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Conserved domains on  [gi|26346797|dbj|BAC37047|]
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unnamed protein product [Mus musculus]

Protein Classification

DEXHc_HARP_SMARCAL1 and SF2_C_SNF domain-containing protein( domain architecture ID 13725686)

protein containing domains HARP, DEXHc_HARP_SMARCAL1, and SF2_C_SNF

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 395-604 4.18e-111

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: 336.87  E-value: 4.18e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVSFAISKRGRLLLADDMGLGKTVQAICIAAFYRKEWPLLVVVPSSVRFTWEQAFLRWLPSLSPENINVVVTG 474
Cdd:cd18010   1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLPPDDIQVIVKS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 475 KGRLTAG--LVNIVSFDLL-CKLERQLKTPFKVVIIDESHFLKNIKTARCRAAVPILKVAKRVILLSGTPAMSRPAELYT 551
Cdd:cd18010  81 KDGLRDGdaKVVIVSYDLLrRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLLKRAKRVILLSGTPALSRPIELFT 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 26346797 552 QIIAVKPTFFPQFHAFGLRYCDAKRLPWGWDYSGSSNLGELKLLLEEAIMLRR 604
Cdd:cd18010 161 QLDALDPKLFGRFHDFGRRYCAAKQGGFGWDYSGSSNLEELHLLLLATIMIRR 213
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 329-768 9.61e-59

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 212.01  E-value: 9.61e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 329 RKWSFLLEEHNKLIARSRELKQVQLDPLPKTVTLAFASQLEKTSPKLKADVPEADLSGVDAKLVSSLMPFQREGVSFAIS 408
Cdd:COG0553 176 LLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLF 255

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 409 KR---GRLLLADDMGLGKTVQAICIAAFYRKE---WPLLVVVPSSVRFTWEQAFLRWLPSLSPeninVVVTGKGRLTAGL 482
Cdd:COG0553 256 LRrlgLGGLLADDMGLGKTIQALALLLELKERglaRPVLIVAPTSLVGNWQRELAKFAPGLRV----LVLDGTRERAKGA 331

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 483 -------VNIVSFDLLCKLERQLK-TPFKVVIIDESHFLKNIKTARCRAaVPILKvAKRVILLSGTPAMSRPAELYTQII 554
Cdd:COG0553 332 npfedadLVITSYGLLRRDIELLAaVDWDLVILDEAQHIKNPATKRAKA-VRALK-ARHRLALTGTPVENRLEELWSLLD 409

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 555 AVKPTFFPQFHAFGLRYCDAKRlpwgwdySGSSNLGELKLLLEEAIMLRRLKSDVLSQLPAKQRKMVVVNPG-------- 626
Cdd:COG0553 410 FLNPGLLGSLKAFRERFARPIE-------KGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTpeqralye 482

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 627 RISSRAKAALDAAAKEMTKDK-----TKQQQKEALLVFFNRTAE------AKIPCVVEYILDLLDSGrEKFLVFAHHKVI 695
Cdd:COG0553 483 AVLEYLRRELEGAEGIRRRGLilaalTRLRQICSHPALLLEEGAelsgrsAKLEALLELLEELLAEG-EKVLVFSQFTDT 561

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26346797 696 LDAVAKELERKNVQHIRIDGSTPSADREAQCQRFQLSKGHTVALLSITAANMGLTFSTADLVVFAELFWNPGV 768
Cdd:COG0553 562 LDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAV 634
HARP pfam07443
HepA-related protein (HARP); This family represents a conserved region approximately 60 ...
 214-268 2.16e-25

HepA-related protein (HARP); This family represents a conserved region approximately 60 residues long within eukaryotic HepA-related protein (HARP). This exhibits single-stranded DNA-dependent ATPase activity, and is ubiquitously expressed in human and mouse tissues. Family members may contain more than one copy of this region.


:

Pssm-ID: 462166  Cd Length: 55  Bit Score: 99.16  E-value: 2.16e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 26346797   214 FRVKIGYNQELIAVFKSLPSRHYDSFTKTWDFSMSDYRALMKAVERLSTVSLKPL 268
Cdd:pfam07443   1 FEVEIGYHAELIAVFKQMPSRNYDPKTKKWNFSLEDYSKLMEAARALPQVELEPL 55
 
Name Accession Description Interval E-value
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 395-604 4.18e-111

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: 336.87  E-value: 4.18e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVSFAISKRGRLLLADDMGLGKTVQAICIAAFYRKEWPLLVVVPSSVRFTWEQAFLRWLPSLSPENINVVVTG 474
Cdd:cd18010   1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLPPDDIQVIVKS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 475 KGRLTAG--LVNIVSFDLL-CKLERQLKTPFKVVIIDESHFLKNIKTARCRAAVPILKVAKRVILLSGTPAMSRPAELYT 551
Cdd:cd18010  81 KDGLRDGdaKVVIVSYDLLrRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLLKRAKRVILLSGTPALSRPIELFT 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 26346797 552 QIIAVKPTFFPQFHAFGLRYCDAKRLPWGWDYSGSSNLGELKLLLEEAIMLRR 604
Cdd:cd18010 161 QLDALDPKLFGRFHDFGRRYCAAKQGGFGWDYSGSSNLEELHLLLLATIMIRR 213
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 329-768 9.61e-59

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 212.01  E-value: 9.61e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 329 RKWSFLLEEHNKLIARSRELKQVQLDPLPKTVTLAFASQLEKTSPKLKADVPEADLSGVDAKLVSSLMPFQREGVSFAIS 408
Cdd:COG0553 176 LLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLF 255

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 409 KR---GRLLLADDMGLGKTVQAICIAAFYRKE---WPLLVVVPSSVRFTWEQAFLRWLPSLSPeninVVVTGKGRLTAGL 482
Cdd:COG0553 256 LRrlgLGGLLADDMGLGKTIQALALLLELKERglaRPVLIVAPTSLVGNWQRELAKFAPGLRV----LVLDGTRERAKGA 331

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 483 -------VNIVSFDLLCKLERQLK-TPFKVVIIDESHFLKNIKTARCRAaVPILKvAKRVILLSGTPAMSRPAELYTQII 554
Cdd:COG0553 332 npfedadLVITSYGLLRRDIELLAaVDWDLVILDEAQHIKNPATKRAKA-VRALK-ARHRLALTGTPVENRLEELWSLLD 409

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 555 AVKPTFFPQFHAFGLRYCDAKRlpwgwdySGSSNLGELKLLLEEAIMLRRLKSDVLSQLPAKQRKMVVVNPG-------- 626
Cdd:COG0553 410 FLNPGLLGSLKAFRERFARPIE-------KGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTpeqralye 482

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 627 RISSRAKAALDAAAKEMTKDK-----TKQQQKEALLVFFNRTAE------AKIPCVVEYILDLLDSGrEKFLVFAHHKVI 695
Cdd:COG0553 483 AVLEYLRRELEGAEGIRRRGLilaalTRLRQICSHPALLLEEGAelsgrsAKLEALLELLEELLAEG-EKVLVFSQFTDT 561

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26346797 696 LDAVAKELERKNVQHIRIDGSTPSADREAQCQRFQLSKGHTVALLSITAANMGLTFSTADLVVFAELFWNPGV 768
Cdd:COG0553 562 LDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAV 634
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 666-768 2.35e-30

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: 116.42  E-value: 2.35e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 666 AKIPCVVEYILDLLDSGrEKFLVFAHHKVILDAVAKELERKNVQHIRIDGSTPSADREAQCQRFQLSKGHTVALLSITAA 745
Cdd:cd18793  11 GKLEALLELLEELREPG-EKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89

                        90       100
                ....*....|....*....|...
gi 26346797 746 NMGLTFSTADLVVFAELFWNPGV 768
Cdd:cd18793  90 GVGLNLTAANRVILYDPWWNPAV 112
HARP pfam07443
HepA-related protein (HARP); This family represents a conserved region approximately 60 ...
 214-268 2.16e-25

HepA-related protein (HARP); This family represents a conserved region approximately 60 residues long within eukaryotic HepA-related protein (HARP). This exhibits single-stranded DNA-dependent ATPase activity, and is ubiquitously expressed in human and mouse tissues. Family members may contain more than one copy of this region.


Pssm-ID: 462166  Cd Length: 55  Bit Score: 99.16  E-value: 2.16e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 26346797   214 FRVKIGYNQELIAVFKSLPSRHYDSFTKTWDFSMSDYRALMKAVERLSTVSLKPL 268
Cdd:pfam07443   1 FEVEIGYHAELIAVFKQMPSRNYDPKTKKWNFSLEDYSKLMEAARALPQVELEPL 55
HARP pfam07443
HepA-related protein (HARP); This family represents a conserved region approximately 60 ...
 302-356 7.55e-24

HepA-related protein (HARP); This family represents a conserved region approximately 60 residues long within eukaryotic HepA-related protein (HARP). This exhibits single-stranded DNA-dependent ATPase activity, and is ubiquitously expressed in human and mouse tissues. Family members may contain more than one copy of this region.


