NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2033488177|gb|KAG5813046|]
View 

hypothetical protein H9Q71_003994 [Fusarium xylarioides]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 1000678)

DEAD/DEAH box containing ATP-dependent helicase, similar to ISWI chromatin-remodeling complex ATPases, which are catalytic components of ISW1-type complexes, which act by remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
30-786 3.05e-126

Probable chromatin-remodeling complex ATPase chain; Provisional


The actual alignment was detected with superfamily member PLN03142:

Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 405.34  E-value: 3.05e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177   30 EQQDDLEGADEALIKEEQEARL-ENERNEEKRRQAMLKRKKKKKAETKSEReAKAReLDDLLAKSAAFSDILT------- 101
Cdd:PLN03142    44 EDDEEAESPAKAEISKREKARLkELKKQKKQEIQKILEQQNAAIDADMNNK-GKGR-LKYLLQQTEIFAHFAKgdqsasa 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  102 KKTQVLGRVGSSL-------------DGKTLGEHSLEMAQQPKCmINGTMRDYQLEGLTWMYEICSQGMSGILADEMGLG 168
Cdd:PLN03142   122 KKAKGRGRHASKLteeeedeeylkeeEDGLGGSGGTRLLVQPSC-IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLG 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  169 KTVQTIALIALLREQENYLGPHLIVAPLSTLSNWEDEFTKWTPSIPVIMYHGNKDDREKIfRTKMLKhlkAGrpttKFPV 248
Cdd:PLN03142   201 KTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQ-REELLV---AG----KFDV 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  249 VCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQLRQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDW 328
Cdd:PLN03142   273 CVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSA 352
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  329 EAFESWFDFSDLEDEqgteefiadqkkQELVKKIHLILQPMLLRRIKQDVAAYLPKKREYVLFAPMTKEQTDLYNVLTNK 408
Cdd:PLN03142   353 ETFDEWFQISGENDQ------------QEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQK 420
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  409 KVDtrqyledkvhekiygtksteastkssrsssvaapntmtlpvresprkqqvepeepAANvfsvmmakrgrgrprknpk 488
Cdd:PLN03142   421 DLD-------------------------------------------------------VVN------------------- 426
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  489 leeapvtpkSGGKRkgapaslepepksakstrqstpvstrgrprktrtykdagsdeekmsddefeaklakemvsddedls 568
Cdd:PLN03142   427 ---------AGGER------------------------------------------------------------------ 431
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  569 gqvpltleeraqaeafelakkqigqKKLGNPLAQLRLVCNSPHNFYN-----PWIAstdlpvDDSIVTASGKMLLLDRLL 643
Cdd:PLN03142   432 -------------------------KRLLNIAMQLRKCCNHPYLFQGaepgpPYTT------GEHLVENSGKMVLLDKLL 480
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  644 PRLFQDDHKVLIFSQFTTQLDILEDYCReLRGWKVCRIDGSVAQESRRTQIADFNSDPEYK-IFLLSTRAGGQGINLASA 722
Cdd:PLN03142   481 PKLKERDSRVLIFSQMTRLLDILEDYLM-YRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATA 559
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2033488177  723 DTVILFDSDFNPQQDLQAQDRCHRIGQTRPVVVFRLATKDTVEENLLNSADAKRRLEKLVIKKG 786
Cdd:PLN03142   560 DIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQG 623
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
30-786 3.05e-126

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 405.34  E-value: 3.05e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177   30 EQQDDLEGADEALIKEEQEARL-ENERNEEKRRQAMLKRKKKKKAETKSEReAKAReLDDLLAKSAAFSDILT------- 101
Cdd:PLN03142    44 EDDEEAESPAKAEISKREKARLkELKKQKKQEIQKILEQQNAAIDADMNNK-GKGR-LKYLLQQTEIFAHFAKgdqsasa 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  102 KKTQVLGRVGSSL-------------DGKTLGEHSLEMAQQPKCmINGTMRDYQLEGLTWMYEICSQGMSGILADEMGLG 168
Cdd:PLN03142   122 KKAKGRGRHASKLteeeedeeylkeeEDGLGGSGGTRLLVQPSC-IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLG 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  169 KTVQTIALIALLREQENYLGPHLIVAPLSTLSNWEDEFTKWTPSIPVIMYHGNKDDREKIfRTKMLKhlkAGrpttKFPV 248
Cdd:PLN03142   201 KTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQ-REELLV---AG----KFDV 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  249 VCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQLRQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDW 328
Cdd:PLN03142   273 CVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSA 352
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  329 EAFESWFDFSDLEDEqgteefiadqkkQELVKKIHLILQPMLLRRIKQDVAAYLPKKREYVLFAPMTKEQTDLYNVLTNK 408
Cdd:PLN03142   353 ETFDEWFQISGENDQ------------QEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQK 420
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  409 KVDtrqyledkvhekiygtksteastkssrsssvaapntmtlpvresprkqqvepeepAANvfsvmmakrgrgrprknpk 488
Cdd:PLN03142   421 DLD-------------------------------------------------------VVN------------------- 426
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  489 leeapvtpkSGGKRkgapaslepepksakstrqstpvstrgrprktrtykdagsdeekmsddefeaklakemvsddedls 568
Cdd:PLN03142   427 ---------AGGER------------------------------------------------------------------ 431
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  569 gqvpltleeraqaeafelakkqigqKKLGNPLAQLRLVCNSPHNFYN-----PWIAstdlpvDDSIVTASGKMLLLDRLL 643
Cdd:PLN03142   432 -------------------------KRLLNIAMQLRKCCNHPYLFQGaepgpPYTT------GEHLVENSGKMVLLDKLL 480
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  644 PRLFQDDHKVLIFSQFTTQLDILEDYCReLRGWKVCRIDGSVAQESRRTQIADFNSDPEYK-IFLLSTRAGGQGINLASA 722
Cdd:PLN03142   481 PKLKERDSRVLIFSQMTRLLDILEDYLM-YRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATA 559
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2033488177  723 DTVILFDSDFNPQQDLQAQDRCHRIGQTRPVVVFRLATKDTVEENLLNSADAKRRLEKLVIKKG 786
Cdd:PLN03142   560 DIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQG 623
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
135-375 3.04e-115

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: 350.53  E-value: 3.04e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 135 NGTMRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYlGPHLIVAPLSTLSNWEDEFTKWTPSIP 214
Cdd:cd18009     1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVW-GPFLVIAPLSTLPNWVNEFARFTPSVP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 215 VIMYHGNKDDREKIfRTKMLKHLKAGRpttKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQLRQFS 294
Cdd:cd18009    80 VLLYHGTKEERERL-RKKIMKREGTLQ---DFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 295 SATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWFDFSDLEDEQGTEEFIADQKKQELVKKIHLILQPMLLRRI 374
Cdd:cd18009   156 SDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADISNLSEEREQNIVHMLHAILKPFLLRRL 235

                  .
gi 2033488177 375 K 375
Cdd:cd18009   236 K 236
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
33-783 8.02e-113

