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Conserved domains on  [gi|1072319335|ref|WP_069941394|]
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MULTISPECIES: DEAD/DEAH box helicase [Micrococcus]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11654201)

DEAD/DEAH box-containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA

EC:  3.6.4.-
PubMed:  20206133
SCOP:  3002019

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
436-1116 0e+00

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 569.09  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  436 EPPVLRLRADFRPGHELVLRWSWLYFDPPRELGLDAGGDPLRDTRHEDAVLRAVAELWPRAGRAEEQVLEGVGAARFSEQ 515
Cdd:COG0553      1 LLLLLLLLALGALGLLLTELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSAL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  516 VLPLLQRADHVRVDVTGDRPDYRELKAAPRIEVGTKATQNDWFDLGVQVSVDGHVLPFVELFTALVQGRTTLILADGSYL 595
Cdd:COG0553     81 ALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  596 GLDHPAFDRLRALLSEAATLQEWTPEHTPVSRHQVGFWEDLKELADEVDEDPEWTAAVGRLAAVERLPEAPR--PAGLKA 673
Cdd:COG0553    161 RLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALEslPAGLKA 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  674 DLRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPpFLVVAPSSVVSVWAAEAEKFTPDLDVR 753
Cdd:COG0553    241 TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARP-VLIVAPTSLVGNWQRELAKFAPGLRVL 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  754 VLD-TTTRKRGtavADEVAGADVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRLAITGTP 832
Cdd:COG0553    320 VLDgTRERAKG---ANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTP 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  833 MENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETGgDPERMAALRRRVRPFMLRRSKELVAKDLPSKQEQILQVELEP 912
Cdd:COG0553    397 VENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKG-DEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTP 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  913 AHRKLYDRVLQRERRKVLGLLGDmdGNRFTIFTSLTLLRMLALAPQIVDD--QYASVPSSKLERFLDDLTEVIGEGHRVI 990
Cdd:COG0553    476 EQRALYEAVLEYLRRELEGAEGI--RRRGLILAALTRLRQICSHPALLLEegAELSGRSAKLEALLELLEELLAEGEKVL 553
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  991 VFSQFTSFLRVIAEELDHLEIEHAYLDGST--RGRADVIRGFREG-EAPVFLISLKAGGFGLTLTEADYVFLMDPWWNPA 1067
Cdd:COG0553    554 VFSQFTDTLDLLEERLEERGIEYAYLHGGTsaEERDELVDRFQEGpEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPA 633
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 1072319335 1068 AEAQAVDRAHRIGQERTVMVYRLVSEGTIEEKVLELQRRKAELFGALMD 1116
Cdd:COG0553    634 VEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
SWIM COG4715
Uncharacterized protein, contains SWIM-type Zn finger domain [Function unknown];
16-518 7.71e-10

Uncharacterized protein, contains SWIM-type Zn finger domain [Function unknown];


:

Pssm-ID: 443750 [Multi-domain]  Cd Length: 508  Bit Score: 62.92  E-value: 7.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335   16 EAIRAVVGPTSADRGFAVAASGAVGRLRYDAatGRLSASVQGTapSPYRVQVQLQEAYDdaaedgagalmepVGGRCTCP 95
Cdd:COG4715      9 DDIRRLAGPRIFERGREYAREGRVLDLDVED--GRLEATVQGS--EDYRVRVDLDDGGD-------------LDSSCTCP 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335   96 VGTD--CKHVAAALYQVVRLDAD-QALDDARRKLAEMV------TTADALPAPAGRGHDGGGPAGLDAPAADGAAPPPPA 166
Cdd:COG4715     72 YGGGgfCKHVVAVLLALLDQPEEgAPRQSEREALEELLerlskeELVELLLELAAEDPELRELRRALDDSGGDYLREELL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  167 GLDWRRVMEPLAGLHGPRRVGTPPALAIGVELVAESSRNAFQQWGPATAGEEQVREGRPLYVTVRPLKRGAKGT-----W 241
Cdd:COG4715    152 ELSRLAALSLTATLAALAPRSTLALRLALLRLLLLLLAPSSLDGAPPGLSLALVRELLPALAERALALLLLVPApagllK 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  242 IKGGLTWKAFQFPRAEFAPAQERAMRLIWRQVQAEDSYPGDAWFGLHVFDSPRIWQLLAEAREVGVELVPLGLLTDVVLE 321
Cdd:COG4715    232 LRLLLARPGALLLSLLDLLLRLDLLLGLLLLALLLLLLLLLQLLALLLLALRTLAALLLLLRLRLRLGLAAGLALAVLLL 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  322 APVAVGLDVTAAPDGGLDVAPSLDPAPPGPGLSGVHAVGGIGFYRVELTDEEAVLHLIPAARPVPEAVQQLVLAGGPVRV 401
Cdd:COG4715    312 LLLLLLPLPLALLALSLLLRLLLALLRLALLVLLYLLLILLLLALLLLALLLLLELLLLLALLLLLAEVELARLLEEALL 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  402 PAADREEFLGRIYPRLRGALPVTSGDASVELPEFEPPVLRLRADFRPGHELVLRWSWLYFDPPRELGLDAGGDPLRDTRH 481
Cdd:COG4715    392 IRRRLLLLLLLLLRLLDLLALLALRLLLLLLLAVLSEAEDLLLELLETLGLHRLLLLEAREELLPELAADLALLLLLEAL 471
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1072319335  482 EDAVLRAVAELWPRAGRAEEQVLEGVGAARFSEQVLP 518
Cdd:COG4715    472 DLLALEALALLLLLELLLLLAVTLLLLAIDELLLLAL 508
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
436-1116 0e+00

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 569.09  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  436 EPPVLRLRADFRPGHELVLRWSWLYFDPPRELGLDAGGDPLRDTRHEDAVLRAVAELWPRAGRAEEQVLEGVGAARFSEQ 515
Cdd:COG0553      1 LLLLLLLLALGALGLLLTELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSAL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  516 VLPLLQRADHVRVDVTGDRPDYRELKAAPRIEVGTKATQNDWFDLGVQVSVDGHVLPFVELFTALVQGRTTLILADGSYL 595
Cdd:COG0553     81 ALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  596 GLDHPAFDRLRALLSEAATLQEWTPEHTPVSRHQVGFWEDLKELADEVDEDPEWTAAVGRLAAVERLPEAPR--PAGLKA 673
Cdd:COG0553    161 RLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALEslPAGLKA 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  674 DLRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPpFLVVAPSSVVSVWAAEAEKFTPDLDVR 753
Cdd:COG0553    241 TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARP-VLIVAPTSLVGNWQRELAKFAPGLRVL 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  754 VLD-TTTRKRGtavADEVAGADVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRLAITGTP 832
Cdd:COG0553    320 VLDgTRERAKG---ANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTP 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  833 MENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETGgDPERMAALRRRVRPFMLRRSKELVAKDLPSKQEQILQVELEP 912
Cdd:COG0553    397 VENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKG-DEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTP 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  913 AHRKLYDRVLQRERRKVLGLLGDmdGNRFTIFTSLTLLRMLALAPQIVDD--QYASVPSSKLERFLDDLTEVIGEGHRVI 990
Cdd:COG0553    476 EQRALYEAVLEYLRRELEGAEGI--RRRGLILAALTRLRQICSHPALLLEegAELSGRSAKLEALLELLEELLAEGEKVL 553
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  991 VFSQFTSFLRVIAEELDHLEIEHAYLDGST--RGRADVIRGFREG-EAPVFLISLKAGGFGLTLTEADYVFLMDPWWNPA 1067
Cdd:COG0553    554 VFSQFTDTLDLLEERLEERGIEYAYLHGGTsaEERDELVDRFQEGpEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPA 633
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 1072319335 1068 AEAQAVDRAHRIGQERTVMVYRLVSEGTIEEKVLELQRRKAELFGALMD 1116
Cdd:COG0553    634 VEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
671-891 1.90e-90

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: 289.47  E-value: 1.90e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  671 LKADLRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPpFLVVAPSSVVSVWAAEAEKFTPDL 750
Cdd:cd18012      1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGP-SLVVAPTSLIYNWEEEAAKFAPEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  751 DVRVLDTTTRKRGtaVADEVAGADVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRLAITG 830
Cdd:cd18012     80 KVLVIHGTKRKRE--KLRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTG 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072319335  831 TPMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETGGDPERMAALRRRVRPFMLRRSK 891
Cdd:cd18012    158 TPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEEALEELKKLISPFILRRLK 218
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
626-1110 1.88e-68

