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Conserved domains on  [gi|195446151|ref|XP_002070651|]
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TATA-binding protein-associated factor 172 [Drosophila willistoni]

Protein Classification

Mot1 family DEAD/DEAH box helicase( domain architecture ID 13778164)

Mot1 family DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA, similar to Modifier of transcription 1 (Mot1, also known as TAF172 in eukaryotes) that regulates transcription in association with TATA binding protein (TBP); contains a DUF3535 domain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
1377-1609 2.39e-143

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: 443.33  E-value: 2.39e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAGDHIQREN-TNQSNLPSLVICPPTLTGHWVYEVEKFLAQ 1455
Cdd:cd17999     1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHHKRANsFNSENLPSLVVCPPTLVGHWVAEIKKYFPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1456 SpILRPLHYFGFPVGREKLRSQiGTTCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIKQLKANHRL 1535
Cdd:cd17999    81 A-FLKPLAYVGPPQERRRLREQ-GEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHRL 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 195446151 1536 ILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSRPILASRDAKSSPKDQEAGVLAMEALHRQVLPFLLRR 1609
Cdd:cd17999   159 ILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
1369-1880 1.10e-140

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 454.30  E-value: 1.10e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1369 VPVTLSVELRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAgdHIQRENTNQsnlPSLVICPPTLTGHWVYE 1448
Cdd:COG0553   234 LPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLL--ELKERGLAR---PVLIVAPTSLVGNWQRE 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1449 VEKFLaqsPILRPLHYFGfPVGREKLRSQIGTtCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIKQ 1528
Cdd:COG0553   309 LAKFA---PGLRVLVLDG-TRERAKGANPFED-ADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRA 383
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1529 LKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSRPIlasrdaksSPKDQEagvlAMEALHRQVLPFLLR 1608
Cdd:COG0553   384 LKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPI--------EKGDEE----ALERLRRLLRPFLLR 451
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1609 RVKEDVLKDLPPKITQDLLCELSPLQLRLYEDfskkHLKDCLDKLGDSpgaatgtttstENLNGRTHIFQALRYLQNVCN 1688
Cdd:COG0553   452 RTKEDVLKDLPEKTEETLYVELTPEQRALYEA----VLEYLRRELEGA-----------EGIRRRGLILAALTRLRQICS 516
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1689 HPKLVLRQSEELGpivtqlalsnstlddiEHSAKLPALKQLLldcgigvQTESVSQHRALIFCQLKAMLDIVEHDLLRRH 1768
Cdd:COG0553   517 HPALLLEEGAELS----------------GRSAKLEALLELL-------EELLAEGEKVLVFSQFTDTLDLLEERLEERG 573
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1769 LPsvtYLRLDGSVPASQRQDIVNNFNSDPSIDvlllttlvgglgL------------NLTGADTVIFVEHDWNPMKDLQA 1836
Cdd:COG0553   574 IE---YAYLHGGTSAEERDELVDRFQEGPEAP------------VflislkaggeglNLTAADHVIHYDLWWNPAVEEQA 638
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 195446151 1837 MDRAHRIGQKKVVNVYRLITRNSLEEKIMGLQKFKILTANTVVS 1880
Cdd:COG0553   639 IDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DUF3535 pfam12054
Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. ...
669-1163 1.36e-120

Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 439 to 459 amino acids in length. This domain is found associated with pfam00271, pfam02985, pfam00176. This domain has two completely conserved residues (P and K) that may be functionally important.


:

Pssm-ID: 463447  Cd Length: 445  Bit Score: 388.53  E-value: 1.36e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151   669 VWSNLIQHA-DLGALLNAACPFVSSWICLAMQPPRLAFDSAVLIRACGGGGGVAGDASSTSSRRRIPKLGDDLGGSALAH 747
Cdd:pfam12054    1 VWEALLRSLkPPEALLHAFCPHLSPWLTLLMTPIGVPMDASLLLKPSGQPYSPPERRKSKKKEEPPPSDIPSPGRQGSSS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151   748 SNaTLKLYLGGSEATPLEVreaNFVRARITSSRALGALSHYLvqpapgvvytpQMESPTDCYTKVLLGHLNAHSAVQRIV 827
Cdd:pfam12054   81 HN-VDKPMIGGDVTLVGMD---VVIRTRIAAAKALGLLLSYW-----------PEESPLDFFTKLLLPYLNSPSALQRLL 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151   828 CGLIIAFWALEDE-----PVRPGPPNLQEKLHQCVA---EYFYYDEVAVSLTRLLQETQDFIATL---------KQNKIP 890
Cdd:pfam12054  146 AAIIIEEWAKNCKkekssSVSTLPETLSEKLLEILEnpsRPPYYRELVPYLTRLRTQCQQLLNTFrdvgkvsqsKLPKLA 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151   891 INDFNNA----KILTLDQIEAVAFS-LSENIRHFPLKPKVMDT--LLERRRSLQASYQQTTTEQGSYHVSAQAALAGAIC 963
Cdd:pfam12054  226 VVVQGEPeagpGAFSIEQAEKLVGEdYDKLKKSLSPKQKLLALqqLEDRRRRVQAAIEEAKEAKEQRDVRVLAAAAGALV 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151   964 ALHCLPEKLNPVVKPLMESIKREQCVPLQQLSAEFLVHLMDQVCDRN-PSPNSKILNNLCTLLRSDGDHTPKLIMPFHTv 1042
Cdd:pfam12054  306 ALKGLPKKLNPIIKPLMDSIKKEENEELQQRSADALAHLIDLCVDRGkPGPNDKIVKNLCTFLCVDTSETPEFHPNAKL- 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151  1043 mdtmastvadsncaYYGIVTLTLQQAVKSnstanrgpgsgsttagsgtptaprgpgRPPASEIlanaaaaaatieqsvll 1122
Cdd:pfam12054  385 --------------TDGILTLRKEEDKAD---------------------------HADAAKF----------------- 406
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 195446151  1123 arEAEAKQCRIQRLGSACAITKLCSSFGEHIVEKVPIFEQL 1163
Cdd:pfam12054  407 --EEEAKEARIQRRGAKLALEQLAKKFGASLFEKVPKLWEL 445
 
Name Accession Description Interval E-value
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
1377-1609 2.39e-143

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: 443.33  E-value: 2.39e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAGDHIQREN-TNQSNLPSLVICPPTLTGHWVYEVEKFLAQ 1455
Cdd:cd17999     1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHHKRANsFNSENLPSLVVCPPTLVGHWVAEIKKYFPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1456 SpILRPLHYFGFPVGREKLRSQiGTTCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIKQLKANHRL 1535
Cdd:cd17999    81 A-FLKPLAYVGPPQERRRLREQ-GEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHRL 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 195446151 1536 ILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSRPILASRDAKSSPKDQEAGVLAMEALHRQVLPFLLRR 1609
Cdd:cd17999   159 ILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
1369-1880 1.10e-140