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 360.31  E-value: 8.02e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  33 DDLEGADEALIKEEQEARLENERNEEKRRQAMLKRKKKKKAETKSEREAKARELDDLLAKSAAFSDILTKKTQVLGRVGS 112
Cdd:COG0553   138 LLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEA 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 113 SLDGKTLGEHSLEMAQQPKCMiNGTMRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENyLGPHLI 192
Cdd:COG0553   218 AVDAFRLRRLREALESLPAGL-KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGL-ARPVLI 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 193 VAPLSTLSNWEDEFTKWTPSIPVIMYHGNKDdrekifRTKMLKHLKagrpttKFPVVCTSYEMVLRDQHNLSKINWEFII 272
Cdd:COG0553   296 VAPTSLVGNWQRELAKFAPGLRVLVLDGTRE------RAKGANPFE------DADLVITSYGLLRRDIELLAAVDWDLVI 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 273 IDEGHRMKNADAKLFQQLRQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWFDFSDLEDeqgteefiaD 352
Cdd:COG0553   364 LDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKG---------D 434
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 353 QKKQELVKKihlILQPMLLRRIKQDVAAYLPKKREYVLFAPMTKEQTDLYnvltnkkvdtrqyledkvhekiygtkstea 432
Cdd:COG0553   435 EEALERLRR---LLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALY------------------------------ 481
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 433 stkssrsssvaapntmtlpvresprkqqvepeepaanvfsvmmakrgrgrprknpkleeapvtpksggkrkgapaslepe 512
Cdd:COG0553       --------------------------------------------------------------------------------
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 513 pksakstrqstpvstrgrprktrtykdagsdeekmsdDEFEAKLAKEMVSDDEDLSGQVPLTLeeraqaeafelakkqig 592
Cdd:COG0553   482 -------------------------------------EAVLEYLRRELEGAEGIRRRGLILAA----------------- 507
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 593 qkklgnpLAQLRLVCNSPHNFynpwiastdLPVDDSIVTASGKMLLLDRLLPRLFQDDHKVLIFSQFTTQLDILEDYCRE 672
Cdd:COG0553   508 -------LTRLRQICSHPALL---------LEEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEE 571
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 673 lRGWKVCRIDGSVAQESRRTQIADFNSDPEYKIFLLSTRAGGQGINLASADTVILFDSDFNPQQDLQAQDRCHRIGQTRP 752
Cdd:COG0553   572 -RGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRD 650
                         730       740       750
                  ....*....|....*....|....*....|.
gi 2033488177 753 VVVFRLATKDTVEENLLNSADAKRRLEKLVI 783
Cdd:COG0553   651 VQVYKLVAEGTIEEKILELLEEKRALAESVL 681
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
141-403 7.14e-97

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: 304.61  E-value: 7.14e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 141 YQLEGLTWMYEICSQ-GMSGILADEMGLGKTVQTIALI-ALLREQENYLGPHLIVAPLSTLSNWEDEFTKWT--PSIPVI 216
Cdd:pfam00176   1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLlYLKHVDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 217 MYHGNKDDREKIFRTKMLKHlkagrpttKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQLRQFSSA 296
Cdd:pfam00176  81 VLHGNKRPQERWKNDPNFLA--------DFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 297 TRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWFDFSdledeqgteefIADQKKQELVKKIHLILQPMLLRRIKQ 376
Cdd:pfam00176 153 NRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRP-----------IERGGGKKGVSRLHKLLKPFLLRRTKK 221
                         250       260
                  ....*....|....*....|....*..
gi 2033488177 377 DVAAYLPKKREYVLFAPMTKEQTDLYN 403
Cdd:pfam00176 222 DVEKSLPPKVEYILFCRLSKLQRKLYQ 248
DEXDc smart00487
DEAD-like helicases superfamily;
137-326 3.55e-30

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 118.36  E-value: 3.55e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  137 TMRDYQLEGLTWMYEIcsqGMSGILADEMGLGKTVQtIALIALLREQENYLGPHLIVAPLSTL-SNWEDEFTKWTPS--- 212
Cdd:smart00487   8 PLRPYQKEAIEALLSG---LRDVILAAPTGSGKTLA-ALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKLGPSlgl 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  213 IPVIMYHGNKddrekifRTKMLKHLKAGRPttkfPVVCTSYEMVLRD--QHNLSKINWEFIIIDEGHRMKNAD-----AK 285
Cdd:smart00487  84 KVVGLYGGDS-------KREQLRKLESGKT----DILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDGGfgdqlEK 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2033488177  286 LFQQLRqfSSATRLLITGTP---LQNNLKELWSLLHFLLPNIFT 326
Cdd:smart00487 153 LLKLLP--KNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTP 194
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
30-786 3.05e-126

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 405.34  E-value: 3.05e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177   30 EQQDDLEGADEALIKEEQEARL-ENERNEEKRRQAMLKRKKKKKAETKSEReAKAReLDDLLAKSAAFSDILT------- 101
Cdd:PLN03142    44 EDDEEAESPAKAEISKREKARLkELKKQKKQEIQKILEQQNAAIDADMNNK-GKGR-LKYLLQQTEIFAHFAKgdqsasa 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  102 KKTQVLGRVGSSL-------------DGKTLGEHSLEMAQQPKCmINGTMRDYQLEGLTWMYEICSQGMSGILADEMGLG 168
Cdd:PLN03142   122 KKAKGRGRHASKLteeeedeeylkeeEDGLGGSGGTRLLVQPSC-IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLG 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  169 KTVQTIALIALLREQENYLGPHLIVAPLSTLSNWEDEFTKWTPSIPVIMYHGNKDDREKIfRTKMLKhlkAGrpttKFPV 248
Cdd:PLN03142   201 KTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQ-REELLV---AG----KFDV 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  249 VCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQLRQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDW 328
Cdd:PLN03142   273 CVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSA 352
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  329 EAFESWFDFSDLEDEqgteefiadqkkQELVKKIHLILQPMLLRRIKQDVAAYLPKKREYVLFAPMTKEQTDLYNVLTNK 408
Cdd:PLN03142   353 ETFDEWFQISGENDQ------------QEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQK 420
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  409 KVDtrqyledkvhekiygtksteastkssrsssvaapntmtlpvresprkqqvepeepAANvfsvmmakrgrgrprknpk 488
Cdd:PLN03142   421 DLD-------------------------------------------------------VVN------------------- 426
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  489 leeapvtpkSGGKRkgapaslepepksakstrqstpvstrgrprktrtykdagsdeekmsddefeaklakemvsddedls 568
Cdd:PLN03142   427 ---------AGGER------------------------------------------------------------------ 431
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  569 gqvpltleeraqaeafelakkqigqKKLGNPLAQLRLVCNSPHNFYN-----PWIAstdlpvDDSIVTASGKMLLLDRLL 643
Cdd:PLN03142   432 -------------------------KRLLNIAMQLRKCCNHPYLFQGaepgpPYTT------GEHLVENSGKMVLLDKLL 480
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  644 PRLFQDDHKVLIFSQFTTQLDILEDYCReLRGWKVCRIDGSVAQESRRTQIADFNSDPEYK-IFLLSTRAGGQGINLASA 722
Cdd:PLN03142   481 PKLKERDSRVLIFSQMTRLLDILEDYLM-YRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATA 559
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2033488177  723 DTVILFDSDFNPQQDLQAQDRCHRIGQTRPVVVFRLATKDTVEENLLNSADAKRRLEKLVIKKG 786
Cdd:PLN03142   560 DIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQG 623
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
135-375 3.04e-115

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: 350.53  E-value: 3.04e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 135 NGTMRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYlGPHLIVAPLSTLSNWEDEFTKWTPSIP 214
Cdd:cd18009     1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVW-GPFLVIAPLSTLPNWVNEFARFTPSVP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 215 VIMYHGNKDDREKIfRTKMLKHLKAGRpttKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQLRQFS 294
Cdd:cd18009    80 VLLYHGTKEERERL-RKKIMKREGTLQ---DFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 295 SATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWFDFSDLEDEQGTEEFIADQKKQELVKKIHLILQPMLLRRI 374
Cdd:cd18009   156 SDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADISNLSEEREQNIVHMLHAILKPFLLRRL 235

                  .
gi 2033488177 375 K 375
Cdd:cd18009   236 K 236
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
33-783 8.02e-113