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 250.10  E-value: 1.88e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  626 SRHQVGFWEDL--KELADEVDEDPEWTAAVgRLAAverlpeapRPAGLKADLRPYQEEGLRWLAFLWEQDLGGILADDMG 703
Cdd:PLN03142   128 GRHASKLTEEEedEEYLKEEEDGLGGSGGT-RLLV--------QPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMG 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  704 LGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPDLDVRVLDTTTRKRgTAVADE--VAGA-DVVVTSY 780
Cdd:PLN03142   199 LGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEER-AHQREEllVAGKfDVCVTSF 277
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  781 TLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRE 860
Cdd:PLN03142   278 EMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDE 357
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  861 TYVTPIEtGGDPERMAALRRRVRPFMLRRSKELVAKDLPSKQEQILQVELEPAHRKLYDRVLQRERRKVlgllgDMDGNR 940
Cdd:PLN03142   358 WFQISGE-NDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVV-----NAGGER 431
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  941 FTIFTSLTLLRMLALAPQIVDDQYASVP----------SSK---LERFLDDLTEvigEGHRVIVFSQFTSFLRVIAEELD 1007
Cdd:PLN03142   432 KRLLNIAMQLRKCCNHPYLFQGAEPGPPyttgehlvenSGKmvlLDKLLPKLKE---RDSRVLIFSQMTRLLDILEDYLM 508
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335 1008 HLEIEHAYLDGSTRG--RADVIRGF-REG-EAPVFLISLKAGGFGLTLTEADYVFLMDPWWNPAAEAQAVDRAHRIGQER 1083
Cdd:PLN03142   509 YRGYQYCRIDGNTGGedRDASIDAFnKPGsEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKK 588
                          490       500
                   ....*....|....*....|....*..
gi 1072319335 1084 TVMVYRLVSEGTIEEKVLELQRRKAEL 1110
Cdd:PLN03142   589 EVQVFRFCTEYTIEEKVIERAYKKLAL 615
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
678-951 2.20e-59

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 206.00  E-value: 2.20e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  678 YQEEGLRWLAFLWEQD-LGGILADDMGLGKTVQTLALFAHARQARPER-PPFLVVAPSSVVSVWAAEAEKFT--PDLDVR 753
Cdd:pfam00176    1 YQIEGVNWMLSLENNLgRGGILADEMGLGKTLQTISLLLYLKHVDKNWgGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  754 VLDTTTRKRGTAVADE--VAGADVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRLAITGT 831
Cdd:pfam00176   81 VLHGNKRPQERWKNDPnfLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  832 PMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETGGDPERMAALRRRVRPFMLRRSKELVAKDLPSKQEQILQVELE 911
Cdd:pfam00176  161 PLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLS 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1072319335  912 PAHRKLYDRVLQRERRKVLGLLGDMDGNRFTIFTSLTLLR 951
Cdd:pfam00176  241 KLQRKLYQTFLLKKDLNAIKTGEGGREIKASLLNILMRLR 280
HELICc smart00490
helicase superfamily c-terminal domain;
1002-1080 1.90e-17

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 78.02  E-value: 1.90e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  1002 IAEELDHLEIEHAYLDGST--RGRADVIRGFREGEApVFLISLKAGGFGLTLTEADYVFLMDPWWNPAAEAQAVDRAHRI 1079
Cdd:smart00490    3 LAELLKELGIKVARLHGGLsqEEREEILDKFNNGKI-KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRA 81

                    .
gi 1072319335  1080 G 1080
Cdd:smart00490   82 G 82
SWIM COG4715
Uncharacterized protein, contains SWIM-type Zn finger domain [Function unknown];
16-518 7.71e-10

Uncharacterized protein, contains SWIM-type Zn finger domain [Function unknown];


Pssm-ID: 443750 [Multi-domain]  Cd Length: 508  Bit Score: 62.92  E-value: 7.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335   16 EAIRAVVGPTSADRGFAVAASGAVGRLRYDAatGRLSASVQGTapSPYRVQVQLQEAYDdaaedgagalmepVGGRCTCP 95
Cdd:COG4715      9 DDIRRLAGPRIFERGREYAREGRVLDLDVED--GRLEATVQGS--EDYRVRVDLDDGGD-------------LDSSCTCP 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335   96 VGTD--CKHVAAALYQVVRLDAD-QALDDARRKLAEMV------TTADALPAPAGRGHDGGGPAGLDAPAADGAAPPPPA 166
Cdd:COG4715     72 YGGGgfCKHVVAVLLALLDQPEEgAPRQSEREALEELLerlskeELVELLLELAAEDPELRELRRALDDSGGDYLREELL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  167 GLDWRRVMEPLAGLHGPRRVGTPPALAIGVELVAESSRNAFQQWGPATAGEEQVREGRPLYVTVRPLKRGAKGT-----W 241
Cdd:COG4715    152 ELSRLAALSLTATLAALAPRSTLALRLALLRLLLLLLAPSSLDGAPPGLSLALVRELLPALAERALALLLLVPApagllK 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  242 IKGGLTWKAFQFPRAEFAPAQERAMRLIWRQVQAEDSYPGDAWFGLHVFDSPRIWQLLAEAREVGVELVPLGLLTDVVLE 321
Cdd:COG4715    232 LRLLLARPGALLLSLLDLLLRLDLLLGLLLLALLLLLLLLLQLLALLLLALRTLAALLLLLRLRLRLGLAAGLALAVLLL 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  322 APVAVGLDVTAAPDGGLDVAPSLDPAPPGPGLSGVHAVGGIGFYRVELTDEEAVLHLIPAARPVPEAVQQLVLAGGPVRV 401
Cdd:COG4715    312 LLLLLLPLPLALLALSLLLRLLLALLRLALLVLLYLLLILLLLALLLLALLLLLELLLLLALLLLLAEVELARLLEEALL 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  402 PAADREEFLGRIYPRLRGALPVTSGDASVELPEFEPPVLRLRADFRPGHELVLRWSWLYFDPPRELGLDAGGDPLRDTRH 481
Cdd:COG4715    392 IRRRLLLLLLLLLRLLDLLALLALRLLLLLLLAVLSEAEDLLLELLETLGLHRLLLLEAREELLPELAADLALLLLLEAL 471
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1072319335  482 EDAVLRAVAELWPRAGRAEEQVLEGVGAARFSEQVLP 518
Cdd:COG4715    472 DLLALEALALLLLLELLLLLAVTLLLLAIDELLLLAL 508
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
436-1116 0e+00

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 569.09  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  436 EPPVLRLRADFRPGHELVLRWSWLYFDPPRELGLDAGGDPLRDTRHEDAVLRAVAELWPRAGRAEEQVLEGVGAARFSEQ 515
Cdd:COG0553      1 LLLLLLLLALGALGLLLTELLLLLRLGALLLELVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSAL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  516 VLPLLQRADHVRVDVTGDRPDYRELKAAPRIEVGTKATQNDWFDLGVQVSVDGHVLPFVELFTALVQGRTTLILADGSYL 595
Cdd:COG0553     81 ALLLLRLLLALLLLALLLLLAGLLALALLLLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  596 GLDHPAFDRLRALLSEAATLQEWTPEHTPVSRHQVGFWEDLKELADEVDEDPEWTAAVGRLAAVERLPEAPR--PAGLKA 673
Cdd:COG0553    161 RLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALEslPAGLKA 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  674 DLRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPpFLVVAPSSVVSVWAAEAEKFTPDLDVR 753
Cdd:COG0553    241 TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARP-VLIVAPTSLVGNWQRELAKFAPGLRVL 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  754 VLD-TTTRKRGtavADEVAGADVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRLAITGTP 832
Cdd:COG0553    320 VLDgTRERAKG---ANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTP 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  833 MENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETGgDPERMAALRRRVRPFMLRRSKELVAKDLPSKQEQILQVELEP 912
Cdd:COG0553    397 VENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKG-DEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTP 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  913 AHRKLYDRVLQRERRKVLGLLGDmdGNRFTIFTSLTLLRMLALAPQIVDD--QYASVPSSKLERFLDDLTEVIGEGHRVI 990
Cdd:COG0553    476 EQRALYEAVLEYLRRELEGAEGI--RRRGLILAALTRLRQICSHPALLLEegAELSGRSAKLEALLELLEELLAEGEKVL 553
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  991 VFSQFTSFLRVIAEELDHLEIEHAYLDGST--RGRADVIRGFREG-EAPVFLISLKAGGFGLTLTEADYVFLMDPWWNPA 1067
Cdd:COG0553    554 VFSQFTDTLDLLEERLEERGIEYAYLHGGTsaEERDELVDRFQEGpEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPA 633
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 1072319335 1068 AEAQAVDRAHRIGQERTVMVYRLVSEGTIEEKVLELQRRKAELFGALMD 1116
Cdd:COG0553    634 VEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
671-891 1.90e-90

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: 289.47  E-value: 1.90e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  671 LKADLRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPpFLVVAPSSVVSVWAAEAEKFTPDL 750
Cdd:cd18012      1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGP-SLVVAPTSLIYNWEEEAAKFAPEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  751 DVRVLDTTTRKRGtaVADEVAGADVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRLAITG 830
Cdd:cd18012     80 KVLVIHGTKRKRE--KLRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTG 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072319335  831 TPMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETGGDPERMAALRRRVRPFMLRRSK 891
Cdd:cd18012    158 TPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEEALEELKKLISPFILRRLK 218
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
626-1110 1.88e-68

