikPPPTTPIPQL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 608 SSAlQFAQQPQVVEAQTQLQIPVKTQQP-------NVPIPAPPSS------------QLPIPPSQPaqlalhvPTPGKVQ 668
Cdd:pfam03154 367 PNP-QSHKHPPHLSGPSPFQMNSNLPPPpalkplsSLSTHHPPSAhppplqlmpqsqQLPPPPAQP-------PVLTQSQ 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 669 VQASQLSSLPQMVASTRLPVDPAPPCPRPLPTSSTSSLAPvsgSGPGPSPARSSPVNRPSSATNKALSpvtsrtpGVVAS 748
Cdd:pfam03154 439 SLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPPITPP---SGPPTSTSSAMPGIQPPSSASVSSS-------GPVPA 508
|
250 260
....*....|....*....|.
9C62_G 749 APTKPQSPAQNATSSQDSSQD 769
Cdd:pfam03154 509 AVSCPLPPVQIKEEALDEAEE 529
|
|
| DEXHc_HLTF1_SMARC3 |
cd18071 |
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ... |
1112-1307 |
8.64e-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: 8.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1112 GILADEAGLGKTVQIIAFFAHlacnegnwGPHLVVVRSCNILKWELELKRWC-PG-LKILSYIGSHRELKAKrqewaEPN 1189
Cdd:cd18071 51 GILADDMGLGKTLTTISLILA--------NFTLIVCPLSVLSNWETQFEEHVkPGqLKVYTYHGGERNRDPK-----LLS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1190 SFHVCITSYTQF-----FRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSPLHNTFLELWTMVHF 1264
Cdd:cd18071 118 KYDIVLTTYNTLasdfgAKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSF 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
9C62_G 1265 L--VPGISRPYLSSPLRAPSEESQDyyhKVVIRLHRVTQPFILRR 1307
Cdd:cd18071 198 LhlKPFSNPEYWRRLIQRPLTMGDP---TGLKRLQVLMKQITLRR 239
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
1113-1268 |
9.38e-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: 52.29 E-value: 9.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1113 ILADEAGLGKTVQIIAfFAHLACNEGNWGPHLVVVRSCNILKWELELKRWCpGLKILSYIGSHRElKAKRQEWAEPNSFH 1192
Cdd:cd18011 21 LLADEVGLGKTIEAGL-IIKELLLRGDAKRVLILCPASLVEQWQDELQDKF-GLPFLILDRETAA-QLRRLIGNPFEEFP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1193 VCITSYTQFFRG---LTAFTRVRWKCLVIDEMQRVKGM-----TERhWEAVFTLQSQQR--LLLIDSPLHNTFLELWTMV 1262
Cdd:cd18011 98 IVIVSLDLLKRSeerRGLLLSEEWDLVVVDEAHKLRNSgggkeTKR-YKLGRLLAKRARhvLLLTATPHNGKEEDFRALL 176
|
....*.
9C62_G 1263 HFLVPG 1268
Cdd:cd18011 177 SLLDPG 182
|
|
| DEXQc_SHPRH |
cd18070 |
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ... |
1091-1228 |
5.12e-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: 50.81 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLaklyrKNLNGILADEAGLGKTVQIIAF-FAH-----------LACNEGNWGPHLVV---VRSCN---- 1151
Cdd:cd18070 1 LLPYQRRAVNWM-----LVPGGILADEMGLGKTVEVLALiLLHprpdndldaadDDSDEMVCCPDCLVaetPVSSKatli 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1152 -----ILK-WELELKRWCP-GLKILSYIGSHRELKAKRQEWAEPNSFHVCITSYT-------------------QFFRGL 1205
Cdd:cd18070 76 vcpsaILAqWLDEINRHVPsSLKVLTYQGVKKDGALASPAPEILAEYDIVVTTYDvlrtelhyaeanrsnrrrrRQKRYE 155
|
170 180
....*....|....*....|....*.