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 360.31  E-value: 8.02e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  33 DDLEGADEALIKEEQEARLENERNEEKRRQAMLKRKKKKKAETKSEREAKARELDDLLAKSAAFSDILTKKTQVLGRVGS 112
Cdd:COG0553   138 LLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEA 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 113 SLDGKTLGEHSLEMAQQPKCMiNGTMRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENyLGPHLI 192
Cdd:COG0553   218 AVDAFRLRRLREALESLPAGL-KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGL-ARPVLI 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 193 VAPLSTLSNWEDEFTKWTPSIPVIMYHGNKDdrekifRTKMLKHLKagrpttKFPVVCTSYEMVLRDQHNLSKINWEFII 272
Cdd:COG0553   296 VAPTSLVGNWQRELAKFAPGLRVLVLDGTRE------RAKGANPFE------DADLVITSYGLLRRDIELLAAVDWDLVI 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 273 IDEGHRMKNADAKLFQQLRQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWFDFSDLEDeqgteefiaD 352
Cdd:COG0553   364 LDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKG---------D 434
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 353 QKKQELVKKihlILQPMLLRRIKQDVAAYLPKKREYVLFAPMTKEQTDLYnvltnkkvdtrqyledkvhekiygtkstea 432
Cdd:COG0553   435 EEALERLRR---LLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALY------------------------------ 481
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 433 stkssrsssvaapntmtlpvresprkqqvepeepaanvfsvmmakrgrgrprknpkleeapvtpksggkrkgapaslepe 512
Cdd:COG0553       --------------------------------------------------------------------------------
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 513 pksakstrqstpvstrgrprktrtykdagsdeekmsdDEFEAKLAKEMVSDDEDLSGQVPLTLeeraqaeafelakkqig 592
Cdd:COG0553   482 -------------------------------------EAVLEYLRRELEGAEGIRRRGLILAA----------------- 507
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 593 qkklgnpLAQLRLVCNSPHNFynpwiastdLPVDDSIVTASGKMLLLDRLLPRLFQDDHKVLIFSQFTTQLDILEDYCRE 672
Cdd:COG0553   508 -------LTRLRQICSHPALL---------LEEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEE 571
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 673 lRGWKVCRIDGSVAQESRRTQIADFNSDPEYKIFLLSTRAGGQGINLASADTVILFDSDFNPQQDLQAQDRCHRIGQTRP 752
Cdd:COG0553   572 -RGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRD 650
                         730       740       750
                  ....*....|....*....|....*....|.
gi 2033488177 753 VVVFRLATKDTVEENLLNSADAKRRLEKLVI 783
Cdd:COG0553   651 VQVYKLVAEGTIEEKILELLEEKRALAESVL 681
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
135-375 1.09e-104

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: 322.73  E-value: 1.09e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 135 NGTMRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYLGPHLIVAPLSTLSNWEDEFTKWTPSIP 214
Cdd:cd17997     1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 215 VIMYHGNKDDREKIFRTKMLkhlkagrpTTKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQLRQFS 294
Cdd:cd17997    81 VVVLIGDKEERADIIRDVLL--------PGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 295 SATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWFDFSDLEDEQgteefiadqkkQELVKKIHLILQPMLLRRI 374
Cdd:cd17997   153 SRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDN-----------QEVVQRLHKVLRPFLLRRI 221

                  .
gi 2033488177 375 K 375
Cdd:cd17997   222 K 222
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
141-403 7.14e-97

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: 304.61  E-value: 7.14e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 141 YQLEGLTWMYEICSQ-GMSGILADEMGLGKTVQTIALI-ALLREQENYLGPHLIVAPLSTLSNWEDEFTKWT--PSIPVI 216
Cdd:pfam00176   1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLlYLKHVDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 217 MYHGNKDDREKIFRTKMLKHlkagrpttKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQLRQFSSA 296
Cdd:pfam00176  81 VLHGNKRPQERWKNDPNFLA--------DFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 297 TRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWFDFSdledeqgteefIADQKKQELVKKIHLILQPMLLRRIKQ 376
Cdd:pfam00176 153 NRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRP-----------IERGGGKKGVSRLHKLLKPFLLRRTKK 221
                         250       260
                  ....*....|....*....|....*..
gi 2033488177 377 DVAAYLPKKREYVLFAPMTKEQTDLYN 403
Cdd:pfam00176 222 DVEKSLPPKVEYILFCRLSKLQRKLYQ 248
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
135-375 3.95e-93

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: 292.74  E-value: 3.95e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 135 NGTMRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYLGPHLIVAPLSTLSNWEDEFTKWTPSIP 214
Cdd:cd17996     1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 215 VIMYHGNKDDREKIFRTKMlkhlkagrpTTKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQL-RQF 293
Cdd:cd17996    81 KIVYKGTPDVRKKLQSQIR---------AGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLnTYY 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 294 SSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWFDfSDLEDEQGTEEFIADQKKQELV-KKIHLILQPMLLR 372
Cdd:cd17996   152 HARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFN-TPFANTGEQVKIELNEEETLLIiRRLHKVLRPFLLR 230

                  ...
gi 2033488177 373 RIK 375
Cdd:cd17996   231 RLK 233
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
138-322 5.21e-85

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: 269.05  E-value: 5.21e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYLGPHLIVAPLSTLSNWEDEFTKWTPSIPVIM 217
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 218 YHGNKDDREKIFRTKMLKhlkagrpttKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQLRQFSSAT 297
Cdd:cd17919    81 YHGSQRERAQIRAKEKLD---------KFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKR 151
                         170       180
                  ....*....|....*....|....*
gi 2033488177 298 RLLITGTPLQNNLKELWSLLHFLLP 322
Cdd:cd17919   152 RLLLTGTPLQNNLEELWALLDFLDP 176
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
137-373 8.43e-83

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: 264.99  E-value: 8.43e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 137 TMRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYLGPHLIVAPLSTLSNWEDEFTKWTPSIPVI 216
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 217 MYHGNKDDREKIFRTKMLKhlkAGRPTTKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQLRQFSSA 296
Cdd:cd17993    81 VYLGDIKSRDTIREYEFYF---SQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTN 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2033488177 297 TRLLITGTPLQNNLKELWSLLHFLLPniftdwEAFESWFDFSDLEDEqgteefiaDQKKQelVKKIHLILQPMLLRR 373
Cdd:cd17993   158 NRLLITGTPLQNSLKELWALLHFLMP------GKFDIWEEFEEEHDE--------EQEKG--IADLHKELEPFILRR 218
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
138-373 1.14e-81

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: 261.80  E-value: 1.14e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYLGPHLIVAPLSTLSNWEDEFTKWTPsIPVIM 217
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 218 YHGNKDDREKIFRTKMLKHLKAGRP---TTKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQLRQFS 294
Cdd:cd17995    80 YHGSGESRQIIQQYEMYFKDAQGRKkkgVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2033488177 295 SATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESwfDFSDLedeqgteefiadqKKQELVKKIHLILQPMLLRR 373
Cdd:cd17995   160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLE--EFGDL-------------KTAEQVEKLQALLKPYMLRR 223
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
138-373 2.49e-78

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: 253.04  E-value: 2.49e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYLGPHLIVAPLSTLSNWEDEFTKWTPSIPVIM 217
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 218 YHGNKDDREkifrtkmLKHLKAGRPTTkFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQLRQFSSAT 297
Cdd:cd18003    81 YYGSAKERK-------LKRQGWMKPNS-FHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQR 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2033488177 298 RLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWF-DFSDLEDEQGTEEfiadqkKQELVKKIHLILQPMLLRR 373
Cdd:cd18003   153 RLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFsNPLTAMSEGSQEE------NEELVRRLHKVLRPFLLRR 223
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
128-375 3.66e-72

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: 236.84  E-value: 3.66e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 128 QQPKCMINGTMRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYLGPHLIVAPLSTLSNWEDEFT 207
Cdd:cd18065     6 ESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 208 KWTPSIPVIMYHGNKDDREKIFRTKMLKhlkagrptTKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLF 287
Cdd:cd18065    86 RWVPSLRAVCLIGDKDARAAFIRDVMMP--------GEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 288 QQLRQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWFDfsdledeqgTEEFIADQKkqeLVKKIHLILQ 367
Cdd:cd18065   158 EIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFD---------TKNCLGDQK---LVERLHAVLK 225