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 250.10  E-value: 1.88e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  626 SRHQVGFWEDL--KELADEVDEDPEWTAAVgRLAAverlpeapRPAGLKADLRPYQEEGLRWLAFLWEQDLGGILADDMG 703
Cdd:PLN03142   128 GRHASKLTEEEedEEYLKEEEDGLGGSGGT-RLLV--------QPSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMG 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  704 LGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPDLDVRVLDTTTRKRgTAVADE--VAGA-DVVVTSY 780
Cdd:PLN03142   199 LGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEER-AHQREEllVAGKfDVCVTSF 277
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  781 TLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRE 860
Cdd:PLN03142   278 EMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDE 357
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  861 TYVTPIEtGGDPERMAALRRRVRPFMLRRSKELVAKDLPSKQEQILQVELEPAHRKLYDRVLQRERRKVlgllgDMDGNR 940
Cdd:PLN03142   358 WFQISGE-NDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVV-----NAGGER 431
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  941 FTIFTSLTLLRMLALAPQIVDDQYASVP----------SSK---LERFLDDLTEvigEGHRVIVFSQFTSFLRVIAEELD 1007
Cdd:PLN03142   432 KRLLNIAMQLRKCCNHPYLFQGAEPGPPyttgehlvenSGKmvlLDKLLPKLKE---RDSRVLIFSQMTRLLDILEDYLM 508
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335 1008 HLEIEHAYLDGSTRG--RADVIRGF-REG-EAPVFLISLKAGGFGLTLTEADYVFLMDPWWNPAAEAQAVDRAHRIGQER 1083
Cdd:PLN03142   509 YRGYQYCRIDGNTGGedRDASIDAFnKPGsEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKK 588
                          490       500
                   ....*....|....*....|....*..
gi 1072319335 1084 TVMVYRLVSEGTIEEKVLELQRRKAEL 1110
Cdd:PLN03142   589 EVQVFRFCTEYTIEEKVIERAYKKLAL 615
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
678-951 2.20e-59

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 206.00  E-value: 2.20e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  678 YQEEGLRWLAFLWEQD-LGGILADDMGLGKTVQTLALFAHARQARPER-PPFLVVAPSSVVSVWAAEAEKFT--PDLDVR 753
Cdd:pfam00176    1 YQIEGVNWMLSLENNLgRGGILADEMGLGKTLQTISLLLYLKHVDKNWgGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  754 VLDTTTRKRGTAVADE--VAGADVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRLAITGT 831
Cdd:pfam00176   81 VLHGNKRPQERWKNDPnfLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  832 PMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETGGDPERMAALRRRVRPFMLRRSKELVAKDLPSKQEQILQVELE 911
Cdd:pfam00176  161 PLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLS 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1072319335  912 PAHRKLYDRVLQRERRKVLGLLGDMDGNRFTIFTSLTLLR 951
Cdd:pfam00176  241 KLQRKLYQTFLLKKDLNAIKTGEGGREIKASLLNILMRLR 280
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
675-849 2.80e-56

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: 192.78  E-value: 2.80e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPDLDVRV 754
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  755 LDTTTRKRGTAVADEVAG-ADVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRLAITGTPM 833
Cdd:cd17919     81 YHGSQRERAQIRAKEKLDkFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPL 160
                          170
                   ....*....|....*.
gi 1072319335  834 ENSLSDLWALLGVVVP 849
Cdd:cd17919    161 QNNLEELWALLDFLDP 176
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
969-1091 6.32e-53

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: 181.14  E-value: 6.32e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  969 SSKLERFLDDLTEVIGEGHRVIVFSQFTSFLRVIAEELDHLEIEHAYLDGSTRG--RADVIRGFREGEAP-VFLISLKAG 1045
Cdd:cd18793     10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSkeRQKLVDRFNEDPDIrVFLLSTKAG 89
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1072319335 1046 GFGLTLTEADYVFLMDPWWNPAAEAQAVDRAHRIGQERTVMVYRLV 1091
Cdd:cd18793     90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
675-889 2.04e-50

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: 177.93  E-value: 2.04e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERP-----PFLVVAPSSVVSVWAAEAEKFTPD 749
Cdd:cd17999      1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHHKRANSFnsenlPSLVVCPPTLVGHWVAEIKKYFPN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  750 LDVRVLD----TTTRKRgtaVADEVAGADVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFR 825
Cdd:cd17999     81 AFLKPLAyvgpPQERRR---LREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072319335  826 LAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETGGDPE-----------RMAALRRRVRPFMLRR 889
Cdd:cd17999    158 LILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKasakeqeagalALEALHKQVLPFLLRR 232
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
675-891 3.56e-46

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: 165.57  E-value: 3.56e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPDLDVRV 754
Cdd:cd17997      4 MRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLRVVV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  755 LDTTTRKRGTAVADEVAGA--DVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRLAITGTP 832
Cdd:cd17997     84 LIGDKEERADIIRDVLLPGkfDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGTP 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1072319335  833 MENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETGGDPERMAALRRRVRPFMLRRSK 891
Cdd:cd17997    164 LQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
675-889 7.16e-43

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: 156.77  E-value: 7.16e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQ----------ARPER----------PPFLVVAPSS 734
Cdd:cd18005      1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGktgtrrdrenNRPRFkkkppassakKPVLIVAPLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  735 VVSVWAAEAEK---FTpdldVRVLDTTTRKRGTAVADEVAGADVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAA 811
Cdd:cd18005     81 VLYNWKDELDTwghFE----VGVYHGSRKDDELEGRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  812 KVHTVARDLRAPFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETG------------GDpERMAALR 879
Cdd:cd18005    157 KLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGqrhtatarelrlGR-KRKQELA 235
                          250
                   ....*....|
gi 1072319335  880 RRVRPFMLRR 889
Cdd:cd18005    236 VKLSKFFLRR 245
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
675-889 6.45e-42

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: 153.17  E-value: 6.45e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTpDLDVRV 754
Cdd:cd17995      1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWT-DMNVVV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  755 L-DTTTRKR------------GTAVADEVAGADVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLR 821
Cdd:cd17995     80 YhGSGESRQiiqqyemyfkdaQGRKKKGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072319335  822 APFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYvtpietgGD---PERMAALRRRVRPFMLRR 889
Cdd:cd17995    160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF-------GDlktAEQVEKLQALLKPYMLRR 223
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
675-889 2.21e-41

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: 151.89  E-value: 2.21e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPDLDVRV 754
Cdd:cd18002      1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  755 LDTTTRKRGT--------AVADEVAGADVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRL 826
Cdd:cd18002     81 YWGNPKDRKVlrkfwdrkNLYTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1072319335  827 AITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIE------TGGDPERMAALRRRVRPFMLRR 889
Cdd:cd18002    161 LLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIEshaenkTGLNEHQLKRLHMILKPFMLRR 229
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
674-891 9.53e-41

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: 150.21  E-value: 9.53e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  674 DLRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPDLDVR 753
Cdd:cd17996      3 TLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSKI 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  754 VLDTTTRKRGTAVADEVAGA-DVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKV-HTVARDLRAPFRLAITGT 831
Cdd:cd17996     83 VYKGTPDVRKKLQSQIRAGKfNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLtQTLNTYYHARYRLLLTGT 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072319335  832 PMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETGG--------DPERMAALRRR---VRPFMLRRSK 891
Cdd:cd17996    163 PLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGeqvkielnEEETLLIIRRLhkvLRPFLLRRLK 233
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
675-891 4.70e-40

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: 148.30  E-value: 4.70e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQaRPERPPFLVVAPSSVVSVWAAEAEKFTPDLDVRV 754
Cdd:cd18009      4 MRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRE-RGVWGPFLVIAPLSTLPNWVNEFARFTPSVPVLL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  755 LDTTTRKRGTAV----ADEVAGAD--VVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRLAI 828
Cdd:cd18009     83 YHGTKEERERLRkkimKREGTLQDfpVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLLL 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1072319335  829 TGTPMENSLSDLWALLGVVVPGLFPSHRRF-----------RETYVTPIETGGDPERMAALRRRVRPFMLRRSK 891
Cdd:cd18009    163 TGTPLQNNLSELWSLLNFLLPDVFDDLSSFeswfdfsslsdNAADISNLSEEREQNIVHMLHAILKPFLLRRLK 236
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
675-889 1.58e-39

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: 146.34  E-value: 1.58e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPDLDVRV 754
Cdd:cd18003      1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  755 LDTTTRKR-----GTAVADEVagaDVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRLAIT 829
Cdd:cd18003     81 YYGSAKERklkrqGWMKPNSF---HVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLT 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072319335  830 GTPMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIE---TGGDPERMAALRR--RV-RPFMLRR 889
Cdd:cd18003    158 GTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLTamsEGSQEENEELVRRlhKVlRPFLLRR 223
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
675-889 6.01e-39