9C62_G 1206 ---TAFTRVRWKCLVIDEMQRVKGMT 1228
Cdd:cd18070 156 appSPLVLVEWWRVCLDEAQMVESST 181
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
513-679 |
5.49e-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: 52.35 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 513 MAEQSKRPRlevghQGVVFQHPGADAGVPLQQLMPTAQGgmPPTPQAAQLAGQRQSQQQYDPSTGPPVQnaaslhtPLPQ 592
Cdd:pfam09770 203 MRAQAKKPA-----QQPAPAPAQPPAAPPAQQAQQQQQF--PPQIQQQQQPQQQPQQPQQHPGQGHPVT-------ILQR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 593 LPGRLPPAGVPTAALSSALQFAQQPQVVEAQTQ-LQIPVKTQQPNVPIPAPPSSQLPIPPSQPAQLALHV-PTPGKVQVQ 670
Cdd:pfam09770 269 PQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQiLQNPNRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSfGRQAPIITH 348
|
....*....
9C62_G 671 ASQLSSLPQ 679
Cdd:pfam09770 349 PQQLAQLSE 357
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
3040-3159 |
2.96e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 49.77 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 3040 TQIQVAKLPQVVQQQTPVASIQQVASA--SQQAS-PQTVALTQATAAGQQVQMIPAVTATAQVVQQKLIQQQVVT--TAS 3114
Cdd:PRK14971 355 TLIQLAQLTQKGDDASGGRGPKQHIKPvfTQPAAaPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVSVdpPAA 434
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
9C62_G 3115 APLQTPGAPNPAQVPASSDSPSQQPKLQMRVPAVRLKTPTKPPCQ 3159
Cdd:PRK14971 435 VPVNPPSTAPQAVRPAQFKEEKKIPVSKVSSLGPSTLRPIQEKAE 479
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
574-762 |
6.10e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.17 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 574 PSTGPPVQNAASLHTPLPQLPgrlPPAGVPTAALSSalqfaqqpqvveaqtqLQIPVKTQQPNVPIPAPPSSqlPIPPSQ 653
Cdd:PHA03247 2686 RAARPTVGSLTSLADPPPPPP---TPEPAPHALVSA----------------TPLPPGPAAARQASPALPAA--PAPPAV 2744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 654 PAQLAlhvpTPGKVQVQAS-QLSSLPQMVASTRLPVDPAPPCPRPLPTSSTSSLAPVSGSGPGPSPArSSPVNRPSSATN 732
Cdd:PHA03247 2745 PAGPA----TPGGPARPARpPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADP-PAAVLAPAAALP 2819
|
170 180 190
....*....|....*....|....*....|..
9C62_G 733 KALSPVTSRTP--GVVASAPTKPQSPAQNATS 762
Cdd:PHA03247 2820 PAASPAGPLPPptSAQPTAPPPPPGPPPPSLP 2851
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
505-758 |
7.46e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.78 E-value: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 505 QQAMPSTGMAEQSKRPRLEVGHQGVVFQHPGADAGVPLQQLMPTAQGGMPPTPQAAQLAGQRQSQQQYDPSTGPPVQNAA 584
Cdd:PHA03247 2572 RPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPER 2651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 585 SLHTPLP---QLPGRLPPAGVPTAAlSSALQFAQQPQV---VEAQTQLQIPVKTQQPNVPIPAPPSSQLPIPPSQPAQLA 658
Cdd:PHA03247 2652 PRDDPAPgrvSRPRRARRLGRAAQA-SSPPQRPRRRAArptVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQ 2730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 659 LHVPTPGKvqvqasqlSSLPQMVASTRLPVDPAPPCPRPLPTSSTSSLAPVSGSGPGPSPARSSPVNRPSSATNKALSPV 738
Cdd:PHA03247 2731 ASPALPAA--------PAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPW 2802
|
250 260
....*....|....*....|
9C62_G 739 TSRTPGVVASAPTKPQSPAQ 758
Cdd:PHA03247 2803 DPADPPAAVLAPAAALPPAA 2822
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
531-808 |
1.40e-04 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 47.60 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 531 FQHPGADAGVPLQQLMPT---AQGGMPPTPQAAQL-----AGQRQSQQQYDPSTGP----PVQNAASLHTPLPQLPGRLP 598
Cdd:pfam05109 439 FAAPNTTTGLPSSTHVPTnltAPASTGPTVSTADVtsptpAGTTSGASPVTPSPSPrdngTESKAPDMTSPTSAVTTPTP 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 599 PAGVPTAALSSALQFAQQPQVveAQTQLQIPVKTQQPNVPIPAPPSSQlPIPPSQpaqlalhVPTPGKVQVQASQLSSLP 678
Cdd:pfam05109 519 NATSPTPAVTTPTPNATSPTL--GKTSPTSAVTTPTPNATSPTPAVTT-PTPNAT-------IPTLGKTSPTSAVTTPTP 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 679 QMVASTrlpvdpappcprPLPTSSTSSLAPVSGSGPGPSPARSSPVNRPSSATNKALSPVTSRTpgvVASAPTKPQSPAQ 758
Cdd:pfam05109 589 NATSPT------------VGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSS---TSSMSLRPSSISE 653
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
9C62_G 759 NATSsqdSSQDTLTEQITLENQVH----QRIAELRKAGLwSQRRLPKLQEAPRP 808
Cdd:pfam05109 654 TLSP---STSDNSTSHMPLLTSAHptggENITQVTPAST-STHHVSTSSPAPRP 703
|
|
| SP1-4_arthropods_N |
cd22553 |
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ... |
3010-3142 |
2.12e-04 |
|
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. One SP is clade SP1-4, which is expressed ubiquitously throughout development. SP1-4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. This model represents the N-terminal domain of SP1-4 from arthropods.
