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Conserved domains on  [gi|574275430|ref|NP_001275998|]
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lymphoid-specific helicase isoform 4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
221-791 2.36e-151

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: 469.28  E-value: 2.36e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  221 GVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPT 299
Cdd:PLN03142  168 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEyRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  300 MLYHGTQEERQ------------------------------KLHcyWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLL 349
Cdd:PLN03142  248 VKFHGNPEERAhqreellvagkfdvcvtsfemaikektalkRFS--WRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLI 325
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  350 TGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSlsetaediiaKEREQNVLHMLHQILTPFLLRRLKSDVALEVP 429
Cdd:PLN03142  326 TGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISG----------ENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLP 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  430 PKREVVVYAPLSKKQEIFYTAIvnrtianmfgsseketielsptgrpkrrtrksinyskiddfpneLEKLISQIQPEVDR 509
Cdd:PLN03142  396 PKKETILKVGMSQMQKQYYKAL--------------------------------------------LQKDLDVVNAGGER 431
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  510 ERavvevnipvesevnlkLQNIMMLLRKCCNHPYLIE--YPIDPvtqeFKIDEELVTNSGKFLILDRMLPELKKRGHKVL 587
Cdd:PLN03142  432 KR----------------LLNIAMQLRKCCNHPYLFQgaEPGPP----YTTGEHLVENSGKMVLLDKLLPKLKERDSRVL 491
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  588 LFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTD-PEVFIFLVSTRAGGLGINLTAADTVIIYDSDWNP 666
Cdd:PLN03142  492 IFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTRAGGLGINLATADIVILYDSDWNP 571
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  667 QSDLQAQDRCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLIIHKNHFkggQSGLNLSKNfldpkelmELLKSR 746
Cdd:PLN03142  572 QVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD--------ELLQMV 640
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*.
gi 574275430  747 DYERE-IKGSREKVISDKDLELLLDRSDlidqmNASGPIKEKMGIF 791
Cdd:PLN03142  641 RYGAEmVFSSKDSTITDEDIDRIIAKGE-----EATAELDAKMKKF 681
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
221-791 2.36e-151

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 469.28  E-value: 2.36e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  221 GVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPT 299
Cdd:PLN03142  168 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEyRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  300 MLYHGTQEERQ------------------------------KLHcyWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLL 349
Cdd:PLN03142  248 VKFHGNPEERAhqreellvagkfdvcvtsfemaikektalkRFS--WRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLI 325
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  350 TGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSlsetaediiaKEREQNVLHMLHQILTPFLLRRLKSDVALEVP 429
Cdd:PLN03142  326 TGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISG----------ENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLP 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  430 PKREVVVYAPLSKKQEIFYTAIvnrtianmfgsseketielsptgrpkrrtrksinyskiddfpneLEKLISQIQPEVDR 509
Cdd:PLN03142  396 PKKETILKVGMSQMQKQYYKAL--------------------------------------------LQKDLDVVNAGGER 431
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  510 ERavvevnipvesevnlkLQNIMMLLRKCCNHPYLIE--YPIDPvtqeFKIDEELVTNSGKFLILDRMLPELKKRGHKVL 587
Cdd:PLN03142  432 KR----------------LLNIAMQLRKCCNHPYLFQgaEPGPP----YTTGEHLVENSGKMVLLDKLLPKLKERDSRVL 491
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  588 LFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTD-PEVFIFLVSTRAGGLGINLTAADTVIIYDSDWNP 666
Cdd:PLN03142  492 IFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTRAGGLGINLATADIVILYDSDWNP 571
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  667 QSDLQAQDRCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLIIHKNHFkggQSGLNLSKNfldpkelmELLKSR 746
Cdd:PLN03142  572 QVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD--------ELLQMV 640
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*.
gi 574275430  747 DYERE-IKGSREKVISDKDLELLLDRSDlidqmNASGPIKEKMGIF 791
Cdd:PLN03142  641 RYGAEmVFSSKDSTITDEDIDRIIAKGE-----EATAELDAKMKKF 681
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
220-421 1.74e-141

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: 416.40  E-value: 1.74e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 220 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPT 299
Cdd:cd18009    1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 300 MLYHGTQEERQKL--------------------------------HCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKL 347
Cdd:cd18009   81 LLYHGTKEERERLrkkimkregtlqdfpvvvtsyeiamrdrkalqHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 574275430 348 LLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDI--IAKEREQNVLHMLHQILTPFLLRRLK 421
Cdd:cd18009  161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADIsnLSEEREQNIVHMLHAILKPFLLRRLK 236
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination and ...
112-746 9.87e-96

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


Pssm-ID: 223627 [Multi-domain]  Cd Length: 866  Bit Score: 317.83  E-value: 9.87e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 112 GKNSIDASEEKPVMRKKRGRED--ESYNISEVMSKEEILSVAKKNKKENEDENSSSTNLCVEDLQKNKDSNSIIKDRLSE 189
Cdd:COG0553  225 GSSEGTRKLAPLETLEYELLKQlaEKIPSKLLDLKVLLLSATPEQLKEEDLFARLRLLDPLRLADLSQILEKFVRETLKL 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 190 TVRQNTKFFFDPVRKCNGQPVPFQQP-KHFTGGVMRWYQVEGMEWL-RMLWENGINGILADEMGLGKTVQCIATIALMIQ 267
Cdd:COG0553  305 SARDLKDELKELLAELRLSEDLLNAPePVDLSAELRPYQLEGVNWLsELLRSNLLGGILADDMGLGKTVQTIALLLSLLE 384
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 268 RG--VPGPFLVCGPLSTLPNWMAEFKRFTPDIPTML-YHGTQEERQK--------------------LHCY--------- 315
Cdd:COG0553  385 SIkvYLGPALIVVPASLLSNWKREFEKFAPDLRLVLvYHGEKSELDKkrealrdllklhlviifdvvITTYellrrflvd 464
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 316 --------WKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLN-FLLPDVFD-DLKSFESWFDI 385
Cdd:COG0553  465 hgglkkieWDRVVLDEAHRIKNDQSSEGKALQFLKALNRLDLTGTPLENRLGELWSLLQeFLNPGLLGtSFAIFTRLFEK 544
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 386 TSLSEtaEDIIAKEREQNVLHMLHQILTPFLLRRLKSDVAL--EVPPKREVVVYAPLSKKQEIFYTAIVNRtianmfgss 463
Cdd:COG0553  545 PIQAE--EDIGPLEARELGIELLRKLLSPFILRRTKEDVEVlkELPPKIEKVLECELSEEQRELYEALLEG--------- 613
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 464 eketielsptgrpkrrtrKSINYSKIDDFPNELEKLISQIQPEvdreravvevnipvesevnLKLQNIMMLLRKCCNHPY 543
Cdd:COG0553  614 ------------------AEKNQQLLEDLEKADSDENRIGDSE-------------------LNILALLTRLRQICNHPA 656
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 544 LIEYPIDPVTQEFKIDEE-----------LVTNS-GKFLILDRML-PELKKRGH--KVLLFSQMTSMLDILMDYCHLRDF 608
Cdd:COG0553  657 LVDEGLEATFDRIVLLLRedkdfdylkkpLIQLSkGKLQALDELLlDKLLEEGHyhKVLIFSQFTPVLDLLEDYLKALGI 736
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 609 NFSRLDGSMSYSEREKNMHSFNTDPEVFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVY 688
Cdd:COG0553  737 KYVRLDGSTPAKRRQELIDRFNADEEEKVFLLSLKAGGLGLNLTGADTVILFDPWWNPAVELQAIDRAHRIGQKRPVKVY 816
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 574275430 689 RLVTANTIDQKIVERAAAKRKLEKLIIhknhfkgGQSGLNLsKNFLDPKELMELLKSR 746
Cdd:COG0553  817 RLITRGTIEEKILELQEKKQELLDSLI-------DAEGEKE-LSKLSIEDLLDLFSLG 866
SNF2_N pfam00176
SNF2 family N-terminal domain; This domain is found in proteins involved in a variety of ...
226-545 1.76e-79

SNF2 family N-terminal 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).