Pssm-ID: 462166  Cd Length: 55  Bit Score: 94.93  E-value: 7.55e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 26346797   302 FEVDIGYSEAVIGLFKQMESRSYDIKTRKWSFLLEEHNKLIARSRELKQVQLDPL 356
Cdd:pfam07443   1 FEVEIGYHAELIAVFKQMPSRNYDPKTKKWNFSLEDYSKLMEAARALPQVELEPL 55
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 399-625 2.56e-22

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: 97.75  E-value: 2.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797   399 QREGVSFAIS---KRGR-LLLADDMGLGKTVQAICIAAF---YRKEW--PLLVVVPSSVRFTWEQAFLRWlpsLSPENIN 469
Cdd:pfam00176   2 QIEGVNWMLSlenNLGRgGILADEMGLGKTLQTISLLLYlkhVDKNWggPTLIVVPLSLLHNWMNEFERW---VSPPALR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797   470 VVV-TGKGRLTAGL-----------VNIVSFDLLCKLERQL-KTPFKVVIIDESHFLKNIKtARCRAAVPILKVAKRvIL 536
Cdd:pfam00176  79 VVVlHGNKRPQERWkndpnfladfdVVITTYETLRKHKELLkKVHWHRIVLDEGHRLKNSK-SKLSKALKSLKTRNR-WI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797   537 LSGTPAMSRPAELYTQIIAVKP-------TFFPQFHAFGLRYCDAKRLpwgwdysgssnlgELKLLLEEAIMLRRLKSDV 609
Cdd:pfam00176 157 LTGTPLQNNLEELWALLNFLRPgpfgslsTFRNWFDRPIERGGGKKGV-------------SRLHKLLKPFLLRRTKKDV 223

                         250
                  ....*....|....*.
gi 26346797   610 LSQLPAKQRKMVVVNP 625
Cdd:pfam00176 224 EKSLPPKVEYILFCRL 239
DEXDc smart00487
DEAD-like helicases superfamily;
387-541 4.50e-17

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 80.23  E-value: 4.50e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797    387 VDAKLVSSLMPFQREGVSFAISKRGRLLLADDMGLGKTVQA---ICIAAFYRKEWPLLVVVP-SSVRFTWEQAFLRWLPS 462
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAAllpALEALKRGKGGRVLVLVPtRELAEQWAEELKKLGPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797    463 LSPENINVVVTGKGR-----LTAGLVNIV-----SFDLLCKLERQLKTPFKVVIIDESHFLKNIK-TARCRAAVPILKVA 531
Cdd:smart00487  81 LGLKVVGLYGGDSKReqlrkLESGKTDILvttpgRLLDLLENDKLSLSNVDLVILDEAHRLLDGGfGDQLEKLLKLLPKN 160

                          170
                   ....*....|
gi 26346797    532 KRVILLSGTP 541
Cdd:smart00487 161 VQLLLLSATP 170
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 414-768 8.19e-17

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 85.24  E-value: 8.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797   414 LLADDMGLGKTVQAICIAAF---YRK-EWPLLVVVPSSVRFTWEQAFLRWLPSLSP------------ENINVVVTGKGR 477
Cdd:PLN03142  192 ILADEMGLGKTLQTISLLGYlheYRGiTGPHMVVAPKSTLGNWMNEIRRFCPVLRAvkfhgnpeerahQREELLVAGKFD 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797   478 ltaglVNIVSFDLLCKLERQLKT-PFKVVIIDESHFLKNiKTARCRAAVPILKVAKRvILLSGTPAMSRPAELYTQIIAV 556
Cdd:PLN03142  272 -----VCVTSFEMAIKEKTALKRfSWRYIIIDEAHRIKN-ENSLLSKTMRLFSTNYR-LLITGTPLQNNLHELWALLNFL 344

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797   557 KPTFFPQFHAFGlrycdakrlpwGWDYSGSSNLGELKLLLEEAI----MLRRLKSDVLSQLPAK---------------- 616
Cdd:PLN03142  345 LPEIFSSAETFD-----------EWFQISGENDQQEVVQQLHKVlrpfLLRRLKSDVEKGLPPKketilkvgmsqmqkqy 413

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797   617 -----QRKMVVVNPGRISSRAKaaldaaakemtkDKTKQQQKEALLVFFNRTAEAKIPC-----VVE-----YILD-LLD 680
Cdd:PLN03142  414 ykallQKDLDVVNAGGERKRLL------------NIAMQLRKCCNHPYLFQGAEPGPPYttgehLVEnsgkmVLLDkLLP 481

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797   681 SGREK---FLVFAHHKVILDAVAKELERKNVQHIRIDGSTPSADREAQCQRFQLSKGHT-VALLSITAANMGLTFSTADL 756
Cdd:PLN03142  482 KLKERdsrVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATADI 561

                         410
                  ....*....|..
gi 26346797   757 VVFAELFWNPGV 768
Cdd:PLN03142  562 VILYDSDWNPQV 573
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
394-760 4.62e-12

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 69.28  E-value: 4.62e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 394 SLMPFQREGV----SFAISKRGRLLLADDMGLGKTVQAICIAAFYRKEWPLLVVVPS-SVRFTWEQAFLRWLPslspeni 468
Cdd:COG1061  80 ELRPYQQEALeallAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRVLVLVPRrELLEQWAEELRRFLG------- 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 469 NVVVTGKGRLTAGLVNIVSFDLLCKLE--RQLKTPFKVVIIDESHflkNIKTARCRAAVPILKvAKRVILLSGTP----A 542
Cdd:COG1061 153 DPLAGGGKKDSDAPITVATYQSLARRAhlDELGDRFGLVIIDEAH---HAGAPSYRRILEAFP-AAYRLGLTATPfrsdG 228

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 543 MSRPAELYTQIIavkptffpqfhaFGLRYCDAkrlpwgwdysgssnlgelkllleeaimlrrLKSDVLSQLpakqrkMVV 622
Cdd:COG1061 229 REILLFLFDGIV------------YEYSLKEA------------------------------IEDGYLAPP------EYY 260

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 623 VNPGRISSRakaaldaaakEMTKDKTKQQQKEALLvffnRTAEAKIPCVVEYILDLLDsgREKFLVFAHHKVILDAVAKE 702
Cdd:COG1061 261 GIRVDLTDE----------RAEYDALSERLREALA----ADAERKDKILRELLREHPD--DRKTLVFCSSVDHAEALAEL 324

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 26346797 703 LERKNVQHIRIDGSTPSADREAQCQRFqlSKGHTVALLSITAANMGLTFSTADLVVFA 760
Cdd:COG1061 325 LNEAGIRAAVVTGDTPKKEREEILEAF--RDGELRILVTVDVLNEGVDVPRLDVAILL 380
HELICc smart00490
helicase superfamily c-terminal domain;
697-766 1.51e-10

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 57.99  E-value: 1.51e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797    697 DAVAKELERKNVQHIRIDGSTPSADREAQCQRFQlsKGHTVALLSITAANMGLTFSTADLVVFAELFWNP 766
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFN--NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSP 68
 
Name Accession Description Interval E-value
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 395-604 4.18e-111

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: 336.87  E-value: 4.18e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVSFAISKRGRLLLADDMGLGKTVQAICIAAFYRKEWPLLVVVPSSVRFTWEQAFLRWLPSLSPENINVVVTG 474
Cdd:cd18010   1 LLPFQREGVCFALRRGGRVLIADEMGLGKTVQAIAIAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLPPDDIQVIVKS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 475 KGRLTAG--LVNIVSFDLL-CKLERQLKTPFKVVIIDESHFLKNIKTARCRAAVPILKVAKRVILLSGTPAMSRPAELYT 551
Cdd:cd18010  81 KDGLRDGdaKVVIVSYDLLrRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLLKRAKRVILLSGTPALSRPIELFT 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 26346797 552 QIIAVKPTFFPQFHAFGLRYCDAKRLPWGWDYSGSSNLGELKLLLEEAIMLRR 604
Cdd:cd18010 161 QLDALDPKLFGRFHDFGRRYCAAKQGGFGWDYSGSSNLEELHLLLLATIMIRR 213
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 329-768 9.61e-59

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 212.01  E-value: 9.61e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 329 RKWSFLLEEHNKLIARSRELKQVQLDPLPKTVTLAFASQLEKTSPKLKADVPEADLSGVDAKLVSSLMPFQREGVSFAIS 408
Cdd:COG0553 176 LLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLF 255

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 409 KR---GRLLLADDMGLGKTVQAICIAAFYRKE---WPLLVVVPSSVRFTWEQAFLRWLPSLSPeninVVVTGKGRLTAGL 482
Cdd:COG0553 256 LRrlgLGGLLADDMGLGKTIQALALLLELKERglaRPVLIVAPTSLVGNWQRELAKFAPGLRV----LVLDGTRERAKGA 331

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 483 -------VNIVSFDLLCKLERQLK-TPFKVVIIDESHFLKNIKTARCRAaVPILKvAKRVILLSGTPAMSRPAELYTQII 554
Cdd:COG0553 332 npfedadLVITSYGLLRRDIELLAaVDWDLVILDEAQHIKNPATKRAKA-VRALK-ARHRLALTGTPVENRLEELWSLLD 409