Pssm-ID: 411778 [Multi-domain] Cd Length: 384 Bit Score: 46.56 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 3010 AYAAQPALKTQFLTtPISQAQKLAGAQ--QVQTQIQVAKLPQVVQQQTPVAsIQQVASASQQASPQTvaltqATAAGQQV 3087
Cdd:cd22553 188 AGGGNQALQAQVIP-QLAQAAQLQPQQlaQVSSQGYIQQIPANASQQQPQM-VQQGPNQSGQIIGQV-----ASASSIQA 260
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
9C62_G 3088 QMIPAVT-ATAQVVQQKLIQQQVVTTASAPLQTPGAPNPAQVPASSDSPSQQPKLQ 3142
Cdd:cd22553 261 AAIPLTVyTGALAGQNGSNQQQVGQIVTSPIQGMTQGLTAPASSSIPTVVQQQAIQ 316
|
|
| PHA03269 |
PHA03269 |
envelope glycoprotein C; Provisional |
624-757 |
2.19e-04 |
|
envelope glycoprotein C; Provisional
Pssm-ID: 165527 [Multi-domain] Cd Length: 566 Bit Score: 47.03 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 624 TQLQIPVKTQQPNVPIP---APPSSQLPIPPSQPAQLALHVPTPGKVQVQAS----QLSSLPQMVASTRLpvDPAPPCPR 696
Cdd:PHA03269 13 ACINLIIANLNTNIPIPelhTSAATQKPDPAPAPHQAASRAPDPAVAPTSAAsrkpDLAQAPTPAASEKF--DPAPAPHQ 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
9C62_G 697 PLPTSSTSSLAPVSGSGPGPSPArSSPVNRPSSATNKALSPVT--SRTPGVVASAPTKPQSPA 757
Cdd:PHA03269 91 AASRAPDPAVAPQLAAAPKPDAA-EAFTSAAQAHEAPADAGTSaaSKKPDPAAHTQHSPPPFA 152
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
622-806 |
2.54e-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: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 622 AQTQLQipvKTQQPNVPIPAPPSSQLPIPPSQPAQLALHVPTPGKVQVQ---ASQLSSLPQMVASTRLPVDPAPPCPRPL 698
Cdd:pfam03154 162 AQQQIL---QTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPpqgSPATSQPPNQTQSTAAPHTLIQQTPTLH 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 699 PTSSTSSLAPVSGSGPGPSPARSSPVNRPSSATNKALSPVtsrtPGVVASAPTKPQSPAQ----NATSSQDSSQDTLTEQ 774
Cdd:pfam03154 239 PQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPM----PHSLQTGPSHMQHPVPpqpfPLTPQSSQSQVPPGPS 314
|
170 180 190
....*....|....*....|....*....|..
9C62_G 775 ITLENQVHQRIAELRKAGLWSQRRLPKLQEAP 806
Cdd:pfam03154 315 PAAPGQSQQRIHTPPSQSQLQSQQPPREQPLP 346
|
|
| SP1-4_arthropods_N |
cd22553 |
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ... |
2876-3101 |
2.80e-04 |
|
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. One SP is clade SP1-4, which is expressed ubiquitously throughout development. SP1-4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. This model represents the N-terminal domain of SP1-4 from arthropods.