Pssm-ID: 306645 [Multi-domain]  Cd Length: 305  Bit Score: 257.71  E-value: 1.76e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA----LMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTML 301
Cdd:pfam00176   1 YQIEGVNWMLSRENNQRGGILADEMGLGKTLQTISLLLtlkyLYHIKKLPGPTLIVVPLSLLDNWMNEFERWVPSLRLVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  302 YHGTQEERQKLH----------CY------------------------WKYLIVDEGHRIKNMKCRLIRELKRFNADNKL 347
Cdd:pfam00176  81 LVGDGGSRMDKMnvrllpkvlaDYdvvittyetlrrdkknrsllkklkWHRVILDEGHRLKNSKSKLSEALSKLRTRNRW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  348 LLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKereqnvlhmLHQILTPFLLRRLKSDVALE 427
Cdd:pfam00176 161 ILTGTPIQNNLEELWALLNFLRPGPFGSLQTFDKWFVRPIERGGGEKGVAR---------LHKLLKPFLLRRTKKDVEKS 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  428 VPPKREVVVYAPLSKKQEIFYTAIVN----RTIANMFGSSEKETIELSPTGRPKRRtrksinyskiddfpneleklisqi 503
Cdd:pfam00176 232 LPPKVEEILFCRLSKGQRKLYQTALQalrgNGILKLLIRNRAATKFSSKSFRGKPG------------------------ 287
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 574275430  504 qpevdreravvevnipvesevnlkLQNIMMLLRKCCNHPYLI 545
Cdd:pfam00176 288 ------------------------LLNILLRLRKICNHPDLF 305
HELICc smart00490
helicase superfamily c-terminal domain;
597-680 3.61e-24

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 96.51  E-value: 3.61e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430   597 DILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTDPevFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRC 676
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGK--IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                   ....
gi 574275430   677 HRIG 680
Cdd:smart00490  79 GRAG 82
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
221-791 2.36e-151

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 469.28  E-value: 2.36e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  221 GVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPT 299
Cdd:PLN03142  168 GKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEyRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  300 MLYHGTQEERQ------------------------------KLHcyWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLL 349
Cdd:PLN03142  248 VKFHGNPEERAhqreellvagkfdvcvtsfemaikektalkRFS--WRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLI 325
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  350 TGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSlsetaediiaKEREQNVLHMLHQILTPFLLRRLKSDVALEVP 429
Cdd:PLN03142  326 TGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISG----------ENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLP 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  430 PKREVVVYAPLSKKQEIFYTAIvnrtianmfgsseketielsptgrpkrrtrksinyskiddfpneLEKLISQIQPEVDR 509
Cdd:PLN03142  396 PKKETILKVGMSQMQKQYYKAL--------------------------------------------LQKDLDVVNAGGER 431
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  510 ERavvevnipvesevnlkLQNIMMLLRKCCNHPYLIE--YPIDPvtqeFKIDEELVTNSGKFLILDRMLPELKKRGHKVL 587
Cdd:PLN03142  432 KR----------------LLNIAMQLRKCCNHPYLFQgaEPGPP----YTTGEHLVENSGKMVLLDKLLPKLKERDSRVL 491
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  588 LFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTD-PEVFIFLVSTRAGGLGINLTAADTVIIYDSDWNP 666
Cdd:PLN03142  492 IFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPgSEKFVFLLSTRAGGLGINLATADIVILYDSDWNP 571
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  667 QSDLQAQDRCHRIGQTKPVVVYRLVTANTIDQKIVERAAAKRKLEKLIIHKNHFkggQSGLNLSKNfldpkelmELLKSR 746
Cdd:PLN03142  572 QVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD--------ELLQMV 640
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*.
gi 574275430  747 DYERE-IKGSREKVISDKDLELLLDRSDlidqmNASGPIKEKMGIF 791
Cdd:PLN03142  641 RYGAEmVFSSKDSTITDEDIDRIIAKGE-----EATAELDAKMKKF 681
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
220-421 1.74e-141

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: 416.40  E-value: 1.74e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 220 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPT 299
Cdd:cd18009    1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 300 MLYHGTQEERQKL--------------------------------HCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKL 347
Cdd:cd18009   81 LLYHGTKEERERLrkkimkregtlqdfpvvvtsyeiamrdrkalqHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 574275430 348 LLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDI--IAKEREQNVLHMLHQILTPFLLRRLK 421
Cdd:cd18009  161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADIsnLSEEREQNIVHMLHAILKPFLLRRLK 236
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination and ...
112-746 9.87e-96

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


Pssm-ID: 223627 [Multi-domain]  Cd Length: 866  Bit Score: 317.83  E-value: 9.87e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 112 GKNSIDASEEKPVMRKKRGRED--ESYNISEVMSKEEILSVAKKNKKENEDENSSSTNLCVEDLQKNKDSNSIIKDRLSE 189
Cdd:COG0553  225 GSSEGTRKLAPLETLEYELLKQlaEKIPSKLLDLKVLLLSATPEQLKEEDLFARLRLLDPLRLADLSQILEKFVRETLKL 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 190 TVRQNTKFFFDPVRKCNGQPVPFQQP-KHFTGGVMRWYQVEGMEWL-RMLWENGINGILADEMGLGKTVQCIATIALMIQ 267
Cdd:COG0553  305 SARDLKDELKELLAELRLSEDLLNAPePVDLSAELRPYQLEGVNWLsELLRSNLLGGILADDMGLGKTVQTIALLLSLLE 384
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 268 RG--VPGPFLVCGPLSTLPNWMAEFKRFTPDIPTML-YHGTQEERQK--------------------LHCY--------- 315
Cdd:COG0553  385 SIkvYLGPALIVVPASLLSNWKREFEKFAPDLRLVLvYHGEKSELDKkrealrdllklhlviifdvvITTYellrrflvd 464
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 316 --------WKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLN-FLLPDVFD-DLKSFESWFDI 385
Cdd:COG0553  465 hgglkkieWDRVVLDEAHRIKNDQSSEGKALQFLKALNRLDLTGTPLENRLGELWSLLQeFLNPGLLGtSFAIFTRLFEK 544
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 386 TSLSEtaEDIIAKEREQNVLHMLHQILTPFLLRRLKSDVAL--EVPPKREVVVYAPLSKKQEIFYTAIVNRtianmfgss 463
Cdd:COG0553  545 PIQAE--EDIGPLEARELGIELLRKLLSPFILRRTKEDVEVlkELPPKIEKVLECELSEEQRELYEALLEG--------- 613
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 464 eketielsptgrpkrrtrKSINYSKIDDFPNELEKLISQIQPEvdreravvevnipvesevnLKLQNIMMLLRKCCNHPY 543
Cdd:COG0553  614 ------------------AEKNQQLLEDLEKADSDENRIGDSE-------------------LNILALLTRLRQICNHPA 656
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 544 LIEYPIDPVTQEFKIDEE-----------LVTNS-GKFLILDRML-PELKKRGH--KVLLFSQMTSMLDILMDYCHLRDF 608
Cdd:COG0553  657 LVDEGLEATFDRIVLLLRedkdfdylkkpLIQLSkGKLQALDELLlDKLLEEGHyhKVLIFSQFTPVLDLLEDYLKALGI 736
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 609 NFSRLDGSMSYSEREKNMHSFNTDPEVFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVY 688
Cdd:COG0553  737 KYVRLDGSTPAKRRQELIDRFNADEEEKVFLLSLKAGGLGLNLTGADTVILFDPWWNPAVELQAIDRAHRIGQKRPVKVY 816
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 574275430 689 RLVTANTIDQKIVERAAAKRKLEKLIIhknhfkgGQSGLNLsKNFLDPKELMELLKSR 746
Cdd:COG0553  817 RLITRGTIEEKILELQEKKQELLDSLI-------DAEGEKE-LSKLSIEDLLDLFSLG 866
SNF2_N pfam00176
SNF2 family N-terminal domain; This domain is found in proteins involved in a variety of ...
226-545 1.76e-79