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: 144.42  E-value: 6.01e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPDLDVRV 754
Cdd:cd17993      2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  755 LDTTTRKRGTAVADEVAGA-------DVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRLA 827
Cdd:cd17993     82 YLGDIKSRDTIREYEFYFSqtkklkfNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRLL 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072319335  828 ITGTPMENSLSDLWALLGVVVPGLFPSHRRFREtyvtpiETGGDPER-MAALRRRVRPFMLRR 889
Cdd:cd17993    162 ITGTPLQNSLKELWALLHFLMPGKFDIWEEFEE------EHDEEQEKgIADLHKELEPFILRR 218
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
675-889 7.58e-39

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: 144.12  E-value: 7.58e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPDLDVRV 754
Cdd:cd18006      1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  755 LDTTTRKRGTAVAD--EVAGADVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRLAITGTP 832
Cdd:cd18006     81 YMGDKEKRLDLQQDikSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1072319335  833 MENSLSDLWALLGVVVPGLFPSHR--RFRETYVtpiETGGDPERMAALRRRVRPFMLRR 889
Cdd:cd18006    161 IQNSLQELYALLSFIEPNVFPKDKldDFIKAYS---ETDDESETVEELHLLLQPFLLRR 216
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
675-889 8.25e-39

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: 145.12  E-value: 8.25e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLweqdlGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSV---------------- 738
Cdd:cd18008      1 LLPYQKQGLAWMLPR-----GGILADEMGLGKTIQALALILATRPQDPKIPEELEENSSDPKKLylskttlivvplslls 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  739 -WAAEAEKFT--PDLDVRVLDTTTRKRgtaVADEVAGADVVVTSYTLLRIDAGQYGGLD----------------WGGVV 799
Cdd:cd18008     76 qWKDEIEKHTkpGSLKVYVYHGSKRIK---SIEELSDYDIVITTYGTLASEFPKNKKGGgrdskekeasplhrirWYRVI 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  800 FDEAQFLKNRAAKVHTVARDLRAPFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFReTYVTPIETGGDPERMAALR 879
Cdd:cd18008    153 LDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFN-SDISKPFSKNDRKALERLQ 231
                          250
                   ....*....|
gi 1072319335  880 RRVRPFMLRR 889
Cdd:cd18008    232 ALLKPILLRR 241
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
675-902 7.10e-38

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: 142.50  E-value: 7.10e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPDLDVRV 754
Cdd:cd18064     16 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRAVC 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  755 LDTTTRKRGTAVADEVAGA--DVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRLAITGTP 832
Cdd:cd18064     96 LIGDKDQRAAFVRDVLLPGewDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTP 175
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  833 MENSLSDLWALLGVVVPGLFPSHRRFrETYVTPIETGGDPERMAALRRRVRPFMLRRSKELVAKDLPSKQ 902
Cdd:cd18064    176 LQNNLHELWALLNFLLPDVFNSAEDF-DSWFDTNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSLPPKK 244
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
655-889 4.64e-35

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: 133.98  E-value: 4.64e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  655 RLAAVERLPEAPRPAGLkaDLRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSS 734
Cdd:cd18054      3 RFVALKKQPSYIGGENL--ELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  735 VVSVWAAEAEKFTPDLDVRVLDTTTRKRGTAVADEVAGA-------DVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLK 807
Cdd:cd18054     81 TLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSqtkrlkfNALITTYEILLKDKTVLGSINWAFLGVDEAHRLK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  808 NRAAKVHTVARDLRAPFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETGgdperMAALRRRVRPFML 887
Cdd:cd18054    161 NDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENG-----YQSLHKVLEPFLL 235

                   ..
gi 1072319335  888 RR 889
Cdd:cd18054    236 RR 237
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
675-891 3.08e-34

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: 131.68  E-value: 3.08e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPDLDVRV 754
Cdd:cd18065     16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRAVC 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  755 LDTTTRKRGTAVADEVAGA--DVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRLAITGTP 832
Cdd:cd18065     96 LIGDKDARAAFIRDVMMPGewDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTP 175
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1072319335  833 MENSLSDLWALLGVVVPGLFPSHRRFrETYVTPIETGGDPERMAALRRRVRPFMLRRSK 891
Cdd:cd18065    176 LQNNLHELWALLNFLLPDVFNSADDF-DSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 233
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
675-889 1.56e-33

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: 129.41  E-value: 1.56e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFA------HARQArperppfLVVAPSSVVSVWAAEAEKFTP 748
Cdd:cd18001      1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSgmfdsgLIKSV-------LVVMPTSLIPHWVKEFAKWTP 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  749 DLDVRVLDTTTRKRGTAVADEVA-GADVVVTSYTLLRIDAGQYGGLD-----WGGVVFDEAQFLKNRAAKVHTVARDLRA 822
Cdd:cd18001     74 GLRVKVFHGTSKKERERNLERIQrGGGVLLTTYGMVLSNTEQLSADDhdefkWDYVILDEGHKIKNSKTKSAKSLREIPA 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1072319335  823 PFRLAITGTPMENSLSDLWALLGVVVPG-LFPSHRRFRETYVTPIETGGDPE----------RMAA-LRRRVRPFMLRR 889
Cdd:cd18001    154 KNRIILTGTPIQNNLKELWALFDFACNGsLLGTRKTFKMEFENPITRGRDKDatqgekalgsEVAEnLRQIIKPYFLRR 232
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
675-889 2.18e-33

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: 127.94  E-value: 2.18e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPDLDVRv 754
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVV- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  755 ldtttrkrgTAVADEVagadvVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRLAITGTPME 834
Cdd:cd17994     80 ---------TYVGDHV-----LLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQ 145
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1072319335  835 NSLSDLWALLGVVVPGLFPSHRRFRETYvtpiETGGDPERMAALRRRVRPFMLRR 889
Cdd:cd17994    146 NNLEELFHLLNFLTPERFNNLQGFLEEF----ADISKEDQIKKLHDLLGPHMLRR 196
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
675-889 4.76e-33

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: 128.17  E-value: 4.76e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRwlaFLWEQDLGG--------ILADDMGLGKTVQTLAL----FAHARQARPERPPFLVVAPSSVVSVWAAE 742
Cdd:cd18004      1 LRPHQREGVQ---FLYDCLTGRrgyggggaILADEMGLGKTLQAIALvwtlLKQGPYGKPTAKKALIVCPSSLVGNWKAE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  743 AEKFTPDLDVRVLdtttRKRGTAVADEVAGA--------DVVVTSYTLLRIDAGQYG-GLDWGGVVFDEAQFLKNRAAKV 813
Cdd:cd18004     78 FDKWLGLRRIKVV----TADGNAKDVKASLDffssastyPVLIISYETLRRHAEKLSkKISIDLLICDEGHRLKNSESKT 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  814 HTVARDLRAPFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETGGDP-----------ERMAALRRRV 882
Cdd:cd18004    154 TKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPdaseedkelgaERSQELSELT 233

                   ....*..
gi 1072319335  883 RPFMLRR 889
Cdd:cd18004    234 SRFILRR 240
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
675-849 4.81e-31

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: 120.89  E-value: 4.81e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPDLDVRV 754
Cdd:cd18000      1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  755 LDTT-----------TRKRGTAVADEVAG-ADVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRA 822
Cdd:cd18000     81 LHSSgsgtgseeklgSIERKSQLIRKVVGdGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRT 160
                          170       180
                   ....*....|....*....|....*..
gi 1072319335  823 PFRLAITGTPMENSLSDLWALLGVVVP 849
Cdd:cd18000    161 PHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
675-891 1.16e-30

DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4, also known as transcription activator BRG1) is a component of the CREST-BRG1 complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. Mutation of SMARCA4 (BRG1), the ATPase of BAF (mSWI/SNF) and PBAF complexes, contributes to a range of malignancies and neurologic disorders. SMARCA4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350820 [Multi-domain]  Cd Length: 251  Bit Score: 121.69  E-value: 1.16e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPD-LDVR 753
Cdd:cd18062     24 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWVYEFDKWAPSvVKVS 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  754 VLDTTTRKRGTAVADEVAGADVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARD-LRAPFRLAITGTP 832
Cdd:cd18062    104 YKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRLLLTGTP 183
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1072319335  833 MENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETGGDP------ERMAALRRR---VRPFMLRRSK 891
Cdd:cd18062    184 LQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeETILIIRRLhkvLRPFLLRRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
671-891 2.35e-30

DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (SMARCA2, also known as brahma homolog) is a component of the BAF complex. SMARCA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350821 [Multi-domain]  Cd Length: 251  Bit Score: 120.94  E-value: 2.35e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  671 LKADLRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPDL 750
Cdd:cd18063     20 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSV 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  751 DVRVLDTTTRKRGTAVADEVAGA-DVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARD-LRAPFRLAI 828
Cdd:cd18063    100 VKISYKGTPAMRRSLVPQLRSGKfNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRILL 179
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1072319335  829 TGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETGG------DPERMAALRRR---VRPFMLRRSK 891
Cdd:cd18063    180 TGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGervdlnEEETILIIRRLhkvLRPFLLRRLK 251
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
674-889 4.29e-30