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 454.30  E-value: 1.10e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1369 VPVTLSVELRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAgdHIQRENTNQsnlPSLVICPPTLTGHWVYE 1448
Cdd:COG0553   234 LPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLL--ELKERGLAR---PVLIVAPTSLVGNWQRE 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1449 VEKFLaqsPILRPLHYFGfPVGREKLRSQIGTtCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIKQ 1528
Cdd:COG0553   309 LAKFA---PGLRVLVLDG-TRERAKGANPFED-ADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRA 383
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1529 LKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSRPIlasrdaksSPKDQEagvlAMEALHRQVLPFLLR 1608
Cdd:COG0553   384 LKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPI--------EKGDEE----ALERLRRLLRPFLLR 451
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1609 RVKEDVLKDLPPKITQDLLCELSPLQLRLYEDfskkHLKDCLDKLGDSpgaatgtttstENLNGRTHIFQALRYLQNVCN 1688
Cdd:COG0553   452 RTKEDVLKDLPEKTEETLYVELTPEQRALYEA----VLEYLRRELEGA-----------EGIRRRGLILAALTRLRQICS 516
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1689 HPKLVLRQSEELGpivtqlalsnstlddiEHSAKLPALKQLLldcgigvQTESVSQHRALIFCQLKAMLDIVEHDLLRRH 1768
Cdd:COG0553   517 HPALLLEEGAELS----------------GRSAKLEALLELL-------EELLAEGEKVLVFSQFTDTLDLLEERLEERG 573
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1769 LPsvtYLRLDGSVPASQRQDIVNNFNSDPSIDvlllttlvgglgL------------NLTGADTVIFVEHDWNPMKDLQA 1836
Cdd:COG0553   574 IE---YAYLHGGTSAEERDELVDRFQEGPEAP------------VflislkaggeglNLTAADHVIHYDLWWNPAVEEQA 638
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 195446151 1837 MDRAHRIGQKKVVNVYRLITRNSLEEKIMGLQKFKILTANTVVS 1880
Cdd:COG0553   639 IDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DUF3535 pfam12054
Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. ...
669-1163 1.36e-120

Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 439 to 459 amino acids in length. This domain is found associated with pfam00271, pfam02985, pfam00176. This domain has two completely conserved residues (P and K) that may be functionally important.


Pssm-ID: 463447  Cd Length: 445  Bit Score: 388.53  E-value: 1.36e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151   669 VWSNLIQHA-DLGALLNAACPFVSSWICLAMQPPRLAFDSAVLIRACGGGGGVAGDASSTSSRRRIPKLGDDLGGSALAH 747
Cdd:pfam12054    1 VWEALLRSLkPPEALLHAFCPHLSPWLTLLMTPIGVPMDASLLLKPSGQPYSPPERRKSKKKEEPPPSDIPSPGRQGSSS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151   748 SNaTLKLYLGGSEATPLEVreaNFVRARITSSRALGALSHYLvqpapgvvytpQMESPTDCYTKVLLGHLNAHSAVQRIV 827
Cdd:pfam12054   81 HN-VDKPMIGGDVTLVGMD---VVIRTRIAAAKALGLLLSYW-----------PEESPLDFFTKLLLPYLNSPSALQRLL 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151   828 CGLIIAFWALEDE-----PVRPGPPNLQEKLHQCVA---EYFYYDEVAVSLTRLLQETQDFIATL---------KQNKIP 890
Cdd:pfam12054  146 AAIIIEEWAKNCKkekssSVSTLPETLSEKLLEILEnpsRPPYYRELVPYLTRLRTQCQQLLNTFrdvgkvsqsKLPKLA 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151   891 INDFNNA----KILTLDQIEAVAFS-LSENIRHFPLKPKVMDT--LLERRRSLQASYQQTTTEQGSYHVSAQAALAGAIC 963
Cdd:pfam12054  226 VVVQGEPeagpGAFSIEQAEKLVGEdYDKLKKSLSPKQKLLALqqLEDRRRRVQAAIEEAKEAKEQRDVRVLAAAAGALV 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151   964 ALHCLPEKLNPVVKPLMESIKREQCVPLQQLSAEFLVHLMDQVCDRN-PSPNSKILNNLCTLLRSDGDHTPKLIMPFHTv 1042
Cdd:pfam12054  306 ALKGLPKKLNPIIKPLMDSIKKEENEELQQRSADALAHLIDLCVDRGkPGPNDKIVKNLCTFLCVDTSETPEFHPNAKL- 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151  1043 mdtmastvadsncaYYGIVTLTLQQAVKSnstanrgpgsgsttagsgtptaprgpgRPPASEIlanaaaaaatieqsvll 1122
Cdd:pfam12054  385 --------------TDGILTLRKEEDKAD---------------------------HADAAKF----------------- 406
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 195446151  1123 arEAEAKQCRIQRLGSACAITKLCSSFGEHIVEKVPIFEQL 1163
Cdd:pfam12054  407 --EEEAKEARIQRRGAKLALEQLAKKFGASLFEKVPKLWEL 445
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
1377-1865 3.82e-80

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 288.24  E-value: 3.82e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAGDHIQRENTNqsnlPSLVICPPTLTGHWVYEVEKFlaqS 1456
Cdd:PLN03142  170 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITG----PHMVVAPKSTLGNWMNEIRRF---C 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1457 PILRPLHYFGFPVGREKLRSQ--IGTTCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIKQLKANHR 1534
Cdd:PLN03142  243 PVLRAVKFHGNPEERAHQREEllVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYR 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1535 LILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSrpilasrdaKSSPKDQEAGVlamEALHRQVLPFLLRRVKEDV 1614
Cdd:PLN03142  323 LLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQ---------ISGENDQQEVV---QQLHKVLRPFLLRRLKSDV 390
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1615 LKDLPPKITQDLLCELSPLQLRLYEDFSKKHLkDCLDKLGDspgaatgtttstenlngRTHIFQALRYLQNVCNHPKLVl 1694
Cdd:PLN03142  391 EKGLPPKKETILKVGMSQMQKQYYKALLQKDL-DVVNAGGE-----------------RKRLLNIAMQLRKCCNHPYLF- 451
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1695 rQSEELGPIVTqlalsnsTLDD-IEHSAKLPALKQLLLDCGigvQTESvsqhRALIFCQLKAMLDIVEHDLLRRHLPsvt 1773
Cdd:PLN03142  452 -QGAEPGPPYT-------TGEHlVENSGKMVLLDKLLPKLK---ERDS----RVLIFSQMTRLLDILEDYLMYRGYQ--- 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1774 YLRLDGSVPASQRQDIVNNFNSDPSIDVLLLTTLVGGLG-LNLTGADTVIFVEHDWNPMKDLQAMDRAHRIGQKKVVNVY 1852
Cdd:PLN03142  514 YCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLgINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVF 593
                         490
                  ....*....|...
gi 195446151 1853 RLITRNSLEEKIM 1865
Cdd:PLN03142  594 RFCTEYTIEEKVI 606
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
1380-1693 2.35e-74

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: 249.91  E-value: 2.35e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151  1380 YQQAGINWLWFL-NKYNLHGILCDDMGLGKTLQTICILAGDHIQRENTNqsnLPSLVICPPTLTGHWVYEVEKFlAQSPI 1458
Cdd:pfam00176    1 YQIEGVNWMLSLeNNLGRGGILADEMGLGKTLQTISLLLYLKHVDKNWG---GPTLIVVPLSLLHNWMNEFERW-VSPPA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151  1459 LRPLHYFGFPVGREKLRSQIGTTC--NLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIKQLKANHRLI 1536
Cdd:pfam00176   77 LRVVVLHGNKRPQERWKNDPNFLAdfDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151  1537 LSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSRPILASrdaksspkDQEAGVlamEALHRQVLPFLLRRVKEDVLK 1616
Cdd:pfam00176  157 LTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERG--------GGKKGV---SRLHKLLKPFLLRRTKKDVEK 225
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 195446151  1617 DLPPKITQDLLCELSPLQLRLYEDFSKKHLkdcLDKLGDSPGAATGTttstenlngrTHIFQALRYLQNVCNHPKLV 1693
Cdd:pfam00176  226 SLPPKVEYILFCRLSKLQRKLYQTFLLKKD---LNAIKTGEGGREIK----------ASLLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1719-1855 1.05e-42