SNF2 family N-terminal 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).


Pssm-ID: 306645 [Multi-domain]  Cd Length: 305  Bit Score: 257.71  E-value: 1.76e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA----LMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTML 301
Cdd:pfam00176   1 YQIEGVNWMLSRENNQRGGILADEMGLGKTLQTISLLLtlkyLYHIKKLPGPTLIVVPLSLLDNWMNEFERWVPSLRLVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  302 YHGTQEERQKLH----------CY------------------------WKYLIVDEGHRIKNMKCRLIRELKRFNADNKL 347
Cdd:pfam00176  81 LVGDGGSRMDKMnvrllpkvlaDYdvvittyetlrrdkknrsllkklkWHRVILDEGHRLKNSKSKLSEALSKLRTRNRW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  348 LLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKereqnvlhmLHQILTPFLLRRLKSDVALE 427
Cdd:pfam00176 161 ILTGTPIQNNLEELWALLNFLRPGPFGSLQTFDKWFVRPIERGGGEKGVAR---------LHKLLKPFLLRRTKKDVEKS 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  428 VPPKREVVVYAPLSKKQEIFYTAIVN----RTIANMFGSSEKETIELSPTGRPKRRtrksinyskiddfpneleklisqi 503
Cdd:pfam00176 232 LPPKVEEILFCRLSKGQRKLYQTALQalrgNGILKLLIRNRAATKFSSKSFRGKPG------------------------ 287
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 574275430  504 qpevdreravvevnipvesevnlkLQNIMMLLRKCCNHPYLI 545
Cdd:pfam00176 288 ------------------------LLNILLRLRKICNHPDLF 305
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
220-421 2.11e-78

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: 251.86  E-value: 2.11e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 220 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRFTPDIP 298
Cdd:cd17997    1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHyKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 299 TMLYHGTQEERQKL-----------------HCY-----------WKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLT 350
Cdd:cd17997   81 VVVLIGDKEERADIirdvllpgkfdvcitsyEMVikektvlkkfnWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLT 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 574275430 351 GTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKereqnvlhmLHQILTPFLLRRLK 421
Cdd:cd17997  161 GTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDNQEVVQR---------LHKVLRPFLLRRIK 222
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
220-421 6.72e-75

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: 243.04  E-value: 6.72e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 220 GGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIP 298
Cdd:cd17996    1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITyLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 299 TMLYHGTQEERQKLH-------------CY--------------WKYLIVDEGHRIKNMKCRLIRELKR-FNADNKLLLT 350
Cdd:cd17996   81 KIVYKGTPDVRKKLQsqiragkfnvlltTYeyiikdkpllskikWKYMIIDEGHRMKNAQSKLTQTLNTyYHARYRLLLT 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 574275430 351 GTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKEREQNVL--HMLHQILTPFLLRRLK 421
Cdd:cd17996  161 GTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVKIELNEEETLLiiRRLHKVLRPFLLRRLK 233
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
223-373 1.79e-69

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: 226.29  E-value: 1.79e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMI-QRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTML 301
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLkEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 302 YHGTQEERQKLHCY---------------------------WKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPL 354
Cdd:cd17919   81 YHGSQRERAQIRAKekldkfdvvlttyetlrrdkaslrkfrWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPL 160
                        170
                 ....*....|....*....
gi 574275430 355 QNNLSELWSLLNFLLPDVF 373
Cdd:cd17919  161 QNNLEELWALLDFLDPPFL 179
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
223-419 1.72e-64

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: 214.52  E-value: 1.72e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTML 301
Cdd:cd18003    1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAhLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 302 YHGTQEER------------------------QKLHCY----WKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTP 353
Cdd:cd18003   81 YYGSAKERklkrqgwmkpnsfhvcitsyqlvvQDHQVFkrkkWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 574275430 354 LQNNLSELWSLLNFLLPDVFDDLKSFESWFD--ITSLSETAEDIiakerEQNVLHMLHQILTPFLLRR 419
Cdd:cd18003  161 LQNSLMELWSLMHFLMPHIFQSHQEFKEWFSnpLTAMSEGSQEE-----NEELVRRLHKVLRPFLLRR 223
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
566-691 4.49e-64

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: 210.03  E-value: 4.49e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 566 SGKFLILDRMLPELKKRGHKVLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTDPEVFIFLVSTRAG 645
Cdd:cd18793   10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 574275430 646 GLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLV 691
Cdd:cd18793   90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
221-421 1.40e-61

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: 206.65  E-value: 1.40e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 221 GVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTM 300
Cdd:cd18012    3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKVL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 301 LYHGTQEERQKLHCY------------------------WKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQN 356
Cdd:cd18012   83 VIHGTKRKREKLRALedydlvitsygllrrdiellkevkFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTPIEN 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 574275430 357 NLSELWSLLNFLLPDVFDDLKSFESWFDITslsetaediIAKEREQNVLHMLHQILTPFLLRRLK 421
Cdd:cd18012  163 HLGELWSIFDFLNPGLLGSYKRFKKRFAKP---------IEKDGDEEALEELKKLISPFILRRLK 218
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
215-432 3.70e-61

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: 206.44  E-value: 3.70e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 215 PKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFKRF 293
Cdd:cd18064    8 PSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHyRNIPGPHMVLVPKSTLHNWMAEFKRW 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 294 TPDIPTMLYHGTQEERQKL----------------------------HCYWKYLIVDEGHRIKNMKCRLIRELKRFNADN 345
Cdd:cd18064   88 VPTLRAVCLIGDKDQRAAFvrdvllpgewdvcvtsyemlikeksvfkKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTN 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 346 KLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSEtaediiakerEQNVLHMLHQILTPFLLRRLKSDVA 425
Cdd:cd18064  168 RLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLG----------DQKLVERLHMVLRPFLLRRIKADVE 237

                 ....*..
gi 574275430 426 LEVPPKR 432
Cdd:cd18064  238 KSLPPKK 244
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
223-419 5.33e-59

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: 199.78  E-value: 5.33e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQR-GVPGPFLVCGPLSTLPNWMAEFKRFTpDIPTML 301
Cdd:cd17995    1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVeGIRGPFLVIAPLSTIPNWQREFETWT-DMNVVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 302 YHGTQEERQKLHCY---------------------------------------WKYLIVDEGHRIKNMKCRLIRELKRFN 342
Cdd:cd17995   80 YHGSGESRQIIQQYemyfkdaqgrkkkgvykfdvlittyemviadaeelrkipWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 574275430 343 ADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWF-DItslsETAEDIiakEReqnvlhmLHQILTPFLLRR 419
Cdd:cd17995  160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFgDL----KTAEQV---EK-------LQALLKPYMLRR 223
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
223-419 1.27e-57

