|
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 ... |
1-451 |
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: 594.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1 MHHGSGPQNVQHQLQRSRSFTGSEE----EQPAHPNLPPSPAAPFAPSASPSAPQSPGYQIqqLMSRSPVAGQNVNITLQ 76
Cdd:pfam15790 1 MHHGSGSQNVQRQLQRSKSVSGSEEqqqeQQPATVNHPQSPVTTFAPAASPSAPQSPNYQI--IMSRSPVTGQNVNITLQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 77 NVGPVVGGNQQITLAPLPLPNPTSPGFQFGAQQRRFEHGSPSYIQVTSPMSQQVQTQSPTQPSPGPGQTLQnvRAGAPGP 156
Cdd:pfam15790 79 NVGQMVAGNQQITLTPLPLQSPASPGFQHSAPQWRFEHGSPSYIQVTSPLPQQVQPQSPTQHSPVPLQGVQ--RPGAPGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 157 GLGICSNSPTGgFVDASVLVRQISL-SPSSGGHFVFQEAPGLTQMAQG-AQVQLQHSGAPITVRERRLSQPHAQSGGTIH 234
Cdd:pfam15790 157 GLGVCGQSPTR-FVDASMLVRQISLgSPSGGGHFVYQDGTGLAQIAPGaGQVQLASPGTPGSVRERRLSQPHSQTGGTIH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 235 HLGPQSPAAAGgTGLQPLASPNHITTASLPPQISSIIQGQliqqqqqvlqgqpMNRSLGFERTPGVLLPGVGGPSA-FGM 313
Cdd:pfam15790 236 HLGPQSPAAAG-AGLQTLGSPGHITTSNLPPQISSIIQGQ-------------LARPLGFEKTAQVVVAGAGGPAAsFGI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 314 TSPPPPTSPSRTTMPPGLSSVPLTSMGSSG-MKKVPKKLEEIPPASQEMAQMRKQCLDYHYKEMEALKEVFKEYLIELFF 392
Cdd:pfam15790 302 PSSIPPTSPSRTSPPPGLSSNPLTSTGMSGsVKKVPKKLEEIAPATPEIAQLRKQCLDHHTKKMESLKEVFKEYLIELFF 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 190194425 393 LQHLQGNMMDFLAFKKKHYAPLQAYLRQNDLDIEEEEEEEEeeegKSEVINDEHQSLTG 451
Cdd:pfam15790 382 LQHLQGNMMDFLAFKKKHCVPLYTYLRQNDLDLEEEEEEEE----QSEVINDEVKVVTG 436
|
|
| DEXQc_SRCAP |
cd18003 |
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ... |
1017-1233 |
1.98e-125 |
|
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: 394.03 E-value: 1.98e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVMRSCNILKWELELKRWCPGLKTLS 1096
Cdd:cd18003 1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1097 YVGSHRELKAKRQEWTEPNNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQSQQRLLLIDVP 1176
Cdd:cd18003 81 YYGSAKERKLKRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190194425 1177 LHNTFLELWTMVHFLIPGI------SRPYLSFPLKAPNEENQDYYHKMVIRLHRVTQPFILRR 1233
Cdd:cd18003 161 LQNSLMELWSLMHFLMPHIfqshqeFKEWFSNPLTAMSEGSQEENEELVRRLHKVLRPFLLRR 223
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
1020-1300 |
3.92e-62 |
|
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: 215.24 E-value: 3.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1020 YQKIGLDWLAKLYRK-NLNGILADEAGLGKTVQIIAFFAHLACNEGNWG-PHLVVMRSCNILKWELELKRWC--PGLKTL 1095
Cdd:pfam00176 1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1096 SYVGSHRELKAKRQEWTEPNNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQSQQRLLLIDV 1175
Cdd:pfam00176 81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1176 PLHNTFLELWTMVHFLIPGI------SRPYLSFPLKAPNEEnqdyyhKMVIRLHRVTQPFILRRTKRDVEKQLTRKYEHV 1249
Cdd:pfam00176 161 PLQNNLEELWALLNFLRPGPfgslstFRNWFDRPIERGGGK------KGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYI 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 190194425 1250 LKCRLSSRQKALYEDVILQPRTQEALKS----GHFVSVLSVLTRLQRICNHPGLV 1300
Cdd:pfam00176 235 LFCRLSKLQRKLYQTFLLKKDLNAIKTGeggrEIKASLLNILMRLRKICNHPGLI 289
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
779-1300 |
1.81e-61 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 225.49 E-value: 1.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 779 LREERGKKEEQSRLRRIAATTAREIEYFWSNIEQVVEIKLQVELEEKRKKALNLQKVSRRGKESRLKGFDTSPEHSLDLG 858
Cdd:COG0553 17 LTELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLRLLLALLLLAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 859 ISGRKRKASTSLTDDEVEDEEETIEEEEAHEGLVDHHTELTNLAKEAELPLIDLMKLYEGAFLPNFQWPQPEPDHEESSG 938
Cdd:COG0553 97 LLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 939 EEDVEDCPSDRESRRDSVLIDSLFIMDQFKAAERMSIGKSNTKDITEVTAVAEAILPkgsarvttavkfsAPSLLYGALR 1018
Cdd:COG0553 177 LLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALES-------------LPAGLKATLR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1019 DYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLAcNEGNWGPHLVVM-RSCnILKWELELKRWCPGLKTLSY 1097
Cdd:COG0553 244 PYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELK-ERGLARPVLIVApTSL-VGNWQRELAKFAPGLRVLVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1098 VGShrelkAKRQEWTEP-NNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQSQQRLLLIDVP 1176
Cdd:COG0553 322 DGT-----RERAKGANPfEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1177 LHNTFLELWTMVHFLIPGISRPYLSF------PLKAPNEENQDyyhkmviRLHRVTQPFILRRTKRDVEKQLTRKYEHVL 1250
Cdd:COG0553 397 VENRLEELWSLLDFLNPGLLGSLKAFrerfarPIEKGDEEALE-------RLRRLLRPFLLRRTKEDVLKDLPEKTEETL 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 190194425 1251 KCRLSSRQKALYEDVILQPRTQ--EALKSGHFVSVLSVLTRLQRICNHPGLV 1300
Cdd:COG0553 470 YVELTPEQRALYEAVLEYLRREleGAEGIRRRGLILAALTRLRQICSHPALL 521
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
1007-1312 |
7.26e-57 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 217.36 E-value: 7.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1007 FSAPSLLYGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVMRSCNILKWELELK 1086
Cdd:PLN03142 160 LVQPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIR 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1087 RWCPGLKTLSYVGSHRELKAKRQEWTEPNNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQS 1166
Cdd:PLN03142 240 RFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFST 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1167 QQRLLLIDVPLHNTFLELWTMVHFLIPGISRPYLSFP--LKAPNEENQdyyHKMVIRLHRVTQPFILRRTKRDVEKQLTR 1244
Cdd:PLN03142 320 NYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDewFQISGENDQ---QEVVQQLHKVLRPFLLRRLKSDVEKGLPP 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 190194425 1245 KYEHVLKCRLSSRQKALYEdVILQpRTQEALKSGHFVS-VLSVLTRLQRICNHPGLVEPRVPGSSFAAG 1312
Cdd:PLN03142 397 KKETILKVGMSQMQKQYYK-ALLQ-KDLDVVNAGGERKrLLNIAMQLRKCCNHPYLFQGAEPGPPYTTG 463
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
1740-1865 |
3.96e-39 |
|
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: 143.00 E-value: 3.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1740 SGKLEALAILLQKLKSEGRRVLILSQMVLMLDILEMFLNFHYLTYVRIDENANSEQRQELMRSFNRDRRIFCALLSTHSR 1819
Cdd:cd18793 10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 190194425 1820 ATGINLVEADTVVFYDNDLNPVMDAKAQEWCDRIGRCKDIHIYRLV 1865
Cdd:cd18793 90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
1739-1882 |
1.84e-31 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 135.70 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1739 DSGKLEALAILLQKLKSEGRRVLILSQMVLMLDILEMFLNFHYLTYVRIDENANSEQRQELMRSFNRD-RRIFCALLSTH 1817
Cdd:PLN03142 469 NSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTR 548
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190194425 1818 SRATGINLVEADTVVFYDNDLNPVMDAKAQEWCDRIGRCKDIHIYRLVSGNSIEEKLLKNGTKDL 1882
Cdd:PLN03142 549 AGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKL 613
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
1695-1876 |
3.11e-29 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 127.26 E-value: 3.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1695 SLYSSRLRALRQCLREHTGPYHR--QLQQLTALR------SLQFPELRLVQFDSGKLEALAILLQKLKSEGRRVLILSQM 1766
Cdd:COG0553 479 ALYEAVLEYLRRELEGAEGIRRRglILAALTRLRqicshpALLLEEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQF 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1767 VLMLDILEMFLNFHYLTYVRIDENANSEQRQELMRSFNRDRRIFCALLSTHSRATGINLVEADTVVFYDNDLNPVMDAKA 1846
Cdd:COG0553 559 TDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQA 638
|
170 180 190
....*....|....*....|....*....|
gi 190194425 1847 QEWCDRIGRCKDIHIYRLVSGNSIEEKLLK 1876
Cdd:COG0553 639 IDRAHRIGQTRDVQVYKLVAEGTIEEKILE 668
|
|
| HSA |
smart00573 |
domain in helicases and associated with SANT domains; |
726-797 |
3.18e-26 |
|
domain in helicases and associated with SANT domains;
Pssm-ID: 214727 [Multi-domain] Cd Length: 73 Bit Score: 104.02 E-value: 3.18e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190194425 726 PKLQEAPRPKSHWDYLLEEMQWMATDFAQERRWKLAAAKKLVRTVARHHEEKKLREERG-KKEEQSRLRRIAA 797
Cdd:smart00573 1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERReEKNEKRRLRKLAA 73
|
|
| HSA |
pfam07529 |
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ... |
728-794 |
1.63e-21 |
|
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. This region does not form a compact domain in the known structures.
Pssm-ID: 462194 [Multi-domain] Cd Length: 67 Bit Score: 90.32 E-value: 1.63e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 190194425 728 LQEAPR-PKSHWDYLLEEMQWMATDFAQERRWKLAAAKKLVRTVARHHEEKKLREERgKKEEQSRLRR 794
Cdd:pfam07529 1 RDEPERrEKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHKNIEKEEQK-RIEREEKQRL 67
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1010-1198 |
3.45e-17 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 82.54 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1010 PSLLYGALRDYQKIGLDWLAKLYRknlNGILADEAGLGKTVQIIAfFAHLACNEGNWGPHLVV--MRScniLK--WELEL 1085
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALL-PALEALKRGKGGRVLVLvpTRE---LAeqWAEEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1086 KRWCP--GLKTLSYVGSHRELKAKRQEWTepNNFHICITSYKQFFRGYT--AFSRVHWKCLVVDEMQRVKGMTER-HWEA 1160
Cdd:smart00487 75 KKLGPslGLKVVGLYGGDSKREQLRKLES--GKTDILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGGFGdQLEK 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 190194425 1161 IFKL--QSQQRLLL---IDVPLHNTFLELWTMVHFLIPGISRP 1198
Cdd:smart00487 153 LLKLlpKNVQLLLLsatPPEEIENLLELFLNDPVFIDVGFTPL 195
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1741-1856 |
1.02e-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: 72.63 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1741 GKLEALAILLQKlkSEGRRVLILSQMVLMLDIlEMFLNFHYLTYVRIDENANSEQRQELMRSFNRDRRIFcaLLSTHSRA 1820
Cdd:pfam00271 1 EKLEALLELLKK--ERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDV--LVATDVAE 75
|
90 100 110
....*....|....*....|....*....|....*.
gi 190194425 1821 TGINLVEADTVVFYDNDLNPVMDakAQewcdRIGRC 1856
Cdd:pfam00271 76 RGLDLPDVDLVINYDLPWNPASY--IQ----RIGRA 105
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1771-1856 |
8.85e-11 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 60.30 E-value: 8.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1771 DILEMFLNFHYLTYVRIDENANSEQRQELMRSFNRDRRIFcaLLSTHSRATGINLVEADTVVFYDNDLNPVMDakAQewc 1850
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKV--LVATDVAERGLDLPGVDLVIIYDLPWSPASY--IQ--- 73
|
....*.
gi 190194425 1851 dRIGRC 1856
Cdd:smart00490 74 -RIGRA 78
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
499-689 |
4.93e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.10 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 499 PSTGPPVQNAASLHTPPPQ--LPARLPPASVPATALPSTLQFSQQSQMVEASTQLQIPVKTQQLNAPIPAPLPS-QLPAP 575
Cdd:PHA03247 2686 RAARPTVGSLTSLADPPPPppTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARpPTTAG 2765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 576 SSQPAQPALHVPMPGKAQMQTSQLSSQTQTVASTRPPLDSAQPCQRSLPTSSSSSSLVPVSGSGPGPSPARSSPvNRPSS 655
Cdd:PHA03247 2766 PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP-PPPPG 2844
|
170 180 190
....*....|....*....|....*....|....
gi 190194425 656 ATNKALSPITSRSPGVAVSAPPKPQSPAQNAASS 689
Cdd:PHA03247 2845 PPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAP 2878
|
|
| SP4_N |
cd22536 |
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ... |
2779-2991 |
3.87e-06 |
|
N-terminal domain of transcription factor Specificity Protein (SP) 4; 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. Human SP4 is a risk gene of multiple psychiatric disorders including schizophrenia, bipolar disorder, and major depression. SP4 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. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP4.