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: 152.63  E-value: 1.05e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1719 HSAKLPALKQLLLDCGIgvqtesvSQHRALIFCQLKAMLDIVEHDLLRRHlpsVTYLRLDGSVPASQRQDIVNNFNSDPS 1798
Cdd:cd18793     9 VSGKLEALLELLEELRE-------PGEKVLIFSQFTDTLDILEEALRERG---IKYLRLDGSTSSKERQKLVDRFNEDPD 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 195446151 1799 IDVLLLTTLVGGLGLNLTGADTVIFVEHDWNPMKDLQAMDRAHRIGQKKVVNVYRLI 1855
Cdd:cd18793    79 IRVFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXDc smart00487
DEAD-like helicases superfamily;
1376-1565 3.14e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 105.27  E-value: 3.14e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151   1376 ELRGYQQAGINWLWFLNKynlHGILCDDMGLGKTLQtICILAGDHIQRentnQSNLPSLVICP-PTLTGHWVYEVEKFLA 1454
Cdd:smart00487    8 PLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLA-ALLPALEALKR----GKGGRVLVLVPtRELAEQWAEELKKLGP 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151   1455 QSPILRPLhYFGFPVGREKLRSQIGTTCNLVVASYDTVRKDI--DYFSGIHFNYCVLDEGHIIKNGKTKSS--KAIKQL- 1529
Cdd:smart00487   80 SLGLKVVG-LYGGDSKREQLRKLESGKTDILVTTPGRLLDLLenDKLSLSNVDLVILDEAHRLLDGGFGDQleKLLKLLp 158
                           170       180       190
                    ....*....|....*....|....*....|....*....
gi 195446151   1530 KANHRLILSGTP---IQNNVLELWSLFDFLMPGFLGTEK 1565
Cdd:smart00487  159 KNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEP 197
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1721-1844 1.61e-14

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: 71.47  E-value: 1.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151  1721 AKLPALKQLLldcgigvqtESVSQHRALIFCQLKAMLDIvehDLLRRHLpSVTYLRLDGSVPASQRQDIVNNFNSDP--- 1797
Cdd:pfam00271    1 EKLEALLELL---------KKERGGKVLIFSQTKKTLEA---ELLLEKE-GIKVARLHGDLSQEEREEILEDFRKGKidv 67
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 195446151  1798 ---------SIDvlllttlvgglglnLTGADTVIFVEHDWNPMKDLQAMDRAHRIG 1844
Cdd:pfam00271   68 lvatdvaerGLD--------------LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
1758-1844 1.12e-09

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 56.45  E-value: 1.12e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151   1758 DIVEHDLLRRHLPsvtYLRLDGSVPASQRQDIVNNFNSDP------------SIDvlllttlvgglglnLTGADTVIFVE 1825
Cdd:smart00490    1 EELAELLKELGIK---VARLHGGLSQEEREEILDKFNNGKikvlvatdvaerGLD--------------LPGVDLVIIYD 63
                            90
                    ....*....|....*....
gi 195446151   1826 HDWNPMKDLQAMDRAHRIG 1844
Cdd:smart00490   64 LPWSPASYIQRIGRAGRAG 82
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
1337-1541 3.44e-06

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 51.95  E-value: 3.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1337 EQLKSEPLQARKSRDKEFLDYLFNPKTIPDYKVPVTLSVELRGYQQAGIN-WLWFLNKYNLHGILCDDMGLGKTLqTICI 1415
Cdd:COG1061    41 AIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTV-LALA 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1416 LAGDHIQRENTnqsnlpsLVICP-PTLTGHWVYEVEKFLAQSPILRPLHYFGFPVgreklrsqigttcnlVVASYDTV-- 1492
Cdd:COG1061   120 LAAELLRGKRV-------LVLVPrRELLEQWAEELRRFLGDPLAGGGKKDSDAPI---------------TVATYQSLar 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 195446151 1493 RKDIDYFSGiHFNYCVLDEGHiikNGKTKS-SKAIKQLKANHRLILSGTP 1541
Cdd:COG1061   178 RAHLDELGD-RFGLVIIDEAH---HAGAPSyRRILEAFPAAYRLGLTATP 223
 
Name Accession Description Interval E-value
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
1377-1609 2.39e-143

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: 443.33  E-value: 2.39e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAGDHIQREN-TNQSNLPSLVICPPTLTGHWVYEVEKFLAQ 1455
Cdd:cd17999     1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHHKRANsFNSENLPSLVVCPPTLVGHWVAEIKKYFPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1456 SpILRPLHYFGFPVGREKLRSQiGTTCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIKQLKANHRL 1535
Cdd:cd17999    81 A-FLKPLAYVGPPQERRRLREQ-GEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHRL 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 195446151 1536 ILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSRPILASRDAKSSPKDQEAGVLAMEALHRQVLPFLLRR 1609
Cdd:cd17999   159 ILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
1369-1880 1.10e-140

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 454.30  E-value: 1.10e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1369 VPVTLSVELRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAgdHIQRENTNQsnlPSLVICPPTLTGHWVYE 1448
Cdd:COG0553   234 LPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLL--ELKERGLAR---PVLIVAPTSLVGNWQRE 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1449 VEKFLaqsPILRPLHYFGfPVGREKLRSQIGTtCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIKQ 1528
Cdd:COG0553   309 LAKFA---PGLRVLVLDG-TRERAKGANPFED-ADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRA 383
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1529 LKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSRPIlasrdaksSPKDQEagvlAMEALHRQVLPFLLR 1608
Cdd:COG0553   384 LKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPI--------EKGDEE----ALERLRRLLRPFLLR 451
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1609 RVKEDVLKDLPPKITQDLLCELSPLQLRLYEDfskkHLKDCLDKLGDSpgaatgtttstENLNGRTHIFQALRYLQNVCN 1688
Cdd:COG0553   452 RTKEDVLKDLPEKTEETLYVELTPEQRALYEA----VLEYLRRELEGA-----------EGIRRRGLILAALTRLRQICS 516
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1689 HPKLVLRQSEELGpivtqlalsnstlddiEHSAKLPALKQLLldcgigvQTESVSQHRALIFCQLKAMLDIVEHDLLRRH 1768
Cdd:COG0553   517 HPALLLEEGAELS----------------GRSAKLEALLELL-------EELLAEGEKVLVFSQFTDTLDLLEERLEERG 573
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1769 LPsvtYLRLDGSVPASQRQDIVNNFNSDPSIDvlllttlvgglgL------------NLTGADTVIFVEHDWNPMKDLQA 1836
Cdd:COG0553   574 IE---YAYLHGGTSAEERDELVDRFQEGPEAP------------VflislkaggeglNLTAADHVIHYDLWWNPAVEEQA 638
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 195446151 1837 MDRAHRIGQKKVVNVYRLITRNSLEEKIMGLQKFKILTANTVVS 1880
Cdd:COG0553   639 IDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DUF3535 pfam12054
Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. ...
669-1163 1.36e-120

Domain of unknown function (DUF3535); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 439 to 459 amino acids in length. This domain is found associated with pfam00271, pfam02985, pfam00176. This domain has two completely conserved residues (P and K) that may be functionally important.