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350811 [Multi-domain]  Cd Length: 237  Bit Score: 119.77  E-value: 4.29e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  674 DLRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPDLDVR 753
Cdd:cd18053     20 ELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAV 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  754 VLDTTTRKRGTAVADEVAGA-------DVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRL 826
Cdd:cd18053    100 VYLGDINSRNMIRTHEWMHPqtkrlkfNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRL 179
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072319335  827 AITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETGgdperMAALRRRVRPFMLRR 889
Cdd:cd18053    180 LITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYG-----YASLHKELEPFLLRR 237
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
675-889 6.90e-30

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: 119.01  E-value: 6.90e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPDLDVRV 754
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  755 LDTTTRKRGTAVADEVAGAD---------------------VVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKV 813
Cdd:cd18057     81 YTGDKESRSVIRENEFSFEDnairsgkkvfrmkkeaqikfhVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072319335  814 HTVARDLRAPFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPietgGDPERMAALRRRVRPFMLRR 889
Cdd:cd18057    161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADI----SKEDQIKKLHDLLGPHMLRR 232
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
675-852 1.42e-29

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: 116.33  E-value: 1.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARpERPPFLVVAPSSVVSVWAAEAEKFTPDLDVRV 754
Cdd:cd17998      1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIG-IPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  755 ----LDTTTRKRGtAVADEVAGADVVVTSYTLL---RIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRLA 827
Cdd:cd17998     80 yygsQEERKHLRY-DILKGLEDFDVIVTTYNLAtsnPDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLL 158
                          170       180
                   ....*....|....*....|....*
gi 1072319335  828 ITGTPMENSLSDLWALLGVVVPGLF 852
Cdd:cd17998    159 LTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
675-889 2.16e-28

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. CHD4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350814 [Multi-domain]  Cd Length: 232  Bit Score: 114.78  E-value: 2.16e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPDL---- 750
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMyvvt 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  751 -----DVRVL---------DTTTR--KRGTAVADEVA-GADVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKV 813
Cdd:cd18056     81 yvgdkDSRAIirenefsfeDNAIRggKKASRMKKEASvKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072319335  814 HTVARDLRAPFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETggdpERMAALRRRVRPFMLRR 889
Cdd:cd18056    161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKE----DQIKKLHDMLGPHMLRR 232
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
675-889 1.83e-27

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: 112.03  E-value: 1.83e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPDLDVRV 754
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  755 LDTTTRKRGTAVADEVAGAD---------------------VVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKV 813
Cdd:cd18055     81 YTGDKDSRAIIRENEFSFDDnavkggkkafkmkreaqvkfhVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072319335  814 HTVARDLRAPFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPietgGDPERMAALRRRVRPFMLRR 889
Cdd:cd18055    161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADI----SKEDQIKKLHDLLGPHMLRR 232
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
675-883 4.83e-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 [Multi-domain]  Cd Length: 239  Bit Score: 108.15  E-value: 4.83e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRwlaFLWEQ----------DLGGILADDMGLGKTVQTLA-LFAHARQARPER------PPFLVVApssvvs 737
Cdd:cd18007      1 LKPHQVEGVR---FLWSNlvgtdvgsdeGGGCILAHTMGLGKTLQVITfLHTYLAAAPRRSrplvlcPASTLYN------ 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  738 vWAAEAEKFTPDLDVRVLDTTTRKR-GTAVADEVAGAD------VVVTSYTLLRIDAGQYGGLDWGG------------- 797
Cdd:cd18007     72 -WEDEFKKWLPPDLRPLLVLVSLSAsKRADARLRKINKwhkeggVLLIGYELFRNLASNATTDPRLKqefiaalldpgpd 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  798 -VVFDEAQFLKNRAAKVHTVARDLRAPFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETGGDPERMA 876
Cdd:cd18007    151 lLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDSTE 230

                   ....*..
gi 1072319335  877 ALRRRVR 883
Cdd:cd18007    231 EDVRLML 237
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
675-888 5.57e-26

DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously expressed protein that contains motifs characteristic of several DNA repair proteins, transcription factors, and helicases. SHPRH is a functional homolog of S. cerevisiae RAD5 and is involved in DNA repair. SHPRH is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 108.20  E-value: 5.57e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLafLWeqdLGGILADDMGLGKTVQTLAL-FAHARQARPERPPFLVVAPSSVVSV--------------- 738
Cdd:cd18070      1 LLPYQRRAVNWM--LV---PGGILADEMGLGKTVEVLALiLLHPRPDNDLDAADDDSDEMVCCPDclvaetpvsskatli 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  739 ---------WAAEAEKFTPDlDVRVLD-TTTRKRG---TAVADEVAGADVVVTSYTLLR-----IDAGQYGG-------- 792
Cdd:cd18070     76 vcpsailaqWLDEINRHVPS-SLKVLTyQGVKKDGalaSPAPEILAEYDIVVTTYDVLRtelhyAEANRSNRrrrrqkry 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  793 ---------LDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYv 863
Cdd:cd18070    155 eappsplvlVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCDSDWWARVL- 233
                          250       260
                   ....*....|....*....|....*
gi 1072319335  864 tpIETGGDPERMAALRRRVRPFMLR 888
Cdd:cd18070    234 --IRPQGRNKAREPLAALLKELLWR 256
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
675-889 1.18e-25

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; Chromodomain-helicase-DNA-binding protein 6 (CHD6) is a DNA-dependent ATPase that plays a role in chromatin remodeling. It regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. It activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2.2 and acts as a transcriptional repressor of different viruses including influenza virus or papillomavirus. During influenza virus infection, the viral polymerase complex localizes CHD6 to inactive chromatin where it gets degraded in a proteasome independent-manner. CHD6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350816 [Multi-domain]  Cd Length: 222  Bit Score: 106.28  E-value: 1.18e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLAlFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTpDLDVRV 754
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSIT-FLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWT-EMNAIV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  755 LDTTTRKRGTAVADEVAGAD-------------VVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLR 821
Cdd:cd18058     79 YHGSQISRQMIQQYEMYYRDeqgnplsgifkfqVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072319335  822 APFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYvtpietgGD---PERMAALRRRVRPFMLRR 889
Cdd:cd18058    159 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF-------GDlktEEQVKKLQSILKPMMLRR 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
675-889 3.77e-25

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: 105.14  E-value: 3.77e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPeRPPFLVVAPSSVVSVWAAEAEKFTpDLDVRV 754
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGI-HGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  755 LDTTTRKRGTAVADE----------VAGA---DVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLR 821
Cdd:cd18060     79 YHGSLASRQMIQQYEmyckdsrgrlIPGAykfDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072319335  822 APFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYvtpietgGD---PERMAALRRRVRPFMLRR 889
Cdd:cd18060    159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF-------GDlktEEQVQKLQAILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
675-889 8.09e-25

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; Chromodomain-helicase-DNA-binding protein 7 (CHD7) is a probable transcription regulator. It may be involved in the 45S precursor rRNA production. CHD7 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350817 [Multi-domain]  Cd Length: 222  Bit Score: 103.96  E-value: 8.09e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLAlFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTpDLDVRV 754
Cdd:cd18059      1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSIT-FLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  755 LDTTTRKRGTAVADEVAGAD-------------VVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLR 821
Cdd:cd18059     79 YHGSQASRRTIQLYEMYFKDpqgrvikgsykfhAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072319335  822 APFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYvtpietgGD---PERMAALRRRVRPFMLRR 889
Cdd:cd18059    159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF-------GDlktEEQVQKLQAILKPMMLRR 222
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
675-889 1.96e-24

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: 102.67  E-value: 1.96e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRW-LAFlweqdlGG--ILADDMGLGKTVQTLALFAHARqarpERPPFLVVAPSSVVSVWAAEAEKFTPDL- 750
Cdd:cd18010      1 LLPFQREGVCFaLRR------GGrvLIADEMGLGKTVQAIAIAAYYR----EEWPLLIVCPSSLRLTWADEIERWLPSLp 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  751 --DVRVLDTTTRKRgtavadEVAGADVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDL--RAPFRL 826
Cdd:cd18010     71 pdDIQVIVKSKDGL------RDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLlkRAKRVI 144
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072319335  827 AITGTPmenSLS---DLWALLGVVVPGLFPSHRRFRETYVTPIET--GGD-------PERMAALRRRVrpfMLRR 889
Cdd:cd18010    145 LLSGTP---ALSrpiELFTQLDALDPKLFGRFHDFGRRYCAAKQGgfGWDysgssnlEELHLLLLATI---MIRR 213
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
675-889 3.44e-23