                  ....*...
gi 2033488177 368 PMLLRRIK 375
Cdd:cd18065   226 PFLLRRIK 233
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
136-386 3.35e-71

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: 234.95  E-value: 3.35e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 136 GTMRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYLGPHLIVAPLSTLSNWEDEFTKWTPSIPV 215
Cdd:cd18064    14 GKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 216 IMYHGNKDDREKIFRTKMLKhlkagrptTKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQLRQFSS 295
Cdd:cd18064    94 VCLIGDKDQRAAFVRDVLLP--------GEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 296 ATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWFDfsdledeqgTEEFIADQKkqeLVKKIHLILQPMLLRRIK 375
Cdd:cd18064   166 TNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFD---------TNNCLGDQK---LVERLHMVLRPFLLRRIK 233
                         250
                  ....*....|.
gi 2033488177 376 QDVAAYLPKKR 386
Cdd:cd18064   234 ADVEKSLPPKK 244
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
138-373 2.98e-70

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: 231.82  E-value: 2.98e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYLGPHLIVAPLSTLSNWEDEFTKWTPSIPVIM 217
Cdd:cd18054    21 LRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVVV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 218 YHGNKDDREKIfRTKMLKHLKAGRptTKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQLRQFSSAT 297
Cdd:cd18054   101 YIGDLMSRNTI-REYEWIHSQTKR--LKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNH 177
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2033488177 298 RLLITGTPLQNNLKELWSLLHFLLPniftdwEAFESWFDFsdlEDEQGteefiadQKKQELVKKIHLILQPMLLRR 373
Cdd:cd18054   178 RLLITGTPLQNSLKELWSLLHFIMP------EKFEFWEDF---EEDHG-------KGRENGYQSLHKVLEPFLLRR 237
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
123-375 9.40e-70

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: 231.11  E-value: 9.40e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 123 SLEMAQQPKCMINGTMRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYLGPHLIVAPLSTLSNW 202
Cdd:cd18063     9 TERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNW 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 203 EDEFTKWTPSIPVIMYHGNkddreKIFRTKMLKHLKAGrpttKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNA 282
Cdd:cd18063    89 TYEFDKWAPSVVKISYKGT-----PAMRRSLVPQLRSG----KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 283 DAKLFQQLR-QFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWFD--FSdledEQGTEEFIADQKKQELV 359
Cdd:cd18063   160 HCKLTQVLNtHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapFA----MTGERVDLNEEETILII 235
                         250
                  ....*....|....*.
gi 2033488177 360 KKIHLILQPMLLRRIK 375
Cdd:cd18063   236 RRLHKVLRPFLLRRLK 251
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
138-373 8.81e-68

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: 225.08  E-value: 8.81e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYLGPHLIVAPLSTLSNWEDEFTKWTPSIPVIM 217
Cdd:cd18002     1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 218 YHGNKDDREKIFRTKMLKHLKagRPTTKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQLRQFSSAT 297
Cdd:cd18002    81 YWGNPKDRKVLRKFWDRKNLY--TRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRN 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2033488177 298 RLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWFDfSDLEDEQGTEEFIadqkKQELVKKIHLILQPMLLRR 373
Cdd:cd18002   159 RLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFS-KDIESHAENKTGL----NEHQLKRLHMILKPFMLRR 229
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
128-375 5.55e-66

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: 221.07  E-value: 5.55e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 128 QQPKCMINGTMRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYLGPHLIVAPLSTLSNWEDEFT 207
Cdd:cd18062    14 KQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWVYEFD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 208 KWTPSIPVIMYHGNKDDREkifrtKMLKHLKAGrpttKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLF 287
Cdd:cd18062    94 KWAPSVVKVSYKGSPAARR-----AFVPQLRSG----KFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 288 QQLR-QFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWFD--FSdledEQGTEEFIADQKKQELVKKIHL 364
Cdd:cd18062   165 QVLNtHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapFA----MTGEKVDLNEEETILIIRRLHK 240
                         250
                  ....*....|.
gi 2033488177 365 ILQPMLLRRIK 375
Cdd:cd18062   241 VLRPFLLRRLK 251
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
134-375 2.72e-65

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: 217.82  E-value: 2.72e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 134 INGTMRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIaLLREQENYLGPHLIVAPLSTLSNWEDEFTKWTPSI 213
Cdd:cd18012     1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALL-LSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 214 PVIMYHGNKDDREKIFRTKmlkhlkagrpttKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQLRQF 293
Cdd:cd18012    80 KVLVIHGTKRKREKLRALE------------DYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKAL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 294 SSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESwfDFSDLEDEQGTEEfiadqKKQELVKKIhlilQPMLLRR 373
Cdd:cd18012   148 KADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKK--RFAKPIEKDGDEE-----ALEELKKLI----SPFILRR 216

                  ..
gi 2033488177 374 IK 375
Cdd:cd18012   217 LK 218
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
138-373 2.50e-64

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: 214.99  E-value: 2.50e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYLGPHLIVAPLSTLSNWEDEFTKWTPSIPVIM 217
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 218 YHGnkdDREKifRTKMLKHLKAgrpTTKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQLRQFSSAT 297
Cdd:cd18006    81 YMG---DKEK--RLDLQQDIKS---TNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDF 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2033488177 298 RLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWFDFSDLEDEQGTeefiadqkkqelVKKIHLILQPMLLRR 373
Cdd:cd18006   153 RLLLTGTPIQNSLQELYALLSFIEPNVFPKDKLDDFIKAYSETDDESET------------VEELHLLLQPFLLRR 216
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
141-373 4.96e-61

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: 205.37  E-value: 4.96e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 141 YQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYLGPHLIVAPLSTLSNWEDEFTKWTPSIPVIMYHG 220
Cdd:cd17994     4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVTYVG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 221 NKddrekifrtkmlkhlkagrpttkfpVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQLRQFSSATRLL 300
Cdd:cd17994    84 DH-------------------------VLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLL 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2033488177 301 ITGTPLQNNLKELWSLLHFLLPNIFTDWEAFeswfdfsdledeqgTEEFiADQKKQELVKKIHLILQPMLLRR 373
Cdd:cd17994   139 LTGTPLQNNLEELFHLLNFLTPERFNNLQGF--------------LEEF-ADISKEDQIKKLHDLLGPHMLRR 196
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
138-373 6.46e-59

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: 201.05  E-value: 6.46e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYLGPHLIVAPLSTLSNWEDEFTKWTPSIPVIM 217
Cdd:cd18053    21 LRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAVV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 218 YHGNKDDREKIfRTKMLKHLKAGRptTKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQLRQFSSAT 297
Cdd:cd18053   101 YLGDINSRNMI-RTHEWMHPQTKR--LKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNH 177
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2033488177 298 RLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFeswfdfsdlEDEQGteefiadQKKQELVKKIHLILQPMLLRR 373
Cdd:cd18053   178 RLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDF---------EEEHG-------KGREYGYASLHKELEPFLLRR 237
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
138-325 8.46e-58

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: 196.07  E-value: 8.46e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYlGPHLIVAPLSTLSNWEDEFTKWTPSIPVIM 217
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIP-GPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 218 YHGNKDDREKIfRTKMLKHLkagrptTKFPVVCTSYEMVLRDQHN---LSKINWEFIIIDEGHRMKNADAKLFQQLRQFS 294
Cdd:cd17998    80 YYGSQEERKHL-RYDILKGL------EDFDVIVTTYNLATSNPDDrsfFKRLKLNYVVYDEGHMLKNMTSERYRHLMTIN 152
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2033488177 295 SATRLLITGTPLQNNLKELWSLLHFLLPNIF 325
Cdd:cd17998   153 ANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
138-373 5.02e-56