Pssm-ID: 463447  Cd Length: 445  Bit Score: 388.53  E-value: 1.36e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151   669 VWSNLIQHA-DLGALLNAACPFVSSWICLAMQPPRLAFDSAVLIRACGGGGGVAGDASSTSSRRRIPKLGDDLGGSALAH 747
Cdd:pfam12054    1 VWEALLRSLkPPEALLHAFCPHLSPWLTLLMTPIGVPMDASLLLKPSGQPYSPPERRKSKKKEEPPPSDIPSPGRQGSSS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151   748 SNaTLKLYLGGSEATPLEVreaNFVRARITSSRALGALSHYLvqpapgvvytpQMESPTDCYTKVLLGHLNAHSAVQRIV 827
Cdd:pfam12054   81 HN-VDKPMIGGDVTLVGMD---VVIRTRIAAAKALGLLLSYW-----------PEESPLDFFTKLLLPYLNSPSALQRLL 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151   828 CGLIIAFWALEDE-----PVRPGPPNLQEKLHQCVA---EYFYYDEVAVSLTRLLQETQDFIATL---------KQNKIP 890
Cdd:pfam12054  146 AAIIIEEWAKNCKkekssSVSTLPETLSEKLLEILEnpsRPPYYRELVPYLTRLRTQCQQLLNTFrdvgkvsqsKLPKLA 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151   891 INDFNNA----KILTLDQIEAVAFS-LSENIRHFPLKPKVMDT--LLERRRSLQASYQQTTTEQGSYHVSAQAALAGAIC 963
Cdd:pfam12054  226 VVVQGEPeagpGAFSIEQAEKLVGEdYDKLKKSLSPKQKLLALqqLEDRRRRVQAAIEEAKEAKEQRDVRVLAAAAGALV 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151   964 ALHCLPEKLNPVVKPLMESIKREQCVPLQQLSAEFLVHLMDQVCDRN-PSPNSKILNNLCTLLRSDGDHTPKLIMPFHTv 1042
Cdd:pfam12054  306 ALKGLPKKLNPIIKPLMDSIKKEENEELQQRSADALAHLIDLCVDRGkPGPNDKIVKNLCTFLCVDTSETPEFHPNAKL- 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151  1043 mdtmastvadsncaYYGIVTLTLQQAVKSnstanrgpgsgsttagsgtptaprgpgRPPASEIlanaaaaaatieqsvll 1122
Cdd:pfam12054  385 --------------TDGILTLRKEEDKAD---------------------------HADAAKF----------------- 406
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 195446151  1123 arEAEAKQCRIQRLGSACAITKLCSSFGEHIVEKVPIFEQL 1163
Cdd:pfam12054  407 --EEEAKEARIQRRGAKLALEQLAKKFGASLFEKVPKLWEL 445
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
1376-1611 1.68e-82

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: 270.21  E-value: 1.68e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1376 ELRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICilagdHIQRENTNQSNLPSLVICPPTLTGHWVYEVEKFlaq 1455
Cdd:cd18012     4 TLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLA-----LLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKF--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1456 SPILRPLHYFGfpVGREKLRSQIGTTCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIKQLKANHRL 1535
Cdd:cd18012    76 APELKVLVIHG--TKRKREKLRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRL 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 195446151 1536 ILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSRPILASRDAKsspkdqeagvlAMEALHRQVLPFLLRRVK 1611
Cdd:cd18012   154 ALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEE-----------ALEELKKLISPFILRRLK 218
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
1377-1865 3.82e-80

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 288.24  E-value: 3.82e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAGDHIQRENTNqsnlPSLVICPPTLTGHWVYEVEKFlaqS 1456
Cdd:PLN03142  170 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITG----PHMVVAPKSTLGNWMNEIRRF---C 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1457 PILRPLHYFGFPVGREKLRSQ--IGTTCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIKQLKANHR 1534
Cdd:PLN03142  243 PVLRAVKFHGNPEERAHQREEllVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYR 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1535 LILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSrpilasrdaKSSPKDQEAGVlamEALHRQVLPFLLRRVKEDV 1614
Cdd:PLN03142  323 LLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQ---------ISGENDQQEVV---QQLHKVLRPFLLRRLKSDV 390
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1615 LKDLPPKITQDLLCELSPLQLRLYEDFSKKHLkDCLDKLGDspgaatgtttstenlngRTHIFQALRYLQNVCNHPKLVl 1694
Cdd:PLN03142  391 EKGLPPKKETILKVGMSQMQKQYYKALLQKDL-DVVNAGGE-----------------RKRLLNIAMQLRKCCNHPYLF- 451
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1695 rQSEELGPIVTqlalsnsTLDD-IEHSAKLPALKQLLLDCGigvQTESvsqhRALIFCQLKAMLDIVEHDLLRRHLPsvt 1773
Cdd:PLN03142  452 -QGAEPGPPYT-------TGEHlVENSGKMVLLDKLLPKLK---ERDS----RVLIFSQMTRLLDILEDYLMYRGYQ--- 513
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1774 YLRLDGSVPASQRQDIVNNFNSDPSIDVLLLTTLVGGLG-LNLTGADTVIFVEHDWNPMKDLQAMDRAHRIGQKKVVNVY 1852
Cdd:PLN03142  514 YCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLgINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVF 593
                         490
                  ....*....|...
gi 195446151 1853 RLITRNSLEEKIM 1865
Cdd:PLN03142  594 RFCTEYTIEEKVI 606
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
1380-1693 2.35e-74

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: 249.91  E-value: 2.35e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151  1380 YQQAGINWLWFL-NKYNLHGILCDDMGLGKTLQTICILAGDHIQRENTNqsnLPSLVICPPTLTGHWVYEVEKFlAQSPI 1458
Cdd:pfam00176    1 YQIEGVNWMLSLeNNLGRGGILADEMGLGKTLQTISLLLYLKHVDKNWG---GPTLIVVPLSLLHNWMNEFERW-VSPPA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151  1459 LRPLHYFGFPVGREKLRSQIGTTC--NLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIKQLKANHRLI 1536
Cdd:pfam00176   77 LRVVVLHGNKRPQERWKNDPNFLAdfDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151  1537 LSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSRPILASrdaksspkDQEAGVlamEALHRQVLPFLLRRVKEDVLK 1616
Cdd:pfam00176  157 LTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERG--------GGKKGV---SRLHKLLKPFLLRRTKKDVEK 225
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 195446151  1617 DLPPKITQDLLCELSPLQLRLYEDFSKKHLkdcLDKLGDSPGAATGTttstenlngrTHIFQALRYLQNVCNHPKLV 1693
Cdd:pfam00176  226 SLPPKVEYILFCRLSKLQRKLYQTFLLKKD---LNAIKTGEGGREIK----------ASLLNILMRLRKICNHPGLI 289
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
1377-1561 2.57e-63

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: 213.58  E-value: 2.57e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAGdHIQRENTNQsnlPSLVICPPTLTGHWVYEVEKFLaqs 1456
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAY-LLKEGKERG---PVLVVCPLSVLENWEREFEKWT--- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1457 PILRPLHYFGFPVGREKLRSQIG-TTCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIKQLKANHRL 1535
Cdd:cd17919    74 PDLRVVVYHGSQRERAQIRAKEKlDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRL 153
                         170       180
                  ....*....|....*....|....*.
gi 195446151 1536 ILSGTPIQNNVLELWSLFDFLMPGFL 1561
Cdd:cd17919   154 LLTGTPLQNNLEELWALLDFLDPPFL 179
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
1380-1609 4.06e-58