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: 195.65  E-value: 1.27e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTML 301
Cdd:cd17993    2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSyLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 302 YHGTQEERQKLHCY---------------------------------WKYLIVDEGHRIKNMKCRLIRELKRFNADNKLL 348
Cdd:cd17993   82 YLGDIKSRDTIREYefyfsqtkklkfnvllttyeiilkdkaflgsikWQYLAVDEAHRLKNDESLLYEALKEFKTNNRLL 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 574275430 349 LTGTPLQNNLSELWSLLNFLLPDVFDDLKSFEswfdiTSLSETAEDIIAKereqnvlhmLHQILTPFLLRR 419
Cdd:cd17993  162 ITGTPLQNSLKELWALLHFLMPGKFDIWEEFE-----EEHDEEQEKGIAD---------LHKELEPFILRR 218
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
213-421 4.77e-57

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: 194.85  E-value: 4.77e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 213 QQPKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQ-RGVPGPFLVCGPLSTLPNWMAEFK 291
Cdd:cd18065    6 ESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHyRNIPGPHMVLVPKSTLHNWMNEFK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 292 RFTPDIPTMLYHGTQEER------------------------------QKLHcyWKYLIVDEGHRIKNMKCRLIRELKRF 341
Cdd:cd18065   86 RWVPSLRAVCLIGDKDARaafirdvmmpgewdvcvtsyemvikeksvfKKFN--WRYLVIDEAHRIKNEKSKLSEIVREF 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 342 NADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSEtaediiakerEQNVLHMLHQILTPFLLRRLK 421
Cdd:cd18065  164 KTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLG----------DQKLVERLHAVLKPFLLRRIK 233
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
226-419 1.64e-54

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: 187.71  E-value: 1.64e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQR-GVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHG 304
Cdd:cd18002    4 YQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEhNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLPYWG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 305 TQEERQKLHCY----------------------------------WKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLT 350
Cdd:cd18002   84 NPKDRKVLRKFwdrknlytrdapfhvvitsyqlvvqdekyfqrvkWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLT 163
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 574275430 351 GTPLQNNLSELWSLLNFLLPDVFDDLKSFESWF--DITSLSETAEDIiakerEQNVLHMLHQILTPFLLRR 419
Cdd:cd18002  164 GTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFskDIESHAENKTGL-----NEHQLKRLHMILKPFMLRR 229
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
213-421 1.20e-53

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  Cd Length: 251  Bit Score: 186.02  E-value: 1.20e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 213 QQPKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFK 291
Cdd:cd18062   14 KQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITyLMEHKRINGPFLIIVPLSTLSNWVYEFD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 292 RFTPDIPTMLYHGTQEERQKL---------------------------HCYWKYLIVDEGHRIKNMKCRLIRELK-RFNA 343
Cdd:cd18062   94 KWAPSVVKVSYKGSPAARRAFvpqlrsgkfnvllttyeyiikdkqilaKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVA 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 574275430 344 DNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDiTSLSETAEDIIAKEREQN-VLHMLHQILTPFLLRRLK 421
Cdd:cd18062  174 PRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFN-APFAMTGEKVDLNEEETIlIIRRLHKVLRPFLLRRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
213-421 2.69e-53

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  Cd Length: 251  Bit Score: 185.27  E-value: 2.69e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 213 QQPKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAEFK 291
Cdd:cd18063   14 KQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITyLMEHKRLNGPYLIIVPLSTLSNWTYEFD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 292 RFTPDIPTMLYHGTQEERQKL---------------------------HCYWKYLIVDEGHRIKNMKCRLIRELK-RFNA 343
Cdd:cd18063   94 KWAPSVVKISYKGTPAMRRSLvpqlrsgkfnvllttyeyiikdkhilaKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVA 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 574275430 344 DNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDiTSLSETAEDIIAKEREQN-VLHMLHQILTPFLLRRLK 421
Cdd:cd18063  174 PRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFN-APFAMTGERVDLNEEETIlIIRRLHKVLRPFLLRRLK 251
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
226-419 2.14e-52

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: 180.71  E-value: 2.14e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATI-ALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHG 304
Cdd:cd17994    4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLySLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVTYVG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 305 tqeERQKLHCY--------------WKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLP 370
Cdd:cd17994   84 ---DHVLLTSYelisidqailgsidWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTP 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 574275430 371 DVFDDLKSFESWFDITSlsetAEDIIAKereqnvlhmLHQILTPFLLRR 419
Cdd:cd17994  161 ERFNNLQGFLEEFADIS----KEDQIKK---------LHDLLGPHMLRR 196
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
226-373 2.06e-51

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: 177.58  E-value: 2.06e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHGT 305
Cdd:cd17998    4 YQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEPYYGS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 306 QEERQKL--------------------------------HCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTP 353
Cdd:cd17998   84 QEERKHLrydilkgledfdvivttynlatsnpddrsffkRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLLTGTP 163
                        170       180
                 ....*....|....*....|
gi 574275430 354 LQNNLSELWSLLNFLLPDVF 373
Cdd:cd17998  164 LQNNLLELMSLLNFIMPKPF 183
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
213-419 1.79e-47

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: 168.65  E-value: 1.79e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 213 QQPKHFTGG--VMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLPNWMAE 289
Cdd:cd18054    9 KQPSYIGGEnlELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSyLFHQHQLYGPFLLVVPLSTLTSWQRE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 290 FKRFTPDIPTMLYHGTQEERQKLHCY---------------------------------WKYLIVDEGHRIKNMKCRLIR 336
Cdd:cd18054   89 FEIWAPEINVVVYIGDLMSRNTIREYewihsqtkrlkfnalittyeillkdktvlgsinWAFLGVDEAHRLKNDDSLLYK 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 337 ELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDvfddlkSFESWFDItslsetaEDIIAKEREqNVLHMLHQILTPFL 416
Cdd:cd18054  169 TLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPE------KFEFWEDF-------EEDHGKGRE-NGYQSLHKVLEPFL 234

                 ...
gi 574275430 417 LRR 419
Cdd:cd18054  235 LRR 237
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
223-419 1.07e-46

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: 165.69  E-value: 1.07e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQR-GVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTML 301
Cdd:cd18006    1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRlKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 302 YHGTQEERQKLH------------------C----------YWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTP 353
Cdd:cd18006   81 YMGDKEKRLDLQqdikstnrfhvllttyeiClkdasflksfPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 574275430 354 LQNNLSELWSLLNFLLPDVF--DDLKSFESWF-DITSLSETAEDiiakereqnvlhmLHQILTPFLLRR 419
Cdd:cd18006  161 IQNSLQELYALLSFIEPNVFpkDKLDDFIKAYsETDDESETVEE-------------LHLLLQPFLLRR 216
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
225-419 4.86e-45

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: 161.39  E-value: 4.86e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 225 WYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHG 304
Cdd:cd18001    3 PHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKVFHG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 305 T---QEERQKLHCY-----------------------------WKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGT 352
Cdd:cd18001   83 TskkERERNLERIQrgggvllttygmvlsnteqlsaddhdefkWDYVILDEGHKIKNSKTKSAKSLREIPAKNRIILTGT 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 353 PLQNNLSELWSLLNFLLP-DVFDDLKSFESWFDITSLSETAEDIIAKERE--QNVLHMLHQILTPFLLRR 419
Cdd:cd18001  163 PIQNNLKELWALFDFACNgSLLGTRKTFKMEFENPITRGRDKDATQGEKAlgSEVAENLRQIIKPYFLRR 232
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
223-419 6.00e-44