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: 99.85  E-value: 3.44e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAF---------LWEQD--------------------LGGILADDMGLGKTVQTLALFAHARQarperp 725
Cdd:cd18071      1 LLPHQKQALAWMVSrensqdlppFWEEAvglflntitnfsqkkrpelvRGGILADDMGLGKTLTTISLILANFT------ 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  726 pfLVVAPSSVVSVWAAEAEKFTPDLDVRVLDTTTRKRGTAVAdEVAGADVVVTSYTLLRIDAGQYGG-----LDWGGVVF 800
Cdd:cd18071     75 --LIVCPLSVLSNWETQFEEHVKPGQLKVYTYHGGERNRDPK-LLSKYDIVLTTYNTLASDFGAKGDsplhtINWLRVVL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  801 DEAQFLKNRAAKVHTVARDLRAPFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIeTGGDPERMAALRR 880
Cdd:cd18071    152 DEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPL-TMGDPTGLKRLQV 230

                   ....*....
gi 1072319335  881 RVRPFMLRR 889
Cdd:cd18071    231 LMKQITLRR 239
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
675-889 1.48e-22

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: 97.38  E-value: 1.48e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLAlFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTpDLDVRV 754
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSIT-FLYEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVVV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  755 LDTTTRKRGTAVADEVAGAD-------------VVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLR 821
Cdd:cd18061     79 YHGSLISRQMIQQYEMYFRDsqgriirgayrfqAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072319335  822 APFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYvtpietgGD---PERMAALRRRVRPFMLRR 889
Cdd:cd18061    159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF-------GDlktEEQVQKLQAILKPMMLRR 222
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
675-889 5.44e-22

DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as RDH54, binds to double-stranded DNA, displays ATPase activity in the presence of DNA, and may have a role in meiotic and mitotic recombination. RAD54B is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350824 [Multi-domain]  Cd Length: 235  Bit Score: 96.07  E-value: 5.44e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLrwlAFLWE--------QDLGGILADDMGLGKTVQTLALFAHA-RQ----ARPERPPFLVVAPSSVVSVWAA 741
Cdd:cd18066      1 LRPHQREGI---EFLYEcvmgmrvnERFGAILADEMGLGKTLQCISLIWTLlRQgpygGKPVIKRALIVTPGSLVKNWKK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  742 EAEKFTPDLDVRVLdttTRKRGTAVADEVAGA--DVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARD 819
Cdd:cd18066     78 EFQKWLGSERIKVF---TVDQDHKVEEFIASPlySVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTS 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  820 LRAPFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETGGDP-----------ERMAALRRRVRPFMLR 888
Cdd:cd18066    155 LSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPtatpeekklgeARAAELTRLTGLFILR 234

                   .
gi 1072319335  889 R 889
Cdd:cd18066    235 R 235
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
970-1080 5.88e-22

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 91.89  E-value: 5.88e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  970 SKLERFLDDLTEviGEGHRVIVFSQFTSFLRviAEELDHLE-IEHAYLDGST--RGRADVIRGFREGEAPVfLISLKAGG 1046
Cdd:pfam00271    1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLsqEEREEILEDFRKGKIDV-LVATDVAE 75
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1072319335 1047 FGLTLTEADYVFLMDPWWNPAAEAQAVDRAHRIG 1080
Cdd:pfam00271   76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
675-889 6.32e-22

DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as RAD54L or RAD54, plays a role in homologous recombination related repair of DNA double-strand breaks. RAD54A is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350825 [Multi-domain]  Cd Length: 243  Bit Score: 96.00  E-value: 6.32e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRwlaFLWE--------QDLGGILADDMGLGKTVQTLAL----FAHARQARPERPPFLVVAPSSVVSVWAAE 742
Cdd:cd18067      1 LRPHQREGVK---FLYRcvtgrrirGSHGCIMADEMGLGKTLQCITLmwtlLRQSPQCKPEIDKAIVVSPSSLVKNWANE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  743 AEKFT-PDLDVRVLDTTTRKRGTAVADEVAGAD-------VVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVH 814
Cdd:cd18067     78 LGKWLgGRLQPLAIDGGSKKEIDRKLVQWASQQgrrvstpVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  815 TVARDLRAPFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETGGDP-----------ERMAALRRRVR 883
Cdd:cd18067    158 QALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDAdasekerqlgeEKLQELISIVN 237

                   ....*.
gi 1072319335  884 PFMLRR 889
Cdd:cd18067    238 RCIIRR 243
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
675-870 1.20e-19

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: 88.95  E-value: 1.20e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRwlaFLWEQDLGGILADdMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFT--PDLDV 752
Cdd:cd18013      1 PHPYQKVAIN---FIIEHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARSTWPDEVEKWNhlRNLTV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  753 RVLDTTTRKRGTAVAdevAGADVVVTSYTLLRIDAGQYGGL-DWGGVVFDEAQFLKNRAAKVHTVARDLRAPFR--LAIT 829
Cdd:cd18013     77 SVAVGTERQRSKAAN---TPADLYVINRENLKWLVNKSGDPwPFDMVVIDELSSFKSPRSKRFKALRKVRPVIKrlIGLT 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1072319335  830 GTPMENSLSDLWALLGVVVPG--LFPSHRRFRETYVTPIETGG 870
Cdd:cd18013    154 GTPSPNGLMDLWAQIALLDQGerLGRSITAYRERWFDPDKRNG 196
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
675-889 3.73e-19

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: 87.92  E-value: 3.73e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRWLAFLWEQDL-GGILADDMGLGKTVQTLALFAHARQARPERPpflVVAPSSVVSVWAAEAEKFTPD---- 749
Cdd:cd18072      1 LLLHQKQALAWLLWRERQKPrGGILADDMGLGKTLTMIALILAQKNTQNRKE---EEKEKALTEWESKKDSTLVPSagtl 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  750 -----------------------LDVRVLDTTTRKRGTAVadeVAGADVVVTSYTLLRIDAGQYG---------GLDWGG 797
Cdd:cd18072     78 vvcpaslvhqwknevesrvasnkLRVCLYHGPNRERIGEV---LRDYDIVITTYSLVAKEIPTYKeesrssplfRIAWAR 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  798 VVFDEAQFLKNRAAKVHTVARDLRAPFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETGGdpERMAA 877
Cdd:cd18072    155 IILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGG--ERLNI 232
                          250
                   ....*....|..
gi 1072319335  878 LrrrVRPFMLRR 889
Cdd:cd18072    233 L---TKSLLLRR 241
HELICc smart00490
helicase superfamily c-terminal domain;
1002-1080 1.90e-17

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 78.02  E-value: 1.90e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  1002 IAEELDHLEIEHAYLDGST--RGRADVIRGFREGEApVFLISLKAGGFGLTLTEADYVFLMDPWWNPAAEAQAVDRAHRI 1079
Cdd:smart00490    3 LAELLKELGIKVARLHGGLsqEEREEILDKFNNGKI-KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRA 81

                    .
gi 1072319335  1080 G 1080
Cdd:smart00490   82 G 82
DEXDc smart00487
DEAD-like helicases superfamily;
675-857 3.46e-16

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 78.30  E-value: 3.46e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335   675 LRPYQEEGLRWLaflWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPDLDVRV 754
Cdd:smart00487    9 LRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKV 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335   755 LDTTTRKRGTAVADEVAG--ADVVVTSY-TLLR-IDAGQYGGLDWGGVVFDEAQFLKN--RAAKVHTVARDLR-APFRLA 827
Cdd:smart00487   86 VGLYGGDSKREQLRKLESgkTDILVTTPgRLLDlLENDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPkNVQLLL 165
                           170       180       190
                    ....*....|....*....|....*....|...
gi 1072319335   828 ITGTP---MENSLSDLWALLGVVVPGLFPSHRR 857
Cdd:smart00487  166 LSATPpeeIENLLELFLNDPVFIDVGFTPLEPI 198
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
675-869 4.24e-15

DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called RAD54 like 2 or RAD54L2 ) modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. ARIP4 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350827 [Multi-domain]  Cd Length: 227  Bit Score: 76.01  E-value: 4.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRwlaFLWE------------QDLGGILADDMGLGKTVQTLALFAHARQARPERPpFLVVAPSSVVSVWAAE 742
Cdd:cd18069      1 LKPHQIGGIR---FLYDniieslerykgsSGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKT-VLAIVPVNTLQNWLSE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  743 AEKFTP-----------DLDVRVLD---TTTRKRGTAVADEVAGADVVVTSYTLLRIDAGQyggldwGGVVFDEAQFLKN 808
Cdd:cd18069     77 FNKWLPppealpnvrprPFKVFILNdehKTTAARAKVIEDWVKDGGVLLMGYEMFRLRPGP------DVVICDEGHRIKN 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072319335  809 RAAKVHTVARDLRAPFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETG 869
Cdd:cd18069    151 CHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNG 211
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
675-869 1.64e-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 [Multi-domain]  Cd Length: 246  Bit Score: 71.46  E-value: 1.64e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRwlaFLWE------------QDLGGILADDMGLGKTVQTLAlFAHARQARPERPPF---LVVAPSSVVSVW 739
Cdd:cd18068      1 LKPHQVDGVQ---FMWDccceslkktkksPGSGCILAHCMGLGKTLQVVT-FLHTVLLCEKLENFsrvLVVCPLNTVLNW 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  740 AAEAEKF------TPDLDVRVLDTTTRK--RGTAVADEVAGADVVVTSYTLLRI------------------DAGQYGGL 793
Cdd:cd18068     77 LNEFEKWqeglkdEEKIEVNELATYKRPqeRSYKLQRWQEEGGVMIIGYDMYRIlaqernvksreklkeifnKALVDPGP 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072319335  794 DWggVVFDEAQFLKNRAAKVHTVARDLRAPFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIETG 869
Cdd:cd18068    157 DF--VVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNG 230
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
632-1128 1.65e-13