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: 201.06  E-value: 4.06e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1380 YQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAGDHiQRENTNQSnlpsLVICPPTLTGHWVYEVEKFlaqSPIL 1459
Cdd:cd18001     4 HQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMF-DSGLIKSV----LVVMPTSLIPHWVKEFAKW---TPGL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1460 RPLHYFGF-PVGREKLRSQIGTTCNLVVASYDTVRKDIDYFS-----GIHFNYCVLDEGHIIKNGKTKSSKAIKQLKANH 1533
Cdd:cd18001    76 RVKVFHGTsKKERERNLERIQRGGGVLLTTYGMVLSNTEQLSaddhdEFKWDYVILDEGHKIKNSKTKSAKSLREIPAKN 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 195446151 1534 RLILSGTPIQNNVLELWSLFDFLMPG-FLGTEKQFIQRFSRPILASRDAKSSPKDQEAGVLAMEALHRQVLPFLLRR 1609
Cdd:cd18001   156 RIILTGTPIQNNLKELWALFDFACNGsLLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQIIKPYFLRR 232
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
1377-1611 1.21e-52

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: 185.28  E-value: 1.21e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAgdHIqRENtnQSNLPSLVICPPTLTGHWVYEVEKFLAQS 1456
Cdd:cd18009     4 MRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLA--HL-RER--GVWGPFLVIAPLSTLPNWVNEFARFTPSV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1457 PILRplhYFGFPVGREKLRSQI------GTTCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIKQLK 1530
Cdd:cd18009    79 PVLL---YHGTKEERERLRKKImkregtLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1531 ANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRF--SRPILASRDAKSSPKDQEAGVLAMeaLHRQVLPFLLR 1608
Cdd:cd18009   156 SDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFdfSSLSDNAADISNLSEEREQNIVHM--LHAILKPFLLR 233

                  ...
gi 195446151 1609 RVK 1611
Cdd:cd18009   234 RLK 236
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
1380-1561 9.09e-51

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: 178.29  E-value: 9.09e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1380 YQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAGDHiqreNTNQSNLPSLVICPPTLTGHWVYEVEKFLaqsPIL 1459
Cdd:cd18000     4 YQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALH----HSKLGLGPSLIVCPATVLKQWVKEFHRWW---PPF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1460 RP--LH----------YFGFPVGREKLRSQIGTTCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIK 1527
Cdd:cd18000    77 RVvvLHssgsgtgseeKLGSIERKSQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACK 156
                         170       180       190
                  ....*....|....*....|....*....|....
gi 195446151 1528 QLKANHRLILSGTPIQNNVLELWSLFDFLMPGFL 1561
Cdd:cd18000   157 QLRTPHRLILSGTPIQNNLKELWSLFDFVFPPYL 190
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
1377-1609 8.01e-49

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: 173.69  E-value: 8.01e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAgdHIQRENTNQSnlPSLVICPPTLTGHWVYEVEKFLaqs 1456
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLA--HLACEKGNWG--PHLIVVPTSVMLNWEMEFKRWC--- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1457 PILRPLHYFGFPVGREKLRSqiG----TTCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIKQLKAN 1532
Cdd:cd18003    74 PGFKILTYYGSAKERKLKRQ--GwmkpNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQ 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 195446151 1533 HRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSRPIlasrDAKSSPKDQEAGVLaMEALHRQVLPFLLRR 1609
Cdd:cd18003   152 RRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPL----TAMSEGSQEENEEL-VRRLHKVLRPFLLRR 223
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
1377-1609 5.83e-47

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: 169.00  E-value: 5.83e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLW----FLNKYNLHG-ILCDDMGLGKTLQTICILAGDHIQRENTNQSNLPSLVICPPTLTGHWVYEVEK 1451
Cdd:cd18004     1 LRPHQREGVQFLYdcltGRRGYGGGGaILADEMGLGKTLQAIALVWTLLKQGPYGKPTAKKALIVCPSSLVGNWKAEFDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1452 FLAqspiLRPLHYFGFPVGREKLRSQI-----GTTCNLVVASYDTVRKDID-YFSGIHFNYCVLDEGHIIKNGKTKSSKA 1525
Cdd:cd18004    81 WLG----LRRIKVVTADGNAKDVKASLdffssASTYPVLIISYETLRRHAEkLSKKISIDLLICDEGHRLKNSESKTTKA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1526 IKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSRPILASRDAKSSPKDQEAGVLAMEALHRQVLPF 1605
Cdd:cd18004   157 LNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELTSRF 236

                  ....
gi 195446151 1606 LLRR 1609
Cdd:cd18004   237 ILRR 240
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
1377-1611 1.22e-45

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: 165.23  E-value: 1.22e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAgdHIQRENTNQSnlPSLVICP-PTLTGhWVYEVEKFLaq 1455
Cdd:cd17996     4 LKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLIT--YLMEKKKNNG--PYLVIVPlSTLSN-WVSEFEKWA-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1456 sPILRPLHYFGFPVGREKLRSQIGTT-CNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIKQ-LKANH 1533
Cdd:cd17996    77 -PSVSKIVYKGTPDVRKKLQSQIRAGkFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyYHARY 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 195446151 1534 RLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSRPILASRDAKSSPKDQEAGVLAMEALHRQVLPFLLRRVK 1611
Cdd:cd17996   156 RLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVKIELNEEETLLIIRRLHKVLRPFLLRRLK 233
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
1377-1609 6.59e-45

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: 163.32  E-value: 6.59e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILA------GDHIQREN----------TNQSNLPSLVICPPT 1440
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAavlgktGTRRDRENnrprfkkkppASSAKKPVLIVAPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1441 LTGHWVYEVEKFlaqspilrplHYF-----------GFPVGREKLRSqigttCNLVVASYDTVRKDIDYFSGIHFNYCVL 1509
Cdd:cd18005    81 VLYNWKDELDTW----------GHFevgvyhgsrkdDELEGRLKAGR-----LEVVVTTYDTLRRCIDSLNSINWSAVIA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1510 DEGHIIKNGKTKSSKAIKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSRPILASRDAKSSPKDQE 1589
Cdd:cd18005   146 DEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELR 225
                         250       260
                  ....*....|....*....|
gi 195446151 1590 AGVLAMEALHRQVLPFLLRR 1609
Cdd:cd18005   226 LGRKRKQELAVKLSKFFLRR 245
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
1376-1611 3.74e-43

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: 157.48  E-value: 3.74e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1376 ELRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAgdhIQRENTNQSNlPSLVICPPTLTGHWVYEVEKFLaq 1455
Cdd:cd17997     3 TMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLG---YLKHYKNING-PHLIIVPKSTLDNWMREFKRWC-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1456 sPILRPLHYFGFPVGREK-LRSQIGT-TCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIKQLKANH 1533
Cdd:cd17997    77 -PSLRVVVLIGDKEERADiIRDVLLPgKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRN 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 195446151 1534 RLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFsrpilaSRDAKSSPKDQeagvlAMEALHRQVLPFLLRRVK 1611
Cdd:cd17997   156 RLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWF------NVNNCDDDNQE-----VVQRLHKVLRPFLLRRIK 222
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
1377-1609 6.86e-43