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 555 AVKPTFFPQFHAFGLRYCDAKRlpwgwdySGSSNLGELKLLLEEAIMLRRLKSDVLSQLPAKQRKMVVVNPG-------- 626
Cdd:COG0553 410 FLNPGLLGSLKAFRERFARPIE-------KGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTpeqralye 482

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 627 RISSRAKAALDAAAKEMTKDK-----TKQQQKEALLVFFNRTAE------AKIPCVVEYILDLLDSGrEKFLVFAHHKVI 695
Cdd:COG0553 483 AVLEYLRRELEGAEGIRRRGLilaalTRLRQICSHPALLLEEGAelsgrsAKLEALLELLEELLAEG-EKVLVFSQFTDT 561

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26346797 696 LDAVAKELERKNVQHIRIDGSTPSADREAQCQRFQLSKGHTVALLSITAANMGLTFSTADLVVFAELFWNPGV 768
Cdd:COG0553 562 LDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAV 634
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
 395-561 1.02e-43

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: 155.80  E-value: 1.02e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVSFAIS---KRGRLLLADDMGLGKTVQAICIAAFYRKE----WPLLVVVPSSVRFTWEQAFLRWLPSLSPen 467
Cdd:cd17919   1 LRPYQLEGLNFLLElyeNGPGGILADEMGLGKTLQAIAFLAYLLKEgkerGPVLVVCPLSVLENWEREFEKWTPDLRV-- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 468 inVVVTG----------KGRLTAGLVNIVSFDLLCKLERQL-KTPFKVVIIDESHFLKNIKTARCRAAVPILkvAKRVIL 536
Cdd:cd17919  79 --VVYHGsqreraqiraKEKLDKFDVVLTTYETLRRDKASLrKFRWDLVVVDEAHRLKNPKSQLSKALKALR--AKRRLL 154

                       170       180
                ....*....|....*....|....*
gi 26346797 537 LSGTPAMSRPAELYTQIIAVKPTFF 561
Cdd:cd17919 155 LTGTPLQNNLEELWALLDFLDPPFL 179
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 666-768 2.35e-30

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: 116.42  E-value: 2.35e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 666 AKIPCVVEYILDLLDSGrEKFLVFAHHKVILDAVAKELERKNVQHIRIDGSTPSADREAQCQRFQLSKGHTVALLSITAA 745
Cdd:cd18793  11 GKLEALLELLEELREPG-EKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKAG 89

                        90       100
                ....*....|....*....|...
gi 26346797 746 NMGLTFSTADLVVFAELFWNPGV 768
Cdd:cd18793  90 GVGLNLTAANRVILYDPWWNPAV 112
HARP pfam07443
HepA-related protein (HARP); This family represents a conserved region approximately 60 ...
 214-268 2.16e-25

HepA-related protein (HARP); This family represents a conserved region approximately 60 residues long within eukaryotic HepA-related protein (HARP). This exhibits single-stranded DNA-dependent ATPase activity, and is ubiquitously expressed in human and mouse tissues. Family members may contain more than one copy of this region.


Pssm-ID: 462166  Cd Length: 55  Bit Score: 99.16  E-value: 2.16e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 26346797   214 FRVKIGYNQELIAVFKSLPSRHYDSFTKTWDFSMSDYRALMKAVERLSTVSLKPL 268
Cdd:pfam07443   1 FEVEIGYHAELIAVFKQMPSRNYDPKTKKWNFSLEDYSKLMEAARALPQVELEPL 55
HARP pfam07443
HepA-related protein (HARP); This family represents a conserved region approximately 60 ...
 302-356 7.55e-24

HepA-related protein (HARP); This family represents a conserved region approximately 60 residues long within eukaryotic HepA-related protein (HARP). This exhibits single-stranded DNA-dependent ATPase activity, and is ubiquitously expressed in human and mouse tissues. Family members may contain more than one copy of this region.


Pssm-ID: 462166  Cd Length: 55  Bit Score: 94.93  E-value: 7.55e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 26346797   302 FEVDIGYSEAVIGLFKQMESRSYDIKTRKWSFLLEEHNKLIARSRELKQVQLDPL 356
Cdd:pfam07443   1 FEVEIGYHAELIAVFKQMPSRNYDPKTKKWNFSLEDYSKLMEAARALPQVELEPL 55
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
 391-571 2.08e-23

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: 99.18  E-value: 2.08e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 391 LVSSLMPFQREGVSFaISKRGRL----LLADDMGLGKTVQAIC-IAAFYRKEW--PLLVVVPSSVRFTWEQAFLRWLPSL 463
Cdd:cd18012   1 LKATLRPYQKEGFNW-LSFLRHYglggILADDMGLGKTLQTLAlLLSRKEEGRkgPSLVVAPTSLIYNWEEEAAKFAPEL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 464 SPeninVVVTGKGR-------LTAGLVNIVSFDLLCKLERQLKT-PFKVVIIDESHFLKNIKTARCRaAVPILKVAKRvI 535
Cdd:cd18012  80 KV----LVIHGTKRkreklraLEDYDLVITSYGLLRRDIELLKEvKFHYLVLDEAQNIKNPQTKTAK-AVKALKADHR-L 153

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 26346797 536 LLSGTPAMSRPAELYTQIIAVKPTFFPQFHAFGLRY 571
Cdd:cd18012 154 ALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRF 189
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
 395-561 6.87e-23

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: 97.36  E-value: 6.87e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVSFAISK-RGRLLLADDMGLGKTVQAICIAAFYRKEW---PLLVVVPSSVRFTWEQ----AFLRWLPSLSPE 466
Cdd:cd18011   1 PLPHQIDAVLRALRKpPVRLLLADEVGLGKTIEAGLIIKELLLRGdakRVLILCPASLVEQWQDelqdKFGLPFLILDRE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 467 NINVVVTGKGR-LTAGLVNIVSFDLLCKLERQ----LKTPFKVVIIDESHFLKN----IKTARCRAAVPILKVAKRVILL 537
Cdd:cd18011  81 TAAQLRRLIGNpFEEFPIVIVSLDLLKRSEERrgllLSEEWDLVVVDEAHKLRNsgggKETKRYKLGRLLAKRARHVLLL 160

                       170       180
                ....*....|....*....|....
gi 26346797 538 SGTPAMSRPAELYTQIIAVKPTFF 561
Cdd:cd18011 161 TATPHNGKEEDFRALLSLLDPGRF 184
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 399-625 2.56e-22

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: 97.75  E-value: 2.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797   399 QREGVSFAIS---KRGR-LLLADDMGLGKTVQAICIAAF---YRKEW--PLLVVVPSSVRFTWEQAFLRWlpsLSPENIN 469
Cdd:pfam00176   2 QIEGVNWMLSlenNLGRgGILADEMGLGKTLQTISLLLYlkhVDKNWggPTLIVVPLSLLHNWMNEFERW---VSPPALR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797   470 VVV-TGKGRLTAGL-----------VNIVSFDLLCKLERQL-KTPFKVVIIDESHFLKNIKtARCRAAVPILKVAKRvIL 536
Cdd:pfam00176  79 VVVlHGNKRPQERWkndpnfladfdVVITTYETLRKHKELLkKVHWHRIVLDEGHRLKNSK-SKLSKALKSLKTRNR-WI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797   537 LSGTPAMSRPAELYTQIIAVKP-------TFFPQFHAFGLRYCDAKRLpwgwdysgssnlgELKLLLEEAIMLRRLKSDV 609
Cdd:pfam00176 157 LTGTPLQNNLEELWALLNFLRPgpfgslsTFRNWFDRPIERGGGKKGV-------------SRLHKLLKPFLLRRTKKDV 223

                         250
                  ....*....|....*.
gi 26346797   610 LSQLPAKQRKMVVVNP 625
Cdd:pfam00176 224 EKSLPPKVEYILFCRL 239
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
 395-571 6.33e-21

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: 92.73  E-value: 6.33e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVSF--------AISKRGRLLLADDMGLGKTVQAICIAafyrkeWPLL--------------VVVPSSVRFTW 452
Cdd:cd18004   1 LRPHQREGVQFlydcltgrRGYGGGGAILADEMGLGKTLQAIALV------WTLLkqgpygkptakkalIVCPSSLVGNW 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 453 EQAFLRWLP-------SLSPENINVVVTGKGRLTAGL--VNIVSFDLLCKLERQLKTP--FKVVIIDESHFLKN--IKTA 519
Cdd:cd18004  75 KAEFDKWLGlrrikvvTADGNAKDVKASLDFFSSASTypVLIISYETLRRHAEKLSKKisIDLLICDEGHRLKNseSKTT 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 26346797 520 RcraAVPILKVAKRvILLSGTPAMSRPAELYTQIIAVKPTFFPQFHAFGLRY 571
Cdd:cd18004 155 K---ALNSLPCRRR-LLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVF 202
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
 395-567 2.89e-19