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: 192.56  E-value: 5.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIAllreqENYL----GPHLIVAPLSTLSNWEDEFTKWTpSI 213
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLS-----EIFLmgirGPFLIIAPLSTITNWEREFRTWT-EM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 214 PVIMYHGNKDDREKIFRTKMLKHLKAGRPTT---KFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQL 290
Cdd:cd18058    75 NAIVYHGSQISRQMIQQYEMYYRDEQGNPLSgifKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 291 RQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFeswfdfsdledeqgTEEFiADQKKQELVKKIHLILQPML 370
Cdd:cd18058   155 KLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTF--------------LEEF-GDLKTEEQVKKLQSILKPMM 219

                  ...
gi 2033488177 371 LRR 373
Cdd:cd18058   220 LRR 222
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
141-373 1.64e-54

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: 188.68  E-value: 1.64e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 141 YQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYLGPHLIVAPLSTLSNWEDEFTKWTPSIPVIMYHG 220
Cdd:cd18055     4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVTYTG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 221 NKDDREKI------FRTKMLKHLKAG-----RPTTKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQ 289
Cdd:cd18055    84 DKDSRAIIrenefsFDDNAVKGGKKAfkmkrEAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKFFRV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 290 LRQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFeswfdfsdledeqgTEEFiADQKKQELVKKIHLILQPM 369
Cdd:cd18055   164 LNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGF--------------LEEF-ADISKEDQIKKLHDLLGPH 228

                  ....
gi 2033488177 370 LLRR 373
Cdd:cd18055   229 MLRR 232
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
629-758 4.25e-54

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: 183.83  E-value: 4.25e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 629 IVTASGKMLLLDRLLPRLFQDDHKVLIFSQFTTQLDILEDYCRElRGWKVCRIDGSVAQESRRTQIADFNSDPEYKIFLL 708
Cdd:cd18793     6 EEVVSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRE-RGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLL 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2033488177 709 STRAGGQGINLASADTVILFDSDFNPQQDLQAQDRCHRIGQTRPVVVFRL 758
Cdd:cd18793    85 STKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRL 134
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
140-322 5.68e-53

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: 182.91  E-value: 5.68e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 140 DYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYLGPHLIVAPLSTLSNWEDEFTKWTPSIPVIMYH 219
Cdd:cd18000     3 KYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVVLH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 220 ------GNKDDREKIFRTKMLKHLKAGRPTtkfpVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQLRQF 293
Cdd:cd18000    83 ssgsgtGSEEKLGSIERKSQLIRKVVGDGG----ILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQL 158
                         170       180
                  ....*....|....*....|....*....
gi 2033488177 294 SSATRLLITGTPLQNNLKELWSLLHFLLP 322
Cdd:cd18000   159 RTPHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
138-373 5.94e-53

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: 184.50  E-value: 5.94e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYLGPHLIVAPLSTLSNWEDEFTKWTPSIPVIM 217
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 218 YHGNKDDR------------------EKIFRTKMLKHLkagrpttKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRM 279
Cdd:cd18057    81 YTGDKESRsvirenefsfednairsgKKVFRMKKEAQI-------KFHVLLTSYELITIDQAILGSIEWACLVVDEAHRL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 280 KNADAKLFQQLRQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFeswfdfsdledeqgTEEFiADQKKQELV 359
Cdd:cd18057   154 KNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGF--------------LEEF-ADISKEDQI 218
                         250
                  ....*....|....
gi 2033488177 360 KKIHLILQPMLLRR 373
Cdd:cd18057   219 KKLHDLLGPHMLRR 232
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
138-373 1.86e-52

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: 183.35  E-value: 1.86e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALL-------REQENYL-------------GPHLIVAPLS 197
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVlgktgtrRDRENNRprfkkkppassakKPVLIVAPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 198 TLSNWEDEFTKWTpSIPVIMYHGNKDDREKIFRtkmlkhLKAGRpttkFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGH 277
Cdd:cd18005    81 VLYNWKDELDTWG-HFEVGVYHGSRKDDELEGR------LKAGR----LEVVVTTYDTLRRCIDSLNSINWSAVIADEAH 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 278 RMKNADAKLFQQLRQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESwfDFSD-LEDEQ---GTEEFI--A 351
Cdd:cd18005   150 RIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKK--HFSEpIKRGQrhtATARELrlG 227
                         250       260
                  ....*....|....*....|..
gi 2033488177 352 DQKKQELVKKihliLQPMLLRR 373
Cdd:cd18005   228 RKRKQELAVK----LSKFFLRR 245
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
140-373 5.47e-52

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: 181.42  E-value: 5.47e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 140 DYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQEnYLGPHLIVAPLSTLSNWEDEFTKWTPSIPVIMYH 219
Cdd:cd18001     3 PHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSG-LIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKVFH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 220 G-NKDDREKIfrtkmLKHLKagrptTKFPVVCTSYEMVLRDQHNLSKIN-----WEFIIIDEGHRMKNADAKLFQQLRQF 293
Cdd:cd18001    82 GtSKKERERN-----LERIQ-----RGGGVLLTTYGMVLSNTEQLSADDhdefkWDYVILDEGHKIKNSKTKSAKSLREI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 294 SSATRLLITGTPLQNNLKELWSLLHFLLPNIFTdweAFESWFDfSDLED--EQGTEEFIADQKK---QELVKKIHLILQP 368
Cdd:cd18001   152 PAKNRIILTGTPIQNNLKELWALFDFACNGSLL---GTRKTFK-MEFENpiTRGRDKDATQGEKalgSEVAENLRQIIKP 227

                  ....*
gi 2033488177 369 MLLRR 373
Cdd:cd18001   228 YFLRR 232
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
138-373 7.59e-52

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: 181.02  E-value: 7.59e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIallreQENY----LGPHLIVAPLSTLSNWEDEFTKWTpSI 213
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFL-----QEVYnvgiHGPFLVIAPLSTITNWEREFNTWT-EM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 214 PVIMYHGNKDDREKIFRTKMLKHLKAGR---PTTKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQL 290
Cdd:cd18060    75 NTIVYHGSLASRQMIQQYEMYCKDSRGRlipGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 291 RQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESwfDFSDLedeqgteefiadqKKQELVKKIHLILQPML 370
Cdd:cd18060   155 KHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLK--DFGDL-------------KTEEQVQKLQAILKPMM 219

                  ...
gi 2033488177 371 LRR 373
Cdd:cd18060   220 LRR 222
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
138-373 1.61e-51

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: 180.26  E-value: 1.61e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYLGPHLIVAPLSTLSNWEDEFTKWTPSIPVIM 217
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 218 YHGNKDDREKI------FRTKMLK-HLKAGR----PTTKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKL 286
Cdd:cd18056    81 YVGDKDSRAIIrenefsFEDNAIRgGKKASRmkkeASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 287 FQQLRQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFeswfdfsdledeqgTEEFiADQKKQELVKKIHLIL 366
Cdd:cd18056   161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGF--------------LEEF-ADIAKEDQIKKLHDML 225

                  ....*..
gi 2033488177 367 QPMLLRR 373
Cdd:cd18056   226 GPHMLRR 232
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
138-373 8.05e-49

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: 172.52  E-value: 8.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIallreQENYL----GPHLIVAPLSTLSNWEDEFTKWTpSI 213
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-----YEIYLkgihGPFLVIAPLSTIPNWEREFRTWT-EL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 214 PVIMYHGNKDDREKIFRTKMLKHLKAGR---PTTKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQL 290
Cdd:cd18059    75 NVVVYHGSQASRRTIQLYEMYFKDPQGRvikGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 291 RQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFeswfdfsdledeqgTEEFiADQKKQELVKKIHLILQPML 370
Cdd:cd18059   155 KMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTF--------------MQEF-GDLKTEEQVQKLQAILKPMM 219