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: 157.45  E-value: 6.86e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLwflnkynLH--GILCDDMGLGKTLQTI-CILAGDHIQRENTNQSNLPS------------LVICPPTL 1441
Cdd:cd18008     1 LLPYQKQGLAWM-------LPrgGILADEMGLGKTIQALaLILATRPQDPKIPEELEENSsdpkklylskttLIVVPLSL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1442 TGHWVYEVEKFLaQSPILRPLHYFGFPVGR--EKLRSqigttCNLVVASYDTVRKDIDYFSG----------------IH 1503
Cdd:cd18008    74 LSQWKDEIEKHT-KPGSLKVYVYHGSKRIKsiEELSD-----YDIVITTYGTLASEFPKNKKgggrdskekeasplhrIR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1504 FNYCVLDEGHIIKNGKTKSSKAIKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSRPILASRDAks 1583
Cdd:cd18008   148 WYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRK-- 225
                         250       260
                  ....*....|....*....|....*.
gi 195446151 1584 spkdqeagvlAMEALHRQVLPFLLRR 1609
Cdd:cd18008   226 ----------ALERLQALLKPILLRR 241
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1719-1855 1.05e-42

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: 152.63  E-value: 1.05e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1719 HSAKLPALKQLLLDCGIgvqtesvSQHRALIFCQLKAMLDIVEHDLLRRHlpsVTYLRLDGSVPASQRQDIVNNFNSDPS 1798
Cdd:cd18793     9 VSGKLEALLELLEELRE-------PGEKVLIFSQFTDTLDILEEALRERG---IKYLRLDGSTSSKERQKLVDRFNEDPD 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 195446151 1799 IDVLLLTTLVGGLGLNLTGADTVIFVEHDWNPMKDLQAMDRAHRIGQKKVVNVYRLI 1855
Cdd:cd18793    79 IRVFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
1377-1609 1.88e-41

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: 152.79  E-value: 1.88e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFlNKYNLHG-ILCDDMGLGKTLQTICILagDHI-QRENTNQsnlPSLVICPPTLTGHWVYEVEKFLA 1454
Cdd:cd17995     1 LRDYQLEGVNWLLF-NWYNRRNcILADEMGLGKTIQSIAFL--EHLyQVEGIRG---PFLVIAPLSTIPNWQREFETWTD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1455 QSPI----------LRPLHYFGFPVGREKLRSQIGTTcNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSK 1524
Cdd:cd17995    75 MNVVvyhgsgesrqIIQQYEMYFKDAQGRKKKGVYKF-DVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1525 AIKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSrpilasrDAKSSpkDQeagvlaMEALHRQVLP 1604
Cdd:cd17995   154 GLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFG-------DLKTA--EQ------VEKLQALLKP 218

                  ....*
gi 195446151 1605 FLLRR 1609
Cdd:cd17995   219 YMLRR 223
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
1377-1609 3.88e-41

DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 chromatin remodeling complex. INO80 removes histone H3-containing nucleosomes from associated chromatin, promotes CENP-ACnp1 chromatin assembly at the centromere in a redundant manner with another chromatin-remodeling factor Chd1Hrp1. INO80 mutants have severe defects in oxygen consumption and promiscuous cell division that is no longer coupled with metabolic status. INO80 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350760 [Multi-domain]  Cd Length: 229  Bit Score: 151.89  E-value: 3.88e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAgdHIQRENtnqsNL--PSLVICPPTLTGHWVYEVEKFLa 1454
Cdd:cd18002     1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLA--HLAEEH----NIwgPFLVIAPASTLHNWQQEISRFV- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1455 qsPILRPLHYFGFPVGREKLRSQIG--------TTCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAI 1526
Cdd:cd18002    74 --PQFKVLPYWGNPKDRKVLRKFWDrknlytrdAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1527 KQLKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSRPILASRDAKSSPKDQEagvlaMEALHRQVLPFL 1606
Cdd:cd18002   152 LSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENKTGLNEHQ-----LKRLHMILKPFM 226

                  ...
gi 195446151 1607 LRR 1609
Cdd:cd18002   227 LRR 229
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
1377-1570 3.17e-40

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: 147.92  E-value: 3.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAgdHIQRENtnqSNLPSLVICPPTLTGHWVYEVEKFlaqS 1456
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLA--YLKEIG---IPGPHLVVVPSSTLDNWLREFKRW---C 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1457 PILRPLHYFGFPVGREKLRSQ----------IGTTCNLVVASYDtvrkDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAI 1526
Cdd:cd17998    73 PSLKVEPYYGSQEERKHLRYDilkgledfdvIVTTYNLATSNPD----DRSFFKRLKLNYVVYDEGHMLKNMTSERYRHL 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 195446151 1527 KQLKANHRLILSGTPIQNNVLELWSLFDFLMPgflgteKQFIQR 1570
Cdd:cd17998   149 MTINANFRLLLTGTPLQNNLLELMSLLNFIMP------KPFILR 186
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
1376-1621 1.74e-39

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: 147.89  E-value: 1.74e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1376 ELRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAGDHIQRENTNqsnlPSLVICPPTLTGHWVYEVEKFLaq 1455
Cdd:cd18064    15 KLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPG----PHMVLVPKSTLHNWMAEFKRWV-- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1456 sPILRPLHYFGFPVGREKLRSQI--GTTCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIKQLKANH 1533
Cdd:cd18064    89 -PTLRAVCLIGDKDQRAAFVRDVllPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTN 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1534 RLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFsrpilasrDAKSSPKDQEagvlAMEALHRQVLPFLLRRVKED 1613
Cdd:cd18064   168 RLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWF--------DTNNCLGDQK----LVERLHMVLRPFLLRRIKAD 235

                  ....*...
gi 195446151 1614 VLKDLPPK 1621
Cdd:cd18064   236 VEKSLPPK 243
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
1376-1609 2.00e-38

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: 143.65  E-value: 2.00e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1376 ELRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAgdhiQRENTNQSNLPSLVICPPTLTGHWVYEVEKFLaq 1455
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLS----YLFHSQQQYGPFLVVVPLSTMPAWQREFAKWA-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1456 sPILRPLHYFGFPVGREKLR----SQIGTT---CNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIKQ 1528
Cdd:cd17993    75 -PDMNVIVYLGDIKSRDTIReyefYFSQTKklkFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1529 LKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFiqrfsrpilasrdAKSSPKDQEAGVlamEALHRQVLPFLLR 1608
Cdd:cd17993   154 FKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEF-------------EEEHDEEQEKGI---ADLHKELEPFILR 217

                  .
gi 195446151 1609 R 1609
Cdd:cd17993   218 R 218
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
1377-1609 7.73e-38

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: 142.19  E-value: 7.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWL--WFLNKYNlhGILCDDMGLGKTLQTIC---ILAGdhiqRENTNQsnlPSLVICPPTLTGHWVYEVEK 1451
Cdd:cd18006     1 LRPYQLEGVNWLlqCRAEQHG--CILGDEMGLGKTCQTISllwYLAG----RLKLLG---PFLVLCPLSVLDNWKEELNR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1452 FlaqSPILRPLHYFGFPVGREKLRSQIGTTC--NLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIKQL 1529
Cdd:cd18006    72 F---APDLSVITYMGDKEKRLDLQQDIKSTNrfHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1530 KANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEK--QFIQRFsrpilasrdaksspKDQEAGVLAMEALHRQVLPFLL 1607
Cdd:cd18006   149 SVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKldDFIKAY--------------SETDDESETVEELHLLLQPFLL 214

                  ..
gi 195446151 1608 RR 1609
Cdd:cd18006   215 RR 216
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
1377-1611 6.92e-35