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: 87.41  E-value: 2.89e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVSFAIS---KRGRLLLADDMGLGKTVQAICIAAF---YRKEW-PLLVVVPSSVRFTWEQAFLRWLPSL---- 463
Cdd:cd18003   1 LREYQHIGLDWLATlyeKNLNGILADEMGLGKTIQTIALLAHlacEKGNWgPHLIVVPTSVMLNWEMEFKRWCPGFkilt 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 464 ---SPENINVVVTGKGRLTAGLVNIVSFDLLCKLERQLK-TPFKVVIIDESHFLKNIKTARCRAavpILKV-AKRVILLS 538
Cdd:cd18003  81 yygSAKERKLKRQGWMKPNSFHVCITSYQLVVQDHQVFKrKKWKYLILDEAHNIKNFKSQRWQT---LLNFnTQRRLLLT 157

                       170       180
                ....*....|....*....|....*....
gi 26346797 539 GTPAMSRPAELYTQIIAVKPTFFPQFHAF 567
Cdd:cd18003 158 GTPLQNSLMELWSLMHFLMPHIFQSHQEF 186
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
 395-604 2.75e-18

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: 85.03  E-value: 2.75e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVSFAISKRGrlLLADDMGLGKTVQAI-CIAA------FYRKEWPL--------------LVVVPSSVRFTWE 453
Cdd:cd18008   1 LLPYQKQGLAWMLPRGG--ILADEMGLGKTIQALaLILAtrpqdpKIPEELEEnssdpkklylskttLIVVPLSLLSQWK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 454 Q--------AFLRWL---------PSLSPENINVVVTGKGRLTAGLVNIVSFDLLCKLERQ----LKTPFKVVIIDESHF 512
Cdd:cd18008  79 DeiekhtkpGSLKVYvyhgskrikSIEELSDYDIVITTYGTLASEFPKNKKGGGRDSKEKEasplHRIRWYRVILDEAHN 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 513 LKNIKTARCRAAVPIlkVAKRVILLSGTPAMSRPAELYTQIIavkptfFPQFHAFGLRYCDAKRLPWGWDYsGSSNLGEL 592
Cdd:cd18008 159 IKNRSTKTSRAVCAL--KAERRWCLTGTPIQNSLDDLYSLLR------FLRVEPFGDYPWFNSDISKPFSK-NDRKALER 229

                       250
                ....*....|..
gi 26346797 593 KLLLEEAIMLRR 604
Cdd:cd18008 230 LQALLKPILLRR 241
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
 395-561 3.57e-18

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: 84.65  E-value: 3.57e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVSF-----AISKRGR-----LLLADDMGLGKTVQAICI-----AAFYRKEWPLlVVVPSSVRFTWEQAFLRW 459
Cdd:cd18007   1 LKPHQVEGVRFlwsnlVGTDVGSdegggCILAHTMGLGKTLQVITFlhtylAAAPRRSRPL-VLCPASTLYNWEDEFKKW 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 460 LPSLSPENINVVV-----TGKGRLTA-------GLVNIVSFDLLCKL----------------ERQLKTPfKVVIIDESH 511
Cdd:cd18007  80 LPPDLRPLLVLVSlsaskRADARLRKinkwhkeGGVLLIGYELFRNLasnattdprlkqefiaALLDPGP-DLLVLDEGH 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 26346797 512 FLKNIKTARCRAavpILKV-AKRVILLSGTPAMSRPAELYTQIIAVKPTFF 561
Cdd:cd18007 159 RLKNEKSQLSKA---LSKVkTKRRILLTGTPLQNNLKEYWTMVDFARPKYL 206
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
 395-575 7.57e-18

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: 83.07  E-value: 7.57e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVSFAIS----KRGrLLLADDMGLGKTVQAIC----IAAFYRKEWPLLVVVPSSVRFTWEQAFLRWlpslspE 466
Cdd:cd17995   1 LRDYQLEGVNWLLFnwynRRN-CILADEMGLGKTIQSIAflehLYQVEGIRGPFLVIAPLSTIPNWQREFETW------T 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 467 NINVVV---TGKGRLTA-------------GLVNIVSFDLL--------CKLERQLKTPFKVVIIDESHFLKNiktARCR 522
Cdd:cd17995  74 DMNVVVyhgSGESRQIIqqyemyfkdaqgrKKKGVYKFDVLittyemviADAEELRKIPWRVVVVDEAHRLKN---RNSK 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 26346797 523 AAVPILKVAK-RVILLSGTPAMSRPAELYTQIIAVKPTFFPQFHAFGLRYCDAK 575
Cdd:cd17995 151 LLQGLKKLTLeHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLK 204
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
 395-550 1.54e-17

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: 82.40  E-value: 1.54e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVSF-AISKRGRL--LLADDMGLGKTVQAICIAA---FYRKEW------PLLVVVPSSVRFTWEQAFLRWLP- 461
Cdd:cd17999   1 LRPYQQEGINWlAFLNKYNLhgILCDDMGLGKTLQTLCILAsdhHKRANSfnsenlPSLVVCPPTLVGHWVAEIKKYFPn 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 462 -SLSPENINVVVTGKGRLTAGLVN----IVSFDLLCK-LERQLKTPFKVVIIDESHFLKNIKTaRCRAAVPILKVAKRVI 535
Cdd:cd17999  81 aFLKPLAYVGPPQERRRLREQGEKhnviVASYDVLRNdIEVLTKIEWNYCVLDEGHIIKNSKT-KLSKAVKQLKANHRLI 159

                       170
                ....*....|....*
gi 26346797 536 lLSGTPAMSRPAELY 550
Cdd:cd17999 160 -LSGTPIQNNVLELW 173
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
 395-561 1.69e-17

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: 81.28  E-value: 1.69e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVSFAI---SKRGRLLLADDMGLGKTVQAICIAAfYRKE----WPLLVVVPSSVRFTWEQAFLRWLPSLSPE- 466
Cdd:cd17998   1 LKDYQLIGLNWLNllyQKKLSGILADEMGLGKTIQVIAFLA-YLKEigipGPHLVVVPSSTLDNWLREFKRWCPSLKVEp 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 467 --------------------NINVVVTgkgrlTAGLVNIVSFDLlcKLERQLKtpFKVVIIDESHFLKNIKTARCRAAVP 526
Cdd:cd17998  80 yygsqeerkhlrydilkgleDFDVIVT-----TYNLATSNPDDR--SFFKRLK--LNYVVYDEGHMLKNMTSERYRHLMT 150

                       170       180       190
                ....*....|....*....|....*....|....*
gi 26346797 527 IlKVAKRvILLSGTPAMSRPAELYTQIIAVKPTFF 561
Cdd:cd17998 151 I-NANFR-LLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXDc smart00487
DEAD-like helicases superfamily;
387-541 4.50e-17

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 80.23  E-value: 4.50e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797    387 VDAKLVSSLMPFQREGVSFAISKRGRLLLADDMGLGKTVQA---ICIAAFYRKEWPLLVVVP-SSVRFTWEQAFLRWLPS 462
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLRDVILAAPTGSGKTLAAllpALEALKRGKGGRVLVLVPtRELAEQWAEELKKLGPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797    463 LSPENINVVVTGKGR-----LTAGLVNIV-----SFDLLCKLERQLKTPFKVVIIDESHFLKNIK-TARCRAAVPILKVA 531
Cdd:smart00487  81 LGLKVVGLYGGDSKReqlrkLESGKTDILvttpgRLLDLLENDKLSLSNVDLVILDEAHRLLDGGfGDQLEKLLKLLPKN 160

                          170
                   ....*....|
gi 26346797    532 KRVILLSGTP 541
Cdd:smart00487 161 VQLLLLSATP 170
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
 395-540 7.89e-17

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: 80.89  E-value: 7.89e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVSFA----ISKRGrLLLADDMGLGKTVQAIC-IAAFYRKEW-----------------------PLLVVVPS 446
Cdd:cd18005   1 LRDYQREGVEFMydlyKNGRG-GILGDDMGLGKTVQVIAfLAAVLGKTGtrrdrennrprfkkkppassakkPVLIVAPL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 447 SVRFTWEQAFLRWlPSLSPEninvVVTGKG-------RLTAGLVNIV--SFDLL-CKLERQLKTPFKVVIIDESHFLKNI 516
Cdd:cd18005  80 SVLYNWKDELDTW-GHFEVG----VYHGSRkddelegRLKAGRLEVVvtTYDTLrRCIDSLNSINWSAVIADEAHRIKNP 154

                       170       180
                ....*....|....*....|....
gi 26346797 517 KTARCRAAVPIlkVAKRVILLSGT 540
Cdd:cd18005 155 KSKLTQAMKEL--KCKVRIGLTGT 176
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 414-768 8.19e-17