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 74.68  E-value: 1.65e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  632 FWEDLKELADEVDEDPEWTAAVGRLAAVERLPEAPRPAGLKADLRPYQEEGL-RWLAFLWEQDLGGILADDMGLGKTVqt 710
Cdd:COG1061     38 RRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFELRPYQQEALeALLAALERGGGRGLVVAPTGTGKTV-- 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  711 LALFAHARQARPER-----PpflvvaPSSVVSVWAAEAEKFTPDldvrVLDTTTRKRgtavadevAGADVVVTSY-TLLR 784
Cdd:COG1061    116 LALALAAELLRGKRvlvlvP------RRELLEQWAEELRRFLGD----PLAGGGKKD--------SDAPITVATYqSLAR 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  785 IDAGQYGGLDWGGVVFDEAQFLknRAAKVHTVARDLRAPFRLAITGTP--MENSLSDLWALLGVVvpglfpshrrFRETY 862
Cdd:COG1061    178 RAHLDELGDRFGLVIIDEAHHA--GAPSYRRILEAFPAAYRLGLTATPfrSDGREILLFLFDGIV----------YEYSL 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  863 vtpietggdpermaalrrrvrpfmlrrsKELVAKDLpskqeqilqveLEPAHRKLYDRVLQRERrkvlgllgdmdgNRFT 942
Cdd:COG1061    246 ----------------------------KEAIEDGY-----------LAPPEYYGIRVDLTDER------------AEYD 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  943 IFTsltllrmlalapQIVDDQYASVPSSKLERfLDDLTEVIGEGHRVIVFSQFTSFLRVIAEELDHLEIEHAYLDGST-- 1020
Cdd:COG1061    275 ALS------------ERLREALAADAERKDKI-LRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTpk 341
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335 1021 RGRADVIRGFREGEAPVfLISLKAGGFGLTLTEADYVFLMDPWWNPAAEAQAVDRAHRIGQ-ERTVMVYRLVSEGT-IEE 1098
Cdd:COG1061    342 KEREEILEAFRDGELRI-LVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPgKEDALVYDFVGNDVpVLE 420
                          490       500       510
                   ....*....|....*....|....*....|
gi 1072319335 1099 KVLELQRRKAELFGALMDESDDSGAGAFTD 1128
Cdd:COG1061    421 ELAKDLRDLAGYRVEFLDEEESEELALLIA 450
SWIM COG4715
Uncharacterized protein, contains SWIM-type Zn finger domain [Function unknown];
16-518 7.71e-10

Uncharacterized protein, contains SWIM-type Zn finger domain [Function unknown];


Pssm-ID: 443750 [Multi-domain]  Cd Length: 508  Bit Score: 62.92  E-value: 7.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335   16 EAIRAVVGPTSADRGFAVAASGAVGRLRYDAatGRLSASVQGTapSPYRVQVQLQEAYDdaaedgagalmepVGGRCTCP 95
Cdd:COG4715      9 DDIRRLAGPRIFERGREYAREGRVLDLDVED--GRLEATVQGS--EDYRVRVDLDDGGD-------------LDSSCTCP 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335   96 VGTD--CKHVAAALYQVVRLDAD-QALDDARRKLAEMV------TTADALPAPAGRGHDGGGPAGLDAPAADGAAPPPPA 166
Cdd:COG4715     72 YGGGgfCKHVVAVLLALLDQPEEgAPRQSEREALEELLerlskeELVELLLELAAEDPELRELRRALDDSGGDYLREELL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  167 GLDWRRVMEPLAGLHGPRRVGTPPALAIGVELVAESSRNAFQQWGPATAGEEQVREGRPLYVTVRPLKRGAKGT-----W 241
Cdd:COG4715    152 ELSRLAALSLTATLAALAPRSTLALRLALLRLLLLLLAPSSLDGAPPGLSLALVRELLPALAERALALLLLVPApagllK 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  242 IKGGLTWKAFQFPRAEFAPAQERAMRLIWRQVQAEDSYPGDAWFGLHVFDSPRIWQLLAEAREVGVELVPLGLLTDVVLE 321
Cdd:COG4715    232 LRLLLARPGALLLSLLDLLLRLDLLLGLLLLALLLLLLLLLQLLALLLLALRTLAALLLLLRLRLRLGLAAGLALAVLLL 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  322 APVAVGLDVTAAPDGGLDVAPSLDPAPPGPGLSGVHAVGGIGFYRVELTDEEAVLHLIPAARPVPEAVQQLVLAGGPVRV 401
Cdd:COG4715    312 LLLLLLPLPLALLALSLLLRLLLALLRLALLVLLYLLLILLLLALLLLALLLLLELLLLLALLLLLAEVELARLLEEALL 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  402 PAADREEFLGRIYPRLRGALPVTSGDASVELPEFEPPVLRLRADFRPGHELVLRWSWLYFDPPRELGLDAGGDPLRDTRH 481
Cdd:COG4715    392 IRRRLLLLLLLLLRLLDLLALLALRLLLLLLLAVLSEAEDLLLELLETLGLHRLLLLEAREELLPELAADLALLLLLEAL 471
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1072319335  482 EDAVLRAVAELWPRAGRAEEQVLEGVGAARFSEQVLP 518
Cdd:COG4715    472 DLLALEALALLLLLELLLLLAVTLLLLAIDELLLLAL 508
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
675-867 3.77e-09

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: 58.07  E-value: 3.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGLRwlAFLWEQDLGGILADDMGLGKTVQTLALfAHARQARPERPPFLVVAPSSVVSVWAAE-AEKFtpDLDVR 753
Cdd:cd18011      1 PLPHQIDAVL--RALRKPPVRLLLADEVGLGKTIEAGLI-IKELLLRGDAKRVLILCPASLVEQWQDElQDKF--GLPFL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  754 VLDTTTRKRGTAVADEVAGA-DVVVTSYTLLRIDAGQYGGL---DWGGVVFDEAQFLKNRAAKVHT----VARDL--RAP 823
Cdd:cd18011     76 ILDRETAAQLRRLIGNPFEEfPIVIVSLDLLKRSEERRGLLlseEWDLVVVDEAHKLRNSGGGKETkrykLGRLLakRAR 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1072319335  824 FRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPIE 867
Cdd:cd18011    156 HVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLRLDGLREV 199
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
675-832 9.61e-09

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 55.39  E-value: 9.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGL-RWLAFlwEQDLGGILADDMGLGKTVQTLALFAHarqaRPERPPFLVVAPSSVVSVWAAEAEKFTPDLDVR 753
Cdd:cd17926      1 LRPYQEEALeAWLAH--KNNRRGILVLPTGSGKTLTALALIAY----LKELRTLIVVPTDALLDQWKERFEDFLGDSSIG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  754 VLdtttrkrGTAVADEVAGADVVVTSYTLLRIDA--GQYGGLDWGGVVFDEAQFLKNRAAKVhtVARDLRAPFRLAITGT 831
Cdd:cd17926     75 LI-------GGGKKKDFDDANVVVATYQSLSNLAeeEKDLFDQFGLLIVDEAHHLPAKTFSE--ILKELNAKYRLGLTAT 145

                   .
gi 1072319335  832 P 832
Cdd:cd17926    146 P 146
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
969-1107 1.12e-07

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 56.28  E-value: 1.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  969 SSKLERFLDDLTEVIGE--GHRVIVFSQFTSFLRVIAEELDHLEIEHAYLDG-STRG---------RADVIRGFREGEAP 1036
Cdd:COG1111    334 HPKLSKLREILKEQLGTnpDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGqASKEgdkgltqkeQIEILERFRAGEFN 413
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072319335 1037 VfLISLKAGGFGLTLTEADYVFLMDPWWNpaaEAQAVDRAHRIGQERTVMVYRLVSEGTIEEKVLELQRRK 1107
Cdd:COG1111    414 V-LVATSVAEEGLDIPEVDLVIFYEPVPS---EIRSIQRKGRTGRKREGRVVVLIAKGTRDEAYYWSSRRK 480
COG4279 COG4279
Uncharacterized protein, contains SWIM-type Zn finger domain [Function unknown];
29-141 1.18e-07

Uncharacterized protein, contains SWIM-type Zn finger domain [Function unknown];