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: 134.81  E-value: 6.92e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAgdhiQRENTNQSNLPSLVICPPTLTGHWVYEVEKFlaqS 1456
Cdd:cd18063    24 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALIT----YLMEHKRLNGPYLIIVPLSTLSNWTYEFDKW---A 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1457 PILRPLHYFGFPVGREKLRSQIGT-TCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIK-QLKANHR 1534
Cdd:cd18063    97 PSVVKISYKGTPAMRRSLVPQLRSgKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPRR 176
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 195446151 1535 LILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSRPILASrdAKSSPKDQEAGVLAMEALHRQVLPFLLRRVK 1611
Cdd:cd18063   177 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMT--GERVDLNEEETILIIRRLHKVLRPFLLRRLK 251
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
1377-1611 7.61e-35

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: 133.99  E-value: 7.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAGDHIQRENTNqsnlPSLVICPPTLTGHWVYEVEKFLaqs 1456
Cdd:cd18065    16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPG----PHMVLVPKSTLHNWMNEFKRWV--- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1457 PILRPLHYFGFPVGREKL--RSQIGTTCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIKQLKANHR 1534
Cdd:cd18065    89 PSLRAVCLIGDKDARAAFirDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNR 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 195446151 1535 LILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFsrpilasrDAKSSPKDQEagvlAMEALHRQVLPFLLRRVK 1611
Cdd:cd18065   169 LLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF--------DTKNCLGDQK----LVERLHAVLKPFLLRRIK 233
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
1376-1611 8.57e-35

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: 134.40  E-value: 8.57e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1376 ELRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAgdhiQRENTNQSNLPSLVICPPTLTGHWVYEVEKFlaq 1455
Cdd:cd18062    23 VLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALIT----YLMEHKRINGPFLIIVPLSTLSNWVYEFDKW--- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1456 SPILRPLHYFGFPVGREKLRSQIGT-TCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIK-QLKANH 1533
Cdd:cd18062    96 APSVVKVSYKGSPAARRAFVPQLRSgKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPR 175
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 195446151 1534 RLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSRPILASrdAKSSPKDQEAGVLAMEALHRQVLPFLLRRVK 1611
Cdd:cd18062   176 RLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMT--GEKVDLNEEETILIIRRLHKVLRPFLLRRLK 251
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
1377-1589 1.53e-34

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: 133.19  E-value: 1.53e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWflnkYNLHG-----------ILCDDMGLGKTLQTICIL---AGDHIQRENTnqsnlpsLVICPPTLT 1442
Cdd:cd18007     1 LKPHQVEGVRFLW----SNLVGtdvgsdegggcILAHTMGLGKTLQVITFLhtyLAAAPRRSRP-------LVLCPASTL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1443 GHWVYEVEKFLAQSPILRPLHYFGFPVGREKLRSQ-------------IGTTCNLVVASYDTVRKDI--DYFSGIHFNYC 1507
Cdd:cd18007    70 YNWEDEFKKWLPPDLRPLLVLVSLSASKRADARLRkinkwhkeggvllIGYELFRNLASNATTDPRLkqEFIAALLDPGP 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1508 ---VLDEGHIIKNGKTKSSKAIKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSRPILASRDAKSS 1584
Cdd:cd18007   150 dllVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDST 229

                  ....*
gi 195446151 1585 PKDQE 1589
Cdd:cd18007   230 EEDVR 234
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
1377-1609 7.41e-34

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: 131.44  E-value: 7.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLW----FLNKYNLHG-ILCDDMGLGKTLQTICILAGDHIQRENTNQSNLPSLVICPPTLTGHWVYEVEK 1451
Cdd:cd18067     1 LRPHQREGVKFLYrcvtGRRIRGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIDKAIVVSPSSLVKNWANELGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1452 FL------------AQSPILRPLHYFGFPVGReklrsQIGTTcnLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGK 1519
Cdd:cd18067    81 WLggrlqplaidggSKKEIDRKLVQWASQQGR-----RVSTP--VLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1520 TKSSKAIKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSRPILASRDAKSSPKDQEAGVLAMEALH 1599
Cdd:cd18067   154 NQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELI 233
                         250
                  ....*....|
gi 195446151 1600 RQVLPFLLRR 1609
Cdd:cd18067   234 SIVNRCIIRR 243
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
1377-1609 2.37e-31

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: 124.19  E-value: 2.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLW--FLNKYNLHG---ILCDDMGLGKTLQTICILAGdhIQRENTNQSNlP----SLVICPPTLTGHWVY 1447
Cdd:cd18066     1 LRPHQREGIEFLYecVMGMRVNERfgaILADEMGLGKTLQCISLIWT--LLRQGPYGGK-PvikrALIVTPGSLVKNWKK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1448 EVEKFLAQSPILRplhyfgFPVGRE-KLRSQIGTTC-NLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKA 1525
Cdd:cd18066    78 EFQKWLGSERIKV------FTVDQDhKVEEFIASPLySVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1526 IKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSRPILASRDAKSSPKDQEAGVLAMEALHRQVLPF 1605
Cdd:cd18066   152 LTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARAAELTRLTGLF 231

                  ....
gi 195446151 1606 LLRR 1609
Cdd:cd18066   232 ILRR 235
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
1361-1609 6.31e-29

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: 117.03  E-value: 6.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1361 PKTIPDYKVPVTL---SVELRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAGDHIQrentNQSNLPSLVIC 1437
Cdd:cd18054     2 PRFVALKKQPSYIggeNLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQ----HQLYGPFLLVV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1438 PPTLTGHWVYEVEKFlaqSPILRPLHYFGFPVGREKLRSQIGT-------TCNLVVASYDTVRKDIDYFSGIHFNYCVLD 1510
Cdd:cd18054    78 PLSTLTSWQREFEIW---APEINVVVYIGDLMSRNTIREYEWIhsqtkrlKFNALITTYEILLKDKTVLGSINWAFLGVD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1511 EGHIIKNGKTKSSKAIKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFiqrfsrpilasrdAKSSPKDQEA 1590
Cdd:cd18054   155 EAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDF-------------EEDHGKGREN 221
                         250
                  ....*....|....*....
gi 195446151 1591 GvlaMEALHRQVLPFLLRR 1609
Cdd:cd18054   222 G---YQSLHKVLEPFLLRR 237
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
1380-1556 2.06e-28

DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called Forkhead-box E1/FOXE1 ) is a transcription termination factor that couples ATP hydrolysis with the removal of RNA polymerase II from the DNA template. Single nucleotide polymorphism (SNP) within the 5'-UTR of TTF2 is associated with thyroid cancer risk.TTF2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 115.66  E-value: 2.06e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1380 YQQAGINWL-WFLNKYNLHGILCDDMGLGKTLQTIC-ILAGDHIQR--------------ENTNQSNLPS---LVICPPT 1440
Cdd:cd18072     4 HQKQALAWLlWRERQKPRGGILADDMGLGKTLTMIAlILAQKNTQNrkeeekekalteweSKKDSTLVPSagtLVVCPAS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1441 LTGHWVYEVEKFLAQSpILRPLHYFGfpVGREKlRSQIGTTCNLVVASYDTVRKDIDYFS---------GIHFNYCVLDE 1511
Cdd:cd18072    84 LVHQWKNEVESRVASN-KLRVCLYHG--PNRER-IGEVLRDYDIVITTYSLVAKEIPTYKeesrssplfRIAWARIILDE 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 195446151 1512 GHIIKNGKTKSSKAIKQLKANHRLILSGTPIQNNVLELWSLFDFL 1556
Cdd:cd18072   160 AHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFL 204
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
1377-1587 3.85e-28