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 85.24  E-value: 8.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797   414 LLADDMGLGKTVQAICIAAF---YRK-EWPLLVVVPSSVRFTWEQAFLRWLPSLSP------------ENINVVVTGKGR 477
Cdd:PLN03142  192 ILADEMGLGKTLQTISLLGYlheYRGiTGPHMVVAPKSTLGNWMNEIRRFCPVLRAvkfhgnpeerahQREELLVAGKFD 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797   478 ltaglVNIVSFDLLCKLERQLKT-PFKVVIIDESHFLKNiKTARCRAAVPILKVAKRvILLSGTPAMSRPAELYTQIIAV 556
Cdd:PLN03142  272 -----VCVTSFEMAIKEKTALKRfSWRYIIIDEAHRIKN-ENSLLSKTMRLFSTNYR-LLITGTPLQNNLHELWALLNFL 344

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797   557 KPTFFPQFHAFGlrycdakrlpwGWDYSGSSNLGELKLLLEEAI----MLRRLKSDVLSQLPAK---------------- 616
Cdd:PLN03142  345 LPEIFSSAETFD-----------EWFQISGENDQQEVVQQLHKVlrpfLLRRLKSDVEKGLPPKketilkvgmsqmqkqy 413

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797   617 -----QRKMVVVNPGRISSRAKaaldaaakemtkDKTKQQQKEALLVFFNRTAEAKIPC-----VVE-----YILD-LLD 680
Cdd:PLN03142  414 ykallQKDLDVVNAGGERKRLL------------NIAMQLRKCCNHPYLFQGAEPGPPYttgehLVEnsgkmVLLDkLLP 481

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797   681 SGREK---FLVFAHHKVILDAVAKELERKNVQHIRIDGSTPSADREAQCQRFQLSKGHT-VALLSITAANMGLTFSTADL 756
Cdd:PLN03142  482 KLKERdsrVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKfVFLLSTRAGGLGINLATADI 561

                         410
                  ....*....|..
gi 26346797   757 VVFAELFWNPGV 768
Cdd:PLN03142  562 VILYDSDWNPQV 573
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
 395-550 1.21e-16

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: 79.72  E-value: 1.21e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVSFAIS----KRGRLLlADDMGLGKTVQAIC-IAAFYRKEW--PLLVVVPSSVRFTWEQAFLRWLPslspeN 467
Cdd:cd18001   1 LYPHQREGVAWLWSlhdgGKGGIL-ADDMGLGKTVQICAfLSGMFDSGLikSVLVVMPTSLIPHWVKEFAKWTP-----G 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 468 INVVV----TGKGR-------LTAGLVNIVSFDLLCKLERQLKTPFK------VVIIDESHFLKNIKT--ARCRAAVPil 528
Cdd:cd18001  75 LRVKVfhgtSKKERernleriQRGGGVLLTTYGMVLSNTEQLSADDHdefkwdYVILDEGHKIKNSKTksAKSLREIP-- 152

                       170       180
                ....*....|....*....|..
gi 26346797 529 kvAKRVILLSGTPAMSRPAELY 550
Cdd:cd18001 153 --AKNRIILTGTPIQNNLKELW 172
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
 397-553 2.44e-16

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: 78.55  E-value: 2.44e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 397 PFQREGVSFAISKRGRLLLADdMGLGKTV------QAICIAAFYRkewPLLVVVPSSV-RFTWEQAFLRWLpslSPENIN 469
Cdd:cd18013   3 PYQKVAINFIIEHPYCGLFLD-MGLGKTVttltalSDLQLDDFTR---RVLVIAPLRVaRSTWPDEVEKWN---HLRNLT 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 470 V-VVTGKGRLTAGLVN------IVSFDLLCKL-ERQLKT-PFKVVIIDESHFLKNIKTARCRAAVPILKVAKRVILLSGT 540
Cdd:cd18013  76 VsVAVGTERQRSKAANtpadlyVINRENLKWLvNKSGDPwPFDMVVIDELSSFKSPRSKRFKALRKVRPVIKRLIGLTGT 155

                       170
                ....*....|...
gi 26346797 541 PAMSRPAELYTQI 553
Cdd:cd18013 156 PSPNGLMDLWAQI 168
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
 414-567 1.29e-15

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: 76.59  E-value: 1.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 414 LLADDMGLGKTVQAICIAAF---YRK-EWPLLVVVPSSVRFTWEQAFLRWLPSLSPeninVVVTGKGRLTAGLVN----- 484
Cdd:cd17997  26 ILADEMGLGKTLQTISLLGYlkhYKNiNGPHLIIVPKSTLDNWMREFKRWCPSLRV----VVLIGDKEERADIIRdvllp 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 485 ------IVSFDLLCKLERQLKT-PFKVVIIDESHFLKNIKTARCRaAVPILKVAKRvILLSGTPAMSRPAELYTQIIAVK 557
Cdd:cd17997 102 gkfdvcITSYEMVIKEKTVLKKfNWRYIIIDEAHRIKNEKSKLSQ-IVRLFNSRNR-LLLTGTPLQNNLHELWALLNFLL 179

                       170
                ....*....|
gi 26346797 558 PTFFPQFHAF 567
Cdd:cd17997 180 PDVFTSSEDF 189
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
 395-567 2.14e-15

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: 76.27  E-value: 2.14e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVSFAIS--KRG-RLLLADDMGLGKTVQAICIAAFY--RKEW-PLLVVVPSSVRFTWEQAFLRWLPSlspenI 468
Cdd:cd18009   4 MRPYQLEGMEWLRMlwENGiNGILADEMGLGKTIQTIALLAHLreRGVWgPFLVIAPLSTLPNWVNEFARFTPS-----V 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 469 NVVV------------------TGKGRLTAglVNIVSFDlLCKLERQL--KTPFKVVIIDESHFLKNIKtarCR--AAVP 526
Cdd:cd18009  79 PVLLyhgtkeererlrkkimkrEGTLQDFP--VVVTSYE-IAMRDRKAlqHYAWKYLIVDEGHRLKNLN---CRliQELK 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 26346797 527 ILKVAKRvILLSGTPAMSRPAELYTQIIAVKPTFFPQFHAF 567
Cdd:cd18009 153 TFNSDNR-LLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSF 192
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
 414-567 2.32e-15

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: 76.25  E-value: 2.32e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 414 LLADDMGLGKTVQAICIAA----FYRKEWPLLVVVPSSVRFTWEQAFLRWLPSLS------PENINVVVTGKGRLTAGLV 483
Cdd:cd17996  26 ILADEMGLGKTIQTISLITylmeKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSkivykgTPDVRKKLQSQIRAGKFNV 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 484 NIVSFDLLCKlERQL--KTPFKVVIIDESHFLKNiktARCRAAVpILK---VAKRVILLSGTPAMSRPAELYTQIIAVKP 558
Cdd:cd17996 106 LLTTYEYIIK-DKPLlsKIKWKYMIIDEGHRMKN---AQSKLTQ-TLNtyyHARYRLLLTGTPLQNNLPELWALLNFLLP 180


                ....*....
gi 26346797 559 TFFPQFHAF 567
Cdd:cd17996 181 KIFKSCKTF 189
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
 395-562 5.03e-15

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: 74.78  E-value: 5.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVSFAISKRGR---LLLADDMGLGKTVQAICIAAFYRK----EWPLLVVVPSSVRFTWEQAFLRWLPSLSpen 467
Cdd:cd18006   1 LRPYQLEGVNWLLQCRAEqhgCILGDEMGLGKTCQTISLLWYLAGrlklLGPFLVLCPLSVLDNWKEELNRFAPDLS--- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 468 invVVTGKGRLTAGL-------------VNIVSFDLLCKLERQLKT-PFKVVIIDESHFLKNiKTARCRAAVPILKVAKR 533
Cdd:cd18006  78 ---VITYMGDKEKRLdlqqdikstnrfhVLLTTYEICLKDASFLKSfPWASLVVDEAHRLKN-QNSLLHKTLSEFSVDFR 153

                       170       180
                ....*....|....*....|....*....
gi 26346797 534 vILLSGTPAMSRPAELYTQIIAVKPTFFP 562
Cdd:cd18006 154 -LLLTGTPIQNSLQELYALLSFIEPNVFP 181
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
 395-558 5.34e-15

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


Pssm-ID: 350824 [Multi-domain]  Cd Length: 235  Bit Score: 75.27  E-value: 5.34e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVSF--------AISKRGRLLLADDMGLGKTVQAICIAAFYRKEWP---------LLVVVPSSVRFTWEQAFL 457
Cdd:cd18066   1 LRPHQREGIEFlyecvmgmRVNERFGAILADEMGLGKTLQCISLIWTLLRQGPyggkpvikrALIVTPGSLVKNWKKEFQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 458 RWLPSlspENINVVVTGKGRLTAGLVN-------IVSFDLLCK-LERQLKTPFKVVIIDESHFLKNiKTARCRAAVPILK 529
Cdd:cd18066  81 KWLGS---ERIKVFTVDQDHKVEEFIAsplysvlIISYEMLLRsLDQISKLNFDLVICDEGHRLKN-TSIKTTTALTSLS 156

                       170       180
                ....*....|....*....|....*....
gi 26346797 530 VAKRVIlLSGTPAMSRPAELYTQIIAVKP 558
Cdd:cd18066 157 CERRII-LTGTPIQNDLQEFFALIDFVNP 184
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
 395-573 1.06e-13