Pssm-ID: 443420  Cd Length: 193  Bit Score: 53.42  E-value: 1.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335   29 RGFAVAASGAVGRLryDAATGRLSASVQGTAPSPYRVQVQLQ------------------------------EAYDDAAE 78
Cdd:COG4279     33 RGRSYARNGRVLSL--KIEPGRVTARVQGSRPEPYRVSIRLPpfsdedwdrviatlagragflaallagempEEIEEAFE 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335   79 DGAGAL----MEPVGGRCTCPVGTD-CKHVAAALYQV-VRLDAD-------------QALDDAR-RKLAEMVTTADALPA 138
Cdd:COG4279    111 AAGLSLfpssPRDLRTDCSCPDWANpCKHIAAVYYLLaERLDEDpfllfqlrgrdreELLAALReRRAGGALAPAGSASE 190

                   ...
gi 1072319335  139 PAG 141
Cdd:COG4279    191 TAY 193
ResIII pfam04851
Type III restriction enzyme, res subunit;
675-832 1.59e-05

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 46.51  E-value: 1.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  675 LRPYQEEGL-RWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPDLDVR 753
Cdd:pfam04851    4 LRPYQIEAIeNLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYVEI 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  754 VLDTTTRKRgtavADEVAGADVVVTSY-TLLRIDAG---QYGGLDWGGVVFDEA---QFLKNRAAKVHtvardLRAPFRL 826
Cdd:pfam04851   84 GEIISGDKK----DESVDDNKIVVTTIqSLYKALELaslELLPDFFDVIIIDEAhrsGASSYRNILEY-----FKPAFLL 154

                   ....*.
gi 1072319335  827 AITGTP 832
Cdd:pfam04851  155 GLTATP 160
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
970-1055 8.45e-05

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase 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: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 44.16  E-value: 8.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  970 SKLERfLDDLTEVIGEGHRVIVFSQFTSFLRVIAEELDHLEIEHAYldgSTRGRADVIRGFREGEAPVFLISlKAGGFGL 1049
Cdd:cd18789     34 NKLRA-LEELLKRHEQGDKIIVFTDNVEALYRYAKRLLKPFITGET---PQSEREEILQNFREGEYNTLVVS-KVGDEGI 108

                   ....*.
gi 1072319335 1050 TLTEAD 1055
Cdd:cd18789    109 DLPEAN 114
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
1038-1082 3.38e-04

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: 40.38  E-value: 3.38e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1072319335 1038 FLISLKAGGFGLTLTEADYVFLMDPWWNPAAEAQAVDRAHRIGQE 1082
Cdd:cd18785     25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKD 69
SNF2_assoc pfam08455
Bacterial SNF2 helicase associated; This domain is found in bacterial proteins of the SWF/SNF ...
328-611 3.48e-04

Bacterial SNF2 helicase associated; This domain is found in bacterial proteins of the SWF/SNF/SWI helicase family to the N-terminus of the SNF2 family N-terminal domain (pfam00176) and together with the Helicase conserved C-terminal domain (pfam00271). The function of the domain is not clear.


Pssm-ID: 462483  Cd Length: 370  Bit Score: 44.14  E-value: 3.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  328 LDVTAAPDGGLDVAPSLDPAPPGPglSGVHAVGGIGFYRVELTDEEAV--LHLIPAARPVPEavqqlvlaggpVRVPAAD 405
Cdd:pfam08455   44 FSLKKEKDDGIILTLNKDPILLGE--DYLYFLYDGTIYRLSKEQCKLLspLLKLLNLLGTKE-----------ITISKED 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  406 REEFLGRIYPRLRGALPVTSGDASVELPEFEPPVLRLRADfRPGHELVLRWSWLY----FDPPRELGLdaggdpLRDTRH 481
Cdd:pfam08455  111 LPKFLSEVLPKLKKIGEVEIPEELLEKYVPEPLKAKFYLD-RDDDRITARVKFQYgdieFNPLEDLIL------VRDVEK 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  482 EDAVLRAVAELwPRAGRAEEQVLEGVGAA-RFSEQVLPLLQRADHVRVdvtGDRPDYRELKAAPRIEVGTK-ATQNDWFD 559
Cdd:pfam08455  184 EAKILNLLEQY-GFKVDDGKFYLDDEEKIyDFLTEGLPKLQELGEVYY---SDAFKNLKVKPSPSVSVGVSvDEEGNLLE 259
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1072319335  560 lgVQVSVDGhvLPFVEL---FTALVQGRTTLILADGSYLGLDHPAFDRLRALLSE 611
Cdd:pfam08455  260 --ISFDIDG--IDEEELaniLQALREKKKYYRLKDGSFLDLEEEELKELSELLDE 310
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
365-822 3.51e-04

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 44.85  E-value: 3.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  365 YRVELTDEEAVLHLIPA-------ARPVPEAVQQLVLaggpVRVPAADREEFLGRIYPRLRGALPVTSGDASVELPEFEP 437
Cdd:COG1020    881 FRIELGEIEAALLQHPGvreavvvAREDAPGDKRLVA----YVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLP 956
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  438 PVLRLRADFRPghelvlrwswlyfDPPRELGLDAGGDPLRDTRHEDAVLRAVAELWPRAGRAEEQVLEGVGAARFSEQVL 517
Cdd:COG1020    957 LTGNGKLDRLA-------------LPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLAL 1023
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  518 PLLQRADHVRVDVTGDRPDYRELKAAPRIEVGTKATQNDWFDLGVQVSVDGHVLPFVELFTALVQGRTTLILADGSYLGL 597
Cdd:COG1020   1024 ARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLL 1103
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  598 DHPAFDRLRALLSEAATLQEWTPEHTPVSRHQVGFWEDLKELADEVDEDPEWTAAVGRLAAVERLPEAPRPAGLKADLRP 677
Cdd:COG1020   1104 LLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLA 1183
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  678 YQEEGLRWLAFLWEQDLGGILADDMGLGKTVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPDLDVRVLDT 757
Cdd:COG1020   1184 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALA 1263
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072319335  758 TTRKRGTAVADEVAGADVVVTSYTLLRIDAGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRA 822
Cdd:COG1020   1264 LALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLAL 1328
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
476-1029 1.11e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 43.32  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  476 LRDTRHEDA-VLRAVAELWPRAGRAEEQVLEGVGAAR--------FSEQVLPLLQRADHVRVDVTGDRPDYRELKAAPRI 546
Cdd:COG3321    823 LRRGEDELAqLLTALAQLWVAGVPVDWSALYPGRGRRrvplptypFQREDAAAALLAAALAAALAAAAALGALLLAALAA 902
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  547 EVGTKATQNDWFDLGVQVSVDGHVLPFVELFTALVQGRTTLILADGSYLGLDHPAFDRLRALLSEAATLQEWTPEHTPVS 626
Cdd:COG3321    903 ALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAA 982
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  627 RHQVGFWEDLKELADEVDEDPEWTAAVGRLAAVERLPEAPRPAGLKADLRPYQEEGLRWLAFLWEQDLGGILADDMGLGK 706
Cdd:COG3321    983 AAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALA 1062
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  707 TVQTLALFAHARQARPERPPFLVVAPSSVVSVWAAEAEKFTPDLDVRVLDTTTRKRGTAVADEVAGADVVVTSYTLLRID 786
Cdd:COG3321   1063 LALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAA 1142
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  787 AGQYGGLDWGGVVFDEAQFLKNRAAKVHTVARDLRAPFRLAITGTPMENSLSDLWALLGVVVPGLFPSHRRFRETYVTPI 866
Cdd:COG3321   1143 AAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAA 1222
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  867 ETGGDPERMAALRRRVRPFMLRRSKELVAKDLPSKQEQILQVELEPAHRKLYDRVLQRERRKVLGLLGDMDGNRFTIFTS 946
Cdd:COG3321   1223 LLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALL 1302
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  947 LTLLRMLALAPQIVDDQYASVPSSKLERFLDDLTEVIGEGHRVIVFSQFTSFLRVIAEELDHLEIEHAYLDGSTRGRADV 1026
Cdd:COG3321   1303 AAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALA 1382

                   ...
gi 1072319335 1027 IRG 1029
Cdd:COG3321   1383 AAV 1385
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
970-1087 5.14e-03

C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef 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: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 38.49  E-value: 5.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072319335  970 SKLERFLDDLTEVIGEGH--RVIVFSQFTSFLRVIAEELD--------HLEIEHA---YLDG-STRGRADVIRGFREGEA 1035
Cdd:cd18801     12 EKLEEIVKEHFKKKQEGSdtRVIIFSEFRDSAEEIVNFLSkirpgiraTRFIGQAsgkSSKGmSQKEQKEVIEQFRKGGY 91
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1072319335 1036 PVfLISLKAGGFGLTLTEADYVFLMDPWWNPAAEAQAVDRAHRIGQERTVMV 1087
Cdd:cd18801     92 NV-LVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGRKRQGRVVVL 142
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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