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: 158.28  E-value: 6.00e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIAL------MIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPD 296
Cdd:cd17999    1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASdhhkraNSFNSENLPSLVVCPPTLVGHWVAEIKKYFPN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 297 --IPTMLYHGTQEERQKLHCY-------------------------WKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLL 349
Cdd:cd17999   81 afLKPLAYVGPPQERRRLREQgekhnvivasydvlrndievltkieWNYCVLDEGHIIKNSKTKLSKAVKQLKANHRLIL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 574275430 350 TGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFD---ITSLSETAEdiiAKEREQNVLHM--LHQILTPFLLRR 419
Cdd:cd17999  161 SGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLkpiLASRDSKAS---AKEQEAGALALeaLHKQVLPFLLRR 232
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
223-419 1.27e-43

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: 157.13  E-value: 1.27e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTpDIPTMLY 302
Cdd:cd18058    1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWT-EMNAIVY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 303 HGTQEERQKLHCY---------------------------------------WKYLIVDEGHRIKNMKCRLIRELKRFNA 343
Cdd:cd18058   80 HGSQISRQMIQQYemyyrdeqgnplsgifkfqvvittfemiladcpelkkinWSCVIIDEAHRLKNRNCKLLEGLKLMAL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 574275430 344 DNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSF-ESWFDItslsetaediiaKEREQnvLHMLHQILTPFLLRR 419
Cdd:cd18058  160 EHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFlEEFGDL------------KTEEQ--VKKLQSILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
223-419 1.27e-41

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: 151.34  E-value: 1.27e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTpDIPTMLY 302
Cdd:cd18059    1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVVY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 303 HGTQEERQKLHCY---------------------------------------WKYLIVDEGHRIKNMKCRLIRELKRFNA 343
Cdd:cd18059   80 HGSQASRRTIQLYemyfkdpqgrvikgsykfhaiittfemiltdcpelrnipWRCVVIDEAHRLKNRNCKLLEGLKMMDL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 574275430 344 DNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDitslsetaeDIIAKEREQNvlhmLHQILTPFLLRR 419
Cdd:cd18059  160 EHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG---------DLKTEEQVQK----LQAILKPMMLRR 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
223-419 1.86e-41

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: 150.97  E-value: 1.86e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTpDIPTMLY 302
Cdd:cd18060    1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIVY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 303 HGTQEERQKLHCY---------------------------------------WKYLIVDEGHRIKNMKCRLIRELKRFNA 343
Cdd:cd18060   80 HGSLASRQMIQQYemyckdsrgrlipgaykfdalittfemilsdcpelreieWRCVIIDEAHRLKNRNCKLLDSLKHMDL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 574275430 344 DNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDitslsetaeDIIAKEREQNvlhmLHQILTPFLLRR 419
Cdd:cd18060  160 EHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG---------DLKTEEQVQK----LQAILKPMMLRR 222
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
226-419 1.07e-40

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: 149.39  E-value: 1.07e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRG-VPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHG 304
Cdd:cd18055    4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhTKGPFLVSAPLSTIINWEREFQMWAPDFYVVTYTG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 305 TQEERQ-----------------------------KLHCY------------------WKYLIVDEGHRIKNMKCRLIRE 337
Cdd:cd18055   84 DKDSRAiirenefsfddnavkggkkafkmkreaqvKFHVLltsyelvtidqaalgsirWACLVVDEAHRLKNNQSKFFRV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 338 LKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSF-ESWFDITSlsetaEDIIAKereqnvlhmLHQILTPFL 416
Cdd:cd18055  164 LNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFlEEFADISK-----EDQIKK---------LHDLLGPHM 229

                 ...
gi 574275430 417 LRR 419
Cdd:cd18055  230 LRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
226-419 8.31e-40

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: 146.75  E-value: 8.31e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRG-VPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHG 304
Cdd:cd18057    4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWAPDFYVVTYTG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 305 TQEERQ-----------------------------KLHCY------------------WKYLIVDEGHRIKNMKCRLIRE 337
Cdd:cd18057   84 DKESRSvirenefsfednairsgkkvfrmkkeaqiKFHVLltsyelitidqailgsieWACLVVDEAHRLKNNQSKFFRV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 338 LKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSF-ESWFDITSlsetaEDIIAKereqnvlhmLHQILTPFL 416
Cdd:cd18057  164 LNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFlEEFADISK-----EDQIKK---------LHDLLGPHM 229

                 ...
gi 574275430 417 LRR 419
Cdd:cd18057  230 LRR 232
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
223-419 2.61e-38

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: 142.07  E-value: 2.61e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTpDIPTMLY 302
Cdd:cd18061    1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVVVY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 303 HGTQEERQKLHCY---------------------------------------WKYLIVDEGHRIKNMKCRLIRELKRFNA 343
Cdd:cd18061   80 HGSLISRQMIQQYemyfrdsqgriirgayrfqaiittfemilggcpelnaidWRCVIIDEAHRLKNKNCKLLEGLKLMNL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 574275430 344 DNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDitslsetaeDIIAKEREQNvlhmLHQILTPFLLRR 419
Cdd:cd18061  160 EHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG---------DLKTEEQVQK----LQAILKPMMLRR 222
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
226-419 2.86e-38

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  Cd Length: 232  Bit Score: 142.13  E-value: 2.86e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRG-VPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHG 304
Cdd:cd18056    4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWAPDMYVVTYVG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 305 TQEERQ-----------------------------KLHCY------------------WKYLIVDEGHRIKNMKCRLIRE 337
Cdd:cd18056   84 DKDSRAiirenefsfednairggkkasrmkkeasvKFHVLltsyelitidmailgsidWACLIVDEAHRLKNNQSKFFRV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 338 LKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFeswfditsLSETAEdiIAKEREqnvLHMLHQILTPFLL 417
Cdd:cd18056  164 LNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGF--------LEEFAD--IAKEDQ---IKKLHDMLGPHML 230

                 ..
gi 574275430 418 RR 419
Cdd:cd18056  231 RR 232
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
226-419 3.32e-36

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: 136.65  E-value: 3.32e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 226 YQVEGMEWlrMLWeNGinGILADEMGLGKTVQCIATIAL------------------MIQRGVPGPFLVCGPLSTLPNWM 287
Cdd:cd18008    4 YQKQGLAW--MLP-RG--GILADEMGLGKTIQALALILAtrpqdpkipeeleenssdPKKLYLSKTTLIVVPLSLLSQWK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 288 AEFKRFT--PDIPTMLYHG-----------------------TQEERQK---------------LHC-YWKYLIVDEGHR 326
Cdd:cd18008   79 DEIEKHTkpGSLKVYVYHGskriksieelsdydivittygtlASEFPKNkkgggrdskekeaspLHRiRWYRVILDEAHN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 327 IKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFesWFDITSLSetaediiaKEREQNVLH 406
Cdd:cd18008  159 IKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWF--NSDISKPF--------SKNDRKALE 228
                        250
                 ....*....|...
gi 574275430 407 MLHQILTPFLLRR 419
Cdd:cd18008  229 RLQALLKPILLRR 241
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
226-370 1.20e-35