Pssm-ID: 411778 [Multi-domain] Cd Length: 384 Bit Score: 46.17 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 2876 GTTVANLQVARLTRVPTSQLQAQGQMQTQAPQPAQVALAKPPVVSVPAAVVSSPGVTTLPMNVAGiSVAIGQPQKAA-GQ 2954
Cdd:cd22553 92 LLQTNNQQAIQLAPGGTQAILANQQTLIRPNTVQGQANASNVLQNIAQIASGGNAVQLPLNNMTQ-TIPVQVPVSTAnGQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 2955 TV---VAQPVHMQQLLKLKQQAVQQQKAIQPQAAQ-GPAAVQQKITA------QQITTPGAQQK-------------VAY 3011
Cdd:cd22553 171 TVyqtIQVPIQAIQSGNAGGGNQALQAQVIPQLAQaAQLQPQQLAQVssqgyiQQIPANASQQQpqmvqqgpnqsgqIIG 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 3012 AAQPALKTQFLTTPISQAQKLAGAQQVQTQIQVAKLP----QVVQQQTPVASIQQVASASQQASPQTVAL---TQATAAG 3084
Cdd:cd22553 251 QVASASSIQAAAIPLTVYTGALAGQNGSNQQQVGQIVtspiQGMTQGLTAPASSSIPTVVQQQAIQGNPLppgTQIIAAG 330
|
250
....*....|....*..
9C62_G 3085 QQVQMIPAVTATAQVVQ 3101
Cdd:cd22553 331 QQLQQDPNDPTKWQVVA 347
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
505-766 |
2.89e-04 |
|
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: 46.54 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 505 QQAMPSTGMAEQSKRPRLEVGHQGVVFQHPGADAGVPLQQLMPTAQGGMP--------PTPQAAQLAGQRQSQQQYDPST 576
Cdd:pfam09606 171 PNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGqqaqanggMNPQQMGGAPNQVAMQQQQPQQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 577 GPPVQNAASLHTPLPQLPGRLP---PAGVPTAALSSAlqfAQQPQVVEAQTQLQIP-VKTQQPNVpiPAPPSSQLPIPPS 652
Cdd:pfam09606 251 QGQQSQLGMGINQMQQMPQGVGggaGQGGPGQPMGPP---GQQPGAMPNVMSIGDQnNYQQQQTR--QQQQQQGGNHPAA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 653 QPAQLALHVptpgkvqVQASQLSSLP-QMVASTRLPVDPAPPCPRPL--------------PTSSTSSLAPVSGSGPGPS 717
Cdd:pfam09606 326 HQQQMNQSV-------GQGGQVVALGgLNHLETWNPGNFGGLGANPMqrgqpgmmsspspvPGQQVRQVTPNQFMRQSPQ 398
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
9C62_G 718 PARSSPVNrPSSATNKALSPVTSRTPGVVAS-APTKPQSPAQNATSSQDS 766
Cdd:pfam09606 399 PSVPSPQG-PGSQPPQSHPGGMIPSPALIPSpSPQMSQQPAQQRTIGQDS 447
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
1091-1220 |
3.63e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 43.81 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLD-WLAKLYRKNLNGILADEAGLGKTvqIIAFFAHLACNEGNWGPH-LVVVRSCNILK-WELELKRWCPGLK 1167
Cdd:pfam04851 4 LRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKT--LTAAKLIARLFKKGPIKKvLFLVPRKDLLEqALEEFKKFLPNYV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
9C62_G 1168 ILSYIGSHRELKAKRQEWaepnsfHVCITSYTQFFRGLTAFTRV----RWKCLVIDE 1220
Cdd:pfam04851 82 EIGEIISGDKKDESVDDN------KIVVTTIQSLYKALELASLEllpdFFDVIIIDE 132
|
|
| DEXQc_bact_SNF2 |
cd18013 |
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ... |
1091-1265 |
5.40e-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: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1091 LRDYQKIGLDWLAKLYRknlNGILADeAGLGKTVQIIAFFAHLACnEGNWGPHLV-----VVRScnilKWELELKRW--C 1163
Cdd:cd18013 1 PHPYQKVAINFIIEHPY---CGLFLD-MGLGKTVTTLTALSDLQL-DDFTRRVLViaplrVARS----TWPDEVEKWnhL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 1164 PGLKILSYIGSHREL-KAKRQEWaepnsfHVCITSYtQFFRGLTAFTRVRW--KCLVIDEMQRVKGMTERHWEAVFTLQS 1240
Cdd:cd18013 72 RNLTVSVAVGTERQRsKAANTPA------DLYVINR-ENLKWLVNKSGDPWpfDMVVIDELSSFKSPRSKRFKALRKVRP 144
|
170 180
....*....|....*....|....*..