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: 70.55  E-value: 1.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVS---FAISKRGRLLLADDMGLGKTVQAICIAAFYRKE----WPLLVVVPSSVRFTWEQAFLRWLPSLspen 467
Cdd:cd17994   1 LHPYQLEGLNwlrFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEghskGPFLVSAPLSTIINWEREFEMWAPDF---- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 468 inVVVTGKGrltaGLVNIVSFDLLCKLERQLKT-PFKVVIIDESHFLKNIKTARCRaavpIL---KVAKRViLLSGTPAM 543
Cdd:cd17994  77 --YVVTYVG----DHVLLTSYELISIDQAILGSiDWAVLVVDEAHRLKNNQSKFFR----ILnsyKIGYKL-LLTGTPLQ 145

                       170       180       190
                ....*....|....*....|....*....|
gi 26346797 544 SRPAELYTQIIAVKPTFFPQFHAFGLRYCD 573
Cdd:cd17994 146 NNLEELFHLLNFLTPERFNNLQGFLEEFAD 175
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
 395-575 1.52e-13

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: 70.47  E-value: 1.52e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVS---FAISKRGRLLLADDMGLGKTVQAIC-IAAFYRK--EWPLLVVVPSSVRFTWEQAFLRWlpslspENI 468
Cdd:cd18060   1 LREYQLEGVNwllFNWYNRQNCILADEMGLGKTIQSIAfLQEVYNVgiHGPFLVIAPLSTITNWEREFNTW------TEM 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 469 NVVV-------------------TGKGRLTAGLVN----IVSFDLL---CKLERQLKtpFKVVIIDESHFLKNiKTARCR 522
Cdd:cd18060  75 NTIVyhgslasrqmiqqyemyckDSRGRLIPGAYKfdalITTFEMIlsdCPELREIE--WRCVIIDEAHRLKN-RNCKLL 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 26346797 523 AAVPILKVAKRViLLSGTPAMSRPAELYTQIIAVKPTFFPQFHAFGLRYCDAK 575
Cdd:cd18060 152 DSLKHMDLEHKV-LLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLK 203
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 672-766 2.25e-13

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: 66.85  E-value: 2.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797   672 VEYILDLLDSGR-EKFLVFAHHKVILDAvAKELERKNVQHIRIDGSTPSADREAQCQRFQlsKGHTVALLSITAANMGLT 750
Cdd:pfam00271   3 LEALLELLKKERgGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFR--KGKIDVLVATDVAERGLD 79

                          90
                  ....*....|....*.
gi 26346797   751 FSTADLVVFAELFWNP 766
Cdd:pfam00271  80 LPDVDLVINYDLPWNP 95
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
 414-617 2.52e-13

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: 70.46  E-value: 2.52e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 414 LLADDMGLGKTVQAICIAAF---YRK-EWPLLVVVPSSVRFTWEQAFLRWLPSLSpeniNVVVTGKGRLTAGLVN----- 484
Cdd:cd18064  38 ILADEMGLGKTLQTISLLGYmkhYRNiPGPHMVLVPKSTLHNWMAEFKRWVPTLR----AVCLIGDKDQRAAFVRdvllp 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 485 ------IVSFDLLCKLERQLKT-PFKVVIIDESHFLKNIKTaRCRAAVPILKVAKRvILLSGTPAMSRPAELYTQIIAVK 557
Cdd:cd18064 114 gewdvcVTSYEMLIKEKSVFKKfNWRYLVIDEAHRIKNEKS-KLSEIVREFKTTNR-LLLTGTPLQNNLHELWALLNFLL 191

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 558 PTFFPQFHAFGLRYCDAKRLpwgwdysGSSNLGELKLLLEEAIMLRRLKSDVLSQLPAKQ 617
Cdd:cd18064 192 PDVFNSAEDFDSWFDTNNCL-------GDQKLVERLHMVLRPFLLRRIKADVEKSLPPKK 244
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
 394-567 7.16e-13

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: 69.32  E-value: 7.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 394 SLMPFQREGVSFAISKRGRLL---LADDMGLGKTVQAICIAAFY----RKEWPLLVVVPSSVRFTWEQAFLRWLPSLspe 466
Cdd:cd18063  23 TLKHYQLQGLEWMVSLYNNNLngiLADEMGLGKTIQTIALITYLmehkRLNGPYLIIVPLSTLSNWTYEFDKWAPSV--- 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 467 ninVVVTGKG----------RLTAGLVNIV--SFDLLCKLERQL-KTPFKVVIIDESHFLKNiKTARCRAAVPILKVAKR 533
Cdd:cd18063 100 ---VKISYKGtpamrrslvpQLRSGKFNVLltTYEYIIKDKHILaKIRWKYMIVDEGHRMKN-HHCKLTQVLNTHYVAPR 175

                       170       180       190
                ....*....|....*....|....*....|....
gi 26346797 534 VILLSGTPAMSRPAELYTQIIAVKPTFFPQFHAF 567
Cdd:cd18063 176 RILLTGTPLQNKLPELWALLNFLLPTIFKSCSTF 209
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
 395-575 1.62e-12

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: 67.76  E-value: 1.62e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVS---FAISKRGRLLLADDMGLGKTVQAICIAA--FYRK-EWPLLVVVPSSVRFTWEQAFLRWlpslspENI 468
Cdd:cd18058   1 LREYQLEGMNwllFNWYNRKNCILADEMGLGKTIQSITFLSeiFLMGiRGPFLIIAPLSTITNWEREFRTW------TEM 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 469 NVVVTGKGRLTAGLVN-----------------------IVSFDLLCKLERQLKT-PFKVVIIDESHFLKNiKTARCRAA 524
Cdd:cd18058  75 NAIVYHGSQISRQMIQqyemyyrdeqgnplsgifkfqvvITTFEMILADCPELKKiNWSCVIIDEAHRLKN-RNCKLLEG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 26346797 525 VPILKVAKRViLLSGTPAMSRPAELYTQIIAVKPTFFPQFHAFGLRYCDAK 575
Cdd:cd18058 154 LKLMALEHKV-LLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLK 203
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
 395-575 1.74e-12

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: 67.72  E-value: 1.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVS---FAISKRGRLLLADDMGLGKTVQAIC-IAAFYRK--EWPLLVVVPSSVRFTWEQAFLRWlpslspENI 468
Cdd:cd18061   1 LREYQLEGLNwllFNWYNRRNCILADEMGLGKTIQSITfLYEILLTgiRGPFLIIAPLSTIANWEREFRTW------TDL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 469 NVVV-------------------TGKGRLTAGLVN----IVSFDLLCKLERQLKT-PFKVVIIDESHFLKNiKTARCRAA 524
Cdd:cd18061  75 NVVVyhgslisrqmiqqyemyfrDSQGRIIRGAYRfqaiITTFEMILGGCPELNAiDWRCVIIDEAHRLKN-KNCKLLEG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 26346797 525 VPILKVAKRViLLSGTPAMSRPAELYTQIIAVKPTFFPQFHAFGLRYCDAK 575
Cdd:cd18061 154 LKLMNLEHKV-LLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLK 203
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
 395-571 3.80e-12

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: 67.11  E-value: 3.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVSF----AISKRGR----LLLADDMGLGKTVQaiCIAAFyrkeWPLL--------------VVVPSSVRFTW 452
Cdd:cd18067   1 LRPHQREGVKFlyrcVTGRRIRgshgCIMADEMGLGKTLQ--CITLM----WTLLrqspqckpeidkaiVVSPSSLVKNW 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 453 EQAFLRWL-PSLSP--------ENINVVVTG----KGRLTAGLVNIVSFDLL-CKLERQLKTPFKVVIIDESHFLKNIKT 518
Cdd:cd18067  75 ANELGKWLgGRLQPlaidggskKEIDRKLVQwasqQGRRVSTPVLIISYETFrLHVEVLQKGEVGLVICDEGHRLKNSDN 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 26346797 519 aRCRAAVPILKVAKRVIlLSGTPAMSRPAELYTQIIAVKPTFFPQFHAFGLRY 571
Cdd:cd18067 155 -QTYQALDSLNTQRRVL-LSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNF 205
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
 395-575 4.12e-12

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: 66.59  E-value: 4.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVS---FAISKRGRLLLADDMGLGKTVQAIC-IAAFYRK--EWPLLVVVPSSVRFTWEQAFLRWlpslspENI 468
Cdd:cd18059   1 LREYQLEGVNwllFNWYNTRNCILADEMGLGKTIQSITfLYEIYLKgiHGPFLVIAPLSTIPNWEREFRTW------TEL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 469 NVVV-------------------TGKGRLTAGLVN----IVSFDLLCKLERQLKT-PFKVVIIDESHFLKNiKTARCRAA 524
Cdd:cd18059  75 NVVVyhgsqasrrtiqlyemyfkDPQGRVIKGSYKfhaiITTFEMILTDCPELRNiPWRCVVIDEAHRLKN-RNCKLLEG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 26346797 525 VPILKVAKRViLLSGTPAMSRPAELYTQIIAVKPTFFPQFHAFGLRYCDAK 575
Cdd:cd18059 154 LKMMDLEHKV-LLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLK 203
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
394-760 4.62e-12