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: 133.22  E-value: 1.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 226 YQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALM--IQRGVpGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYH 303
Cdd:cd18000    4 YQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALhhSKLGL-GPSLIVCPATVLKQWVKEFHRWWPPFRVVVLH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 304 -------------------------------------GTQEERQKLH-CYWKYLIVDEGHRIKNMKCRLIRELKRFNADN 345
Cdd:cd18000   83 ssgsgtgseeklgsierksqlirkvvgdggilittyeGFRKHKDLLLnHNWQYVILDEGHKIRNPDAEITLACKQLRTPH 162
                        170       180
                 ....*....|....*....|....*
gi 574275430 346 KLLLTGTPLQNNLSELWSLLNFLLP 370
Cdd:cd18000  163 RLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
210-419 8.96e-35

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  Cd Length: 237  Bit Score: 132.48  E-value: 8.96e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 210 VPFQQPKHFTGGV----MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIA-LMIQRGVPGPFLVCGPLSTLP 284
Cdd:cd18053    4 VALKKQPSYIGGHegleLRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNyLFHEHQLYGPFLLVVPLSTLT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 285 NWMAEFKRFTPDIPTMLYHGT---------------QEERQKLHCY------------------WKYLIVDEGHRIKNMK 331
Cdd:cd18053   84 SWQREIQTWAPQMNAVVYLGDinsrnmirthewmhpQTKRLKFNILlttyeillkdksflgglnWAFIGVDEAHRLKNDD 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 332 CRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDvfddlkSFESWfditslsETAEDIIAKEREQNVLHmLHQI 411
Cdd:cd18053  164 SLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPE------KFSSW-------EDFEEEHGKGREYGYAS-LHKE 229

                 ....*...
gi 574275430 412 LTPFLLRR 419
Cdd:cd18053  230 LEPFLLRR 237
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
223-419 4.40e-34

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: 130.48  E-value: 4.40e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 223 MRWYQVEGMEWL--RMLWENGING---ILADEMGLGKTVQCIATIALMIQRGVPGP-----FLVCGPLSTLPNWMAEFKR 292
Cdd:cd18004    1 LRPHQREGVQFLydCLTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKptakkALIVCPSSLVGNWKAEFDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 293 FTPD---IPTMLYHGTQEERQKLHCY-----WKYLIV-----------------------DEGHRIKNMKCRLIRELKRF 341
Cdd:cd18004   81 WLGLrriKVVTADGNAKDVKASLDFFssastYPVLIIsyetlrrhaeklskkisidllicDEGHRLKNSESKTTKALNSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 342 NADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFD--ITSLSETAEDIIAKEREQNVLHMLHQILTPFLLRR 419
Cdd:cd18004  161 PCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEepILRSRDPDASEEDKELGAERSQELSELTSRFILRR 240
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
223-419 1.17e-32

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: 126.72  E-value: 1.17e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 223 MRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQR---------------------GVPGPFLVCGPLS 281
Cdd:cd18005    1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKtgtrrdrennrprfkkkppasSAKKPVLIVAPLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 282 TLPNWMAEFKR---FTpdipTMLYHGTQ-----EERQKLHCY---------------------WKYLIVDEGHRIKNMKC 332
Cdd:cd18005   81 VLYNWKDELDTwghFE----VGVYHGSRkddelEGRLKAGRLevvvttydtlrrcidslnsinWSAVIADEAHRIKNPKS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 333 RLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDI-----TSLSETAEDI-IAKEREQnvlh 406
Cdd:cd18005  157 KLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEpikrgQRHTATARELrLGRKRKQ---- 232
                        250
                 ....*....|...
gi 574275430 407 MLHQILTPFLLRR 419
Cdd:cd18005  233 ELAVKLSKFFLRR 245
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
567-680 3.54e-32

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: 333970 [Multi-domain]  Cd Length: 111  Bit Score: 120.39  E-value: 3.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  567 GKFLILDRMLpELKKRGHKVLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTDPevFIFLVSTRAGG 646
Cdd:pfam00271   1 EKLEALLELL-KLKERGGKVLIFSNTKKRLELLELLLEKEGIKVARLHGDLSQEEREEILEDFRNGK--IDVLVATDVAA 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 574275430  647 LGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIG 680
Cdd:pfam00271  78 RGLDLPDVNLVINYDLPWNPASYIQRIGRAGRAG 111
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
223-383 1.58e-26

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  Cd Length: 239  Bit Score: 108.53  E-value: 1.58e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 223 MRWYQVEGmewLRMLWEN---------GING-ILADEMGLGKTVQCIATIALMIQRGVPG--PFLVCgPLSTLPNWMAEF 290
Cdd:cd18007    1 LKPHQVEG---VRFLWSNlvgtdvgsdEGGGcILAHTMGLGKTLQVITFLHTYLAAAPRRsrPLVLC-PASTLYNWEDEF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 291 KRFTPDIP-----------------------------------------TMLYHGTQEERQKLHCYW------KYLIVDE 323
Cdd:cd18007   77 KKWLPPDLrpllvlvslsaskradarlrkinkwhkeggvlligyelfrnLASNATTDPRLKQEFIAAlldpgpDLLVLDE 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 324 GHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWF 383
Cdd:cd18007  157 GHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
HELICc smart00490
helicase superfamily c-terminal domain;
597-680 3.61e-24

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 96.51  E-value: 3.61e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430   597 DILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNTDPevFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRC 676
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGK--IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                   ....
gi 574275430   677 HRIG 680
Cdd:smart00490  79 GRAG 82
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
226-384 5.58e-22

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  Cd Length: 227  Bit Score: 95.27  E-value: 5.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 226 YQVEGmewLRMLWEN------------GINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRF 293
Cdd:cd18069    4 HQIGG---IRFLYDNiieslerykgssGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 294 TP---DIPTMLY-----------HGTQEERQKLHCYWKY--------------------LIVDEGHRIKNMKCRLIRELK 339
Cdd:cd18069   81 LPppeALPNVRPrpfkvfilndeHKTTAARAKVIEDWVKdggvllmgyemfrlrpgpdvVICDEGHRIKNCHASTSQALK 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 574275430 340 RFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFD 384
Cdd:cd18069  161 NIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFE 205
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
223-419 3.70e-21

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  Cd Length: 243  Bit Score: 93.30  E-value: 3.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 223 MRWYQVEGmewLRMLWE-------NGING-ILADEMGLGKTVQCIATI-ALMIQRGVPGPFL----VCGPLSTLPNWMAE 289
Cdd:cd18067    1 LRPHQREG---VKFLYRcvtgrriRGSHGcIMADEMGLGKTLQCITLMwTLLRQSPQCKPEIdkaiVVSPSSLVKNWANE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 290 F-----KRFTP-----------DIPT---MLYHGTQ---------EERQKLH------CYWKYLIVDEGHRIKNMKCRLI 335
Cdd:cd18067   78 LgkwlgGRLQPlaidggskkeiDRKLvqwASQQGRRvstpvliisYETFRLHvevlqkGEVGLVICDEGHRLKNSDNQTY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 336 RELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSETAEDIIAKEREQNV--LHMLHQILT 413
Cdd:cd18067  158 QALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEekLQELISIVN 237

                 ....*.
gi 574275430 414 PFLLRR 419
Cdd:cd18067  238 RCIIRR 243
DEXDc smart00487
DEAD-like helicases superfamily;
215-371 9.13e-21