                  ...
gi 2033488177 371 LRR 373
Cdd:cd18059   220 LRR 222
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
138-373 2.33e-48

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: 170.96  E-value: 2.33e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIallreQENYL----GPHLIVAPLSTLSNWEDEFTKWTpSI 213
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-----YEILLtgirGPFLIIAPLSTIANWEREFRTWT-DL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 214 PVIMYHGNKDDREKIFRTKMLKHLKAGR---PTTKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQL 290
Cdd:cd18061    75 NVVVYHGSLISRQMIQQYEMYFRDSQGRiirGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 291 RQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFeswfdfsdledeqgTEEFiADQKKQELVKKIHLILQPML 370
Cdd:cd18061   155 KLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTF--------------MQEF-GDLKTEEQVQKLQAILKPMM 219

                  ...
gi 2033488177 371 LRR 373
Cdd:cd18061   220 LRR 222
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
139-373 4.98e-48

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: 170.93  E-value: 4.98e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 139 RDYQLEGLTWMyeiCSQGmsGILADEMGLGKTVQTIALIALLREQENYLGPH-----------------LIVAPLSTLSN 201
Cdd:cd18008     2 LPYQKQGLAWM---LPRG--GILADEMGLGKTIQALALILATRPQDPKIPEEleenssdpkklylskttLIVVPLSLLSQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 202 WEDEFTK--WTPSIPVIMYHGNKddrekifRTKMLKHLKagrpttKFPVVCTSYEMVLRD--QHN--------------L 263
Cdd:cd18008    77 WKDEIEKhtKPGSLKVYVYHGSK-------RIKSIEELS------DYDIVITTYGTLASEfpKNKkgggrdskekeaspL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 264 SKINWEFIIIDEGHRMKNADAKLFQQLRQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWFDFSDLEDE 343
Cdd:cd18008   144 HRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKND 223
                         250       260       270
                  ....*....|....*....|....*....|
gi 2033488177 344 QGTeefiadqkkqelVKKIHLILQPMLLRR 373
Cdd:cd18008   224 RKA------------LERLQALLKPILLRR 241
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
138-373 4.08e-47

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: 167.91  E-value: 4.08e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMYEICSQGMSGILADEMGLGKTVQTIALIAL---LREQENYLG--PHLIVAPLSTLSNWEDEFTKWTP- 211
Cdd:cd17999     1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASdhhKRANSFNSEnlPSLVVCPPTLVGHWVAEIKKYFPn 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 212 -SIPVIMYHGNKDDREKIfRTKMLKHlkagrpttkfPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQL 290
Cdd:cd17999    81 aFLKPLAYVGPPQERRRL-REQGEKH----------NVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 291 RQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWF--DFSDLEDEQGTEEFIADQKKQelVKKIHLILQP 368
Cdd:cd17999   150 KQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFlkPILASRDSKASAKEQEAGALA--LEALHKQVLP 227

                  ....*
gi 2033488177 369 MLLRR 373
Cdd:cd17999   228 FLLRR 232
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
138-373 5.57e-45

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: 162.07  E-value: 5.57e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMYEiCSQGMSG------ILADEMGLGKTVQTIALIALLREQENYLGPH----LIVAPLSTLSNWEDEFT 207
Cdd:cd18004     1 LRPHQREGVQFLYD-CLTGRRGyggggaILADEMGLGKTLQAIALVWTLLKQGPYGKPTakkaLIVCPSSLVGNWKAEFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 208 KWTPS--IPVIMYHGNKDDREKIfrtkmLKHLKAGRPttkFPVVCTSYEMVLRDQHNLSK-INWEFIIIDEGHRMKNADA 284
Cdd:cd18004    80 KWLGLrrIKVVTADGNAKDVKAS-----LDFFSSAST---YPVLIISYETLRRHAEKLSKkISIDLLICDEGHRLKNSES 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 285 KLFQQLRQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWFDFSDLE--DEQGTEEFI--ADQKKQELVK 360
Cdd:cd18004   152 KTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRsrDPDASEEDKelGAERSQELSE 231
                         250
                  ....*....|...
gi 2033488177 361 kihlILQPMLLRR 373
Cdd:cd18004   232 ----LTSRFILRR 240
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
138-335 6.95e-38

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: 141.66  E-value: 6.95e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMYEICSQGMSG-------ILADEMGLGKTVQTIALI-ALLREQENYLGPhLIVAPLSTLSNWEDEFTKW 209
Cdd:cd18007     1 LKPHQVEGVRFLWSNLVGTDVGsdegggcILAHTMGLGKTLQVITFLhTYLAAAPRRSRP-LVLCPASTLYNWEDEFKKW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 210 TPSIPVIMYHGNKDDREKIF--RTKMLK--HLKAGrpttkfpVVCTSYEM---VLRDQHNLSKINWEF-----------I 271
Cdd:cd18007    80 LPPDLRPLLVLVSLSASKRAdaRLRKINkwHKEGG-------VLLIGYELfrnLASNATTDPRLKQEFiaalldpgpdlL 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2033488177 272 IIDEGHRMKNADAKLFQQLRQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWF 335
Cdd:cd18007   153 VLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
138-373 3.49e-36

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: 137.22  E-value: 3.49e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMYEiCSQGMSG------ILADEMGLGKTVQTIALIALLREQENYLGPHL----IVAPLSTLSNWEDEFT 207
Cdd:cd18067     1 LRPHQREGVKFLYR-CVTGRRIrgshgcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaiVVSPSSLVKNWANELG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 208 KWTPS--IPVIMYHGNKDDREKIFRTKMLKHlkaGRPTTKfPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAK 285
Cdd:cd18067    80 KWLGGrlQPLAIDGGSKKEIDRKLVQWASQQ---GRRVST-PVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 286 LFQQLRQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWFDFSDLE--DEQGTEEFI--ADQKKQELVKk 361
Cdd:cd18067   156 TYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKgrDADASEKERqlGEEKLQELIS- 234
                         250
                  ....*....|..
gi 2033488177 362 ihlILQPMLLRR 373
Cdd:cd18067   235 ---IVNRCIIRR 243
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
138-373 9.12e-36

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: 135.74  E-value: 9.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMYEiCSQGM------SGILADEMGLGKTVQTIALIALLREQENY-----LGPHLIVAPLSTLSNWEDEF 206
Cdd:cd18066     1 LRPHQREGIEFLYE-CVMGMrvnerfGAILADEMGLGKTLQCISLIWTLLRQGPYggkpvIKRALIVTPGSLVKNWKKEF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 207 TKWTPSipvimyhgnkdDREKIFRTKMLKHLKAGRPTTKFPVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKL 286
Cdd:cd18066    80 QKWLGS-----------ERIKVFTVDQDHKVEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKT 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 287 FQQLRQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWFDFSDLEDEQGT----EEFIADQKKQELVKKI 362
Cdd:cd18066   149 TTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTatpeEKKLGEARAAELTRLT 228
                         250
                  ....*....|.
gi 2033488177 363 HLilqpMLLRR 373
Cdd:cd18066   229 GL----FILRR 235
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
140-331 9.18e-32

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: 123.08  E-value: 9.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 140 DYQLEGLTWmyeICSQGMSGILADEMGLGKTVQTIALIALLREQenylGPHLIVAPLSTLSNWEDEFTKWTPSIP---VI 216
Cdd:cd18010     3 PFQREGVCF---ALRRGGRVLIADEMGLGKTVQAIAIAAYYREE----WPLLIVCPSSLRLTWADEIERWLPSLPpddIQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 217 MYHGNKDDrekifrtkmlkhLKAGRPTtkfpVVCTSYEMVLRDQHNLSKINWEFIIIDEGHRMKNADAKLFQQLRQFSSA 296
Cdd:cd18010    76 VIVKSKDG------------LRDGDAK----VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLLKR 139
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2033488177 297 TR--LLITGTPLQNNLKELWSLLHFLLPNIFTDWEAF 331
Cdd:cd18010   140 AKrvILLSGTPALSRPIELFTQLDALDPKLFGRFHDF 176
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
159-320 1.35e-31