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 69.28  E-value: 4.62e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 394 SLMPFQREGV----SFAISKRGRLLLADDMGLGKTVQAICIAAFYRKEWPLLVVVPS-SVRFTWEQAFLRWLPslspeni 468
Cdd:COG1061  80 ELRPYQQEALeallAALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRVLVLVPRrELLEQWAEELRRFLG------- 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 469 NVVVTGKGRLTAGLVNIVSFDLLCKLE--RQLKTPFKVVIIDESHflkNIKTARCRAAVPILKvAKRVILLSGTP----A 542
Cdd:COG1061 153 DPLAGGGKKDSDAPITVATYQSLARRAhlDELGDRFGLVIIDEAH---HAGAPSYRRILEAFP-AAYRLGLTATPfrsdG 228

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 543 MSRPAELYTQIIavkptffpqfhaFGLRYCDAkrlpwgwdysgssnlgelkllleeaimlrrLKSDVLSQLpakqrkMVV 622
Cdd:COG1061 229 REILLFLFDGIV------------YEYSLKEA------------------------------IEDGYLAPP------EYY 260

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 623 VNPGRISSRakaaldaaakEMTKDKTKQQQKEALLvffnRTAEAKIPCVVEYILDLLDsgREKFLVFAHHKVILDAVAKE 702
Cdd:COG1061 261 GIRVDLTDE----------RAEYDALSERLREALA----ADAERKDKILRELLREHPD--DRKTLVFCSSVDHAEALAEL 324

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 26346797 703 LERKNVQHIRIDGSTPSADREAQCQRFqlSKGHTVALLSITAANMGLTFSTADLVVFA 760
Cdd:COG1061 325 LNEAGIRAAVVTGDTPKKEREEILEAF--RDGELRILVTVDVLNEGVDVPRLDVAILL 380
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
 395-560 6.25e-12

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: 65.04  E-value: 6.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVSFAISKRGRL---LLADDMGLGKTVQAIC--IAAFYRKEW--PLLVVVPSSVRFTWEQAFLRWLPSLspen 467
Cdd:cd18000   1 LFKYQQTGVQWLWELHCQRvggILGDEMGLGKTIQIIAflAALHHSKLGlgPSLIVCPATVLKQWVKEFHRWWPPF---- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 468 iNVVV---TGKGRL-------------------TAGLVNIVSFDLLCKLERQL-KTPFKVVIIDESHFLKNIKtARCRAA 524
Cdd:cd18000  77 -RVVVlhsSGSGTGseeklgsierksqlirkvvGDGGILITTYEGFRKHKDLLlNHNWQYVILDEGHKIRNPD-AEITLA 154

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 26346797 525 VPILKVAKRVIlLSGTPAMSRPAELYTQIIAVKPTF 560
Cdd:cd18000 155 CKQLRTPHRLI-LSGTPIQNNLKELWSLFDFVFPPY 189
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
 398-541 6.29e-12

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: 65.84  E-value: 6.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 398 FQREGVSFAI---SKRGRLLLADDMGLGKTVQAICIAAFYRKEW----PLLVVVPSSVRFTWEQAFLRWLPSLspeniNV 470
Cdd:cd17993   5 YQLTGLNWLAhswCKGNNGILADEMGLGKTVQTISFLSYLFHSQqqygPFLVVVPLSTMPAWQREFAKWAPDM-----NV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 471 VV-TGkgrltaglvNIVSFDLLCKLE------RQLK-----TPFKVVI---------------IDESHFLKNiKTARCRA 523
Cdd:cd17993  80 IVyLG---------DIKSRDTIREYEfyfsqtKKLKfnvllTTYEIILkdkaflgsikwqylaVDEAHRLKN-DESLLYE 149

                       170
                ....*....|....*...
gi 26346797 524 AVPILKVAKRvILLSGTP 541
Cdd:cd17993 150 ALKEFKTNNR-LLITGTP 166
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
 414-567 7.21e-12

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: 66.22  E-value: 7.21e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 414 LLADDMGLGKTVQAICIAA----FYRKEWPLLVVVPSSVRFTWEQAFLRWLPSLspeninVVVTGKG----------RLT 479
Cdd:cd18062  46 ILADEMGLGKTIQTIALITylmeHKRINGPFLIIVPLSTLSNWVYEFDKWAPSV------VKVSYKGspaarrafvpQLR 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 480 AGLVNIV--SFDLLCKLERQL-KTPFKVVIIDESHFLKNiKTARCRAAVPILKVAKRVILLSGTPAMSRPAELYTQIIAV 556
Cdd:cd18062 120 SGKFNVLltTYEYIIKDKQILaKIRWKYMIVDEGHRMKN-HHCKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFL 198

                       170
                ....*....|.
gi 26346797 557 KPTFFPQFHAF 567
Cdd:cd18062 199 LPTIFKSCSTF 209
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
 414-567 3.90e-11

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: 63.68  E-value: 3.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 414 LLADDMGLGKTVQAICIAAFYRKE---W-PLLVVVPSSVRFTWEQAFLRWLPSL-------SPENINVV------VTGKG 476
Cdd:cd18002  23 ILADEMGLGKTVQSIAVLAHLAEEhniWgPFLVIAPASTLHNWQQEISRFVPQFkvlpywgNPKDRKVLrkfwdrKNLYT 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 477 RLTAGLVNIVSFDLLCKLERQL-KTPFKVVIIDESHFLKNIKTARCRAAVPiLKVAKRvILLSGTPAMSRPAELYTQIIA 555
Cdd:cd18002 103 RDAPFHVVITSYQLVVQDEKYFqRVKWQYMVLDEAQAIKSSSSSRWKTLLS-FHCRNR-LLLTGTPIQNSMAELWALLHF 180

                       170
                ....*....|..
gi 26346797 556 VKPTFFPQFHAF 567
Cdd:cd18002 181 IMPTLFDSHDEF 192
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
 414-561 1.21e-10

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: 62.34  E-value: 1.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 414 LLADDMGLGKTVQAICIAAF---YRK-EWPLLVVVPSSVRFTWEQAFLRWLPSLSPeninVVVTGKGRLTAGLVN----- 484
Cdd:cd18065  38 ILADEMGLGKTLQTIALLGYlkhYRNiPGPHMVLVPKSTLHNWMNEFKRWVPSLRA----VCLIGDKDARAAFIRdvmmp 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 485 ------IVSFDLLCKLERQLKT-PFKVVIIDESHFLKNIKTaRCRAAVPILKVAKRvILLSGTPAMSRPAELYTQIIAVK 557
Cdd:cd18065 114 gewdvcVTSYEMVIKEKSVFKKfNWRYLVIDEAHRIKNEKS-KLSEIVREFKTTNR-LLLTGTPLQNNLHELWALLNFLL 191


                ....
gi 26346797 558 PTFF 561
Cdd:cd18065 192 PDVF 195
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
 395-571 1.45e-10

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: 62.21  E-value: 1.45e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVSFAI-----SKRGRL-------LLADDMGLGKTVQAIC----------IAAFYRkewpLLVVVPSSVRFTW 452
Cdd:cd18068   1 LKPHQVDGVQFMWdccceSLKKTKkspgsgcILAHCMGLGKTLQVVTflhtvllcekLENFSR----VLVVCPLNTVLNW 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 453 EQAFLRWLPSLSPEN------INVVVTGKGRLTA-------GLVNIVSFDLL--------CKLERQLKTPFK-------- 503
Cdd:cd18068  77 LNEFEKWQEGLKDEEkievneLATYKRPQERSYKlqrwqeeGGVMIIGYDMYrilaqernVKSREKLKEIFNkalvdpgp 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26346797 504 -VVIIDESHFLKNIKTARCRAAVPILkvAKRVILLSGTPAMSRPAELYTQIIAVKPTFFPQFHAFGLRY 571
Cdd:cd18068 157 dFVVCDEGHILKNEASAVSKAMNSIR--TKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
HELICc smart00490
helicase superfamily c-terminal domain;
697-766 1.51e-10

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 57.99  E-value: 1.51e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797    697 DAVAKELERKNVQHIRIDGSTPSADREAQCQRFQlsKGHTVALLSITAANMGLTFSTADLVVFAELFWNP 766
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKFN--NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSP 68
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
 395-567 1.72e-10

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: 61.94  E-value: 1.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVSF---AISKRGRLLLADDMGLGKTVQAICIAAF----YRKEWPLLVVVPSSVRFTWEQAFLRWLPslspeN 467
Cdd:cd18054  21 LRDYQLEGLNWlahSWCKNNSVILADEMGLGKTIQTISFLSYlfhqHQLYGPFLLVVPLSTLTSWQREFEIWAP-----E 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 468 INVVVTGKGRLTAGlvNIVSFDLLCKLERQLK-----TPFKVVI---------------IDESHFLKNIKTARCRAAVPI 527
Cdd:cd18054  96 INVVVYIGDLMSRN--TIREYEWIHSQTKRLKfnaliTTYEILLkdktvlgsinwaflgVDEAHRLKNDDSLLYKTLIDF 173