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 91.01  E-value: 9.13e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430   215 PKHFTGGVMRWYQVEGMEWLrmlWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTL-PNWMAEFKRF 293
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430   294 TPD---IPTMLYHGTQEERQKLHCY---------------------------WKYLIVDEGHRIKNM--KCRLIRELKRF 341
Cdd:smart00487  78 GPSlglKVVGLYGGDSKREQLRKLEsgktdilvttpgrlldllendklslsnVDLVILDEAHRLLDGgfGDQLEKLLKLL 157
                          170       180       190
                   ....*....|....*....|....*....|....
gi 574275430   342 NADNK-LLLTGTP---LQNNLSELWSLLNFLLPD 371
Cdd:smart00487 158 PKNVQlLLLSATPpeeIENLLELFLNDPVFIDVG 191
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
226-379 1.41e-19

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: 87.65  E-value: 1.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 226 YQVEGMEW-LRmlweNGINGILADEMGLGKTVQCIAtIALMIQRgvPGPFLVCGPLSTLPNWMAEFKRFTPDIPTM---- 300
Cdd:cd18010    4 FQREGVCFaLR----RGGRVLIADEMGLGKTVQAIA-IAAYYRE--EWPLLIVCPSSLRLTWADEIERWLPSLPPDdiqv 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 301 -------LYHG------------TQEERQKLHCYWKYLIVDEGHRIKNMK---CRLIRELKRfNADNKLLLTGTPLQNNL 358
Cdd:cd18010   77 ivkskdgLRDGdakvvivsydllRRLEKQLLARKFKVVICDESHYLKNSKakrTKAALPLLK-RAKRVILLSGTPALSRP 155
                        170       180
                 ....*....|....*....|.
gi 574275430 359 SELWSLLNFLLPDVFDDLKSF 379
Cdd:cd18010  156 IELFTQLDALDPKLFGRFHDF 176
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
239-368 7.13e-19

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: 86.37  E-value: 7.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 239 ENGINGILADEMGLGKTVQCIATIalmiqrgVPGPFLVCGPLSTLPNWMAEFKRFT-PDIPTM-LYHGTQEERQ--KLHC 314
Cdd:cd18071   46 ELVRGGILADDMGLGKTLTTISLI-------LANFTLIVCPLSVLSNWETQFEEHVkPGQLKVyTYHGGERNRDpkLLSK 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 315 Y--------------------------WKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFL 368
Cdd:cd18071  119 YdivlttyntlasdfgakgdsplhtinWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSFL 198
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
223-419 3.81e-18

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  Cd Length: 235  Bit Score: 84.13  E-value: 3.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 223 MRWYQVEGMEWLR-----MLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGP------FLVCGPLSTLPNWMAEFK 291
Cdd:cd18066    1 LRPHQREGIEFLYecvmgMRVNERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGkpvikrALIVTPGSLVKNWKKEFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 292 R---------FTPD--------IPTMLYH----------GTQEERQKLHcyWKYLIVDEGHRIKNMKCRLIRELKRFNAD 344
Cdd:cd18066   81 KwlgserikvFTVDqdhkveefIASPLYSvliisyemllRSLDQISKLN--FDLVICDEGHRLKNTSIKTTTALTSLSCE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 345 NKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFD---ITSLSETA---EDIIAKEREQNvlhmLHQILTPFLLR 418
Cdd:cd18066  159 RRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEepiVRSREPTAtpeEKKLGEARAAE----LTRLTGLFILR 234

                 .
gi 574275430 419 R 419
Cdd:cd18066  235 R 235
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
226-381 7.59e-17

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: 79.64  E-value: 7.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 226 YQVEGmewLRMLWENGING-ILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFK-RFTPDIP----- 298
Cdd:cd18011    4 HQIDA---VLRALRKPPVRlLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQdKFGLPFLildre 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 299 ---------------------TMLYHGTQEERQKLHCY--WKYLIVDEGHRIKNMKC-------RLIRELKRfNADNKLL 348
Cdd:cd18011   81 taaqlrrlignpfeefpivivSLDLLKRSEERRGLLLSeeWDLVVVDEAHKLRNSGGgketkryKLGRLLAK-RARHVLL 159
                        170       180       190
                 ....*....|....*....|....*....|...
gi 574275430 349 LTGTPLQNNLSELWSLLNFLLPDVFDDLKSFES 381
Cdd:cd18011  160 LTATPHNGKEEDFRALLSLLDPGRFAVLGRFLR 192
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
226-419 2.57e-16

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: 79.06  E-value: 2.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 226 YQVEGMEWlrMLW---ENGINGILADEMGLGKTVQCIATIaLMIQRG-----------------------VP--GPFLVC 277
Cdd:cd18072    4 HQKQALAW--LLWrerQKPRGGILADDMGLGKTLTMIALI-LAQKNTqnrkeeekekalteweskkdstlVPsaGTLVVC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 278 gPLSTLPNWMAEFKRFTPD--IPTMLYHGTQEERQK--------------------------------LHCYWKYLIVDE 323
Cdd:cd18072   81 -PASLVHQWKNEVESRVASnkLRVCLYHGPNRERIGevlrdydivittyslvakeiptykeesrssplFRIAWARIILDE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 324 GHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDITSLSetaediiAKEReqn 403
Cdd:cd18072  160 AHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRK-------GGER--- 229
                        250
                 ....*....|....*.
gi 574275430 404 vlhmLHQILTPFLLRR 419
Cdd:cd18072  230 ----LNILTKSLLLRR 241
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
241-383 2.48e-13

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  Cd Length: 246  Bit Score: 70.30  E-value: 2.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 241 GINGILADEMGLGKTVQCIA---TIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFT-----------------PDIPT- 299
Cdd:cd18068   28 GSGCILAHCMGLGKTLQVVTflhTVLLCEKLENFSRVLVVCPLNTVLNWLNEFEKWQeglkdeekievnelatyKRPQEr 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 300 --MLYHG-----------------TQEERQKLHC-----YWKYL--------IVDEGHRIKNMKCRLIRELKRFNADNKL 347
Cdd:cd18068  108 syKLQRWqeeggvmiigydmyrilAQERNVKSREklkeiFNKALvdpgpdfvVCDEGHILKNEASAVSKAMNSIRTKRRI 187
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 574275430 348 LLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWF 383
Cdd:cd18068  188 VLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
223-418 4.64e-11

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  Cd Length: 257  Bit Score: 63.90  E-value: 4.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 223 MRWYQVEGMEWlrMLWENGIngiLADEMGLGKTVQCIATIAL-------------------MIQRGVP-------GPFLV 276
Cdd:cd18070    1 LLPYQRRAVNW--MLVPGGI---LADEMGLGKTVEVLALILLhprpdndldaadddsdemvCCPDCLVaetpvssKATLI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 277 CGPLSTLPNWMAEFKRFTP----------------------------DIPTMLY--------------HGTQEERQK--- 311
Cdd:cd18070   76 VCPSAILAQWLDEINRHVPsslkvltyqgvkkdgalaspapeilaeyDIVVTTYdvlrtelhyaeanrSNRRRRRQKrye 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 312 ------LHCYWKYLIVDEGHRIKNMKCRLIRELKRFNADNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDlksfESWFdi 385
Cdd:cd18070  156 appsplVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCD----SDWW-- 229
                        250       260       270
                 ....*....|....*....|....*....|...
gi 574275430 386 tslsetAEDIIAKEREQNVLHMLHQILTPFLLR 418
Cdd:cd18070  230 ------ARVLIRPQGRNKAREPLAALLKELLWR 256
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
223-368 9.89e-10