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: 123.73  E-value: 1.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 159 GILADEMGLGKTVQTIALIALlreqenylGPHLIVAPLSTLSNWEDEFTKWTPS--IPVIMYHGNkddrEKIFRTKMLkh 236
Cdd:cd18071    51 GILADDMGLGKTLTTISLILA--------NFTLIVCPLSVLSNWETQFEEHVKPgqLKVYTYHGG----ERNRDPKLL-- 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 237 lkagrptTKFPVVCTSYEMVLRD-----QHNLSKINWEFIIIDEGHRMKNADAKLFQQLRQFSSATRLLITGTPLQNNLK 311
Cdd:cd18071   117 -------SKYDIVLTTYNTLASDfgakgDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPK 189

                  ....*....
gi 2033488177 312 ELWSLLHFL 320
Cdd:cd18071   190 DLGSLLSFL 198
DEXDc smart00487
DEAD-like helicases superfamily;
137-326 3.55e-30

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 118.36  E-value: 3.55e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  137 TMRDYQLEGLTWMYEIcsqGMSGILADEMGLGKTVQtIALIALLREQENYLGPHLIVAPLSTL-SNWEDEFTKWTPS--- 212
Cdd:smart00487   8 PLRPYQKEAIEALLSG---LRDVILAAPTGSGKTLA-ALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKLGPSlgl 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  213 IPVIMYHGNKddrekifRTKMLKHLKAGRPttkfPVVCTSYEMVLRD--QHNLSKINWEFIIIDEGHRMKNAD-----AK 285
Cdd:smart00487  84 KVVGLYGGDS-------KREQLRKLESGKT----DILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDGGfgdqlEK 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2033488177  286 LFQQLRqfSSATRLLITGTP---LQNNLKELWSLLHFLLPNIFT 326
Cdd:smart00487 153 LLKLLP--KNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTP 194
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
648-748 5.32e-26

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: 103.06  E-value: 5.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 648 QDDHKVLIFSQFTTQLDilEDYCRELRGWKVCRIDGSVAQESRRTQIADFNsDPEYKIfLLSTRAGGQGINLASADTVIL 727
Cdd:pfam00271  13 ERGGKVLIFSQTKKTLE--AELLLEKEGIKVARLHGDLSQEEREEILEDFR-KGKIDV-LVATDVAERGLDLPDVDLVIN 88
                          90       100
                  ....*....|....*....|.
gi 2033488177 728 FDSDFNPQQDLQAQDRCHRIG 748
Cdd:pfam00271  89 YDLPWNPASYIQRIGRAGRAG 109
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
141-336 9.44e-26

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: 106.44  E-value: 9.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 141 YQLEGLTWMYEIC---------SQGMSGILADEMGLGKTVQTIALIALLReQENYLGPHLIVAPLSTLSNWEDEFTKWTP 211
Cdd:cd18069     4 HQIGGIRFLYDNIieslerykgSSGFGCILAHSMGLGKTLQVISFLDVLL-RHTGAKTVLAIVPVNTLQNWLSEFNKWLP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 212 SipvimYHGNKDDREKIFRTKML----KHLKAGRP-----TTKFPVVCTSYEMV-LRDQHNLskinwefIIIDEGHRMKN 281
Cdd:cd18069    83 P-----PEALPNVRPRPFKVFILndehKTTAARAKviedwVKDGGVLLMGYEMFrLRPGPDV-------VICDEGHRIKN 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2033488177 282 ADAKLFQQLRQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWFD 336
Cdd:cd18069   151 CHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFE 205
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
141-373 2.55e-25

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: 105.64  E-value: 2.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 141 YQLEGLTWMYEICSQGMSG-ILADEMGLGKTVQTIALIALLREQENYLGPH----------------------LIVAPLS 197
Cdd:cd18072     4 HQKQALAWLLWRERQKPRGgILADDMGLGKTLTMIALILAQKNTQNRKEEEkekalteweskkdstlvpsagtLVVCPAS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 198 TLSNWEDEFTKWTPS--IPVIMYHG-NKDDREKIFRTkmlkhlkagrpttkFPVVCTSYEMVLRD---------QHNLSK 265
Cdd:cd18072    84 LVHQWKNEVESRVASnkLRVCLYHGpNRERIGEVLRD--------------YDIVITTYSLVAKEiptykeesrSSPLFR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 266 INWEFIIIDEGHRMKNADAKLFQQLRQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWFdfsDLEDEQG 345
Cdd:cd18072   150 IAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQV---DNKSRKG 226
                         250       260
                  ....*....|....*....|....*...
gi 2033488177 346 TEefiadqkkqelvkKIHLILQPMLLRR 373
Cdd:cd18072   227 GE-------------RLNILTKSLLLRR 241
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
138-343 2.76e-25

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: 104.29  E-value: 2.76e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLtwmYEICSQGMSG-ILADEMGLGKTVQTIALIALLrEQENYLGPHLIVAPLSTLSNWEDE-FTKWTPSIPV 215
Cdd:cd18011     1 PLPHQIDAV---LRALRKPPVRlLLADEVGLGKTIEAGLIIKEL-LLRGDAKRVLILCPASLVEQWQDElQDKFGLPFLI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 216 ImyhgnkdDREKIFRTKMLkhlkAGRPTTKFPVVCTSYEMVLRD---QHNLSKINWEFIIIDEGHRMKNA----DAKLFQ 288
Cdd:cd18011    77 L-------DRETAAQLRRL----IGNPFEEFPIVIVSLDLLKRSeerRGLLLSEEWDLVVVDEAHKLRNSgggkETKRYK 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2033488177 289 QLRQFSSATR--LLITGTPLQNNLKELWSLLHFLlpniftDWEAFESWFDFSDLEDE 343
Cdd:cd18011   146 LGRLLAKRARhvLLLTATPHNGKEEDFRALLSLL------DPGRFAVLGRFLRLDGL 196
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
138-335 6.63e-25

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: 104.58  E-value: 6.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMYEIC---------SQGMSGILADEMGLGKTVQTIALI--ALLREQENYLGPHLIVAPLSTLSNWEDEF 206
Cdd:cd18068     1 LKPHQVDGVQFMWDCCceslkktkkSPGSGCILAHCMGLGKTLQVVTFLhtVLLCEKLENFSRVLVVCPLNTVLNWLNEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 207 TKWTpsipvimyHGNKDDrEKI-------FRTKMLKHLKAGRPTTKFPVVCTSYEMV--------------LRDQHNLSK 265
Cdd:cd18068    81 EKWQ--------EGLKDE-EKIevnelatYKRPQERSYKLQRWQEEGGVMIIGYDMYrilaqernvksrekLKEIFNKAL 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2033488177 266 INW--EFIIIDEGHRMKNADAKLFQQLRQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDWEAFESWF 335
Cdd:cd18068   152 VDPgpDFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
HELICc smart00490
helicase superfamily c-terminal domain;
664-748 4.86e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 88.04  E-value: 4.86e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177  664 DILEDYCRElRGWKVCRIDGSVAQESRRTQIADFNSDPeyKIFLLSTRAGGQGINLASADTVILFDSDFNPQQDLQAQDR 743
Cdd:smart00490   1 EELAELLKE-LGIKVARLHGGLSQEEREEILDKFNNGK--IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                   ....*
gi 2033488177  744 CHRIG 748
Cdd:smart00490  78 AGRAG 82
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
138-337 5.52e-20