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 26346797 528 LKVAKrvILLSGTPAMSRPAELYTQIIAVKPTFFPQFHAF 567
Cdd:cd18054 174 KSNHR--LLITGTPLQNSLKELWSLLHFIMPEKFEFWEDF 211
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
 395-576 1.29e-08

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: 56.23  E-value: 1.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVS---FAISKRGRLLLADDMGLGKTVQAIC-IAAFYRK---EWPLLVVVPSSVRFTWEQAFLRWLP------ 461
Cdd:cd18057   1 LHPYQLEGLNwlrFSWAQGTDTILADEMGLGKTVQTIVfLYSLYKEghsKGPYLVSAPLSTIINWEREFEMWAPdfyvvt 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 462 --------SLSPEN-----INVVVTGKG--RLTAGL-----VNIVSFDLLCKLERQLKT-PFKVVIIDESHFLKNIKTAR 520
Cdd:cd18057  81 ytgdkesrSVIRENefsfeDNAIRSGKKvfRMKKEAqikfhVLLTSYELITIDQAILGSiEWACLVVDEAHRLKNNQSKF 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 26346797 521 CRaAVPILKVAKRvILLSGTPAMSRPAELYTQIIAVKPTFFPQFHAFGLRYCDAKR 576
Cdd:cd18057 161 FR-VLNSYKIDYK-LLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISK 214
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
 414-560 2.34e-08

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: 55.59  E-value: 2.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 414 LLADDMGLGKTVQAIC-IAAFYR--KEWPLLVVVPSSVRFTWEQAFLRWLPSLS------PENINVVVTGKGRLT----- 479
Cdd:cd18069  32 ILAHSMGLGKTLQVISfLDVLLRhtGAKTVLAIVPVNTLQNWLSEFNKWLPPPEalpnvrPRPFKVFILNDEHKTtaara 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 480 --------AGLVNIVSFDLLcklerQLKTPFKVVIIDESHFLKNIKTARCRAAVPILkvAKRVILLSGTPAMSRPAELYT 551
Cdd:cd18069 112 kviedwvkDGGVLLMGYEMF-----RLRPGPDVVICDEGHRIKNCHASTSQALKNIR--SRRRIVLTGYPLQNNLIEYWC 184


                ....*....
gi 26346797 552 QIIAVKPTF 560
Cdd:cd18069 185 MVDFVRPDF 193
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
 395-576 3.69e-08

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: 55.07  E-value: 3.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVS---FAISKRGRLLLADDMGLGKTVQ-AICIAAFYRK---EWPLLVVVPSSVRFTWEQAFLRWLPSLspen 467
Cdd:cd18056   1 LHPYQLEGLNwlrFSWAQGTDTILADEMGLGKTVQtAVFLYSLYKEghsKGPFLVSAPLSTIINWEREFEMWAPDM---- 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 468 inVVVTGKGRLTAGLV---NIVSFD--------LLCKLERQLKTPFKV----------------------VIIDESHFLK 514
Cdd:cd18056  77 --YVVTYVGDKDSRAIireNEFSFEdnairggkKASRMKKEASVKFHVlltsyelitidmailgsidwacLIVDEAHRLK 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26346797 515 NIKTARCRaavpILK--VAKRVILLSGTPAMSRPAELYTQIIAVKPTFFPQFHAFGLRYCDAKR 576
Cdd:cd18056 155 NNQSKFFR----VLNgySLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAK 214
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
 414-551 7.29e-08

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: 54.01  E-value: 7.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 414 LLADDMGLGKTVQAICIAAFYrkewPLLVVVPSSVRFTWEQAFLRwlpSLSPENINVVV---TGKGRLTAGLV------- 483
Cdd:cd18071  52 ILADDMGLGKTLTTISLILAN----FTLIVCPLSVLSNWETQFEE---HVKPGQLKVYTyhgGERNRDPKLLSkydivlt 124

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26346797 484 --NIVSFDLLCKLERQLKT-PFKVVIIDESHFLKNIKTARCRaAVPILKVAKRVIlLSGTPAMSRPAELYT 551
Cdd:cd18071 125 tyNTLASDFGAKGDSPLHTiNWLRVVLDEGHQIRNPNAQQTK-AVLNLSSERRWV-LTGTPIQNSPKDLGS 193
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
 398-576 2.80e-07

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: 52.32  E-value: 2.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 398 FQREGVS---FAISKRGRLLLADDMGLGKTVQAICIAAFYRKE----WPLLVVVPSSVRFTWEQAFLRWLPSLspeninV 470
Cdd:cd18055   4 YQLEGLNwlrFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEghtkGPFLVSAPLSTIINWEREFQMWAPDF------Y 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 471 VVTGKGRLTAGLV---NIVSFD--------LLCKLERQLKTPFKV----------------------VIIDESHFLKNIK 517
Cdd:cd18055  78 VVTYTGDKDSRAIireNEFSFDdnavkggkKAFKMKREAQVKFHVlltsyelvtidqaalgsirwacLVVDEAHRLKNNQ 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 26346797 518 TARCRaAVPILKVAKRvILLSGTPAMSRPAELYTQIIAVKPTFFPQFHAFGLRYCDAKR 576
Cdd:cd18055 158 SKFFR-VLNGYKIDHK-LLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISK 214
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 395-541 8.18e-07

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: 49.23  E-value: 8.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 395 LMPFQREGVS--FAISKRGRLLLADDMGLGKTVQAICIAAfYRKEWPLLVVVPS-SVRFTWEQAFLRWLPSLS------- 464
Cdd:cd17926   1 LRPYQEEALEawLAHKNNRRGILVLPTGSGKTLTALALIA-YLKELRTLIVVPTdALLDQWKERFEDFLGDSSigliggg 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 465 ----PENINVVVTgkgrltagLVNIVSFDLlcKLERQLKTPFKVVIIDESHFLkNIKTArcRAAVPILKvAKRVILLSGT 540
Cdd:cd17926  80 kkkdFDDANVVVA--------TYQSLSNLA--EEEKDLFDQFGLLIVDEAHHL-PAKTF--SEILKELN-AKYRLGLTAT 145


                .
gi 26346797 541 P 541
Cdd:cd17926 146 P 146
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
 414-567 4.53e-06

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: 48.89  E-value: 4.53e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 414 LLADDMGLGKTVQAICIAAFYRKEW----PLLVVVPSSVRFTWEQAFLRWLPSLSP-------ENINVVVTGK------G 476
Cdd:cd18053  43 ILADEMGLGKTIQTISFLNYLFHEHqlygPFLLVVPLSTLTSWQREIQTWAPQMNAvvylgdiNSRNMIRTHEwmhpqtK 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 477 RLTAGLVnIVSFDLLCKLERQL-KTPFKVVIIDESHFLKNIKTARCRAAVPiLKVAKRvILLSGTPAMSRPAELYTQIIA 555
Cdd:cd18053 123 RLKFNIL-LTTYEILLKDKSFLgGLNWAFIGVDEAHRLKNDDSLLYKTLID-FKSNHR-LLITGTPLQNSLKELWSLLHF 199

                       170
                ....*....|..
gi 26346797 556 VKPTFFPQFHAF 567
Cdd:cd18053 200 IMPEKFSSWEDF 211
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
 395-432 8.41e-04

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: 41.95  E-value: 8.41e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 26346797 395 LMPFQREGVSFAISKRGrlLLADDMGLGKTVQAI-CIAA 432
Cdd:cd18070   1 LLPYQRRAVNWMLVPGG--ILADEMGLGKTVEVLaLILL 37
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 413-540 5.70e-03

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 38.15  E-value: 5.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797 413 LLLADDMGLGKTVQA--ICIAAFYRKEWPLLVVVP-SSVRFTWEQAFLRWLP----------SLSPENINVVVTGKGRLT 479
Cdd:cd00046   4 VLITAPTGSGKTLAAllAALLLLLKKGKKVLVLVPtKALALQTAERLRELFGpgirvavlvgGSSAEEREKNKLGDADII 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26346797 480 AGLVNIVSFDLLcKLERQLKTPFKVVIIDESHFLKNIKTARCRAAVPILKVAK---RVILLSGT 540
Cdd:cd00046  84 IATPDMLLNLLL-REDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLknaQVILLSAT 146
ResIII pfam04851
Type III restriction enzyme, res subunit;
420-511 6.38e-03

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 38.04  E-value: 6.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26346797   420 GLGKTVQAICIAAFYRKEWPL---LVVVPS-SVRFTWEQAFLRWLPSlsPENINVVVTGKGRLTAGLVNIVSF------- 488
Cdd:pfam04851  33 GSGKTLTAAKLIARLFKKGPIkkvLFLVPRkDLLEQALEEFKKFLPN--YVEIGEIISGDKKDESVDDNKIVVttiqsly 110

                          90       100
                  ....*....|....*....|....
gi 26346797   489 -DLLCKLERQLKTPFKVVIIDESH 511
Cdd:pfam04851 111 kALELASLELLPDFFDVIIIDEAH 134
 
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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