9C62_G 1241 Q-QRLL-LIDSPLHNTFLELWTMVHFL 1265
Cdd:cd18013 145 ViKRLIgLTGTPSPNGLMDLWAQIALL 171
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
508-689 |
8.42e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.98 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 508 MPSTGMAEQSKRPRLEvghqgvvfqhpgadagvPLQQLMPTAQGGMPPTPQAAqlagqrqSQQQYDPSTGPPvqnaaslh 587
Cdd:PRK07764 364 LPSASDDERGLLARLE-----------------RLERRLGVAGGAGAPAAAAP-------SAAAAAPAAAPA-------- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 588 tplpqlPGRLPPAGVPTAALSSALQFAQQPQVVEAQTQLQIPVKTQQPNVPIPAPPSSQLPIPPSQPAQLALHVPTPGKV 667
Cdd:PRK07764 412 ------PAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPP 485
|
170 180
....*....|....*....|..
9C62_G 668 QVQASQLSSLPQMVASTRLPVD 689
Cdd:PRK07764 486 AAPAPAAAPAAPAAPAAPAGAD 507
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
535-772 |
1.25e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.48 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 535 GADAGVPLQQLMPTAQggMPPTPQAAQLAGQRQSQQQYDPSTGPPVQNAASlhtPLPQLPGRLPPAGVPTAALSSALQFA 614
Cdd:PRK12323 369 GGGAGPATAAAAPVAQ--PAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAAR---AVAAAPARRSPAPEALAAARQASARG 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 615 QQPQVVEAQTQLQIPVKTQQPNVPIPAPPSSQLPIPPSQPAQLALHVPTPGKVqvqaSQLSSLPQMVAStrlpvdpappc 694
Cdd:PRK12323 444 PGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDP----PPWEELPPEFAS----------- 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 695 prplptsstsslAPVSGSGPGPSPARSSPVNRPS----SATNKALSPVTSRTPGVVASAPTKPQSPAQNATSSQDSSQDT 770
Cdd:PRK12323 509 ------------PAPAQPDAAPAGWVAESIPDPAtadpDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDM 576
|
..
9C62_G 771 LT 772
Cdd:PRK12323 577 FD 578
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
543-764 |
1.64e-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: 44.37 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 543 QQLMPTAQGGMPPTPQAAQLAGQRQSQ------------QQYDPSTGPPVQNAASL--------------------HTPL 590
Cdd:pfam03154 170 QPPVLQAQSGAASPPSPPPPGTTQAATagptpsapsvppQGSPATSQPPNQTQSTAaphtliqqtptlhpqrlpspHPPL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 591 PQLPGRLPPAGVPTAALSSALQFAQQP----QVVEAQTQLQIPVKTQQPNVP-------IPAPPSSQLPIPPSQ-----P 654
Cdd:pfam03154 250 QPMTQPPPPSQVSPQPLPQPSLHGQMPpmphSLQTGPSHMQHPVPPQPFPLTpqssqsqVPPGPSPAAPGQSQQrihtpP 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 655 AQLALHVPTPGKVQVQASQLSSLPQMVASTRLPVDPAPPCPRPLPTSSTSSLAPVSGSG-----PGPSPARSSPVNRPSS 729
Cdd:pfam03154 330 SQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSnlpppPALKPLSSLSTHHPPS 409
|
250 260 270
....*....|....*....|....*....|....*..
9C62_G 730 ATNKALS--PVTSRTPGVVASAPTKPQSPAQNATSSQ 764
Cdd:pfam03154 410 AHPPPLQlmPQSQQLPPPPAQPPVLTQSQSLPPPAAS 446
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
534-767 |
2.37e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.01 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 534 PGADAGVPLQQLMPTAQGGMPPTPQAAQLAGQRQSQ--QQYDPSTGPPVQNAASLHTPLPQLPGRLPPAG--VPTAALSS 609
Cdd:PHA03307 73 PGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPpgPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGspGPPPAASP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 610 ALQFAQQPQVVEAQT---QLQIPVKTQQPNVPIPAPPSSQLPI------------PPSQPAQLALHVPTPGKVQVQASQL 674
Cdd:PHA03307 153 PAAGASPAAVASDAAssrQAALPLSSPEETARAPSSPPAEPPPstppaaasprppRRSSPISASASSPAPAPGRSAADDA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 675 SSLPQMVASTRLPV---DPAPPCPRPLPTSSTSSLAPVSGSGPGPSPARSSPVnRPSSATNKALSPVTSRTPGVVASAPT 751
Cdd:PHA03307 233 GASSSDSSSSESSGcgwGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPA-SSSSSPRERSPSPSPSSPGSGPAPSS 311
|
250
....*....|....*.
9C62_G 752 KPQSPAQNATSSQDSS 767
Cdd:PHA03307 312 PRASSSSSSSRESSSS 327
|
|
| PABP-1234 |
TIGR01628 |
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ... |
504-619 |
2.47e-03 |
|
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: 43.64 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 504 RQQAMPSTGMAEQSKRPRLEVGHQG---VVFQHPGAD-AGVPL----QQLMPTAQG------GMPPTPQAAQLAGQRQSQ 569
Cdd:TIGR01628 372 QDQFMQLQPRMRQLPMGSPMGGAMGqppYYGQGPQQQfNGQPLgwprMSMMPTPMGpggplrPNGLAPMNAVRAPSRNAQ 451
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
9C62_G 570 QQYDPSTGPPVQ-----NAASLHTPLPQlPGRLPPAGVPTAALSSALQFA---QQPQV 619
Cdd:TIGR01628 452 NAAQKPPMQPVMyppnyQSLPLSQDLPQ-PQSTASQGGQNKKLAQVLASAtpqMQKQV 508
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
3002-3126 |
2.69e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 43.54 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 3002 TPGAQQKVAYAAQPALKTQFlttpiSQAQKLAGAQQVQTQIQ--VAKLPQVVQQQTPVASIQQVASASQQASPQTVALTQ 3079
Cdd:PRK10263 746 TPIVEPVQQPQQPVAPQQQY-----QQPQQPVAPQPQYQQPQqpVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQP 820
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
9C62_G 3080 ATAAGQQVQMIPAVTATAQVVQQKLIQQQVVTTA-SAPLQTPGAPNPA 3126
Cdd:PRK10263 821 QQPVAPQPQYQQPQQPVAPQPQDTLLHPLLMRNGdSRPLHKPTTPLPS 868
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
534-684 |
3.84e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 42.78 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 534 PGADAGVPlqqlmPTAQGGMPPTPQAAQLAGQRQSQQQYDPSTGPPV----QNAASLHTPLPQLPGRLPPAGVPTAALSS 609
Cdd:PRK14951 366 PAAAAEAA-----APAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPaaaaSAPAAPPAAAPPAPVAAPAAAAPAAAPAA 440
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
9C62_G 610 ALQFAQQPQVVEAQTQ---LQIPVKTQqpnvPIPAPPSSQlPIPPSQPAQLALHVPTPGKVQVQAsqlssLPQMVAST 684
Cdd:PRK14951 441 APAAVALAPAPPAQAApetVAIPVRVA----PEPAVASAA-PAPAAAPAAARLTPTEEGDVWHAT-----VQQLAAAE 508
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
2894-3146 |
3.95e-03 |
|
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: 43.07 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 2894 QLQAQGQMQTQAPQPAQVALAKPPVVSVPAAVVSSPGVTTLPMNVAGISVAIGQPQKAAGQTVvaqPVHMQQllklKQQA 2973
Cdd:pfam09606 222 QAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGQPM---GPPGQQ----PGAM 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 2974 VQQQKAIQPQAAQGPAAVQQKITAQQITTPGAQQKVAYAAQPAlktqflttpiSQAQKLAGAQQVQTQIQVAKLPQVVQQ 3053
Cdd:pfam09606 295 PNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQG----------GQVVALGGLNHLETWNPGNFGGLGANP 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 3054 QtpvasiqqvasasQQASPQTVALTQATAAGQQVQMipavtATAQVVQQKliQQQVVTTASAPLQTPGA-------PNPA 3126
Cdd:pfam09606 365 M-------------QRGQPGMMSSPSPVPGQQVRQV-----TPNQFMRQS--PQPSVPSPQGPGSQPPQshpggmiPSPA 424
|
250 260
....*....|....*....|
9C62_G 3127 QVPASSDSPSQQPKLQMRVP 3146
Cdd:pfam09606 425 LIPSPSPQMSQQPAQQRTIG 444
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
3025-3157 |
4.03e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 43.10 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 3025 PISQAQKLAGAQQVQTQIQVAkLPQVVQQQTPVASIQQVASASQQASPQTVALTQATAAGQQVQMIPAVTATAQVVQQKL 3104
Cdd:PRK10811 846 PVVRPQDVQVEEQREAEEVQV-QPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETTHPEVIAAPV 924
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
9C62_G 3105 IQQ-QVVT--TASAPLQTPGAPNPAQVPASSDSPSQQPKLQMRVPAVRLKTPTKPP 3157
Cdd:PRK10811 925 TEQpQVITesDVAVAQEVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQPA 980
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
536-761 |
6.74e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.28 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 536 ADAGVPLQQLMPTAQGGMPPTPQAAQLAGQRQSQQQYDPSTGPPvqNAASLHTPLPQLPGRLPPAGVPTAALSSALQFAQ 615
Cdd:PRK07764 589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGA--AAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGG 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 616 QPQVVEAQTqlqiPVKTQQPNVPIPAPPSSQLPIPPSQPAQLALHVPTPGKVQVQASQlsslPQMVASTRLPVDPAPPCP 695
Cdd:PRK07764 667 DGWPAKAGG----AAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQ----PPQAAQGASAPSPAADDP 738
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
9C62_G 696 RPLPtsSTSSLAPVSGSGPGPSPARSSPVNRPSSATNKALSPVTSRTPGVVASAPTKPQSPAQNAT 761
Cdd:PRK07764 739 VPLP--PEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAE 802
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
519-757 |
7.73e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.79 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 519 RPRLEVGHQGVVFQHPGADAGVPLQQLMPTAQGGMPPTPQAAqlagqrqsqqqydPSTGPPVQNAASlhtPLPQLPGRLP 598
Cdd:PRK12323 364 RPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAA-------------PAAAPAAAAAAR---AVAAAPARRS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 599 PAGVPTAALSSALQFAQQPQVVEAQTQLQIPVKTQQPNVPIPAPPSSQLPIPPSQPAQLALHVPTPGKVqvqaSQLSSLP 678
Cdd:PRK12323 428 PAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDP----PPWEELP 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
9C62_G 679 QMVASTRLPVDPAPPCPRPLPTSSTSSLAPVSGSGPGPSPARSSPvnrPSSATNKALSPVTSRTPGVVASAPTKPQSPA 757
Cdd:PRK12323 504 PEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAA---PAPRAAAATEPVVAPRPPRASASGLPDMFDG 579
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
542-808 |
8.49e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 41.98 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 542 LQQLMPTAQGGMPPTPQAAQLAGQrQSQQQYDPSTGPPVQNAASLHtPLPQLPGRLPPAGVPTAALSSALQFAQQPQVVE 621
Cdd:PHA03378 585 LASSAPSYAQTPWPVPHPSQTPEP-PTTQSHIPETSAPRQWPMPLR-PIPMRPLRMQPITFNVLVFPTPHQPPQVEITPY 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 622 AQTQLQIPVKTQQPNvpiPAPPSSQLPI---------PPSQPAQLALHVPTPGKVQVQASQLSSLPQMVASTRLPVDPAP 692
Cdd:PHA03378 663 KPTWTQIGHIPYQPS---PTGANTMLPIqwapgtmqpPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAA 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
9C62_G 693 PCPRPLPTSSTSSLAPVSGSGPGPSPARSSPVNRPSSATNKALSPVTSRTPgvvASAPTKPQSPAQNATSSQDSSQDTLT 772
Cdd:PHA03378 740 APGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRP---RGAPTPQPPPQAGPTSMQLMPRAAPG 816
|
250 260 270 280
....*....|....*....|....*....|....*....|
9C62_G 773 EQITLENQVHQRIAELRKAG---LWSQRRLPKLQEA-PRP 808
Cdd:PHA03378 817 QQGPTKQILRQLLTGGVKRGrpsLKKPAALERQAAAgPTP 856
|
|
| |