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: 59.29  E-value: 9.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 223 MRWYQVEGMEWLRmlwENGINGILADeMGLGKTVQCIATIALMIQRGVPGPFLVCGPL----STLPN----WMAEFK--- 291
Cdd:cd18013    1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLrvarSTWPDevekWNHLRNltv 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 292 ----------RFTPDIPTMLYHGTQE------ERQKLHCYWKYLIVDEGHRIKNMKCRLIRELK--RFNADNKLLLTGTP 353
Cdd:cd18013   77 svavgterqrSKAANTPADLYVINREnlkwlvNKSGDPWPFDMVVIDELSSFKSPRSKRFKALRkvRPVIKRLIGLTGTP 156
                        170
                 ....*....|....*
gi 574275430 354 LQNNLSELWSLLNFL 368
Cdd:cd18013  157 SPNGLMDLWAQIALL 171
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
497-698 3.74e-07

Class II histone deacetylase complex subunits 2 and 3; This family of class II histone deacetylase complex subunits HDA2 and HDA3 is found in fungi, The member from S. pombe is referred to as Ccq1 (coiled-coil quantitatively-enriched protein 1). These proteins associate with HDA1 to generate the activity of the HDA1 histone deacetylase complex. HDA1 interacts with itself and with the HDA2-HDA3 subcomplex to form a probable tetramer and these interactions are necessary for catalytic activity. The HDA1 histone deacetylase complex is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. HDA2 and HDA3 have a conserved coiled-coil domain towards their C-terminus.


Pssm-ID: 338022  Cd Length: 279  Bit Score: 52.33  E-value: 3.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  497 EKLISQIQPEVDREravVEVNIPVEsEVNLKLQNIMMLLRKCC---NHPYL-IEYPIDPVTQEFKIDEELVTNSGKFLIL 572
Cdd:pfam11496  21 EQIVSLHYSDILKY---LETSDSKE-DLSLIQKSITLCLENLSlvaTHPYLlIDHYMPKSLLLKDEPEWLAETSGKFLVL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430  573 DRMLPEL----KKRGHKVLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKnMHSFNTDPEVFIFLVSTRA---- 644
Cdd:pfam11496  97 NDLINLLierdRKRPINVAIVARSVKTLDLVEALLLGKGLSYKRYSGEMLKGENKE-VPDDKISSTVKHLLSTTGQltnd 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 574275430  645 -GGLGInlTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVYRLVTANTIDQ 698
Cdd:pfam11496 176 ySLLEN--YKFDLIIAFDSSVDTSSPSIEHLRTQNRRQGNLAPIIRLVPINSIEH 228
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
634-688 1.54e-06

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: 46.16  E-value: 1.54e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 574275430 634 EVFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKPVVVY 688
Cdd:cd18785   21 SSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVIL 75
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
223-353 2.69e-06

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: 47.69  E-value: 2.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 223 MRWYQVEGMEwlRMLWENGIN-GILADEMGLGKTVqcIAtIALMIQRGvPGPFLVCGPLSTLPN-WMAEFKRFTPDIP-- 298
Cdd:cd17926    1 LRPYQEEALE--AWLAHKNNRrGILVLPTGSGKTL--TA-LALIAYLK-ELRTLIVVPTDALLDqWKERFEDFLGDSSig 74
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 574275430 299 ------------------TM--LYHGTQEERQKLHCYWkYLIVDEGHRIknmKCRLIRE-LKRFNADNKLLLTGTP 353
Cdd:cd17926   75 ligggkkkdfddanvvvaTYqsLSNLAEEEKDLFDQFG-LLIVDEAHHL---PAKTFSEiLKELNAKYRLGLTATP 146
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
552-682 3.39e-06

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 46.73  E-value: 3.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 552 VTQEFkideELVTNSGKFLILDRMLPELKKRGhKVLLFSQMTSMLDILMDYCHLRDFNFSRLDGSMSYSEREKNMHSFNT 631
Cdd:cd18787    1 IKQLY----VVVEEEEKKLLLLLLLLEKLKPG-KAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRS 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 574275430 632 DpEVFIfLVST----RagglGINLTAADTVIIYDsdwNPQSdlqAQDRCHRIGQT 682
Cdd:cd18787   76 G-KVRV-LVATdvaaR----GLDIPGVDHVINYD---LPRD---AEDYVHRIGRT 118
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
531-682 6.79e-06

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


Pssm-ID: 223587 [Multi-domain]  Cd Length: 513  Bit Score: 49.40  E-value: 6.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 531 IMMLLRKCCNHPYLIEypIDPVTQEF---KIDEELVTNSG---KFLILDRMLPELKKRghKVLLFSQMTSMLDILMDYCH 604
Cdd:COG0513  219 IRELARRYLNDPVEIE--VSVEKLERtlkKIKQFYLEVESeeeKLELLLKLLKDEDEG--RVIVFVRTKRLVEELAESLR 294
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 574275430 605 LRDFNFSRLDGSMSYSEREKNMHSFNTDPEVfiFLVSTRAGGLGINLTAADTVIIYDSDWNPqsdlqaQDRCHRIGQT 682
Cdd:COG0513  295 KRGFKVAALHGDLPQEERDRALEKFKDGELR--VLVATDVAARGLDIPDVSHVINYDLPLDP------EDYVHRIGRT 364
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination and repair];
214-398 1.11e-04

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


Pssm-ID: 223989 [Multi-domain]  Cd Length: 442  Bit Score: 45.12  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 214 QPKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVqciatIALMIQRGVPGPFLVCGPLSTLPN-WMAEFKR 292
Cdd:COG1061   28 KLIVAFEFELRPYQEEALDALVKNRRTERRGVIVLPTGAGKTV-----VAAEAIAELKRSTLVLVPTKELLDqWAEALKK 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 293 FT--PDIPTMLYHGTQEER-------------------QKLHCYWKYLIVDEGHRIKNMKCRLIreLKRFNADNKLL-LT 350
Cdd:COG1061  103 FLllNDEIGIYGGGEKELEpakvtvatvqtlarrqlldEFLGNEFGLIIFDEVHHLPAPSYRRI--LELLSAAYPRLgLT 180
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 574275430 351 GTPlqnnlselWSLLNFLLPDVFDDLKSFEswFDITSLSETAEDIIAK 398
Cdd:COG1061  181 ATP--------EREDGGRIGDLFDLIGPIV--YEVSLKELIDEGYLAP 218
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination and repair];
554-713 1.86e-03

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


Pssm-ID: 223989 [Multi-domain]  Cd Length: 442  Bit Score: 41.27  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 554 QEFKIDEELVTNSGKFLILDRMLPeLKKRGHKVLLFSQMTSMLDILMDYChLRDFNFSRLDGSMSYSEREKNMHSFNTDP 633
Cdd:COG1061  255 AENEARRIAIASERKIAAVRGLLL-KHARGDKTLIFASDVEHAYEIAKLF-LAPGIVEAITGETPKEEREAILERFRTGG 332
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574275430 634 evFIFLVSTRAGGLGINLTAADTVIIYDSDWNPQSDLQAQDRCHRIGQTKP---VVVYRLVTANTIDQKIveraAAKRKL 710
Cdd:COG1061  333 --IKVLVTVKVLDEGVDIPDADVLIILRPTGSRRLFIQRLGRGLRPAEGKEdtlALDYSLVPDDLGEEDI----ARRRRL 406

                 ...
gi 574275430 711 EKL 713
Cdd:COG1061  407 FLI 409
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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