Pssm-ID: 411773 [Multi-domain] Cd Length: 623 Bit Score: 52.61 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 2779 GISVAIGQPQKTAGQTVVAQPVNVQQLLkykQQTAVQQQKAIQPQVAQGQAAVQQKLTTQQITTQGPQQKVAYAAQPALK 2858
Cdd:cd22536 355 GLQNVQDQSNSLQQVQIVGQPILQQIQI---QQPQQQIIQAIQPQSFQLQSGQTIQTIQQQPLQNVQLQAVQSPTQVLIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 2859 TQFLTTP--IS----QAQKLAGTQQVQTQIqvAKLPQVVQQqTPVAS------IQQVA-----------SASQQASP--- 2912
Cdd:cd22536 432 APTLTPSgqISwqtvQVQNIQSLSNLQVQN--AGLPQQLTL-TPVSSsaggttIAQIApvavagtpitlNAAQLASVpnl 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 2913 QTVTLTQATAAGQQVQMIP-TVTATAQ--------LVQQKLIQQQVVTTASASLQTPGGPSPAQLPASSDSPSQQPKLQM 2983
Cdd:cd22536 509 QTVNVANLGAAGVQVQGVPvTITSVAGqqqgqdgvKVQQATIAPVTVAVGNIANATIGAVSPDQITQVQLQQAQQASDQE 588
|
....*...
gi 190194425 2984 RVPAVRLK 2991
Cdd:cd22536 589 VQPGKRLR 596
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
466-690 |
1.17e-05 |
|
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: 51.19 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 466 FKRQQVMPPTGGMPPTPQATQLTG----QKQSQQQYDP-STG----------PPVQNAASLHTPPPQLPArlPPASVPAT 530
Cdd:pfam09770 102 FNRQQPAARAAQSSAQPPASSLPQyqyaSQQSQQPSKPvRTGyekykepepiPDLQVDASLWGVAPKKAA--APAPAPQP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 531 ALPSTLQFSQQSQM-----VEASTQLQIPVKTQQlNAPIPAPLPSQLPAPSSQPAQpalHVPMPGKAQMQTSQLSSQTQT 605
Cdd:pfam09770 180 AAQPASLPAPSRKMmsleeVEAAMRAQAKKPAQQ-PAPAPAQPPAAPPAQQAQQQQ---QFPPQIQQQQQPQQQPQQPQQ 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 606 VASTRPPLDSAQPCQRSLPTSSSSSSLVPVSGSGPGPSPARSSPV------NRPSSatnkALSPITSRSPGVAVSAPPKP 679
Cdd:pfam09770 256 HPGQGHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTqilqnpNRLSA----ARVGYPQNPQPGVQPAPAHQ 331
|
250
....*....|.
gi 190194425 680 QSPAQNAASSQ 690
Cdd:pfam09770 332 AHRQQGSFGRQ 342
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1371-1590 |
2.43e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 50.32 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1371 ASPPPSARPAAVKLKASRLFQPVQYGQKPEGRTVAFPSTHPPRMANTNTSTATPQGQVRGRPPIAT-FSANPDTKGGEVV 1449
Cdd:PHA03247 2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPgPPPPSLPLGGSVA 2857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1450 KIAQLASIAGPQSRVAQPETPvtlqfqgnkftlSHSQLRQLTAGQPLQLQGSVLQivSAPGQPYLRAPGPVVMQTVSQAG 1529
Cdd:PHA03247 2858 PGGDVRRRPPSRSPAAKPAAP------------ARPPVRRLARPAVSRSTESFAL--PPDQPERPPQPQAPPPPQPQPQP 2923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1530 AVHSTLGSKPPTSGPSPAPLTPQVG-------------------VPGRVAVSAMAVGEPGLASK-PASPAAGPTQEEKSR 1589
Cdd:PHA03247 2924 PPPPQPQPPPPPPPRPQPPLAPTTDpagagepsgavpqpwlgalVPGRVAVPRFRVPQPAPSREaPASSTPPLTGHSLSR 3003
|
.
gi 190194425 1590 L 1590
Cdd:PHA03247 3004 V 3004
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
2730-2986 |
2.14e-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: 43.84 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 2730 PTSQLQAQGQMQTQTPQPAQVALAKPPVVSVPAAVVSSPGVTTLPMNVAGISV-AIGQPQKTAGQTVVAQpVNVQQLLKY 2808
Cdd:pfam09606 171 PNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAqANGGMNPQQMGGAPNQ-VAMQQQQPQ 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 2809 KQQTAVQQQKAIQP--QVAQGQAAVQQKLTTQQITTQGPQQKVAYAAQPALKTQFLTTPISQAQKLAGTQQVQTQIQVAK 2886
Cdd:pfam09606 250 QQGQQSQLGMGINQmqQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQ 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 2887 LPQVVQQQTPVASI---------QQVASASQQASPQTVTLTQATAAGQQV--QMIPTVTATAQLVQQKliQQQVVTTASA 2955
Cdd:pfam09606 330 MNQSVGQGGQVVALgglnhletwNPGNFGGLGANPMQRGQPGMMSSPSPVpgQQVRQVTPNQFMRQSP--QPSVPSPQGP 407
|
250 260 270
....*....|....*....|....*....|....*..
gi 190194425 2956 SLQTP----GG--PSPAQLPASSDSPSQQPKLQMRVP 2986
Cdd:pfam09606 408 GSQPPqshpGGmiPSPALIPSPSPQMSQQPAQQRTIG 444
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
2461-2602 |
8.16e-03 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 41.66 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 2461 TTVGSAAVLAGTIKTSVTGTSIPTGTVSGNVIVNTIAGVPAATFQSINKRLASPVAPGTLTTSGGSAPAQVVHTqqraVG 2540
Cdd:COG3469 88 AATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATG----GT 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 190194425 2541 SPATATTDLVSMTTTQGVRAVTSVTASAVVTTNLTPVQTPTrslvtqvSQATGVQLPGKTIT 2602
Cdd:COG3469 164 TTTSTTTTTTSASTTPSATTTATATTASGATTPSATTTATT-------TGPPTPGLPKHVLV 218
|
|
| |
|
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 ... |
1-451 |
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: 594.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1 MHHGSGPQNVQHQLQRSRSFTGSEE----EQPAHPNLPPSPAAPFAPSASPSAPQSPGYQIqqLMSRSPVAGQNVNITLQ 76
Cdd:pfam15790 1 MHHGSGSQNVQRQLQRSKSVSGSEEqqqeQQPATVNHPQSPVTTFAPAASPSAPQSPNYQI--IMSRSPVTGQNVNITLQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 77 NVGPVVGGNQQITLAPLPLPNPTSPGFQFGAQQRRFEHGSPSYIQVTSPMSQQVQTQSPTQPSPGPGQTLQnvRAGAPGP 156
Cdd:pfam15790 79 NVGQMVAGNQQITLTPLPLQSPASPGFQHSAPQWRFEHGSPSYIQVTSPLPQQVQPQSPTQHSPVPLQGVQ--RPGAPGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 157 GLGICSNSPTGgFVDASVLVRQISL-SPSSGGHFVFQEAPGLTQMAQG-AQVQLQHSGAPITVRERRLSQPHAQSGGTIH 234
Cdd:pfam15790 157 GLGVCGQSPTR-FVDASMLVRQISLgSPSGGGHFVYQDGTGLAQIAPGaGQVQLASPGTPGSVRERRLSQPHSQTGGTIH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 235 HLGPQSPAAAGgTGLQPLASPNHITTASLPPQISSIIQGQliqqqqqvlqgqpMNRSLGFERTPGVLLPGVGGPSA-FGM 313
Cdd:pfam15790 236 HLGPQSPAAAG-AGLQTLGSPGHITTSNLPPQISSIIQGQ-------------LARPLGFEKTAQVVVAGAGGPAAsFGI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 314 TSPPPPTSPSRTTMPPGLSSVPLTSMGSSG-MKKVPKKLEEIPPASQEMAQMRKQCLDYHYKEMEALKEVFKEYLIELFF 392
Cdd:pfam15790 302 PSSIPPTSPSRTSPPPGLSSNPLTSTGMSGsVKKVPKKLEEIAPATPEIAQLRKQCLDHHTKKMESLKEVFKEYLIELFF 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 190194425 393 LQHLQGNMMDFLAFKKKHYAPLQAYLRQNDLDIEEEEEEEEeeegKSEVINDEHQSLTG 451
Cdd:pfam15790 382 LQHLQGNMMDFLAFKKKHCVPLYTYLRQNDLDLEEEEEEEE----QSEVINDEVKVVTG 436
|
|
| DEXQc_SRCAP |
cd18003 |
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ... |
1017-1233 |
1.98e-125 |
|
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: 394.03 E-value: 1.98e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVMRSCNILKWELELKRWCPGLKTLS 1096
Cdd:cd18003 1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1097 YVGSHRELKAKRQEWTEPNNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQSQQRLLLIDVP 1176
Cdd:cd18003 81 YYGSAKERKLKRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190194425 1177 LHNTFLELWTMVHFLIPGI------SRPYLSFPLKAPNEENQDYYHKMVIRLHRVTQPFILRR 1233
Cdd:cd18003 161 LQNSLMELWSLMHFLMPHIfqshqeFKEWFSNPLTAMSEGSQEENEELVRRLHKVLRPFLLRR 223
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
1020-1300 |
3.92e-62 |
|
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: 215.24 E-value: 3.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1020 YQKIGLDWLAKLYRK-NLNGILADEAGLGKTVQIIAFFAHLACNEGNWG-PHLVVMRSCNILKWELELKRWC--PGLKTL 1095
Cdd:pfam00176 1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1096 SYVGSHRELKAKRQEWTEPNNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQSQQRLLLIDV 1175
Cdd:pfam00176 81 VLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1176 PLHNTFLELWTMVHFLIPGI------SRPYLSFPLKAPNEEnqdyyhKMVIRLHRVTQPFILRRTKRDVEKQLTRKYEHV 1249
Cdd:pfam00176 161 PLQNNLEELWALLNFLRPGPfgslstFRNWFDRPIERGGGK------KGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYI 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 190194425 1250 LKCRLSSRQKALYEDVILQPRTQEALKS----GHFVSVLSVLTRLQRICNHPGLV 1300
Cdd:pfam00176 235 LFCRLSKLQRKLYQTFLLKKDLNAIKTGeggrEIKASLLNILMRLRKICNHPGLI 289
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
779-1300 |
1.81e-61 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 225.49 E-value: 1.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 779 LREERGKKEEQSRLRRIAATTAREIEYFWSNIEQVVEIKLQVELEEKRKKALNLQKVSRRGKESRLKGFDTSPEHSLDLG 858
Cdd:COG0553 17 LTELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLRLLLALLLLAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 859 ISGRKRKASTSLTDDEVEDEEETIEEEEAHEGLVDHHTELTNLAKEAELPLIDLMKLYEGAFLPNFQWPQPEPDHEESSG 938
Cdd:COG0553 97 LLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 939 EEDVEDCPSDRESRRDSVLIDSLFIMDQFKAAERMSIGKSNTKDITEVTAVAEAILPkgsarvttavkfsAPSLLYGALR 1018
Cdd:COG0553 177 LLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALES-------------LPAGLKATLR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1019 DYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLAcNEGNWGPHLVVM-RSCnILKWELELKRWCPGLKTLSY 1097
Cdd:COG0553 244 PYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELK-ERGLARPVLIVApTSL-VGNWQRELAKFAPGLRVLVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1098 VGShrelkAKRQEWTEP-NNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQSQQRLLLIDVP 1176
Cdd:COG0553 322 DGT-----RERAKGANPfEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1177 LHNTFLELWTMVHFLIPGISRPYLSF------PLKAPNEENQDyyhkmviRLHRVTQPFILRRTKRDVEKQLTRKYEHVL 1250
Cdd:COG0553 397 VENRLEELWSLLDFLNPGLLGSLKAFrerfarPIEKGDEEALE-------RLRRLLRPFLLRRTKEDVLKDLPEKTEETL 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 190194425 1251 KCRLSSRQKALYEDVILQPRTQ--EALKSGHFVSVLSVLTRLQRICNHPGLV 1300
Cdd:COG0553 470 YVELTPEQRALYEAVLEYLRREleGAEGIRRRGLILAALTRLRQICSHPALL 521
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
1007-1312 |
7.26e-57 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 217.36 E-value: 7.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1007 FSAPSLLYGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVMRSCNILKWELELK 1086
Cdd:PLN03142 160 LVQPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIR 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1087 RWCPGLKTLSYVGSHRELKAKRQEWTEPNNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQS 1166
Cdd:PLN03142 240 RFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFST 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1167 QQRLLLIDVPLHNTFLELWTMVHFLIPGISRPYLSFP--LKAPNEENQdyyHKMVIRLHRVTQPFILRRTKRDVEKQLTR 1244
Cdd:PLN03142 320 NYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDewFQISGENDQ---QEVVQQLHKVLRPFLLRRLKSDVEKGLPP 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 190194425 1245 KYEHVLKCRLSSRQKALYEdVILQpRTQEALKSGHFVS-VLSVLTRLQRICNHPGLVEPRVPGSSFAAG 1312
Cdd:PLN03142 397 KKETILKVGMSQMQKQYYK-ALLQ-KDLDVVNAGGERKrLLNIAMQLRKCCNHPYLFQGAEPGPPYTTG 463
|
|
| DEXHc_SMARCA1_SMARCA5 |
cd17997 |
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ... |
1015-1235 |
2.32e-54 |
|
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: 190.23 E-value: 2.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1015 GALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVMRSCNILKWELELKRWCPGLKT 1094
Cdd:cd17997 2 GTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1095 LSYVGSHRELKAKRQEWTEPNNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQSQQRLLLID 1174
Cdd:cd17997 82 VVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 190194425 1175 VPLHNTFLELWTMVHFLIPGISRPYLSFPLKAPNEENQDYYHKMVIRLHRVTQPFILRRTK 1235
Cdd:cd17997 162 TPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDNQEVVQRLHKVLRPFLLRRIK 222
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
1017-1193 |
2.06e-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: 185.85 E-value: 2.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVMRSCNILKWELELKRWCPGLKTLS 1096
Cdd:cd17919 1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1097 YVGShRELKAKRQEWTEPNNFHICITSYkQFFRGYTA-FSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQSQQRLLLIDV 1175
Cdd:cd17919 81 YHGS-QRERAQIRAKEKLDKFDVVLTTY-ETLRRDKAsLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGT 158
|
170
....*....|....*...
gi 190194425 1176 PLHNTFLELWTMVHFLIP 1193
Cdd:cd17919 159 PLQNNLEELWALLDFLDP 176
|
|
| DEXQc_INO80 |
cd18002 |
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ... |
1017-1233 |
2.20e-51 |
|
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: 181.93 E-value: 2.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVMRSCNILKWELELKRWCPGLKTLS 1096
Cdd:cd18002 1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1097 YVGSHRELKAKRQEWTEPN------NFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQSQQRL 1170
Cdd:cd18002 81 YWGNPKDRKVLRKFWDRKNlytrdaPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 190194425 1171 LLIDVPLHNTFLELWTMVHFLIPGISRPYLSFP------LKAPNEENQDYYHKMVIRLHRVTQPFILRR 1233
Cdd:cd18002 161 LLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNewfskdIESHAENKTGLNEHQLKRLHMILKPFMLRR 229
|
|
| DEXHc_HELLS_SMARCA6 |
cd18009 |
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ... |
1015-1235 |
1.37e-48 |
|
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or SMARCA6) is a major epigenetic regulator crucial for normal heterochromatin structure and function. HELLS is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350767 [Multi-domain] Cd Length: 236 Bit Score: 174.11 E-value: 1.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1015 GALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNeGNWGPHLVVMRSCNILKWELELKRWCPGLKT 1094
Cdd:cd18009 2 GVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRER-GVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1095 LSYVGSHRE---LKAKRQEWTEP-NNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQSQQRL 1170
Cdd:cd18009 81 LLYHGTKEErerLRKKIMKREGTlQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 190194425 1171 LLIDVPLHNTFLELWTMVHFLIPGISRPYLSF--------------PLKAPNEENQDYYHKMvirLHRVTQPFILRRTK 1235
Cdd:cd18009 161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFeswfdfsslsdnaaDISNLSEEREQNIVHM---LHAILKPFLLRRLK 236
|
|
| DEXHc_SMARCA2_SMARCA4 |
cd17996 |
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ... |
1015-1235 |
4.74e-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: 172.55 E-value: 4.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1015 GALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVMRSCNILKWELELKRWCPGLKT 1094
Cdd:cd17996 2 GTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1095 LSYVGShRELKAKRQEWTEPNNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKgmtERHWEAIFKL----QSQQRL 1170
Cdd:cd17996 82 IVYKGT-PDVRKKLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMK---NAQSKLTQTLntyyHARYRL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 190194425 1171 LLIDVPLHNTFLELWTMVHFLIPGI-----------SRPYLSFPLKAPNEENQDyyHKMVI--RLHRVTQPFILRRTK 1235
Cdd:cd17996 158 LLTGTPLQNNLPELWALLNFLLPKIfkscktfeqwfNTPFANTGEQVKIELNEE--ETLLIirRLHKVLRPFLLRRLK 233
|
|
| DEXHc_SMARCA5 |
cd18064 |
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ... |
1009-1245 |
1.18e-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: 171.77 E-value: 1.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1009 APSLL-YGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVMRSCNILKWELELKR 1087
Cdd:cd18064 7 SPSYVkWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1088 WCPGLKTLSYVGSHRELKAKRQEWTEPNNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQSQ 1167
Cdd:cd18064 87 WVPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTT 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 190194425 1168 QRLLLIDVPLHNTFLELWTMVHFLIPGISRPYLSFPlKAPNEENQDYYHKMVIRLHRVTQPFILRRTKRDVEKQLTRK 1245
Cdd:cd18064 167 NRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFD-SWFDTNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSLPPK 243
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
1015-1235 |
3.05e-46 |
|
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: 166.59 E-value: 3.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1015 GALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLAcNEGNWGPHLVVMRSCNILKWELELKRWCPGLKT 1094
Cdd:cd18012 3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRK-EEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1095 LSYVGShrelKAKRQEWTEPNNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQSQQRLLLID 1174
Cdd:cd18012 82 LVIHGT----KRKREKLRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 190194425 1175 VPLHNTFLELWTMVHFLIPGI-------SRPYLSFPLKAPNEENQDyyhkmviRLHRVTQPFILRRTK 1235
Cdd:cd18012 158 TPIENHLGELWSIFDFLNPGLlgsykrfKKRFAKPIEKDGDEEALE-------ELKKLISPFILRRLK 218
|
|
| DEXHc_CHD1_2 |
cd17993 |
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ... |
1017-1233 |
1.10e-45 |
|
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and similar proteins; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as the substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but is also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. Both are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350751 [Multi-domain] Cd Length: 218 Bit Score: 165.22 E-value: 1.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVMRSCNILKWELELKRWCPGLKTLS 1096
Cdd:cd17993 2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1097 YVGSHRELKAKRQ-EW----TEPNNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQSQQRLL 1171
Cdd:cd17993 82 YLGDIKSRDTIREyEFyfsqTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 190194425 1172 LIDVPLHNTFLELWTMVHFLIPGISRPYLSFPLkAPNEENQDYYHkmviRLHRVTQPFILRR 1233
Cdd:cd17993 162 ITGTPLQNSLKELWALLHFLMPGKFDIWEEFEE-EHDEEQEKGIA----DLHKELEPFILRR 218
|
|
| DEXHc_SMARCA1 |
cd18065 |
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ... |
1005-1235 |
1.28e-44 |
|
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 (SMARCA1, also called SNF2L) is a component of NURF (nucleosome-remodeling factor) and CERF (CECR2-containing-remodeling factor) complexes which promote the perturbation of chromatin structure in an ATP-dependent manner. SMARCA1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350823 [Multi-domain] Cd Length: 233 Bit Score: 162.88 E-value: 1.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1005 VKFS-APSLLYGA-LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVMRSCNILKWE 1082
Cdd:cd18065 2 VRFEeSPSYVKGGtLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1083 LELKRWCPGLKTLSYVGSHRELKAKRQEWTEPNNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIF 1162
Cdd:cd18065 82 NEFKRWVPSLRAVCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190194425 1163 KLQSQQRLLLIDVPLHNTFLELWTMVHFLIPGISRPYLSFPlKAPNEENQDYYHKMVIRLHRVTQPFILRRTK 1235
Cdd:cd18065 162 EFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFD-SWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 233
|
|
| DEXHc_SMARCAD1 |
cd17998 |
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ... |
1017-1193 |
2.70e-43 |
|
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: 157.16 E-value: 2.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLAcNEGNWGPHLVVMRSCNILKWELELKRWCPGLKTLS 1096
Cdd:cd17998 1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLK-EIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1097 YVGSHRELKAKRQ-EWTEPNNFHICITSY---------KQFFRgytafsRVHWKCLVVDEMQRVKGMTERHWEAIFKLQS 1166
Cdd:cd17998 80 YYGSQEERKHLRYdILKGLEDFDVIVTTYnlatsnpddRSFFK------RLKLNYVVYDEGHMLKNMTSERYRHLMTINA 153
|
170 180
....*....|....*....|....*..
gi 190194425 1167 QQRLLLIDVPLHNTFLELWTMVHFLIP 1193
Cdd:cd17998 154 NFRLLLTGTPLQNNLLELMSLLNFIMP 180
|
|
| DEXHc_CHD6_7_8_9 |
cd17995 |
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ... |
1017-1233 |
3.07e-41 |
|
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: 152.79 E-value: 3.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVMRSCNILKWELELKRWCPgLKTLS 1096
Cdd:cd17995 1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1097 YVGS----HRELKAKRQEWTEPNN-------FHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQ 1165
Cdd:cd17995 80 YHGSgesrQIIQQYEMYFKDAQGRkkkgvykFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190194425 1166 SQQRLLLIDVPLHNTFLELWTMVHFLIPGisrpylsfplKAPNEEN-QDYYHKM-----VIRLHRVTQPFILRR 1233
Cdd:cd17995 160 LEHKLLLTGTPLQNNTEELWSLLNFLEPE----------KFPSSEEfLEEFGDLktaeqVEKLQALLKPYMLRR 223
|
|
| DEXHc_CHD2 |
cd18054 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ... |
1010-1233 |
2.07e-39 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. CHD2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350812 [Multi-domain] Cd Length: 237 Bit Score: 147.84 E-value: 2.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1010 PSLLYGA---LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVMRSCNILKWELELK 1086
Cdd:cd18054 11 PSYIGGEnleLRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1087 RWCPGLKTLSYVGSHRELKAKRQ-EWTEPNN----FHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAI 1161
Cdd:cd18054 91 IWAPEINVVVYIGDLMSRNTIREyEWIHSQTkrlkFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 190194425 1162 FKLQSQQRLLLIDVPLHNTFLELWTMVHFLIPGISRPYLSFPLKAPNEENQDYYhkmviRLHRVTQPFILRR 1233
Cdd:cd18054 171 IDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENGYQ-----SLHKVLEPFLLRR 237
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
1740-1865 |
3.96e-39 |
|
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: 143.00 E-value: 3.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1740 SGKLEALAILLQKLKSEGRRVLILSQMVLMLDILEMFLNFHYLTYVRIDENANSEQRQELMRSFNRDRRIFCALLSTHSR 1819
Cdd:cd18793 10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 190194425 1820 ATGINLVEADTVVFYDNDLNPVMDAKAQEWCDRIGRCKDIHIYRLV 1865
Cdd:cd18793 90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
|
|
| DEXHc_CHD1L |
cd18006 |
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ... |
1017-1233 |
2.37e-37 |
|
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: 141.04 E-value: 2.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVMRSCNILKWELELKRWCPGLKTLS 1096
Cdd:cd18006 1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1097 YVGSHRELKAKRQEWTEPNNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQSQQRLLLIDVP 1176
Cdd:cd18006 81 YMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190194425 1177 LHNTFLELWTMVHFLIPGIsrpylsFPLKAPnEENQDYYHKM------VIRLHRVTQPFILRR 1233
Cdd:cd18006 161 IQNSLQELYALLSFIEPNV------FPKDKL-DDFIKAYSETddesetVEELHLLLQPFLLRR 216
|
|
| DEXHc_SMARCA4 |
cd18062 |
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ... |
1001-1235 |
1.26e-34 |
|
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: 134.79 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1001 VTTAVKFSAPSLLYGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVMRSCNILK 1080
Cdd:cd18062 8 VTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1081 WELELKRWCPGLKTLSYVGShrelKAKRQEWT---EPNNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKgmtERH 1157
Cdd:cd18062 88 WVYEFDKWAPSVVKVSYKGS----PAARRAFVpqlRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMK---NHH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1158 WEAIFKLQSQ----QRLLLIDVPLHNTFLELWTMVHFLIPGISRPYLSF------PLKAPNEE---NQDYYHKMVIRLHR 1224
Cdd:cd18062 161 CKLTQVLNTHyvapRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFeqwfnaPFAMTGEKvdlNEEETILIIRRLHK 240
|
250
....*....|.
gi 190194425 1225 VTQPFILRRTK 1235
Cdd:cd18062 241 VLRPFLLRRLK 251
|
|
| DEXHc_SMARCA2 |
cd18063 |
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ... |
1001-1235 |
2.35e-34 |
|
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: 133.65 E-value: 2.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1001 VTTAVKFSAPSLLYGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVMRSCNILK 1080
Cdd:cd18063 8 ITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1081 WELELKRWCPGLKTLSYVGShRELKAKRQEWTEPNNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKgmtERHWEA 1160
Cdd:cd18063 88 WTYEFDKWAPSVVKISYKGT-PAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMK---NHHCKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1161 IFKLQSQ----QRLLLIDVPLHNTFLELWTMVHFLIPGISRPYLSF------PLKAPNEE---NQDYYHKMVIRLHRVTQ 1227
Cdd:cd18063 164 TQVLNTHyvapRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFeqwfnaPFAMTGERvdlNEEETILIIRRLHKVLR 243
|
....*...
gi 190194425 1228 PFILRRTK 1235
Cdd:cd18063 244 PFLLRRLK 251
|
|
| DEXHc_Mot1 |
cd17999 |
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ... |
1017-1233 |
1.91e-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: 127.47 E-value: 1.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQ---IIAFFAHLACNEGNWG--PHLVVMRSCNILKWELELKRWCP- 1090
Cdd:cd17999 1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQtlcILASDHHKRANSFNSEnlPSLVVCPPTLVGHWVAEIKKYFPn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1091 -GLKTLSYVGSHRElkaKRQEWTEPNNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQSQQR 1169
Cdd:cd17999 81 aFLKPLAYVGPPQE---RRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190194425 1170 LLLIDVPLHNTFLELWTMVHFLIPG-----------ISRPYLSFPLKAPNEENQDYYHKMVIRLHRVTQPFILRR 1233
Cdd:cd17999 158 LILSGTPIQNNVLELWSLFDFLMPGylgtekqfqrrFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
|
|
| DEXHc_CHD1 |
cd18053 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ... |
1017-1233 |
2.46e-32 |
|
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: 127.47 E-value: 2.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVMRSCNILKWELELKRWCPGLKTLS 1096
Cdd:cd18053 21 LRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1097 YVGSHRELKAKR-QEWTEPNN----FHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQSQQRLL 1171
Cdd:cd18053 101 YLGDINSRNMIRtHEWMHPQTkrlkFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 190194425 1172 LIDVPLHNTFLELWTMVHFLIPGISRPYLSFplkapNEENQDYYHKMVIRLHRVTQPFILRR 1233
Cdd:cd18053 181 ITGTPLQNSLKELWSLLHFIMPEKFSSWEDF-----EEEHGKGREYGYASLHKELEPFLLRR 237
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
1739-1882 |
1.84e-31 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 135.70 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1739 DSGKLEALAILLQKLKSEGRRVLILSQMVLMLDILEMFLNFHYLTYVRIDENANSEQRQELMRSFNRD-RRIFCALLSTH 1817
Cdd:PLN03142 469 NSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTR 548
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190194425 1818 SRATGINLVEADTVVFYDNDLNPVMDAKAQEWCDRIGRCKDIHIYRLVSGNSIEEKLLKNGTKDL 1882
Cdd:PLN03142 549 AGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKL 613
|
|
| DEXHc_ERCC6 |
cd18000 |
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ... |
1017-1200 |
9.83e-30 |
|
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: 118.58 E-value: 9.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVMRSCNILKWELELKRWCPGLKTL- 1095
Cdd:cd18000 1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1096 -----SYVGSHRELKAKRQEW----TEPNNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQS 1166
Cdd:cd18000 81 lhssgSGTGSEEKLGSIERKSqlirKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRT 160
|
170 180 190
....*....|....*....|....*....|....
gi 190194425 1167 QQRLLLIDVPLHNTFLELWTMVHFLIPgisrPYL 1200
Cdd:cd18000 161 PHRLILSGTPIQNNLKELWSLFDFVFP----PYL 190
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
1695-1876 |
3.11e-29 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 127.26 E-value: 3.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1695 SLYSSRLRALRQCLREHTGPYHR--QLQQLTALR------SLQFPELRLVQFDSGKLEALAILLQKLKSEGRRVLILSQM 1766
Cdd:COG0553 479 ALYEAVLEYLRRELEGAEGIRRRglILAALTRLRqicshpALLLEEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQF 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1767 VLMLDILEMFLNFHYLTYVRIDENANSEQRQELMRSFNRDRRIFCALLSTHSRATGINLVEADTVVFYDNDLNPVMDAKA 1846
Cdd:COG0553 559 TDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQA 638
|
170 180 190
....*....|....*....|....*....|
gi 190194425 1847 QEWCDRIGRCKDIHIYRLVSGNSIEEKLLK 1876
Cdd:COG0553 639 IDRAHRIGQTRDVQVYKLVAEGTIEEKILE 668
|
|
| DEXHc_CHD3_4_5 |
cd17994 |
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ... |
1017-1233 |
1.77e-27 |
|
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: 112.15 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLAcNEGNW-GPHLVVMRSCNILKWELELKRWCPGLKTL 1095
Cdd:cd17994 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLY-KEGHSkGPFLVSAPLSTIINWEREFEMWAPDFYVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1096 SYVGShrelkakrqewtepnnfHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQSQQRLLLIDV 1175
Cdd:cd17994 80 TYVGD-----------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGT 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 190194425 1176 PLHNTFLELWTMVHFLIPGISRPYLSFPLKAPNEENQDyyhkMVIRLHRVTQPFILRR 1233
Cdd:cd17994 143 PLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKED----QIKKLHDLLGPHMLRR 196
|
|
| DEXHc_ERCC6L |
cd18001 |
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ... |
1017-1233 |
2.30e-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: 112.85 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLAcNEGNWGPHLVVMRSCNILKWELELKRWCPGLKTLS 1096
Cdd:cd18001 1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMF-DSGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1097 YVGSHRELKAKRQEWTEpNNFHICITSYKQFFRGYTAFSRVH-----WKCLVVDEMQRVKGMTERHWEAIFKLQSQQRLL 1171
Cdd:cd18001 80 FHGTSKKERERNLERIQ-RGGGVLLTTYGMVLSNTEQLSADDhdefkWDYVILDEGHKIKNSKTKSAKSLREIPAKNRII 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190194425 1172 LIDVPLHNTFLELWTMVHFLIPG--------ISRPYLSfPLKAPNEEN-----QDYYHKMVIRLHRVTQPFILRR 1233
Cdd:cd18001 159 LTGTPIQNNLKELWALFDFACNGsllgtrktFKMEFEN-PITRGRDKDatqgeKALGSEVAENLRQIIKPYFLRR 232
|
|
| HSA |
smart00573 |
domain in helicases and associated with SANT domains; |
726-797 |
3.18e-26 |
|
domain in helicases and associated with SANT domains;
Pssm-ID: 214727 [Multi-domain] Cd Length: 73 Bit Score: 104.02 E-value: 3.18e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190194425 726 PKLQEAPRPKSHWDYLLEEMQWMATDFAQERRWKLAAAKKLVRTVARHHEEKKLREERG-KKEEQSRLRRIAA 797
Cdd:smart00573 1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERReEKNEKRRLRKLAA 73
|
|
| DEXHc_CHD4 |
cd18056 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ... |
1017-1233 |
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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVMRSCNILKWELELKRWCPGLKTLS 1096
Cdd:cd18056 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1097 YVGSH------RE-------------LKAKRQEWTEPNNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERH 1157
Cdd:cd18056 81 YVGDKdsraiiREnefsfednairggKKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190194425 1158 WEAIFKLQSQQRLLLIDVPLHNTFLELWTMVHFLIPGISRPYLSFPLKAPNEENQDyyhkMVIRLHRVTQPFILRR 1233
Cdd:cd18056 161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKED----QIKKLHDMLGPHMLRR 232
|
|
| DEXHc_CHD5 |
cd18057 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ... |
1017-1233 |
1.20e-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: 107.84 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVMRSCNILKWELELKRWCPGLKTLS 1096
Cdd:cd18057 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1097 YVGSHRELKAKRQ-EWTEPNN------------------FHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERH 1157
Cdd:cd18057 81 YTGDKESRSVIREnEFSFEDNairsgkkvfrmkkeaqikFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190194425 1158 WEAIFKLQSQQRLLLIDVPLHNTFLELWTMVHFLIPGISRPYLSFPLKAPNEENQDyyhkMVIRLHRVTQPFILRR 1233
Cdd:cd18057 161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKED----QIKKLHDLLGPHMLRR 232
|
|
| DEXHc_CHD3 |
cd18055 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ... |
1017-1233 |
2.99e-25 |
|
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: 107.02 E-value: 2.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNEGNWGPHLVVMRSCNILKWELELKRWCPGLKTLS 1096
Cdd:cd18055 1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1097 YVGSH------RE-------------LKAKRQEWTEPNNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERH 1157
Cdd:cd18055 81 YTGDKdsraiiREnefsfddnavkggKKAFKMKREAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190194425 1158 WEAIFKLQSQQRLLLIDVPLHNTFLELWTMVHFLIPGISRPYLSFPLKAPNEENQDyyhkMVIRLHRVTQPFILRR 1233
Cdd:cd18055 161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKED----QIKKLHDLLGPHMLRR 232
|
|
| DEXHc_CHD6 |
cd18058 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ... |
1017-1233 |
1.06e-24 |
|
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: 105.12 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACnEGNWGPHLVVMRSCNILKWELELKRWCPgLKTLS 1096
Cdd:cd18058 1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFL-MGIRGPFLIIAPLSTITNWEREFRTWTE-MNAIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1097 YVGSH--RELKAK-----RQEWTEP----NNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQ 1165
Cdd:cd18058 79 YHGSQisRQMIQQyemyyRDEQGNPlsgiFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1166 SQQRLLLIDVPLHNTFLELWTMVHFLIPgisrpyLSFPLKAPN-EENQDY-YHKMVIRLHRVTQPFILRR 1233
Cdd:cd18058 159 LEHKVLLTGTPLQNSVEELFSLLNFLEP------SQFPSETTFlEEFGDLkTEEQVKKLQSILKPMMLRR 222
|
|
| DEXDc_SHPRH-like |
cd18008 |
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ... |
1017-1233 |
2.21e-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: 104.68 E-value: 2.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLakLYRknlNGILADEAGLGKTVQIIA---------------FFAHLACNEGNWGPH--LVVmrsC--N 1077
Cdd:cd18008 1 LLPYQKQGLAWM--LPR---GGILADEMGLGKTIQALAlilatrpqdpkipeeLEENSSDPKKLYLSKttLIV---VplS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1078 ILK-WELELKR--WCPGLKTLSYVGSHRELKAKrqewtEPNNFHICITSY-------KQFFRGYTAFS---------RVH 1138
Cdd:cd18008 73 LLSqWKDEIEKhtKPGSLKVYVYHGSKRIKSIE-----ELSDYDIVITTYgtlasefPKNKKGGGRDSkekeasplhRIR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1139 WKCLVVDEMQRVKGMTERHWEAIFKLQSQQRLLLIDVPLHNTFLELWTMVHFLI------PGISRPYLSFPLKAPNEENQ 1212
Cdd:cd18008 148 WYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRvepfgdYPWFNSDISKPFSKNDRKAL 227
|
250 260
....*....|....*....|.
gi 190194425 1213 DyyhkmviRLHRVTQPFILRR 1233
Cdd:cd18008 228 E-------RLQALLKPILLRR 241
|
|
| DEXHc_CHD7 |
cd18059 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ... |
1017-1233 |
2.58e-24 |
|
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: 103.96 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACnEGNWGPHLVVMRSCNILKWELELKRWCPgLKTLS 1096
Cdd:cd18059 1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYL-KGIHGPFLVIAPLSTIPNWEREFRTWTE-LNVVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1097 YVGSH---RELKAKRQEWTEPN--------NFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQ 1165
Cdd:cd18059 79 YHGSQasrRTIQLYEMYFKDPQgrvikgsyKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1166 SQQRLLLIDVPLHNTFLELWTMVHFLIPGisrpylSFPLKAP--NEENQDYYHKMVIRLHRVTQPFILRR 1233
Cdd:cd18059 159 LEHKVLLTGTPLQNTVEELFSLLHFLEPS------RFPSETTfmQEFGDLKTEEQVQKLQAILKPMMLRR 222
|
|
| DEXHc_ERCC6L2 |
cd18005 |
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ... |
1017-1233 |
2.90e-24 |
|
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: 104.38 E-value: 2.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHL---------ACN-----------EGNWGPHLVVMRSC 1076
Cdd:cd18005 1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVlgktgtrrdRENnrprfkkkppaSSAKKPVLIVAPLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1077 NILKWELELKRWcpG-LKTLSYVGSHRE------LKAKRQEwtepnnfhICITSYKQFFRGYTAFSRVHWKCLVVDEMQR 1149
Cdd:cd18005 81 VLYNWKDELDTW--GhFEVGVYHGSRKDdelegrLKAGRLE--------VVVTTYDTLRRCIDSLNSINWSAVIADEAHR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1150 VKGMTERHWEAIFKLQSQQRLLLIDVPLHNTFLELWTMVHFLIPGISRPYLSF------PLK------APNEENQdYYHK 1217
Cdd:cd18005 151 IKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFkkhfsePIKrgqrhtATARELR-LGRK 229
|
250
....*....|....*.
gi 190194425 1218 MVIRLHRVTQPFILRR 1233
Cdd:cd18005 230 RKQELAVKLSKFFLRR 245
|
|
| DEXHc_CHD8 |
cd18060 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ... |
1017-1233 |
4.52e-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: 103.21 E-value: 4.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLAcNEGNWGPHLVVMRSCNILKWELELKRWCPgLKTLS 1096
Cdd:cd18060 1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVY-NVGIHGPFLVIAPLSTITNWEREFNTWTE-MNTIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1097 YVGS--HRELKAKRQEWTEPNNFHIC---------ITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQ 1165
Cdd:cd18060 79 YHGSlaSRQMIQQYEMYCKDSRGRLIpgaykfdalITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 190194425 1166 SQQRLLLIDVPLHNTFLELWTMVHFLIPGisrpylSFPLKApnEENQDY----YHKMVIRLHRVTQPFILRR 1233
Cdd:cd18060 159 LEHKVLLTGTPLQNTVEELFSLLHFLEPS------QFPSES--EFLKDFgdlkTEEQVQKLQAILKPMMLRR 222
|
|
| DEXHc_RAD54 |
cd18004 |
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ... |
1017-1233 |
1.96e-23 |
|
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: 101.98 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAK--LYRKNLNG---ILADEAGLGKTVQIIAFFAHLACNEGNWGPH----LVVMRSCNILKWELELKR 1087
Cdd:cd18004 1 LRPHQREGVQFLYDclTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKPTakkaLIVCPSSLVGNWKAEFDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1088 WCPG--LKTLSYVGSHRELKAKRQEWTEPNNFHICITSYKQFFRGYTAFSRVHwKC--LVVDEMQRVKGMTERHWEAIFK 1163
Cdd:cd18004 81 WLGLrrIKVVTADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKKI-SIdlLICDEGHRLKNSESKTTKALNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1164 LQSQQRLLLIDVPLHNTFLELWTMVHFLIPGI-----------SRPYLSFPLKAPNEENQDYYHKMVIRLHRVTQPFILR 1232
Cdd:cd18004 160 LPCRRRLLLTGTPIQNDLDEFFALVDFVNPGIlgslasfrkvfEEPILRSRDPDASEEDKELGAERSQELSELTSRFILR 239
|
.
gi 190194425 1233 R 1233
Cdd:cd18004 240 R 240
|
|
| DEXHc_CHD9 |
cd18061 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ... |
1017-1233 |
8.68e-23 |
|
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: 99.31 E-value: 8.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACNeGNWGPHLVVMRSCNILKWELELKRWCpGLKTLS 1096
Cdd:cd18061 1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLT-GIRGPFLIIAPLSTIANWEREFRTWT-DLNVVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1097 YVGS--HRELKAKRQEWTEPNN---------FHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQ 1165
Cdd:cd18061 79 YHGSliSRQMIQQYEMYFRDSQgriirgayrFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 190194425 1166 SQQRLLLIDVPLHNTFLELWTMVHFLIPgisrpyLSFPlkAPNEENQDY----YHKMVIRLHRVTQPFILRR 1233
Cdd:cd18061 159 LEHKVLLTGTPLQNTVEELFSLLHFLEP------LRFP--SESTFMQEFgdlkTEEQVQKLQAILKPMMLRR 222
|
|
| HSA |
pfam07529 |
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ... |
728-794 |
1.63e-21 |
|
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. This region does not form a compact domain in the known structures.
Pssm-ID: 462194 [Multi-domain] Cd Length: 67 Bit Score: 90.32 E-value: 1.63e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 190194425 728 LQEAPR-PKSHWDYLLEEMQWMATDFAQERRWKLAAAKKLVRTVARHHEEKKLREERgKKEEQSRLRR 794
Cdd:pfam07529 1 RDEPERrEKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHKNIEKEEQK-RIEREEKQRL 67
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
1010-1198 |
3.45e-17 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 82.54 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1010 PSLLYGALRDYQKIGLDWLAKLYRknlNGILADEAGLGKTVQIIAfFAHLACNEGNWGPHLVV--MRScniLK--WELEL 1085
Cdd:smart00487 2 EKFGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLAALL-PALEALKRGKGGRVLVLvpTRE---LAeqWAEEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1086 KRWCP--GLKTLSYVGSHRELKAKRQEWTepNNFHICITSYKQFFRGYT--AFSRVHWKCLVVDEMQRVKGMTER-HWEA 1160
Cdd:smart00487 75 KKLGPslGLKVVGLYGGDSKREQLRKLES--GKTDILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGGFGdQLEK 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 190194425 1161 IFKL--QSQQRLLL---IDVPLHNTFLELWTMVHFLIPGISRP 1198
Cdd:smart00487 153 LLKLlpKNVQLLLLsatPPEEIENLLELFLNDPVFIDVGFTPL 195
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1741-1856 |
1.02e-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: 72.63 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1741 GKLEALAILLQKlkSEGRRVLILSQMVLMLDIlEMFLNFHYLTYVRIDENANSEQRQELMRSFNRDRRIFcaLLSTHSRA 1820
Cdd:pfam00271 1 EKLEALLELLKK--ERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDV--LVATDVAE 75
|
90 100 110
....*....|....*....|....*....|....*.
gi 190194425 1821 TGINLVEADTVVFYDNDLNPVMDakAQewcdRIGRC 1856
Cdd:pfam00271 76 RGLDLPDVDLVINYDLPWNPASY--IQ----RIGRA 105
|
|
| DEXHc_RAD54B |
cd18066 |
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ... |
1017-1233 |
2.01e-14 |
|
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: 75.27 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWL-----AKLYRKNLNGILADEAGLGKTVQIIAFFAHLACnEGNWGPH------LVVMRSCNILKWELEL 1085
Cdd:cd18066 1 LRPHQREGIEFLyecvmGMRVNERFGAILADEMGLGKTLQCISLIWTLLR-QGPYGGKpvikraLIVTPGSLVKNWKKEF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1086 KRWcpglktlsyVGSHR------ELKAKRQEWTEPNNFHICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWE 1159
Cdd:cd18066 80 QKW---------LGSERikvftvDQDHKVEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1160 AIFKLQSQQRLLLIDVPLHNTFLELWTMVHFLIPGI-----------SRPYLSFPLKAPNEENQDYYHKMVIRLHRVTQP 1228
Cdd:cd18066 151 ALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGIlgslstyrkvyEEPIVRSREPTATPEEKKLGEARAAELTRLTGL 230
|
....*
gi 190194425 1229 FILRR 1233
Cdd:cd18066 231 FILRR 235
|
|
| DEXHc_ATRX-like |
cd18007 |
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ... |
1039-1202 |
1.69e-13 |
|
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: 72.71 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1039 ILADEAGLGKTVQIIAFF-AHLACNEGNWGPHLVVMRSCnILKWELELKRWC-----PGLKTLSYVGSHRELKAKR--QE 1110
Cdd:cd18007 30 ILAHTMGLGKTLQVITFLhTYLAAAPRRSRPLVLCPAST-LYNWEDEFKKWLppdlrPLLVLVSLSASKRADARLRkiNK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1111 WTEP--------NNFHIcITSYKQFFRGYTAfSRVHWKC------LVVDEMQRVKGMTERHWEAIFKLQSQQRLLLIDVP 1176
Cdd:cd18007 109 WHKEggvlligyELFRN-LASNATTDPRLKQ-EFIAALLdpgpdlLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTP 186
|
170 180
....*....|....*....|....*.
gi 190194425 1177 LHNTFLELWTMVHFLIPGISRPYLSF 1202
Cdd:cd18007 187 LQNNLKEYWTMVDFARPKYLGTLKEF 212
|
|
| DEXHc_HARP_SMARCAL1 |
cd18010 |
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ... |
1017-1195 |
1.56e-12 |
|
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: 69.16 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAklyRKNLNGILADEAGLGKTVQIIAFFAHLacnEGNWgPHLVVMRSCNILKWELELKRWCPGLKTLS 1096
Cdd:cd18010 1 LLPFQREGVCFAL---RRGGRVLIADEMGLGKTVQAIAIAAYY---REEW-PLLIVCPSSLRLTWADEIERWLPSLPPDD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1097 ---YVGSHRELKAKRQEwtepnnfhICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAIFKL--QSQQRLL 1171
Cdd:cd18010 74 iqvIVKSKDGLRDGDAK--------VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLlkRAKRVIL 145
|
170 180
....*....|....*....|....
gi 190194425 1172 LIDVPLHNTFLELWTMVHFLIPGI 1195
Cdd:cd18010 146 LSGTPALSRPIELFTQLDALDPKL 169
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1771-1856 |
8.85e-11 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 60.30 E-value: 8.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1771 DILEMFLNFHYLTYVRIDENANSEQRQELMRSFNRDRRIFcaLLSTHSRATGINLVEADTVVFYDNDLNPVMDakAQewc 1850
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKV--LVATDVAERGLDLPGVDLVIIYDLPWSPASY--IQ--- 73
|
....*.
gi 190194425 1851 dRIGRC 1856
Cdd:smart00490 74 -RIGRA 78
|
|
| DEXHc_RAD54A |
cd18067 |
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ... |
1017-1195 |
1.39e-09 |
|
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: 61.33 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAK----LYRKNLNG-ILADEAGLGKTVQIIAFFAHLACNEGNWGPHL----VVMRSCNILKWELELKR 1087
Cdd:cd18067 1 LRPHQREGVKFLYRcvtgRRIRGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaiVVSPSSLVKNWANELGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1088 WC-PGLKTLSYVG-SHRELKAKRQEWTEPNNFH----ICITSYKQFFRGYTAFSRVHWKCLVVDEMQRVKGMTERHWEAI 1161
Cdd:cd18067 81 WLgGRLQPLAIDGgSKKEIDRKLVQWASQQGRRvstpVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
|
170 180 190
....*....|....*....|....*....|....
gi 190194425 1162 FKLQSQQRLLLIDVPLHNTFLELWTMVHFLIPGI 1195
Cdd:cd18067 161 DSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGI 194
|
|
| DEXHc_ARIP4 |
cd18069 |
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ... |
1039-1212 |
3.51e-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: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1039 ILADEAGLGKTVQIIAF----FAHLACNEGnwgphLVVMRSCNILKWELELKRWCPGLKTLSYVG-----------SHRE 1103
Cdd:cd18069 32 ILAHSMGLGKTLQVISFldvlLRHTGAKTV-----LAIVPVNTLQNWLSEFNKWLPPPEALPNVRprpfkvfilndEHKT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1104 LKAKRQ---EWTEPNNFhicitsykqFFRGYTAFS-RVHWKCLVVDEMQRVKGMTERHWEAIFKLQSQQRLLLIDVPLHN 1179
Cdd:cd18069 107 TAARAKvieDWVKDGGV---------LLMGYEMFRlRPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQN 177
|
170 180 190
....*....|....*....|....*....|....*
gi 190194425 1180 TFLELWTMVHFLIPGI--SRPYLSFPLKAPNEENQ 1212
Cdd:cd18069 178 NLIEYWCMVDFVRPDFlgTRQEFSNMFERPILNGQ 212
|
|
| DEXHc_TTF2 |
cd18072 |
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ... |
1017-1191 |
4.12e-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: 56.72 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLakLYRKNLN---GILADEAGLGKTVQIIAFFahLACNEG-------------NWGPHL--VVMRSCNI 1078
Cdd:cd18072 1 LLLHQKQALAWL--LWRERQKprgGILADDMGLGKTLTMIALI--LAQKNTqnrkeeekekaltEWESKKdsTLVPSAGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1079 L---------KWELELKRWCPG--LKTLSYVGSHRELKAKRQEwtepnNFHICITSYKQFFR---------GYTAFSRVH 1138
Cdd:cd18072 77 LvvcpaslvhQWKNEVESRVASnkLRVCLYHGPNRERIGEVLR-----DYDIVITTYSLVAKeiptykeesRSSPLFRIA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 190194425 1139 WKCLVVDEMQRVKGMTERHWEAIFKLQSQQRLLLIDVPLHNTFLELWTMVHFL 1191
Cdd:cd18072 152 WARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFL 204
|
|
| DEXHc_ATRX |
cd18068 |
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ... |
1038-1195 |
2.31e-07 |
|
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: 54.51 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1038 GILADEAGLGKTVQIIAFFAHLACNE--GNWGPHLVVMRSCNILKWELELKRWCPGLK--------TLSYVGSHRELKAK 1107
Cdd:cd18068 31 CILAHCMGLGKTLQVVTFLHTVLLCEklENFSRVLVVCPLNTVLNWLNEFEKWQEGLKdeekievnELATYKRPQERSYK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1108 RQEWTEPNNfhICITSYkQFFRGYTAFSRVHWKC-----------------LVVDEMQRVKGMTERHWEAIFKLQSQQRL 1170
Cdd:cd18068 111 LQRWQEEGG--VMIIGY-DMYRILAQERNVKSREklkeifnkalvdpgpdfVVCDEGHILKNEASAVSKAMNSIRTKRRI 187
|
170 180
....*....|....*....|....*
gi 190194425 1171 LLIDVPLHNTFLELWTMVHFLIPGI 1195
Cdd:cd18068 188 VLTGTPLQNNLIEYHCMVNFVKPNL 212
|
|
| DEXQc_SHPRH |
cd18070 |
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ... |
1017-1154 |
3.09e-07 |
|
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: 54.27 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLaklyrKNLNGILADEAGLGKTVQIIAF-FAH-----------LACNEGNWGPHLVV---MRSCN---- 1077
Cdd:cd18070 1 LLPYQRRAVNWM-----LVPGGILADEMGLGKTVEVLALiLLHprpdndldaadDDSDEMVCCPDCLVaetPVSSKatli 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1078 -----ILK-WELELKRWCP-GLKTLSYVGSHRELKAKRQEWTEPNNFHICITSYK-------------------QFFRGY 1131
Cdd:cd18070 76 vcpsaILAqWLDEINRHVPsSLKVLTYQGVKKDGALASPAPEILAEYDIVVTTYDvlrtelhyaeanrsnrrrrRQKRYE 155
|
170 180
....*....|....*....|....*.
gi 190194425 1132 ---TAFSRVHWKCLVVDEMQRVKGMT 1154
Cdd:cd18070 156 appSPLVLVEWWRVCLDEAQMVESST 181
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
499-689 |
4.93e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.10 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 499 PSTGPPVQNAASLHTPPPQ--LPARLPPASVPATALPSTLQFSQQSQMVEASTQLQIPVKTQQLNAPIPAPLPS-QLPAP 575
Cdd:PHA03247 2686 RAARPTVGSLTSLADPPPPppTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARpPTTAG 2765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 576 SSQPAQPALHVPMPGKAQMQTSQLSSQTQTVASTRPPLDSAQPCQRSLPTSSSSSSLVPVSGSGPGPSPARSSPvNRPSS 655
Cdd:PHA03247 2766 PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP-PPPPG 2844
|
170 180 190
....*....|....*....|....*....|....
gi 190194425 656 ATNKALSPITSRSPGVAVSAPPKPQSPAQNAASS 689
Cdd:PHA03247 2845 PPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAP 2878
|
|
| SP4_N |
cd22536 |
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ... |
2779-2991 |
3.87e-06 |
|
N-terminal domain of transcription factor Specificity Protein (SP) 4; 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. Human SP4 is a risk gene of multiple psychiatric disorders including schizophrenia, bipolar disorder, and major depression. SP4 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. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP4.
Pssm-ID: 411773 [Multi-domain] Cd Length: 623 Bit Score: 52.61 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 2779 GISVAIGQPQKTAGQTVVAQPVNVQQLLkykQQTAVQQQKAIQPQVAQGQAAVQQKLTTQQITTQGPQQKVAYAAQPALK 2858
Cdd:cd22536 355 GLQNVQDQSNSLQQVQIVGQPILQQIQI---QQPQQQIIQAIQPQSFQLQSGQTIQTIQQQPLQNVQLQAVQSPTQVLIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 2859 TQFLTTP--IS----QAQKLAGTQQVQTQIqvAKLPQVVQQqTPVAS------IQQVA-----------SASQQASP--- 2912
Cdd:cd22536 432 APTLTPSgqISwqtvQVQNIQSLSNLQVQN--AGLPQQLTL-TPVSSsaggttIAQIApvavagtpitlNAAQLASVpnl 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 2913 QTVTLTQATAAGQQVQMIP-TVTATAQ--------LVQQKLIQQQVVTTASASLQTPGGPSPAQLPASSDSPSQQPKLQM 2983
Cdd:cd22536 509 QTVNVANLGAAGVQVQGVPvTITSVAGqqqgqdgvKVQQATIAPVTVAVGNIANATIGAVSPDQITQVQLQQAQQASDQE 588
|
....*...
gi 190194425 2984 RVPAVRLK 2991
Cdd:cd22536 589 VQPGKRLR 596
|
|
| DEXHc_HLTF1_SMARC3 |
cd18071 |
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ... |
1038-1191 |
5.93e-06 |
|
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: 50.16 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1038 GILADEAGLGKTVQIIAFFAhlacnegnWGPHLVVMRSCNILKWELELKRWC-PG-LKTLSYVGSHRELKAkrqewTEPN 1115
Cdd:cd18071 51 GILADDMGLGKTLTTISLIL--------ANFTLIVCPLSVLSNWETQFEEHVkPGqLKVYTYHGGERNRDP-----KLLS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1116 NFHICITSYKQFFRGYTA-----FSRVHWKCLVVDEMQRVKGMTERHWEAIFKLQSQQRLLLIDVPLHNTFLELWTMVHF 1190
Cdd:cd18071 118 KYDIVLTTYNTLASDFGAkgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSF 197
|
.
gi 190194425 1191 L 1191
Cdd:cd18071 198 L 198
|
|
| SP2_N |
cd22540 |
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ... |
2731-2970 |
7.63e-06 |
|
N-terminal domain of transcription factor Specificity Protein (SP) 2; 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. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 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. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.
Pssm-ID: 411776 [Multi-domain] Cd Length: 511 Bit Score: 51.47 E-value: 7.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 2731 TSQLQAQGQMQTQTPQPAQVALAKPPVVSVPAAVVSSPGVT-TLPMNVAG---ISVAIGQPQKTAGQTVVAQPVNVQQLL 2806
Cdd:cd22540 156 TPVQVLQQPQQAHKPVPIKPAPLQTSNTNSASLQVPGNVIKlQSGGNVALtlpVNNLVGTQDGATQLQLAAAPSKPSKKI 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 2807 KYKQQTAVQQQKAIQPQVA----------QGQAAVQQKLTTQQITTQGPQQKVAYAAQPALKTQFLTTPiSQAQKLAGTQ 2876
Cdd:cd22540 236 RKKSAQAAQPAVTVAEQVEtvliettadnIIQAGNNLLIVQSPGTGQPAVLQQVQVLQPKQEQQVVQIP-QQALRVVQAA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 2877 QVQTQIQVAKLPQVVQQQTPVASIQQVASASQQASPQTVTLTQATAAgqqvqMIPTVTATAQLVQQKLIQQQVVTTASAS 2956
Cdd:cd22540 315 SATLPTVPQKPLQNIQIQNSEPTPTQVYIKTPSGEVQTVLLQEAPAA-----TATPSSSTSTVQQQVTANNGTGTSKPNY 389
|
250
....*....|....
gi 190194425 2957 LQTPGGPSPAQLPA 2970
Cdd:cd22540 390 NVRKERTLPKIAPA 403
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
1039-1194 |
8.09e-06 |
|
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: 49.21 E-value: 8.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1039 ILADEAGLGKTVQIIAfFAHLACNEGNWGPHLVVMRSCNILKWELELKRWCpGLKTLSYVGSHRElKAKRQEWTEPNNFH 1118
Cdd:cd18011 21 LLADEVGLGKTIEAGL-IIKELLLRGDAKRVLILCPASLVEQWQDELQDKF-GLPFLILDRETAA-QLRRLIGNPFEEFP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1119 ICITSYKQFFRG---YTAFSRVHWKCLVVDEMQRVKGM-----TERhWEAIFKLQSQQR--LLLIDVPLHNTFLELWTMV 1188
Cdd:cd18011 98 IVIVSLDLLKRSeerRGLLLSEEWDLVVVDEAHKLRNSgggkeTKR-YKLGRLLAKRARhvLLLTATPHNGKEEDFRALL 176
|
....*.
gi 190194425 1189 HFLIPG 1194
Cdd:cd18011 177 SLLDPG 182
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
466-690 |
1.17e-05 |
|
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: 51.19 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 466 FKRQQVMPPTGGMPPTPQATQLTG----QKQSQQQYDP-STG----------PPVQNAASLHTPPPQLPArlPPASVPAT 530
Cdd:pfam09770 102 FNRQQPAARAAQSSAQPPASSLPQyqyaSQQSQQPSKPvRTGyekykepepiPDLQVDASLWGVAPKKAA--APAPAPQP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 531 ALPSTLQFSQQSQM-----VEASTQLQIPVKTQQlNAPIPAPLPSQLPAPSSQPAQpalHVPMPGKAQMQTSQLSSQTQT 605
Cdd:pfam09770 180 AAQPASLPAPSRKMmsleeVEAAMRAQAKKPAQQ-PAPAPAQPPAAPPAQQAQQQQ---QFPPQIQQQQQPQQQPQQPQQ 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 606 VASTRPPLDSAQPCQRSLPTSSSSSSLVPVSGSGPGPSPARSSPV------NRPSSatnkALSPITSRSPGVAVSAPPKP 679
Cdd:pfam09770 256 HPGQGHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTqilqnpNRLSA----ARVGYPQNPQPGVQPAPAHQ 331
|
250
....*....|.
gi 190194425 680 QSPAQNAASSQ 690
Cdd:pfam09770 332 AHRQQGSFGRQ 342
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
490-620 |
1.19e-05 |
|
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: 51.19 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 490 QKQSQQQYDPSTGPPVQNAASLHTPPPQLPARLPPasvpatalPSTLQFSQQSQMVEASTQLQIPVKTQQLNAPIPAPLP 569
Cdd:pfam09770 228 QQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHP--------VTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQP 299
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 190194425 570 SQ-LPAPSSQPA-QPALHVPMPGKAQMQTSQLSSQTQTVASTRPPLdSAQPCQ 620
Cdd:pfam09770 300 TQiLQNPNRLSAaRVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPI-ITHPQQ 351
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
499-695 |
2.07e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 50.26 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 499 PSTGPPVQNAASLHTPPPQLPARLPPASVPATALPS--TLQFSQQSQMVEASTqlqipvktqqlnAPIPAPLPSQLPAPS 576
Cdd:PRK12323 394 AAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPApeALAAARQASARGPGG------------APAPAPAPAAAPAAA 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 577 SQPAQPALHVPMPGKAQMQTSQLSSQTQTVASTRPPLDSAQPCQRSLPTSSSSSSLVPVSGSGPGPSPARSSPvnrpsSA 656
Cdd:PRK12323 462 ARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADP-----DD 536
|
170 180 190
....*....|....*....|....*....|....*....
gi 190194425 657 TNKALSPITSRSPGVAVSAPPKPQSPAQNAASSQDGSQD 695
Cdd:PRK12323 537 AFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPD 575
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1371-1590 |
2.43e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 50.32 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1371 ASPPPSARPAAVKLKASRLFQPVQYGQKPEGRTVAFPSTHPPRMANTNTSTATPQGQVRGRPPIAT-FSANPDTKGGEVV 1449
Cdd:PHA03247 2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPgPPPPSLPLGGSVA 2857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1450 KIAQLASIAGPQSRVAQPETPvtlqfqgnkftlSHSQLRQLTAGQPLQLQGSVLQivSAPGQPYLRAPGPVVMQTVSQAG 1529
Cdd:PHA03247 2858 PGGDVRRRPPSRSPAAKPAAP------------ARPPVRRLARPAVSRSTESFAL--PPDQPERPPQPQAPPPPQPQPQP 2923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1530 AVHSTLGSKPPTSGPSPAPLTPQVG-------------------VPGRVAVSAMAVGEPGLASK-PASPAAGPTQEEKSR 1589
Cdd:PHA03247 2924 PPPPQPQPPPPPPPRPQPPLAPTTDpagagepsgavpqpwlgalVPGRVAVPRFRVPQPAPSREaPASSTPPLTGHSLSR 3003
|
.
gi 190194425 1590 L 1590
Cdd:PHA03247 3004 V 3004
|
|
| DEXQc_bact_SNF2 |
cd18013 |
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ... |
1017-1191 |
3.31e-05 |
|
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: 47.73 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLDWLAKLYRknlNGILADeAGLGKTVQIIAFFAHLACnEGNWGPHLV-----VMRScnilKWELELKRWcPG 1091
Cdd:cd18013 1 PHPYQKVAINFIIEHPY---CGLFLD-MGLGKTVTTLTALSDLQL-DDFTRRVLViaplrVARS----TWPDEVEKW-NH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1092 LKTLSY---VGSHREL-KAKRQEWT----EPNNFHICITSYKQFFrgytafsrvHWKCLVVDEMQRVKGMTERHWEAIFK 1163
Cdd:cd18013 71 LRNLTVsvaVGTERQRsKAANTPADlyviNRENLKWLVNKSGDPW---------PFDMVVIDELSSFKSPRSKRFKALRK 141
|
170 180 190
....*....|....*....|....*....|
gi 190194425 1164 LQSQ-QRLL-LIDVPLHNTFLELWTMVHFL 1191
Cdd:cd18013 142 VRPViKRLIgLTGTPSPNGLMDLWAQIALL 171
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
457-695 |
5.43e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 49.01 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 457 PGSATEADPFKRQQVMPPTGGMPPTPQATQLTGQKQSQQQYDPSTGPPVQNAASLHTPPPQLPARLPP---------ASV 527
Cdd:PHA03307 73 PGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPvgspgpppaASP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 528 PATALPSTLQFSQQSQMVEASTQLQIPVKTQQLNAPIPAPLPSQLPAPSSQPAQPALHVPM--------PGKAQMQTSQL 599
Cdd:PHA03307 153 PAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPIsasasspaPAPGRSAADDA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 600 SSQTQTVASTRPPLDSAQPCQRSLPTSSSSSSLVPVSGSGPGPSPARSSPVNRPSSatnkalSPITSRSPGVAVSAPPKP 679
Cdd:PHA03307 233 GASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSS------SSPRERSPSPSPSSPGSG 306
|
250
....*....|....*.
gi 190194425 680 QSPAQNAASSQDGSQD 695
Cdd:PHA03307 307 PAPSSPRASSSSSSSR 322
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
499-694 |
1.01e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 48.40 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 499 PSTGPPVQNAAslhTPPPQLPArlPPASVPATALPSTLQFSQQSQMVEASTQLQIPVKTQQLNAPIPAPLPSQLPAPSSQ 578
Cdd:PHA03247 2767 PAPAPPAAPAA---GPPRRLTR--PAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPP 2841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 579 PAQPALHVPMPGKAQMQTSQLSSQTQTVASTRPPLDSAQPCQRSLPTSSSSSSLVPVSGSGPGPSPARSSPVNRPSSATN 658
Cdd:PHA03247 2842 PPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQP 2921
|
170 180 190
....*....|....*....|....*....|....*.
gi 190194425 659 KALSPitsRSPGVAVSAPPKPQSPAQNAASSQDGSQ 694
Cdd:PHA03247 2922 QPPPP---PQPQPPPPPPPRPQPPLAPTTDPAGAGE 2954
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
483-681 |
1.19e-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: 47.84 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 483 QATQLTGQKQSQQQYDPSTGPPVQNAASLHTPPPQLPArLPPASVPATALPSTlqfsQQSQMVEASTQLQIPVKTQQLNA 562
Cdd:pfam03154 168 QTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPS-VPPQGSPATSQPPN----QTQSTAAPHTLIQQTPTLHPQRL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 563 PIPAPLPSQLPAP------SSQP-AQPALHVPMP--------GKAQMQ----TSQLSSQTQTVASTRPPLdsaqPCQRSL 623
Cdd:pfam03154 243 PSPHPPLQPMTQPpppsqvSPQPlPQPSLHGQMPpmphslqtGPSHMQhpvpPQPFPLTPQSSQSQVPPG----PSPAAP 318
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 190194425 624 PTSSSSSSLVPVSGSGPGPSPARSSPVNrPSSATNKALSPitsrSPGVAVSAPPKPQS 681
Cdd:pfam03154 319 GQSQQRIHTPPSQSQLQSQQPPREQPLP-PAPLSMPHIKP----PPTTPIPQLPNPQS 371
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
492-660 |
1.63e-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: 47.45 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 492 QSQQQYDPSTGP-PVQNAASLHTPPPQLPARLPPASVPATALPSTLQFSQQSQMVEASTqLQIPVKTQQLNAPIPA---- 566
Cdd:pfam03154 370 QSHKHPPHLSGPsPFQMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPP-AQPPVLTQSQSLPPPAashp 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 567 ------PLPSQLPAP-------SSQPAQPALHVPMPGKAQMQTSQLSSQTQTVASTrpPLDSAQPCQRSLPTSSSSSSLV 633
Cdd:pfam03154 449 ptsglhQVPSQSPFPqhpfvpgGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSG--PVPAAVSCPLPPVQIKEEALDE 526
|
170 180 190
....*....|....*....|....*....|.
gi 190194425 634 PVSGSGPGPSPARSSP----VNRPSSATNKA 660
Cdd:pfam03154 527 AEEPESPPPPPRSPSPeptvVNTPSHASQSA 557
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
499-687 |
3.42e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.47 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 499 PSTGPPVQNAASLHTPPPQLPARLPPASVPATALPSTLQFSQQSQMVEASTQLQIPVKTQQLNAPIPAPLPSQLPAPSSQ 578
Cdd:PHA03247 2609 RGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAA 2688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 579 P---------AQPALHVPMPGKAQMQTSQLSSQTQTVASTRP--PLDSAQPCQRSLPTSSSSSSLVPVSGSGPGPS-PAR 646
Cdd:PHA03247 2689 RptvgsltslADPPPPPPTPEPAPHALVSATPLPPGPAAARQasPALPAAPAPPAVPAGPATPGGPARPARPPTTAgPPA 2768
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 190194425 647 SSPVNRPSSATNKALSPITSRSPGVAVSAPPKPQSPAQNAA 687
Cdd:PHA03247 2769 PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPA 2809
|
|
| SP1-4_arthropods_N |
cd22553 |
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ... |
2707-2997 |
3.98e-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: 45.79 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 2707 PRPGALLTGTtvtNLQVARLTRVPTSQLQAQGQMQTQTPQPAQVALAKPPVVSVPAAVVSSPGVTTLPMNVAGiSVAIGQ 2786
Cdd:cd22553 87 PANSGLLQTN---NQQAIQLAPGGTQAILANQQTLIRPNTVQGQANASNVLQNIAQIASGGNAVQLPLNNMTQ-TIPVQV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 2787 PQKTA-GQTV---VAQPVNVQQLLKYK-QQTAVQQQkaIQPQVAQGQAAVQQKLTtqQITTQGPQQKVAyaaqpalktqf 2861
Cdd:cd22553 163 PVSTAnGQTVyqtIQVPIQAIQSGNAGgGNQALQAQ--VIPQLAQAAQLQPQQLA--QVSSQGYIQQIP----------- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 2862 ltTPISQAQklagtqqvqtqiqvaklPQVVQQQTPV--ASIQQVASAS--QQASPQTVTLTQATAAG-----QQVQMIPT 2932
Cdd:cd22553 228 --ANASQQQ-----------------PQMVQQGPNQsgQIIGQVASASsiQAAAIPLTVYTGALAGQngsnqQQVGQIVT 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190194425 2933 VTATAQLVQQKLIQQQVVTTASAS--LQTPGGPSPAQLPASSDSPSQQPKLQMRVPAVRLKTPTKPP 2997
Cdd:cd22553 289 SPIQGMTQGLTAPASSSIPTVVQQqaIQGNPLPPGTQIIAAGQQLQQDPNDPTKWQVVADGTPGSKK 355
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
499-691 |
4.70e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.08 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 499 PSTGPPVQNAAsLHTPPPQLPARLPPASVPATALPSTLQFSQ----QSQMVEASTQLQIPVKT------QQLNAPIPAPL 568
Cdd:PHA03247 2824 PAGPLPPPTSA-QPTAPPPPPGPPPPSLPLGGSVAPGGDVRRrppsRSPAAKPAAPARPPVRRlarpavSRSTESFALPP 2902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 569 PSQLPAPSSQPAQPALHVPMPGKAQMQTSQLSSQTQTVASTRPPLDSAQPCQRSLPTSSSSSSLVPVSGSG------PGP 642
Cdd:PHA03247 2903 DQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAvprfrvPQP 2982
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 190194425 643 SPARSSPVNRPSSATNKALSPITSRSPGVA--VSAPPKPQSPAQNAASSQD 691
Cdd:PHA03247 2983 APSREAPASSTPPLTGHSLSRVSSWASSLAlhEETDPPPVSLKQTLWPPDD 3033
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
490-735 |
8.54e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 45.08 E-value: 8.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 490 QKQSQQQYDPSTGPPVQNAASLHTP-PPQLPARLPPASVPATALPSTLQFSQQSQMVEASTQLQIPVKTQQLNAPIP--- 565
Cdd:PRK10263 376 APEGYPQQSQYAQPAVQYNEPLQQPvQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQqst 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 566 -APLPSQLP-APSSQP-AQPALHVPMPGKAQMQTSQLSSQTQTVASTRPPLDSAQPCQRSLPTSSSSSSLVPVsgsgPGP 642
Cdd:PRK10263 456 fAPQSTYQTeQTYQQPaAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPLYYFEEVEEKRAREREQLAAWYQ----PIP 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 643 SPARSSPVNRPSSATNKA--LSPITSRSPGVAVSAPPKPQSPAQNAASSQDGSQDKLAEQITLENQIhqriadlrKEGLW 720
Cdd:PRK10263 532 EPVKEPEPIKSSLKAPSVaaVPPVEAAAAVSPLASGVKKATLATGAAATVAAPVFSLANSGGPRPQV--------KEGIG 603
|
250
....*....|....*
gi 190194425 721 slrrlPKLqeaPRPK 735
Cdd:PRK10263 604 -----PQL---PRPK 610
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
501-618 |
8.79e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 44.71 E-value: 8.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 501 TGPPVQNAASLHTPPPQLPARLPPASVPATALPSTLQFSQQSQMVEASTQLQiPVKTQQLNAPIPAPlpsqLPAPSSQPA 580
Cdd:PRK14951 371 EAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAP-PAPVAAPAAAAPAA----APAAAPAAV 445
|
90 100 110
....*....|....*....|....*....|....*...
gi 190194425 581 QPALHVPMPGKAQMQTSQLSSQTQTVASTRPPLDSAQP 618
Cdd:PRK14951 446 ALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAP 483
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
539-690 |
9.36e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 45.14 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 539 SQQSQMVeastQLQIPVKTQQLNAPIPAPLPSQLPAPSSQPAQPALHVPMPGKAQMQTSQLSSQTQTVA----------- 607
Cdd:pfam03154 161 SAQQQIL----QTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAaphtliqqtpt 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 608 -------STRPPLDSA-QPCQRSLPTSSSSSSLVPVSGSGPGPSPARSSPVNRPSSATNKALsPITSRSPGVAVSAPPKP 679
Cdd:pfam03154 237 lhpqrlpSPHPPLQPMtQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPF-PLTPQSSQSQVPPGPSP 315
|
170
....*....|.
gi 190194425 680 QSPAQNAASSQ 690
Cdd:pfam03154 316 AAPGQSQQRIH 326
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1373-1582 |
1.06e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1373 PPPSARPAAVKLKASRLFQPVQYGQKPEGRTVAFPSTHP--PRMANTNTSTATPQGQVRGRPPIAtfSANPDTKggevvk 1450
Cdd:PHA03247 2551 PPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPdaPPQSARPRAPVDDRGDPRGPAPPS--PLPPDTH------ 2622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1451 iAQLASIAGPQSRVAQPETPVTLQFQGNKFTLSHSQLRQLTAGQPLQLQGSVLQIVSAPGQPYLRAPGPVVMQTVSQAGA 1530
Cdd:PHA03247 2623 -APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADP 2701
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 190194425 1531 vhstlGSKPPTSGPSPAPLTPQVGVPGRVAVSAMAVGEPGLASKPASPAAGP 1582
Cdd:PHA03247 2702 -----PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGP 2748
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
508-716 |
1.36e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 44.21 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 508 AASLHTPPPQLPARLPPASVPATALPSTLQFSQQSQMVEASTQLQIPVKTQQLNAPIPAPLPSQLPAPSSQPAQPALHVP 587
Cdd:PRK12727 64 ATAAAPAPAPQAPTKPAAPVHAPLKLSANANMSQRQRVASAAEDMIAAMALRQPVSVPRQAPAAAPVRAASIPSPAAQAL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 588 MPGKA----QMQTSQLSSQTQTV---ASTRPPLDSAqpcqrslPTSSSSSSLVPVSGSGPGPSPARSSPVNR-------P 653
Cdd:PRK12727 144 AHAAAvrtaPRQEHALSAVPEQLfadFLTTAPVPRA-------PVQAPVVAAPAPVPAIAAALAAHAAYAQDddeqlddD 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190194425 654 SSATNKALSPITSRSP-GVAVSAPPKPQSPAQNAASSQDGSQDklaEQITlenQIHQRIADLRK 716
Cdd:PRK12727 217 GFDLDDALPQILPPAAlPPIVVAPAAPAALAAVAAAAPAPQND---EELK---QLRGELALMRQ 274
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
1017-1170 |
1.42e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 41.89 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1017 LRDYQKIGLD-WLAKLYRKNLNGILADEAGLGKTvqIIAFFAHLACNEGNWGPH-LVVMRSCNILK-WELELKRWCPGLK 1093
Cdd:pfam04851 4 LRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKT--LTAAKLIARLFKKGPIKKvLFLVPRKDLLEqALEEFKKFLPNYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 1094 TLSYVGSHRELKAKRQEWtepnnfHICITSYKQFFR----GYTAFSRVHWKCLVVDEMQRVkgmTERHWEAIFK-LQSQQ 1168
Cdd:pfam04851 82 EIGEIISGDKKDESVDDN------KIVVTTIQSLYKalelASLELLPDFFDVIIIDEAHRS---GASSYRNILEyFKPAF 152
|
..
gi 190194425 1169 RL 1170
Cdd:pfam04851 153 LL 154
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
499-617 |
1.46e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.21 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 499 PSTGPPVQNAASLHTPPPQLPArlPPASVPATALPSTLQFSQQSQMVEASTQLQIPVKTQQLNAPIPAPLPSQLPAPSSQ 578
Cdd:PRK07764 394 PAAAAPSAAAAAPAAAPAPAAA--APAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPA 471
|
90 100 110
....*....|....*....|....*....|....*....
gi 190194425 579 PAQPALHVPMPGKAQMQTSQLSSQTQTVASTRPPLDSAQ 617
Cdd:PRK07764 472 AAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAA 510
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
2730-2986 |
2.14e-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: 43.84 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 2730 PTSQLQAQGQMQTQTPQPAQVALAKPPVVSVPAAVVSSPGVTTLPMNVAGISV-AIGQPQKTAGQTVVAQpVNVQQLLKY 2808
Cdd:pfam09606 171 PNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQMGQQAqANGGMNPQQMGGAPNQ-VAMQQQQPQ 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 2809 KQQTAVQQQKAIQP--QVAQGQAAVQQKLTTQQITTQGPQQKVAYAAQPALKTQFLTTPISQAQKLAGTQQVQTQIQVAK 2886
Cdd:pfam09606 250 QQGQQSQLGMGINQmqQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHPAAHQQQ 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 2887 LPQVVQQQTPVASI---------QQVASASQQASPQTVTLTQATAAGQQV--QMIPTVTATAQLVQQKliQQQVVTTASA 2955
Cdd:pfam09606 330 MNQSVGQGGQVVALgglnhletwNPGNFGGLGANPMQRGQPGMMSSPSPVpgQQVRQVTPNQFMRQSP--QPSVPSPQGP 407
|
250 260 270
....*....|....*....|....*....|....*..
gi 190194425 2956 SLQTP----GG--PSPAQLPASSDSPSQQPKLQMRVP 2986
Cdd:pfam09606 408 GSQPPqshpGGmiPSPALIPSPSPQMSQQPAQQRTIG 444
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
500-610 |
2.99e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 43.16 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 500 STGPPVQNAASLHTPPPQLPARLPPASVPATAlPSTLQFSQQSQMVEASTQLQIPVKTQqlnaPIPAPlPSQLPAPSSQP 579
Cdd:PRK14951 410 AASAPAAPPAAAPPAPVAAPAAAAPAAAPAAA-PAAVALAPAPPAQAAPETVAIPVRVA----PEPAV-ASAAPAPAAAP 483
|
90 100 110
....*....|....*....|....*....|..
gi 190194425 580 AQPALHVPMPGKAQMQT-SQLSSQTQTVASTR 610
Cdd:PRK14951 484 AAARLTPTEEGDVWHATvQQLAAAEAITALAR 515
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
499-709 |
3.00e-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: 43.22 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 499 PSTGPPVQNAaslhTPPPqlparlPPASVPATALPstlQFSQQSQMVEASTQLQI-PVKTQQLNAPIPAPLPSQLpAPSS 577
Cdd:pfam03154 243 PSPHPPLQPM----TQPP------PPSQVSPQPLP---QPSLHGQMPPMPHSLQTgPSHMQHPVPPQPFPLTPQS-SQSQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 578 QPAQPALHVPMPGKAQMQTSQLSSQTQTVASTR----PPLDSAQPCQRSLPTSSSSSSLVPVSGSGP----GPSPArSSP 649
Cdd:pfam03154 309 VPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPReqplPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPphlsGPSPF-QMN 387
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 190194425 650 VNRPSSATNKALSPITSRSPGVAVSAP--------PKPQSPAQNAASSQDGSQDKLAEQITLENQIHQ 709
Cdd:pfam03154 388 SNLPPPPALKPLSSLSTHHPPSAHPPPlqlmpqsqQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQ 455
|
|
| SP2_N |
cd22540 |
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ... |
2778-2984 |
4.40e-03 |
|
N-terminal domain of transcription factor Specificity Protein (SP) 2; 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. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 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. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.
Pssm-ID: 411776 [Multi-domain] Cd Length: 511 Bit Score: 42.61 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 2778 AGISVAIGQpQKTAGQTVVAQPVnvqQLLKYKQQTAVQQqkaIQPQVAQG-QAAVQQKLTTQQITTQGPQQKVA------ 2850
Cdd:cd22540 268 AGNNLLIVQ-SPGTGQPAVLQQV---QVLQPKQEQQVVQ---IPQQALRVvQAASATLPTVPQKPLQNIQIQNSeptptq 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 2851 ----------------YAAQPALKTQFLTTPISQAQKLAGTQQVQTQIQVAKLPQVVQQQTPVASIQQVASASQQASPQT 2914
Cdd:cd22540 341 vyiktpsgevqtvllqEAPAATATPSSSTSTVQQQVTANNGTGTSKPNYNVRKERTLPKIAPAGGIISLNAAQLAAAAQA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190194425 2915 VTltQATAAGQQVQMIPtVTATAQLVQQKLiqqqVVTTASASLQTPGGPSPAQ---LPASSDSPSQQPKLQMR 2984
Cdd:cd22540 421 IQ--TININGVQVQGVP-VTITNAGGQQQL----TVQTVSSNNLTISGLSPTQiqlQMEQALEIETQPGEKRR 486
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
500-704 |
6.01e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.62 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 500 STGPPVQNAASLHTPPPQLPARLPPASVPATALPSTLQfsqqsqmvEASTQLQIPVKTQQLNAPIPAPLPSQLPAPSSQP 579
Cdd:PHA03247 2878 PARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPP--------PPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDP 2949
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 580 A---QPALHVPMPGKAQMQTSQLSSQTQTVASTRPPLDSAQpcqrslptsssssslvpvsgsgPGPSPARSSPVNRPSS- 655
Cdd:PHA03247 2950 AgagEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPA----------------------SSTPPLTGHSLSRVSSw 3007
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 190194425 656 ATNKALSPITSRSPgvaVSAPPKPQSPAQNAASSQDGSQDKLAEQITLE 704
Cdd:PHA03247 3008 ASSLALHEETDPPP---VSLKQTLWPPDDTEDSDADSLFDSDSERSDLE 3053
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
2461-2602 |
8.16e-03 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 41.66 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 2461 TTVGSAAVLAGTIKTSVTGTSIPTGTVSGNVIVNTIAGVPAATFQSINKRLASPVAPGTLTTSGGSAPAQVVHTqqraVG 2540
Cdd:COG3469 88 AATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETATG----GT 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 190194425 2541 SPATATTDLVSMTTTQGVRAVTSVTASAVVTTNLTPVQTPTrslvtqvSQATGVQLPGKTIT 2602
Cdd:COG3469 164 TTTSTTTTTTSASTTPSATTTATATTASGATTPSATTTATT-------TGPPTPGLPKHVLV 218
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
514-699 |
8.47e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.85 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 514 PPPQLPARLPPASvPATALPStlqfsqqsqmveastqlqipvktqqlnaPIPAPLPSQlPAPSSQPAQPALHvPMPGKAQ 593
Cdd:PHA03247 2551 PPPPLPPAAPPAA-PDRSVPP----------------------------PRPAPRPSE-PAVTSRARRPDAP-PQSARPR 2599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 594 MQTSQLSSQTQTVASTRPPLDSAQPcqrslPTSSSSSSLVPVSGSGPGPSPARSSPVNRPSSATNKALSPITSRSPGVAV 673
Cdd:PHA03247 2600 APVDDRGDPRGPAPPSPLPPDTHAP-----DPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAA 2674
|
170 180
....*....|....*....|....*.
gi 190194425 674 SAPPKPQSPAQNAASSQDGSQDKLAE 699
Cdd:PHA03247 2675 QASSPPQRPRRRAARPTVGSLTSLAD 2700
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
493-736 |
8.97e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 41.59 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 493 SQQQYDPSTGPPVQNAASLHtPPPQLPARLPPASVPATALPSTLQFSQQSQMVEASTQLQIPVKTQQ-----LNAPIP-- 565
Cdd:PHA03378 610 TTQSHIPETSAPRQWPMPLR-PIPMRPLRMQPITFNVLVFPTPHQPPQVEITPYKPTWTQIGHIPYQpsptgANTMLPiq 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 566 -APLPSQLPAPSSQPAQPALHVPMPGK-AQMQTSQLSSQTQTVASTRPPLDSAQPCQRSLPTSSSSSSLVPVSGSGPGP- 642
Cdd:PHA03378 689 wAPGTMQPPPRAPTPMRPPAAPPGRAQrPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPa 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 643 -SPARSSPVNRPSSATNKALSPITSRSPGVAVSAPPKPQSPAQNAASSQDGSQDKLAEQITLENQIHQRIAdLRKEGlwS 721
Cdd:PHA03378 769 aAPGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQLLTGGVKRGRPS-LKKPA--A 845
|
250
....*....|....*
gi 190194425 722 LRRLPKLQEAPRPKS 736
Cdd:PHA03378 846 LERQAAAGPTPSPGS 860
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
514-694 |
9.88e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 41.76 E-value: 9.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 514 PPPQLPARLP-PASVPATALPSTLQFSQQSQMVEASTQLQIPVKTQQLNAPIPAPLPSQLPAPSSQPAQPALHVPMPgka 592
Cdd:PRK07003 372 VPARVAGAVPaPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAP--- 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194425 593 qmqtSQLSSQTQTVASTRPPLDSAQPCQRSLPTSSSSSSLVPVSGSGPGPSPARSSPVNRPSSATNKALSpITSRSPGVA 672
Cdd:PRK07003 449 ----VPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPA-AASREDAPA 523
|
170 180
....*....|....*....|..
gi 190194425 673 VSAPPKPQSPAQNAASSQDGSQ 694
Cdd:PRK07003 524 AAAPPAPEARPPTPAAAAPAAR 545
|
|
| |