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: 90.48  E-value: 5.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMyeICSQGmsgILADEMGLGKTVQTIALIALLREQEN-------------------------YLGPHLI 192
Cdd:cd18070     1 LLPYQRRAVNWM--LVPGG---ILADEMGLGKTVEVLALILLHPRPDNdldaadddsdemvccpdclvaetpvSSKATLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 193 VAPLSTLSNWEDEFTKWTP-SIPVIMYHGNKDDrekifrtkMLKHLKAGRPTTKFPVVCTSYEmVLRDQ-------HN-- 262
Cdd:cd18070    76 VCPSAILAQWLDEINRHVPsSLKVLTYQGVKKD--------GALASPAPEILAEYDIVVTTYD-VLRTElhyaeanRSnr 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 263 --------------LSKINWEFIIIDEGHRMKNADAKLFQQLRQFSSATRLLITGTPLQNNLKELWSLLHFLLPNIFTDw 328
Cdd:cd18070   147 rrrrqkryeappspLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCD- 225

                  ....*....
gi 2033488177 329 eafESWFDF 337
Cdd:cd18070   226 ---SDWWAR 231
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
138-362 2.13e-15

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: 76.23  E-value: 2.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWmyeICSQGMSGILADeMGLGKTVQTIALIALLREqENYLGPHLIVAPLSTLSN-WEDEFTKWtpSIPVI 216
Cdd:cd18013     1 PHPYQKVAINF---IIEHPYCGLFLD-MGLGKTVTTLTALSDLQL-DDFTRRVLVIAPLRVARStWPDEVEKW--NHLRN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 217 MYHGNKDDREKIfRTKMLkhlkagrpTTKFPVVCTSYEMvLRDQHNLSKINWEF--IIIDEGHRMKNADAKLFQQLRQFS 294
Cdd:cd18013    74 LTVSVAVGTERQ-RSKAA--------NTPADLYVINREN-LKWLVNKSGDPWPFdmVVIDELSSFKSPRSKRFKALRKVR 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2033488177 295 SATRLLI--TGTPLQNNLKELWSLLHFL-----LPNIFTdweAF-ESWFDFSDLEDEQGTEEFIADQKKQELVKKI 362
Cdd:cd18013   144 PVIKRLIglTGTPSPNGLMDLWAQIALLdqgerLGRSIT---AYrERWFDPDKRNGQQVFKYKPKPGAEEEIYRAI 216
ResIII pfam04851
Type III restriction enzyme, res subunit;
137-305 1.22e-10

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 60.76  E-value: 1.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 137 TMRDYQLEGLT-WMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYLgPHLIVAP-LSTLSNWEDEFTKWTPSIP 214
Cdd:pfam04851   3 ELRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIK-KVLFLVPrKDLLEQALEEFKKFLPNYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 215 VIM--YHGNKDDREKifrtkmlkhlkagrptTKFPVVCTSYEMVLRDQHN----LSKINWEFIIIDEGHRmknADAKLFQ 288
Cdd:pfam04851  82 EIGeiISGDKKDESV----------------DDNKIVVTTIQSLYKALELasleLLPDFFDVIIIDEAHR---SGASSYR 142
                         170
                  ....*....|....*...
gi 2033488177 289 Q-LRQFSSATRLLITGTP 305
Cdd:pfam04851 143 NiLEYFKPAFLLGLTATP 160
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
135-305 7.74e-10

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 62.35  E-value: 7.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 135 NGTMRDYQLEGL-TWMYEICSQGMSGILADEMGLGKTVQTIALIALLREQENYLgphlIVAPLSTLSN-WEDEFTKWTPS 212
Cdd:COG1061    78 SFELRPYQQEALeALLAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRVL----VLVPRRELLEqWAEELRRFLGD 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 213 IPVimyHGNKDDREkifrtkmlkhlkagrpttkFPVVCTSYEMVLRDQHnLSKI--NWEFIIIDEGHRmknADAKLFQQ- 289
Cdd:COG1061   154 PLA---GGGKKDSD-------------------APITVATYQSLARRAH-LDELgdRFGLVIIDEAHH---AGAPSYRRi 207
                         170
                  ....*....|....*.
gi 2033488177 290 LRQFSSATRLLITGTP 305
Cdd:COG1061   208 LEAFPAAYRLGLTATP 223
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
138-305 4.96e-09

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are 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: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 55.77  E-value: 4.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 138 MRDYQLEGLTWMYEICSQGmSGILADEMGLGKTVQTIALIALLREQenylgPHLIVAP-LSTLSNWEDEFTKWTPSIPVi 216
Cdd:cd17926     1 LRPYQEEALEAWLAHKNNR-RGILVLPTGSGKTLTALALIAYLKEL-----RTLIVVPtDALLDQWKERFEDFLGDSSI- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 217 myhgnkddreKIFRTKMLKHLkagrptTKFPVVCTSYEMVLRDQHNLSKI--NWEFIIIDEGHRmknADAKLFQQ-LRQF 293
Cdd:cd17926    74 ----------GLIGGGKKKDF------DDANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAHH---LPAKTFSEiLKEL 134
                         170
                  ....*....|..
gi 2033488177 294 SSATRLLITGTP 305
Cdd:cd17926   135 NAKYRLGLTATP 146
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
156-304 8.25e-09

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 55.10  E-value: 8.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 156 GMSGILADEMGLGKTvqTIALIALLREQENYLGPHLIVAPLSTLSN-WEDEFTKW-TPSIPVIMYHGNKDDREKIFRTKM 233
Cdd:cd00046     1 GENVLITAPTGSGKT--LAALLAALLLLLKKGKKVLVLVPTKALALqTAERLRELfGPGIRVAVLVGGSSAEEREKNKLG 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2033488177 234 LKHLkagrpttkfpVVCTsYEMVLRD---QHNLSKINWEFIIIDEGHRMKNADAKLFQ-----QLRQFSSATRLLITGT 304
Cdd:cd00046    79 DADI----------IIAT-PDMLLNLllrEDRLFLKDLKLIIVDEAHALLIDSRGALIldlavRKAGLKNAQVILLSAT 146
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
139-304 7.63e-06

DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 46.91  E-value: 7.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 139 RDYQLEGLTWMYEiCSQGMSGILADEMGLGKTVQTIALIALLREQEnylgphLIVAPlSTLS--NWEDEFTKWTpSIPVI 216
Cdd:cd18029    10 RPYQEKALSKMFG-NGRARSGVIVLPCGAGKTLVGITAACTIKKST------LVLCT-SAVSveQWRRQFLDWT-TIDDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 217 MYHGNKDDREKIFRTKmlkhlkagrpttkfPVVCTSYEMVL---RDQHNLSKIN-------WEFIIIDEGHRMKnadAKL 286
Cdd:cd18029    81 QIGRFTSDKKEIFPEA--------------GVTVSTYSMLAntrKRSPESEKFMefitereWGLIILDEVHVVP---APM 143
                         170
                  ....*....|....*....
gi 2033488177 287 FQQ-LRQFSSATRLLITGT 304
Cdd:cd18029   144 FRRvLTLQKAHCKLGLTAT 162
PTZ00110 PTZ00110
helicase; Provisional
647-750 1.24e-03

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 42.45  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2033488177 647 FQDDHKVLIFSQFTTQLDILedyCRELR--GWKVCRIDGSVAQESRRTQIADFNS--DPeykiFLLSTRAGGQGINLASA 722
Cdd:PTZ00110  374 MRDGDKILIFVETKKGADFL---TKELRldGWPALCIHGDKKQEERTWVLNEFKTgkSP----IMIATDVASRGLDVKDV 446
                          90       100
                  ....*....|....*....|....*...
gi 2033488177 723 DTVILFDSdfnPQqdlQAQDRCHRIGQT 750
Cdd:PTZ00110  447 KYVINFDF---PN---QIEDYVHRIGRT 468
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
706-758 1.57e-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: 38.07  E-value: 1.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2033488177 706 FLLSTRAGGQGINLASADTVILFDSDFNPQQDLQAQDRCHRIGQtRPVVVFRL 758
Cdd:cd18785    25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILF 76
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH