|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_ARIP4 |
cd18069 |
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ... |
219-495 |
2.91e-158 |
|
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: 475.46 E-value: 2.91e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 219 VKPHQIGGIRFLYDNLVESLERFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMW 298
Cdd:cd18069 1 LKPHQIGGIRFLYDNIIESLERYKGSSGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 299 LPPPEALPadnkpeEVQPRFFKVHILNDEHKTMASRAKVMADWVSEGGVLLMGYEMYRLltlkksfatgrpkktkkrshp 378
Cdd:cd18069 81 LPPPEALP------NVRPRPFKVFILNDEHKTTAARAKVIEDWVKDGGVLLMGYEMFRL--------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 379 viidldeedrqqefrrefekalcRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVR 458
Cdd:cd18069 134 -----------------------RPGPDVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVR 190
|
250 260 270
....*....|....*....|....*....|....*..
gi 1917118595 459 PDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYR 495
Cdd:cd18069 191 PDFLGTRQEFSNMFERPILNGQCVDSTPQDVKLMRYR 227
|
|
| DEXHc_ATRX-like |
cd18007 |
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ... |
219-495 |
2.74e-111 |
|
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: 350.44 E-value: 2.74e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 219 VKPHQIGGIRFLYDNLVESleRFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTP-AKTVLAIVPVNTLQNWLAEFNM 297
Cdd:cd18007 1 LKPHQVEGVRFLWSNLVGT--DVGSDEGGGCILAHTMGLGKTLQVITFLHTYLAAAPrRSRPLVLCPASTLYNWEDEFKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 298 WLPPpEALPadnkpeevqprfFKVHILNDEHKTMASRAKVMADWVSEGGVLLMGYEMYRLLTLKKSfatgrpkkTKKRSH 377
Cdd:cd18007 79 WLPP-DLRP------------LLVLVSLSASKRADARLRKINKWHKEGGVLLIGYELFRNLASNAT--------TDPRLK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 378 pviidldeedrqqefrREFEKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFV 457
Cdd:cd18007 138 ----------------QEFIAALLDPGPDLLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFA 201
|
250 260 270
....*....|....*....|....*....|....*...
gi 1917118595 458 RPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYR 495
Cdd:cd18007 202 RPKYLGTLKEFKKKFVKPIEAGQCVDSTEEDVRLMLKR 239
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
58-838 |
6.42e-91 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 310.23 E-value: 6.42e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 58 RRNIRKLLREDQLEPVTKAAQQEELERRKRLEQQRKDYAAPIPTVPLEFLPEEIALRASDGPQLPPRVLAQEVICLDSSS 137
Cdd:COG0553 87 LLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 138 GSEDEKSSRDEVIELSSGEEDTLHIVDSSESVSEDDEEEEKGGTHVNDVLNQRDALgrVLVNLNHPPEEENVFLAPQLar 217
Cdd:COG0553 167 LLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAF--RLRRLREALESLPAGLKATL-- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 218 avKPHQIGGIRFLydnlvesleRFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNM 297
Cdd:COG0553 243 --RPYQLEGAAWL---------LFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAK 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 298 WLPPpealpadnkpeevqprfFKVHILNDEHKtmasRAKvMADWVSEGGVLLMGYEMyrlltlkksfatgrpkktkkrsh 377
Cdd:COG0553 312 FAPG-----------------LRVLVLDGTRE----RAK-GANPFEDADLVITSYGL----------------------- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 378 pviidldeedrqqeFRREFEkALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFV 457
Cdd:COG0553 347 --------------LRRDIE-LLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 458 RPDFLGTRQEFSNMFERPILNGQcidstpqdvrlmRYRSHVLHSLLEGFVQRRGHTVLKIHLPAKEENVILVRLSKIQRD 537
Cdd:COG0553 412 NPGLLGSLKAFRERFARPIEKGD------------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 538 LYTQFMDRFRDCGSSG---------WLGLNPLKAFCvcckiwNHPDVLyealqkesLANEQDLDVEelgsagtsarcppq 608
Cdd:COG0553 480 LYEAVLEYLRRELEGAegirrrgliLAALTRLRQIC------SHPALL--------LEEGAELSGR-------------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 609 gtkgkgedstlassmgeatnskflqgvgfnpfqergnnivtyewakdlltnyqtgvlenSPKMVLLFHLIEESVKLGDKI 688
Cdd:COG0553 532 -----------------------------------------------------------SAKLEALLELLEELLAEGEKV 552
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 689 LVFSQSLSTLALIEEFLGKRevpcppgtegqgaqkwvrNISYFRLDGSTPAFERERLINQFNDPSNltTWLFLLSTRAGC 768
Cdd:COG0553 553 LVFSQFTDTLDLLEERLEER------------------GIEYAYLHGGTSAEERDELVDRFQEGPE--APVFLISLKAGG 612
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 769 LGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQKKPCYIYRLVADYTLEKKIYDRQISKQGMSDRVVD 838
Cdd:COG0553 613 EGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
|
|
| DEXHc_ATRX |
cd18068 |
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ... |
219-495 |
7.05e-84 |
|
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: 274.46 E-value: 7.05e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 219 VKPHQIGGIRFLYDNLVESLERFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTP---AKTVLAIVPVNTLQNWLAEF 295
Cdd:cd18068 1 LKPHQVDGVQFMWDCCCESLKKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKlenFSRVLVVCPLNTVLNWLNEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 296 NMWLpppealpADNKPEEVqprfFKVHILnDEHKTMASRAKVMADWVSEGGVLLMGYEMYRLLTlkksfaTGRPKKTKKR 375
Cdd:cd18068 81 EKWQ-------EGLKDEEK----IEVNEL-ATYKRPQERSYKLQRWQEEGGVMIIGYDMYRILA------QERNVKSREK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 376 ShpviidldeedrqqefRREFEKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVD 455
Cdd:cd18068 143 L----------------KEIFNKALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVN 206
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1917118595 456 FVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYR 495
Cdd:cd18068 207 FVKPNLLGTIKEFRNRFVNPIQNGQCADSTLVDVRVMKKR 246
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
222-576 |
3.30e-60 |
|
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: 208.69 E-value: 3.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 222 HQIGGIRFLYdnlveSLERFktsSGFGCILAHSMGLGKTLQVISFIDVLFRHTP--AKTVLAIVPVNTLQNWLAEFNMWL 299
Cdd:pfam00176 1 YQIEGVNWML-----SLENN---LGRGGILADEMGLGKTLQTISLLLYLKHVDKnwGGPTLIVVPLSLLHNWMNEFERWV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 300 PPPeALPAdnkpeevqprfFKVHILNDEHKTMASRAKVMADWvsegGVLLMGYEMYRlltlkksfatgrpkktkkrSHPV 379
Cdd:pfam00176 73 SPP-ALRV-----------VVLHGNKRPQERWKNDPNFLADF----DVVITTYETLR-------------------KHKE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 380 IIDldeedrQQEFRRefekalcrpgpdvVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRP 459
Cdd:pfam00176 118 LLK------KVHWHR-------------IVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 460 DFLGTRQEFSNMFERPILNGQcidstpqdvrlMRYRSHVLHSLLEGFVQRRGHTVLKIHLPAKEENVILVRLSKIQRDLY 539
Cdd:pfam00176 179 GPFGSLSTFRNWFDRPIERGG-----------GKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLY 247
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1917118595 540 TQFMDrfrdcGSSGWLGLNPLKAFCVCC----------KIWNHPDVL 576
Cdd:pfam00176 248 QTFLL-----KKDLNAIKTGEGGREIKAsllnilmrlrKICNHPGLI 289
|
|
| DEXHc_RAD54 |
cd18004 |
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ... |
221-510 |
4.31e-60 |
|
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: 206.37 E-value: 4.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 221 PHQIGGIRFLYDnlveSLERFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTP-----AKTVLAIVPVNTLQNWLAEF 295
Cdd:cd18004 3 PHQREGVQFLYD----CLTGRRGYGGGGAILADEMGLGKTLQAIALVWTLLKQGPygkptAKKALIVCPSSLVGNWKAEF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 296 NMWLPP----PEALPADNKPEEVQPRFFkvhilndehkTMASRAKVmadwvseggvLLMGYEMyrlltlkksfatgrpkk 371
Cdd:cd18004 79 DKWLGLrrikVVTADGNAKDVKASLDFF----------SSASTYPV----------LIISYET----------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 372 tkkrshpviidldeedrqqeFRREFEKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYW 451
Cdd:cd18004 122 --------------------LRRHAEKLSKKISIDLLICDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFF 181
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1917118595 452 CMVDFVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYRSHVLHSLLEGFVQRR 510
Cdd:cd18004 182 ALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELTSRFILRR 240
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
668-813 |
8.69e-52 |
|
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: 178.44 E-value: 8.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 668 SPKMVLLFHLIEESVKLGDKILVFSQSLSTLALIEEFLGKRevpcppgtegqgaqkwvrNISYFRLDGSTPAFERERLIN 747
Cdd:cd18793 10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRER------------------GIKYLRLDGSTSSKERQKLVD 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1917118595 748 QFNDPSNLTtwLFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQKKPCYIYRLV 813
Cdd:cd18793 72 RFNEDPDIR--VFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
220-462 |
1.77e-48 |
|
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: 170.82 E-value: 1.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 220 KPHQIGGIRFLYDNLveslerfktSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKT-VLAIVPVNTLQNWLAEFNMW 298
Cdd:cd17919 2 RPYQLEGLNFLLELY---------ENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGpVLVVCPLSVLENWEREFEKW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 299 LPPpealpadnkpeevqprfFKVHILndeHKTMASRAKVMAD-WVSEGGVLLMGYEMYRLLTlkksfatgrpkktkkrsh 377
Cdd:cd17919 73 TPD-----------------LRVVVY---HGSQRERAQIRAKeKLDKFDVVLTTYETLRRDK------------------ 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 378 pviidldeedrqqefrrefeKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFV 457
Cdd:cd17919 115 --------------------ASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFL 174
|
....*
gi 1917118595 458 RPDFL 462
Cdd:cd17919 175 DPPFL 179
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
222-829 |
3.38e-48 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 188.09 E-value: 3.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 222 HQIGGIRF---LYDNlveslerfktssGFGCILAHSMGLGKTLQVISFIDVL--FR-----HtpaktvLAIVPVNTLQNW 291
Cdd:PLN03142 173 YQLAGLNWlirLYEN------------GINGILADEMGLGKTLQTISLLGYLheYRgitgpH------MVVAPKSTLGNW 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 292 LAEFNMWLPppealpadnkpeevQPRFFKVHILNDEhktmasRAKVMADWVSEGG--VLLMGYEMyrllTLKKsfatgrp 369
Cdd:PLN03142 235 MNEIRRFCP--------------VLRAVKFHGNPEE------RAHQREELLVAGKfdVCVTSFEM----AIKE------- 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 370 KKTKKRSHpviidldeedrqqeFRrefekalcrpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIE 449
Cdd:PLN03142 284 KTALKRFS--------------WR-------------YIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHE 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 450 YWCMVDFVRPDFLGTRQEFSNMFERPILNGQcidstpQDVrlmryrSHVLHSLLEGFVQRRGHTVLKIHLPAKEENVILV 529
Cdd:PLN03142 337 LWALLNFLLPEIFSSAETFDEWFQISGENDQ------QEV------VQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKV 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 530 RLSKIQRDLYtqfmdrfrdcgssgwlglnplKAfcvcckiwnhpdvlyeALQKeslaneqdlDVEELGSAGTSARCppqg 609
Cdd:PLN03142 405 GMSQMQKQYY---------------------KA----------------LLQK---------DLDVVNAGGERKRL---- 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 610 tkgkgedSTLASSMGEATNSKFL-QGVGFNPfqergnnivtyewakdlltNYQTG--VLENSPKMVLLFHLIEESVKLGD 686
Cdd:PLN03142 435 -------LNIAMQLRKCCNHPYLfQGAEPGP-------------------PYTTGehLVENSGKMVLLDKLLPKLKERDS 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 687 KILVFSQSLSTLALIEEFLgkrevpcppgtegqgaqkWVRNISYFRLDGSTPAFERERLINQFNDPsNLTTWLFLLSTRA 766
Cdd:PLN03142 489 RVLIFSQMTRLLDILEDYL------------------MYRGYQYCRIDGNTGGEDRDASIDAFNKP-GSEKFVFLLSTRA 549
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1917118595 767 GCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQKKPCYIYRLVADYTLEKKIYDRQISK 829
Cdd:PLN03142 550 GGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKK 612
|
|
| DEXHc_RAD54A |
cd18067 |
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ... |
219-510 |
8.59e-42 |
|
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: 153.78 E-value: 8.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 219 VKPHQIGGIRFLYDNLVESLERfktsSGFGCILAHSMGLGKTLQVISFIDVLFRHTP-AKTVL--AIV--PVNTLQNWLA 293
Cdd:cd18067 1 LRPHQREGVKFLYRCVTGRRIR----GSHGCIMADEMGLGKTLQCITLMWTLLRQSPqCKPEIdkAIVvsPSSLVKNWAN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 294 EFNMWLPPpealpadnkpeEVQPRffkvhILNDEHKTMASRAKVmaDWVSEGG------VLLMGYEMYRLltlkksfatg 367
Cdd:cd18067 77 ELGKWLGG-----------RLQPL-----AIDGGSKKEIDRKLV--QWASQQGrrvstpVLIISYETFRL---------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 368 rpkktkkrshpviidldeedrqqefrreFEKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNL 447
Cdd:cd18067 129 ----------------------------HVEVLQKGEVGLVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDL 180
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1917118595 448 IEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYRSHVLHSLLEGFVQRR 510
Cdd:cd18067 181 SEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISIVNRCIIRR 243
|
|
| DEXHc_ERCC6L2 |
cd18005 |
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ... |
220-510 |
8.70e-41 |
|
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: 150.99 E-value: 8.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 220 KPHQIGGIRFLYDNLVEslerfktssGFGCILAHSMGLGKTLQVISFIDVLFRHT---------------------PAKT 278
Cdd:cd18005 2 RDYQREGVEFMYDLYKN---------GRGGILGDDMGLGKTVQVIAFLAAVLGKTgtrrdrennrprfkkkppassAKKP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 279 VLAIVPVNTLQNWLAEFNMWlpppealpadnkpeevqpRFFKVHILNDEHKTMASRAKVMADWVSeggVLLMGYEMYRLl 358
Cdd:cd18005 73 VLIVAPLSVLYNWKDELDTW------------------GHFEVGVYHGSRKDDELEGRLKAGRLE---VVVTTYDTLRR- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 359 tlkksfatgrpkktkkrshpviiDLDEEDrQQEFrrefekalcrpgpDVVICDEGHRIKNCQASTSQALKNIRSRRRVVL 438
Cdd:cd18005 131 -----------------------CIDSLN-SINW-------------SAVIADEAHRIKNPKSKLTQAMKELKCKVRIGL 173
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1917118595 439 TGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYRSHVLHSLLEGFVQRR 510
Cdd:cd18005 174 TGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELAVKLSKFFLRR 245
|
|
| DEXHc_RAD54B |
cd18066 |
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ... |
219-510 |
3.75e-39 |
|
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: 146.14 E-value: 3.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 219 VKPHQIGGIRFLYdnlvESLERFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTP------AKTVLAIVPVNTLQNWL 292
Cdd:cd18066 1 LRPHQREGIEFLY----ECVMGMRVNERFGAILADEMGLGKTLQCISLIWTLLRQGPyggkpvIKRALIVTPGSLVKNWK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 293 AEFNMWLpppealpadnKPEEVqprffKVHILNDEHKTmasRAKVMADWVSeggVLLMGYEMyrLLtlkksfatgrpkkt 372
Cdd:cd18066 77 KEFQKWL----------GSERI-----KVFTVDQDHKV---EEFIASPLYS---VLIISYEM--LL-------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 373 kkRSHPVIIDLDEedrqqefrrefekalcrpgpDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWC 452
Cdd:cd18066 120 --RSLDQISKLNF--------------------DLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFA 177
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1917118595 453 MVDFVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYRSHVLHSLLEGFVQRR 510
Cdd:cd18066 178 LIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARAAELTRLTGLFILRR 235
|
|
| DEXHc_ERCC6L |
cd18001 |
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ... |
221-510 |
6.37e-39 |
|
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: 145.21 E-value: 6.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 221 PHQIGGIRFLYdnlveSLErfktSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWLP 300
Cdd:cd18001 3 PHQREGVAWLW-----SLH----DGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 301 ppealpadnkpeevQPRFFKVHILNdehktMASRAKVMADWVSEGGVLLMGYEMyrlltlkksfatgrpkktkkrshpvi 380
Cdd:cd18001 74 --------------GLRVKVFHGTS-----KKERERNLERIQRGGGVLLTTYGM-------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 381 IDLDEEDRQQEFRREFEKalcrpgpDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRP- 459
Cdd:cd18001 109 VLSNTEQLSADDHDEFKW-------DYVILDEGHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFACNg 181
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1917118595 460 DFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYRSHVLHSLLEGFVQRR 510
Cdd:cd18001 182 SLLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQIIKPYFLRR 232
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
221-510 |
6.77e-32 |
|
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: 124.60 E-value: 6.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 221 PHQIGGIRFLydnlvesleRFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWLP 300
Cdd:cd18012 7 PYQKEGFNWL---------SFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 301 PpealpadnkpeevqprfFKVHILNDehktmASRAKVMADWVSEGGVLLMGYEMYRLltlkksfatgrpkktkkrshpvi 380
Cdd:cd18012 78 E-----------------LKVLVIHG-----TKRKREKLRALEDYDLVITSYGLLRR----------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 381 idlDEEDRQQefrREFekalcrpgpDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPD 460
Cdd:cd18012 113 ---DIELLKE---VKF---------HYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPG 177
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1917118595 461 FLGTRQEFSNMFERPILNGQCIDSTPQdvrlmryrshvLHSLLEGFVQRR 510
Cdd:cd18012 178 LLGSYKRFKKRFAKPIEKDGDEEALEE-----------LKKLISPFILRR 216
|
|
| DEXHc_ERCC6 |
cd18000 |
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ... |
221-462 |
7.52e-32 |
|
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: 123.59 E-value: 7.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 221 PHQIGGIRFLYDnlveslerfKTSSGFGCILAHSMGLGKTLQVISFIDVL-FRHTPAKTVLAIVPVNTLQNWLAEFNMWL 299
Cdd:cd18000 3 KYQQTGVQWLWE---------LHCQRVGGILGDEMGLGKTIQIIAFLAALhHSKLGLGPSLIVCPATVLKQWVKEFHRWW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 300 PPpealpadnkpeevqprfFKVHIL--------NDEHKTMASRAKVMADWV-SEGGVLLMGYEMYRLLtlkksfatgrpk 370
Cdd:cd18000 74 PP-----------------FRVVVLhssgsgtgSEEKLGSIERKSQLIRKVvGDGGILITTYEGFRKH------------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 371 ktkkrSHPVIidldeedrqqefRREFekalcrpgpDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEY 450
Cdd:cd18000 125 -----KDLLL------------NHNW---------QYVILDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKEL 178
|
250
....*....|..
gi 1917118595 451 WCMVDFVRPDFL 462
Cdd:cd18000 179 WSLFDFVFPPYL 190
|
|
| DEXHc_SMARCA1_SMARCA5 |
cd17997 |
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ... |
250-510 |
1.58e-30 |
|
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: 120.89 E-value: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 250 ILAHSMGLGKTLQVISFIDVL--FRHTPAKTvLAIVPVNTLQNWLAEFNMWLPPPEALpadnkpeevqprffKVHILNDE 327
Cdd:cd17997 26 ILADEMGLGKTLQTISLLGYLkhYKNINGPH-LIIVPKSTLDNWMREFKRWCPSLRVV--------------VLIGDKEE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 328 HKTMASRAKVMADWvsegGVLLMGYEMyrlltlkksfatgrpkktkkrshpVIIDldeedrqqefrrefEKALCRPGPDV 407
Cdd:cd17997 91 RADIIRDVLLPGKF----DVCITSYEM------------------------VIKE--------------KTVLKKFNWRY 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 408 VICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFErpilNGQCIDstPQ 487
Cdd:cd17997 129 IIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFN----VNNCDD--DN 202
|
250 260
....*....|....*....|...
gi 1917118595 488 DVRLMRyrshvLHSLLEGFVQRR 510
Cdd:cd17997 203 QEVVQR-----LHKVLRPFLLRR 220
|
|
| DEXHc_HELLS_SMARCA6 |
cd18009 |
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ... |
220-510 |
8.95e-30 |
|
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: 119.03 E-value: 8.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 220 KPHQIGGI---RFLYDNlveslerfktssGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFN 296
Cdd:cd18009 5 RPYQLEGMewlRMLWEN------------GINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 297 MWLPPPEALpadnkpeevqprffKVHILNDEHKTMasRAKVMadwvseggvllmgyemyrlltlkksfatgrPKKTKKRS 376
Cdd:cd18009 73 RFTPSVPVL--------------LYHGTKEERERL--RKKIM------------------------------KREGTLQD 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 377 HPVIIDLDE---EDRqqefrrefeKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCM 453
Cdd:cd18009 107 FPVVVTSYEiamRDR---------KALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSL 177
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1917118595 454 VDFVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRYRSHVLHSLLEGFVQRR 510
Cdd:cd18009 178 LNFLLPDVFDDLSSFESWFDFSSLSDNAADISNLSEEREQNIVHMLHAILKPFLLRR 234
|
|
| DEXHc_SMARCA2_SMARCA4 |
cd17996 |
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ... |
220-510 |
9.95e-28 |
|
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: 112.85 E-value: 9.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 220 KPHQIGGIRF---LYDNLVESlerfktssgfgcILAHSMGLGKTLQVISFIDVLFRHTPAK-TVLAIVPVNTLQNWLAEF 295
Cdd:cd17996 5 KEYQLKGLQWmvsLYNNNLNG------------ILADEMGLGKTIQTISLITYLMEKKKNNgPYLVIVPLSTLSNWVSEF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 296 NMWLPPPEALPADNKPEeVQPRFFKVHIlndehktmasrakvmadwVSEGGVLLMGYEMyrllTLKKsfatgRPKKTKKR 375
Cdd:cd17996 73 EKWAPSVSKIVYKGTPD-VRKKLQSQIR------------------AGKFNVLLTTYEY----IIKD-----KPLLSKIK 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 376 SHPVIIDldeedrqqefrrefekalcrpgpdvvicdEGHRIKNCQASTSQALKN-IRSRRRVVLTGYPLQNNLIEYWCMV 454
Cdd:cd17996 125 WKYMIID-----------------------------EGHRMKNAQSKLTQTLNTyYHARYRLLLTGTPLQNNLPELWALL 175
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1917118595 455 DFVRPDFLGTRQEFSNMFERPILN--GQCIDSTPQDVRLMRYRShvLHSLLEGFVQRR 510
Cdd:cd17996 176 NFLLPKIFKSCKTFEQWFNTPFANtgEQVKIELNEEETLLIIRR--LHKVLRPFLLRR 231
|
|
| DEXHc_SMARCAD1 |
cd17998 |
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ... |
220-459 |
7.07e-26 |
|
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: 106.32 E-value: 7.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 220 KPHQIGGIRFLydNLVESlerfktsSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWL 299
Cdd:cd17998 2 KDYQLIGLNWL--NLLYQ-------KKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWC 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 300 PPPEALPADNKPEEvqprffKVHILNDEHKTmasrakvmadwVSEGGVLLMGYEMyrlltlkksfATGRPkktkkrshpv 379
Cdd:cd17998 73 PSLKVEPYYGSQEE------RKHLRYDILKG-----------LEDFDVIVTTYNL----------ATSNP---------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 380 iidldeEDRQQEFRREFekalcrpgpDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRP 459
Cdd:cd17998 116 ------DDRSFFKRLKL---------NYVVYDEGHMLKNMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMP 180
|
|
| DEXHc_CHD6_7_8_9 |
cd17995 |
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ... |
248-472 |
7.21e-24 |
|
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: 101.56 E-value: 7.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 248 GCILAHSMGLGKTLQVISFIDVLF-RHTPAKTVLAIVPVNTLQNWLAEFNMWLPppealpadnkpeevqprffkvhiLND 326
Cdd:cd17995 21 NCILADEMGLGKTIQSIAFLEHLYqVEGIRGPFLVIAPLSTIPNWQREFETWTD-----------------------MNV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 327 --EHKTMASRAkvmadwvseggvLLMGYEMYRlltlkkSFATGRPKKTKKRSHpVIIDLDE---EDRQqefrrEFEKALC 401
Cdd:cd17995 78 vvYHGSGESRQ------------IIQQYEMYF------KDAQGRKKKGVYKFD-VLITTYEmviADAE-----ELRKIPW 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917118595 402 RpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 472
Cdd:cd17995 134 R----VVVVDEAHRLKNRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF 200
|
|
| DEXDc_SHPRH-like |
cd18008 |
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ... |
247-510 |
1.14e-21 |
|
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: 95.82 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 247 FGCILAHSMGLGKTLQVISFI------------------DVLFRHTPAKTVLAIVPVNTLQNWLAEFNMwlpppealpad 308
Cdd:cd18008 15 RGGILADEMGLGKTIQALALIlatrpqdpkipeeleensSDPKKLYLSKTTLIVVPLSLLSQWKDEIEK----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 309 nkpeEVQPRFFKVHILndeHKtmASRAKVMADWvSEGGVLLMGYEmyrllTLKKSFATGRPKKTKKRSHPVIIDLdeedR 388
Cdd:cd18008 84 ----HTKPGSLKVYVY---HG--SKRIKSIEEL-SDYDIVITTYG-----TLASEFPKNKKGGGRDSKEKEASPL----H 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 389 QQEFRRefekalcrpgpdvVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEF 468
Cdd:cd18008 145 RIRWYR-------------VILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWF 211
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1917118595 469 snmferpilNGQCIDSTPQDVRLMRYRshvLHSLLEGFVQRR 510
Cdd:cd18008 212 ---------NSDISKPFSKNDRKALER---LQALLKPILLRR 241
|
|
| DEXQc_SRCAP |
cd18003 |
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ... |
250-510 |
1.33e-21 |
|
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: 95.11 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 250 ILAHSMGLGKTLQVISFIDVLFRHtpaKTV----LAIVPVNTLQNWLAEFNMWLPPpealpadnkpeevqprfFKVHILN 325
Cdd:cd18003 23 ILADEMGLGKTIQTIALLAHLACE---KGNwgphLIVVPTSVMLNWEMEFKRWCPG-----------------FKILTYY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 326 DEHKtmaSRAKVMADWVSEGG--VLLMGYEMyrlltlkksfatgrpkktkkrshpVIIDldeedrQQEFRREFEKALcrp 403
Cdd:cd18003 83 GSAK---ERKLKRQGWMKPNSfhVCITSYQL------------------------VVQD------HQVFKRKKWKYL--- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 404 gpdvvICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPiLNGQCID 483
Cdd:cd18003 127 -----ILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNP-LTAMSEG 200
|
250 260
....*....|....*....|....*..
gi 1917118595 484 STPQDVRLMRYrshvLHSLLEGFVQRR 510
Cdd:cd18003 201 SQEENEELVRR----LHKVLRPFLLRR 223
|
|
| DEXHc_SMARCA5 |
cd18064 |
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ... |
245-523 |
3.35e-20 |
|
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: 91.65 E-value: 3.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 245 SGFGCILAHSMGLGKTLQVISFIDVL--FRHTPAKTvLAIVPVNTLQNWLAEFNMWLPPPEAlpadnkpeevqprffkVH 322
Cdd:cd18064 33 NGINGILADEMGLGKTLQTISLLGYMkhYRNIPGPH-MVLVPKSTLHNWMAEFKRWVPTLRA----------------VC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 323 ILNDEHKTMASRAKVMADwvSEGGVLLMGYEMyrLLTLKKSFatgrpKKTKKRshpviidldeedrqqefrrefekalcr 402
Cdd:cd18064 96 LIGDKDQRAAFVRDVLLP--GEWDVCVTSYEM--LIKEKSVF-----KKFNWR--------------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 403 pgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFErpilNGQCI 482
Cdd:cd18064 140 ----YLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFD----TNNCL 211
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1917118595 483 DstpqDVRLMRYrshvLHSLLEGFVQRRGHTVLKIHLPAKE 523
Cdd:cd18064 212 G----DQKLVER----LHMVLRPFLLRRIKADVEKSLPPKK 244
|
|
| DEXHc_Mot1 |
cd17999 |
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ... |
220-484 |
3.72e-20 |
|
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: 90.87 E-value: 3.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 220 KPHQIGGIRFLydnlvESLERFKTSSgfgcILAHSMGLGKTLQVISFIDVLFRHTPAKT------VLAIVPVNTLQNWLA 293
Cdd:cd17999 2 RPYQQEGINWL-----AFLNKYNLHG----ILCDDMGLGKTLQTLCILASDHHKRANSFnsenlpSLVVCPPTLVGHWVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 294 EFNMWLPPPealpadnkpeevqprFFKVHILndeHKTMASRAKvMADWVSEGGVLLMGYEMYRlltlkksfatgrpkktk 373
Cdd:cd17999 73 EIKKYFPNA---------------FLKPLAY---VGPPQERRR-LREQGEKHNVIVASYDVLR----------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 374 krshpviidldeedRQQEFRREFEKALCrpgpdvvICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCM 453
Cdd:cd17999 117 --------------NDIEVLTKIEWNYC-------VLDEGHIIKNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSL 175
|
250 260 270
....*....|....*....|....*....|.
gi 1917118595 454 VDFVRPDFLGTRQEFSNMFERPILngQCIDS 484
Cdd:cd17999 176 FDFLMPGYLGTEKQFQRRFLKPIL--ASRDS 204
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
670-802 |
2.75e-19 |
|
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: 84.57 E-value: 2.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 670 KMVLLFHLIEEsvKLGDKILVFSQSLSTLAliEEFLGKREvpcppgtegqgaqkwvrNISYFRLDGSTPAFERERLINQF 749
Cdd:pfam00271 2 KLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEKE-----------------GIKVARLHGDLSQEEREEILEDF 60
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1917118595 750 NDPSNLttwlFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYG 802
Cdd:pfam00271 61 RKGKID----VLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEXHc_CHD1_2 |
cd17993 |
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ... |
249-510 |
4.27e-19 |
|
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: 87.41 E-value: 4.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 249 CILAHSMGLGKTLQVISFIDVLF-RHTPAKTVLAIVPVNTLQNWLAEFNMWLPPPEALpadnkpeevqprffkVHILNde 327
Cdd:cd17993 23 GILADEMGLGKTVQTISFLSYLFhSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI---------------VYLGD-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 328 hktMASRAkvmadwvseggvLLMGYEMYrlltlkksfatgrPKKTKKRSHPVIIDLDE---EDRQ--QEFRREFekalcr 402
Cdd:cd17993 86 ---IKSRD------------TIREYEFY-------------FSQTKKLKFNVLLTTYEiilKDKAflGSIKWQY------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 403 pgpdvVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFsnmferpilngqci 482
Cdd:cd17993 132 -----LAVDEAHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEF-------------- 192
|
250 260
....*....|....*....|....*...
gi 1917118595 483 DSTPQDVRLMRYRShvLHSLLEGFVQRR 510
Cdd:cd17993 193 EEEHDEEQEKGIAD--LHKELEPFILRR 218
|
|
| DEXHc_CHD3_4_5 |
cd17994 |
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ... |
221-473 |
5.38e-19 |
|
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: 86.72 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 221 PHQIGGIRFLydnlvesleRFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAK-TVLAIVPVNTLQNWLAEFNMWl 299
Cdd:cd17994 3 PYQLEGLNWL---------RFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKgPFLVSAPLSTIINWEREFEMW- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 300 pppealpadnkpeevQPRFFKVHILNDEhktmasrakvmadwvseggVLLMGYEmyrLLTLKKsfatgrpkktkkrshPV 379
Cdd:cd17994 73 ---------------APDFYVVTYVGDH-------------------VLLTSYE---LISIDQ---------------AI 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 380 IIDLDEEdrqqefrrefekalcrpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRP 459
Cdd:cd17994 101 LGSIDWA--------------------VLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTP 160
|
250
....*....|....
gi 1917118595 460 DFLGTRQEFSNMFE 473
Cdd:cd17994 161 ERFNNLQGFLEEFA 174
|
|
| DEXHc_SMARCA1 |
cd18065 |
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ... |
245-510 |
9.05e-19 |
|
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: 87.00 E-value: 9.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 245 SGFGCILAHSMGLGKTLQVISFIDVL--FRHTPAKTvLAIVPVNTLQNWLAEFNMWLPPPEAlpadnkpeevqprffkVH 322
Cdd:cd18065 33 NGVNGILADEMGLGKTLQTIALLGYLkhYRNIPGPH-MVLVPKSTLHNWMNEFKRWVPSLRA----------------VC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 323 ILNDEHKTMASRAKVMADwvSEGGVLLMGYEMYrlltlkksfatgrpkktkkrshpviidLDEEDRQQEFRREFekalcr 402
Cdd:cd18065 96 LIGDKDARAAFIRDVMMP--GEWDVCVTSYEMV---------------------------IKEKSVFKKFNWRY------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 403 pgpdvVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFErpilNGQCI 482
Cdd:cd18065 141 -----LVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD----TKNCL 211
|
250 260
....*....|....*....|....*...
gi 1917118595 483 DstpqDVRLMRYrshvLHSLLEGFVQRR 510
Cdd:cd18065 212 G----DQKLVER----LHAVLKPFLLRR 231
|
|
| DEXHc_SMARCA4 |
cd18062 |
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ... |
219-510 |
8.23e-18 |
|
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: 84.71 E-value: 8.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 219 VKPHQIGGIRFL---YDNlveslerfktssGFGCILAHSMGLGKTLQVISFIDVLFRHTPAK-TVLAIVPVNTLQNWLAE 294
Cdd:cd18062 24 LKQYQIKGLEWLvslYNN------------NLNGILADEMGLGKTIQTIALITYLMEHKRINgPFLIIVPLSTLSNWVYE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 295 FNMWLPPPEALPADNKPEevqprffkvhilndehktmASRAKVMADWVSEGGVLLMGYEMyrLLTLKKSFATGRPKktkk 374
Cdd:cd18062 92 FDKWAPSVVKVSYKGSPA-------------------ARRAFVPQLRSGKFNVLLTTYEY--IIKDKQILAKIRWK---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 375 rshpviidldeedrqqefrrefekalcrpgpdVVICDEGHRIKNCQASTSQALK-NIRSRRRVVLTGYPLQNNLIEYWCM 453
Cdd:cd18062 147 --------------------------------YMIVDEGHRMKNHHCKLTQVLNtHYVAPRRLLLTGTPLQNKLPELWAL 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1917118595 454 VDFVRPDFLGTRQEFSNMFERPI-LNGQCIDSTPQDVRLMRYRshvLHSLLEGFVQRR 510
Cdd:cd18062 195 LNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETILIIRR---LHKVLRPFLLRR 249
|
|
| DEXHc_CHD2 |
cd18054 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ... |
250-510 |
1.10e-17 |
|
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: 83.90 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 250 ILAHSMGLGKTLQVISFIDVLF-RHTPAKTVLAIVPVNTLQNWLAEFNMWLPPPEALpadnkpeevqprffkVHILNdeh 328
Cdd:cd18054 43 ILADEMGLGKTIQTISFLSYLFhQHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVV---------------VYIGD--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 329 ktMASRAKVMA-DWVSEggvllmgyemyrlltlkksfatgrpkKTKKRSHPVIIDldeedrQQEFRREFEKALCRPGPDV 407
Cdd:cd18054 105 --LMSRNTIREyEWIHS--------------------------QTKRLKFNALIT------TYEILLKDKTVLGSINWAF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 408 VICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGqcidstpq 487
Cdd:cd18054 151 LGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENG-------- 222
|
250 260
....*....|....*....|...
gi 1917118595 488 dvrlmrYRShvLHSLLEGFVQRR 510
Cdd:cd18054 223 ------YQS--LHKVLEPFLLRR 237
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
726-802 |
1.73e-17 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 78.41 E-value: 1.73e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1917118595 726 RNISYFRLDGSTPAFERERLINQFNDPSNLttwlFLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYG 802
Cdd:smart00490 10 LGIKVARLHGGLSQEEREEILDKFNNGKIK----VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
|
|
| DEXHc_SMARCA2 |
cd18063 |
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ... |
250-510 |
2.60e-17 |
|
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: 83.19 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 250 ILAHSMGLGKTLQVISFIDVLFRHTPAK-TVLAIVPVNTLQNWLAEFNMWLPPpealpadnkpeevqprffkvhILNDEH 328
Cdd:cd18063 46 ILADEMGLGKTIQTIALITYLMEHKRLNgPYLIIVPLSTLSNWTYEFDKWAPS---------------------VVKISY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 329 KTMASRAKVMADWVSEG--GVLLMGYEMyrLLTLKKSFATGRPKktkkrshpviidldeedrqqefrrefekalcrpgpd 406
Cdd:cd18063 105 KGTPAMRRSLVPQLRSGkfNVLLTTYEY--IIKDKHILAKIRWK------------------------------------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 407 VVICDEGHRIKNCQASTSQALK-NIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPI-LNGQCIDS 484
Cdd:cd18063 147 YMIVDEGHRMKNHHCKLTQVLNtHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGERVDL 226
|
250 260
....*....|....*....|....*.
gi 1917118595 485 TPQDVRLMRYRshvLHSLLEGFVQRR 510
Cdd:cd18063 227 NEEETILIIRR---LHKVLRPFLLRR 249
|
|
| DEXQc_INO80 |
cd18002 |
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ... |
219-510 |
5.00e-17 |
|
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: 81.78 E-value: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 219 VKPHQIGGIRFLYdNLVESlerfktssGFGCILAHSMGLGKTLQVISFIDVLF-RHTPAKTVLAIVPVNTLQNWLAEFNM 297
Cdd:cd18002 1 LKEYQLKGLNWLA-NLYEQ--------GINGILADEMGLGKTVQSIAVLAHLAeEHNIWGPFLVIAPASTLHNWQQEISR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 298 WLPPPEALP--ADNKPEEVQPRFFkvhilndEHKTMASRAkvmadwvSEGGVLLMGYEMyrlltlkksfatgrpkktkkr 375
Cdd:cd18002 72 FVPQFKVLPywGNPKDRKVLRKFW-------DRKNLYTRD-------APFHVVITSYQL--------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 376 shpVIIDldeedrqqefrrefEKALCRPGPDVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVD 455
Cdd:cd18002 117 ---VVQD--------------EKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLH 179
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1917118595 456 FVRPDFLGTRQEFSNMFERPILNGQCIDSTPQDVRLMRyrshvLHSLLEGFVQRR 510
Cdd:cd18002 180 FIMPTLFDSHDEFNEWFSKDIESHAENKTGLNEHQLKR-----LHMILKPFMLRR 229
|
|
| DEXHc_CHD5 |
cd18057 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ... |
219-472 |
1.34e-16 |
|
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: 80.88 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 219 VKPHQIGGIRFLydnlvesleRFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAK-TVLAIVPVNTLQNWLAEFNM 297
Cdd:cd18057 1 LHPYQLEGLNWL---------RFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKgPYLVSAPLSTIINWEREFEM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 298 WlpppealpadnkpeevQPRFFKVHILNDEHktmaSRAKVMADWVS-EGGVLLMGYEMYRLltlkksfatgrPKKTKKRS 376
Cdd:cd18057 72 W----------------APDFYVVTYTGDKE----SRSVIRENEFSfEDNAIRSGKKVFRM-----------KKEAQIKF 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 377 HPVIIDLDEEDRQQEFRREFEKAlcrpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDF 456
Cdd:cd18057 121 HVLLTSYELITIDQAILGSIEWA-------CLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNF 193
|
250
....*....|....*.
gi 1917118595 457 VRPDFLGTRQEFSNMF 472
Cdd:cd18057 194 LTPERFNNLEGFLEEF 209
|
|
| DEXHc_CHD1L |
cd18006 |
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ... |
219-510 |
1.60e-16 |
|
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: 80.17 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 219 VKPHQIGGIRFLydnlvesLERFKTssGFGCILAHSMGLGKTLQVISFIDVL-FRHTPAKTVLAIVPVNTLQNWLAEFNM 297
Cdd:cd18006 1 LRPYQLEGVNWL-------LQCRAE--QHGCILGDEMGLGKTCQTISLLWYLaGRLKLLGPFLVLCPLSVLDNWKEELNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 298 WLPPPEALPADNKPEEvqprffkvhilndehktmasRAKVMADWVSEG--GVLLMGYEMyrlltlkksfatgrpkktkkr 375
Cdd:cd18006 72 FAPDLSVITYMGDKEK--------------------RLDLQQDIKSTNrfHVLLTTYEI--------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 376 shpVIIDldeedrqQEFRREFEKAlcrpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVD 455
Cdd:cd18006 111 ---CLKD-------ASFLKSFPWA-------SLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLS 173
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1917118595 456 FVRPDFLG--TRQEFSNMFERpilngqcIDSTPQDVRlmryrshVLHSLLEGFVQRR 510
Cdd:cd18006 174 FIEPNVFPkdKLDDFIKAYSE-------TDDESETVE-------ELHLLLQPFLLRR 216
|
|
| DEXHc_HLTF1_SMARC3 |
cd18071 |
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ... |
245-479 |
3.18e-15 |
|
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: 76.74 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 245 SGFGCILAHSMGLGKTLQVISFIdvLFRHTpaktvLAIVPVNTLQNWLAEFNmwlpppealpadnkpEEVQPRFFKVHIL 324
Cdd:cd18071 47 LVRGGILADDMGLGKTLTTISLI--LANFT-----LIVCPLSVLSNWETQFE---------------EHVKPGQLKVYTY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 325 NDEHKTMAsrakvmADWVSEGGVLLMGYEmyrllTLKKSFATgrpkktkKRSHPViidldeedRQQEFRRefekalcrpg 404
Cdd:cd18071 105 HGGERNRD------PKLLSKYDIVLTTYN-----TLASDFGA-------KGDSPL--------HTINWLR---------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1917118595 405 pdvVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNG 479
Cdd:cd18071 149 ---VVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPLTMG 220
|
|
| DEXHc_CHD3 |
cd18055 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ... |
240-471 |
3.46e-15 |
|
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: 76.59 E-value: 3.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 240 RFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAK-TVLAIVPVNTLQNWLAEFNMWlpppealpadnkpeevQPRF 318
Cdd:cd18055 13 RFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKgPFLVSAPLSTIINWEREFQMW----------------APDF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 319 FKVHILNDEHKTMASRAKVMA--DWVSEGGvllmgyemyrlltlKKSFATGRPKKTKkrSHPVIIDLDEEDRQQEFRREF 396
Cdd:cd18055 77 YVVTYTGDKDSRAIIRENEFSfdDNAVKGG--------------KKAFKMKREAQVK--FHVLLTSYELVTIDQAALGSI 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1917118595 397 EKAlcrpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFL----GTRQEFSNM 471
Cdd:cd18055 141 RWA-------CLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFnnleGFLEEFADI 212
|
|
| DEXHc_CHD1 |
cd18053 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ... |
220-468 |
1.98e-14 |
|
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: 74.32 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 220 KPHQIGGIRFL--YDNLVESLERFKTS--SGFGCILAHSMGLGKTLQVISFIDVLF-RHTPAKTVLAIVPVNTLQNWLAE 294
Cdd:cd18053 9 QPSYIGGHEGLelRDYQLNGLNWLAHSwcKGNSCILADEMGLGKTIQTISFLNYLFhEHQLYGPFLLVVPLSTLTSWQRE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 295 FNMWLPPPEALpadnkpeeVQPRFFKVHILNDEHKTMASRAKVMadwvsEGGVLLMGYEmyrLLTLKKSFATGRPKKtkk 374
Cdd:cd18053 89 IQTWAPQMNAV--------VYLGDINSRNMIRTHEWMHPQTKRL-----KFNILLTTYE---ILLKDKSFLGGLNWA--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 375 rshpviidldeedrqqefrrefekalcrpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMV 454
Cdd:cd18053 150 --------------------------------FIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLL 197
|
250
....*....|....
gi 1917118595 455 DFVRPDFLGTRQEF 468
Cdd:cd18053 198 HFIMPEKFSSWEDF 211
|
|
| DEXHc_CHD7 |
cd18059 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ... |
249-472 |
3.11e-14 |
|
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: 73.53 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 249 CILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWlpppealpadnkpEEVQPRFFkvhilndeH 328
Cdd:cd18059 22 CILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTW-------------TELNVVVY--------H 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 329 KTMASRAKVMAdwvseggvllmgYEMYRLLTlkksfaTGRPKKTKKRSHPVIIDLD------EEDRQQEFRrefekalcr 402
Cdd:cd18059 81 GSQASRRTIQL------------YEMYFKDP------QGRVIKGSYKFHAIITTFEmiltdcPELRNIPWR--------- 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 403 pgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 472
Cdd:cd18059 134 ----CVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF 199
|
|
| DEXHc_CHD8 |
cd18060 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ... |
249-472 |
3.31e-14 |
|
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: 73.55 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 249 CILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWlpppealpadnkpEEVQPRFFkvhilndeH 328
Cdd:cd18060 22 CILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTW-------------TEMNTIVY--------H 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 329 KTMASRAkvmadwvseggvLLMGYEMYrlltLKKSFATGRPKKTK----KRSHPVIIDLDEEDRQQEFRrefekalcrpg 404
Cdd:cd18060 81 GSLASRQ------------MIQQYEMY----CKDSRGRLIPGAYKfdalITTFEMILSDCPELREIEWR----------- 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1917118595 405 pdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 472
Cdd:cd18060 134 --CVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF 199
|
|
| DEXHc_HARP_SMARCAL1 |
cd18010 |
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ... |
220-468 |
1.86e-13 |
|
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a like 1, also known as HARP) is recruited to stalled replication forks to promote repair and helps restart replication. It plays a role in DNA repair, telomere maintenance and replication fork stability in response to DNA replication stress. Mutations cause Schimke Immunoosseous Dysplasia. SMARCAL1 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350768 [Multi-domain] Cd Length: 213 Bit Score: 71.08 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 220 KPHQIGGIRFlydnlveSLERfktssGFGCILAHSMGLGKTLQVISFIDVLFRHTPaktVLAIVPVNTLQNWLAEFNMWL 299
Cdd:cd18010 2 LPFQREGVCF-------ALRR-----GGRVLIADEMGLGKTVQAIAIAAYYREEWP---LLIVCPSSLRLTWADEIERWL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 300 PppealpadnkpeEVQPRffkvhilnDEHKTMASRAKVMADWvseGGVLLMGYEMyrLLTLKKSFATGRPKktkkrshpv 379
Cdd:cd18010 67 P------------SLPPD--------DIQVIVKSKDGLRDGD---AKVVIVSYDL--LRRLEKQLLARKFK--------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 380 iidldeedrqqefrrefekalcrpgpdVVICDEGHRIKNCQASTSQALKNI--RSRRRVVLTGYPLQNNLIEYWCMVDFV 457
Cdd:cd18010 113 ---------------------------VVICDESHYLKNSKAKRTKAALPLlkRAKRVILLSGTPALSRPIELFTQLDAL 165
|
250
....*....|.
gi 1917118595 458 RPDFLGTRQEF 468
Cdd:cd18010 166 DPKLFGRFHDF 176
|
|
| DEXHc_CHD6 |
cd18058 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ... |
249-472 |
2.15e-13 |
|
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: 71.23 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 249 CILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWlpppealpadnkpEEVQPRFFkvhilndeH 328
Cdd:cd18058 22 CILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTW-------------TEMNAIVY--------H 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 329 KTMASRAkvmadwvseggvLLMGYEMYRlltlkkSFATGRPKKTKKRSHPVIIDLdeedrqqefrrEFEKALCrpgPDV- 407
Cdd:cd18058 81 GSQISRQ------------MIQQYEMYY------RDEQGNPLSGIFKFQVVITTF-----------EMILADC---PELk 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917118595 408 ------VICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 472
Cdd:cd18058 129 kinwscVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF 199
|
|
| DEXHc_CHD4 |
cd18056 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ... |
219-471 |
5.76e-13 |
|
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: 70.09 E-value: 5.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 219 VKPHQIGGIRFLydnlvesleRFKTSSGFGCILAHSMGLGKTLQVISFIDVLFRHTPAK-TVLAIVPVNTLQNWLAEFNM 297
Cdd:cd18056 1 LHPYQLEGLNWL---------RFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKgPFLVSAPLSTIINWEREFEM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 298 WlpppealpadnkpeevQPRFFKVHILNDEHktmaSRAKVMADWVS-EGGVLLMGYEMYRLltlkksfatgrPKKTKKRS 376
Cdd:cd18056 72 W----------------APDMYVVTYVGDKD----SRAIIRENEFSfEDNAIRGGKKASRM-----------KKEASVKF 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 377 HPVIIDLDEEDRQQEFRREFEKAlcrpgpdVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDF 456
Cdd:cd18056 121 HVLLTSYELITIDMAILGSIDWA-------CLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNF 193
|
250
....*....|....*....
gi 1917118595 457 VRPDFL----GTRQEFSNM 471
Cdd:cd18056 194 LTPERFhnleGFLEEFADI 212
|
|
| DEXHc_CHD9 |
cd18061 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ... |
249-472 |
1.76e-11 |
|
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: 65.41 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 249 CILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFNMWlpppealpadnkpeevqprffkVHI-LNDE 327
Cdd:cd18061 22 CILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTW----------------------TDLnVVVY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 328 HKTMASRAkvmadwvseggvLLMGYEMYrlltLKKSfaTGRPKKTKKRSHPVIIdldeedrqqefrrEFEKALCRPGP-- 405
Cdd:cd18061 80 HGSLISRQ------------MIQQYEMY----FRDS--QGRIIRGAYRFQAIIT-------------TFEMILGGCPEln 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917118595 406 ----DVVICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMF 472
Cdd:cd18061 129 aidwRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF 199
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
221-492 |
3.79e-10 |
|
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: 61.15 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 221 PHQIggirflyDNLVESLERFKtssgFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQNWLAEFN--MW 298
Cdd:cd18011 3 PHQI-------DAVLRALRKPP----VRLLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQdkFG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 299 LPPPEALPADNKPEEvqprffkvhilndehktmasrakvmadwvseggvllmgyemyrlltlkksfatGRPKKTKKRSHP 378
Cdd:cd18011 72 LPFLILDRETAAQLR-----------------------------------------------------RLIGNPFEEFPI 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 379 VIIDLDEEDRQqefrREFEKALCRPGPDVVICDEGHRIKNCQASTSQ----ALKNI--RSRRRVVLTGYPLQNNLIEYWC 452
Cdd:cd18011 99 VIVSLDLLKRS----EERRGLLLSEEWDLVVVDEAHKLRNSGGGKETkrykLGRLLakRARHVLLLTATPHNGKEEDFRA 174
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1917118595 453 MVDFVRPDFlgtrqefsnmFERPILNGQCIDSTPQDVRLM 492
Cdd:cd18011 175 LLSLLDPGR----------FAVLGRFLRLDGLREVLAKVL 204
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
221-462 |
1.36e-09 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 59.43 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 221 PHQIGGIRFLYDNLveslerfktssgFGCILAHSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTL-QNWLAEFNMWL 299
Cdd:smart00487 11 PYQKEAIEALLSGL------------RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 300 PPPealpadnkpeevqprFFKVHILNDEHKTMASRAKVMADwvsEGGVLLMGYEmyRLLTLKKsfatgrpkktkkrshpv 379
Cdd:smart00487 79 PSL---------------GLKVVGLYGGDSKREQLRKLESG---KTDILVTTPG--RLLDLLE----------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 380 iidldeedrqqefrrefEKALCRPGPDVVICDEGHRIKNcqASTSQALKNI-----RSRRRVVLTGYP---LQNNLIEYW 451
Cdd:smart00487 122 -----------------NDKLSLSNVDLVILDEAHRLLD--GGFGDQLEKLlkllpKNVQLLLLSATPpeeIENLLELFL 182
|
250
....*....|.
gi 1917118595 452 CMVDFVRPDFL 462
Cdd:smart00487 183 NDPVFIDVGFT 193
|
|
| DEXHc_TTF2 |
cd18072 |
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ... |
408-458 |
1.67e-06 |
|
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: 50.94 E-value: 1.67e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1917118595 408 VICDEGHRIKNCQASTSQALKNIRSRRRVVLTGYPLQNNLIEYWCMVDFVR 458
Cdd:cd18072 155 IILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLR 205
|
|
| DEXQc_bact_SNF2 |
cd18013 |
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ... |
220-457 |
3.84e-04 |
|
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprise a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. The bacterial SNF2 present in this family are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350771 [Multi-domain] Cd Length: 218 Bit Score: 43.49 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 220 KPHQIGGIRFLYDNLVeslerfktssgfGCILAhSMGLGKTLQVISFIDVLFRHTPAKTVLAIVPVNTLQN-WLAEFNMW 298
Cdd:cd18013 2 HPYQKVAINFIIEHPY------------CGLFL-DMGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARStWPDEVEKW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 299 lpppealpadnkpeevqprffkvhilndEHktmasrakvmadwvseggvllmgyemyrLLTLKKSFATGRPKK----TKK 374
Cdd:cd18013 69 ----------------------------NH----------------------------LRNLTVSVAVGTERQrskaANT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 375 RSHPVIIDLDEED---RQQEFRREFekalcrpgpDVVICDEGHRIKNCQASTSQALKNIRSR--RRVVLTGYPLQNNLIE 449
Cdd:cd18013 93 PADLYVINRENLKwlvNKSGDPWPF---------DMVVIDELSSFKSPRSKRFKALRKVRPVikRLIGLTGTPSPNGLMD 163
|
....*...
gi 1917118595 450 YWCMVDFV 457
Cdd:cd18013 164 LWAQIALL 171
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
760-813 |
6.06e-03 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The 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: 350172 [Multi-domain] Cd Length: 77 Bit Score: 36.91 E-value: 6.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1917118595 760 FLLSTRAGCLGVNLIGANRVVVFDASWNPCHDAQAVCRVYRYGQkKPCYIYRLV 813
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILFV 77
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1054-1362 |
6.53e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 1054 GTYIRTSDGRIFAVRATGKPKVPEDGRMAASGSQ--GPSCESTSNGRHSASSPKAPDPEGLARPVSPdspeiiselqqya 1131
Cdd:PHA03247 2747 GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPrrLTRPAVASLSESRESLPSPWDPADPPAAVLA------------- 2813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 1132 dvAAARESRQSSPSTnaALPGPPAQLMDSSAVPGTALGTEPRLGGHCLnssllvtgqPCGDrhpvLDLRGHKRKLATPPA 1211
Cdd:PHA03247 2814 --PAAALPPAASPAG--PLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA---------PGGD----VRRRPPSRSPAAKPA 2876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917118595 1212 AqeSSRRRSRKGHLPAPVQPYEhgypvsgGFAMPPVSLNHNLTTPFTSQAgenslfmgSTPSYYQLSNLLADARlvfPVT 1291
Cdd:PHA03247 2877 A--PARPPVRRLARPAVSRSTE-------SFALPPDQPERPPQPQAPPPP--------QPQPQPPPPPQPQPPP---PPP 2936
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917118595 1292 TDPLVPAGPVSSSSTATSVTASNPSFMLNPSVPGilpsySLPFSQPLLSEPRMFAPFPSPVLPSNLSRGMS 1362
Cdd:PHA03247 2937 PRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPG-----RVAVPRFRVPQPAPSREAPASSTPPLTGHSLS 3002
|
|
| |