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: 114.53  E-value: 3.85e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLW-----FLNKYN----LHGILCDDMGLGKTLQTICILagDHIQRENTNQSnlpSLVICPPTLTGHWVY 1447
Cdd:cd18069     1 LKPHQIGGIRFLYdniieSLERYKgssgFGCILAHSMGLGKTLQVISFL--DVLLRHTGAKT---VLAIVPVNTLQNWLS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1448 EVEKFL---AQSPILRPLHYFGFPVG--------REKLRSQIGTTCNLVVASYDTVR----KDIdyfsgihfnyCVLDEG 1512
Cdd:cd18069    76 EFNKWLpppEALPNVRPRPFKVFILNdehkttaaRAKVIEDWVKDGGVLLMGYEMFRlrpgPDV----------VICDEG 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 195446151 1513 HIIKNGKTKSSKAIKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSRPILASRDAKSSPKD 1587
Cdd:cd18069   146 HRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCVDSTPQD 220
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
1399-1570 5.19e-28

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: 113.45  E-value: 5.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1399 ILCDDMGLGKTLQTICILAgdhiqrenTNQSNLPSLVICPPTLTGHWVYEVEKFLaqsPILRPLHYFGFPVGREKLRSQI 1478
Cdd:cd18010    20 LIADEMGLGKTVQAIAIAA--------YYREEWPLLIVCPSSLRLTWADEIERWL---PSLPPDDIQVIVKSKDGLRDGD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1479 GTtcnLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIKQL--KANHRLILSGTPIQNNVLELWSLFDFL 1556
Cdd:cd18010    89 AK---VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLlkRAKRVILLSGTPALSRPIELFTQLDAL 165
                         170
                  ....*....|....
gi 195446151 1557 MPGFLGTEKQFIQR 1570
Cdd:cd18010   166 DPKLFGRFHDFGRR 179
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
1361-1609 3.14e-27

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: 112.07  E-value: 3.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1361 PKTIPDYKVPVTL----SVELRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILagDHIQRENtnQSNLPSLVI 1436
Cdd:cd18053     1 PRFVALKKQPSYIggheGLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFL--NYLFHEH--QLYGPFLLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1437 CPPTLTGHWVYEVEKFlaqSPILRPLHYFGFPVGREKLRSQ-------IGTTCNLVVASYDTVRKDIDYFSGIHFNYCVL 1509
Cdd:cd18053    77 VPLSTLTSWQREIQTW---APQMNAVVYLGDINSRNMIRTHewmhpqtKRLKFNILLTTYEILLKDKSFLGGLNWAFIGV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1510 DEGHIIKNGKTKSSKAIKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSrpilasrdaksspKDQE 1589
Cdd:cd18053   154 DEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHG-------------KGRE 220
                         250       260
                  ....*....|....*....|
gi 195446151 1590 AGvlaMEALHRQVLPFLLRR 1609
Cdd:cd18053   221 YG---YASLHKELEPFLLRR 237
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
1398-1575 1.88e-26

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: 109.87  E-value: 1.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1398 GILCDDMGLGKTLQTICILAGDhiqrentnqsnlPSLVICPPTLTGHWVYEVEKFLAQSpILRPLHYFGFPVGRE--KLR 1475
Cdd:cd18071    51 GILADDMGLGKTLTTISLILAN------------FTLIVCPLSVLSNWETQFEEHVKPG-QLKVYTYHGGERNRDpkLLS 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1476 SQigttcNLVVASYDTVRKDIDY-----FSGIHFNYCVLDEGHIIKNGKTKSSKAIKQLKANHRLILSGTPIQNNVLELW 1550
Cdd:cd18071   118 KY-----DIVLTTYNTLASDFGAkgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLG 192
                         170       180
                  ....*....|....*....|....*
gi 195446151 1551 SLFDFLMPGFLGTEKQFIQRFSRPI 1575
Cdd:cd18071   193 SLLSFLHLKPFSNPEYWRRLIQRPL 217
DEXDc smart00487
DEAD-like helicases superfamily;
1376-1565 3.14e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 105.27  E-value: 3.14e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151   1376 ELRGYQQAGINWLWFLNKynlHGILCDDMGLGKTLQtICILAGDHIQRentnQSNLPSLVICP-PTLTGHWVYEVEKFLA 1454
Cdd:smart00487    8 PLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLA-ALLPALEALKR----GKGGRVLVLVPtRELAEQWAEELKKLGP 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151   1455 QSPILRPLhYFGFPVGREKLRSQIGTTCNLVVASYDTVRKDI--DYFSGIHFNYCVLDEGHIIKNGKTKSS--KAIKQL- 1529
Cdd:smart00487   80 SLGLKVVG-LYGGDSKREQLRKLESGKTDILVTTPGRLLDLLenDKLSLSNVDLVILDEAHRLLDGGFGDQleKLLKLLp 158
                           170       180       190
                    ....*....|....*....|....*....|....*....
gi 195446151   1530 KANHRLILSGTP---IQNNVLELWSLFDFLMPGFLGTEK 1565
Cdd:smart00487  159 KNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEP 197
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
1377-1609 2.07e-23

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: 100.50  E-value: 2.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFlNKYNLHG-ILCDDMGLGKTLQTICILAGDHIQRENTnqsnlPSLVICPPTLTGHWVYEVEKFLAQ 1455
Cdd:cd18058     1 LREYQLEGMNWLLF-NWYNRKNcILADEMGLGKTIQSITFLSEIFLMGIRG-----PFLIIAPLSTITNWEREFRTWTEM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1456 SPILrplhYFGFPVGREKL-------RSQIGTTC------NLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKS 1522
Cdd:cd18058    75 NAIV----YHGSQISRQMIqqyemyyRDEQGNPLsgifkfQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1523 SKAIKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSrpilasrDAKSspkdqEAGVLAMEALHRqv 1602
Cdd:cd18058   151 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFG-------DLKT-----EEQVKKLQSILK-- 216

                  ....*..
gi 195446151 1603 lPFLLRR 1609
Cdd:cd18058   217 -PMMLRR 222
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
1377-1587 9.29e-23

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: 99.58  E-value: 9.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLW---------FLNKYNLHGILCDDMGLGKTLQTICILagdHIQRENTNQSNLPS-LVICPPTLTGHWV 1446
Cdd:cd18068     1 LKPHQVDGVQFMWdccceslkkTKKSPGSGCILAHCMGLGKTLQVVTFL---HTVLLCEKLENFSRvLVVCPLNTVLNWL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1447 YEVEKFLA-------------------QSPILRPLHYF--------GF-----------PVGREKLRSQIGTTcnLVVAS 1488
Cdd:cd18068    78 NEFEKWQEglkdeekievnelatykrpQERSYKLQRWQeeggvmiiGYdmyrilaqernVKSREKLKEIFNKA--LVDPG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1489 YDTVrkdidyfsgihfnycVLDEGHIIKNGKTKSSKAIKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFI 1568
Cdd:cd18068   156 PDFV---------------VCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFR 220
                         250
                  ....*....|....*....
gi 195446151 1569 QRFSRPILASRDAKSSPKD 1587
Cdd:cd18068   221 NRFVNPIQNGQCADSTLVD 239
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
1377-1558 1.23e-22

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: 99.34  E-value: 1.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLwflnkYNLHGILCDDMGLGKTLQTI-CILA--------------------GDHIQRENTNQSNLPSLV 1435
Cdd:cd18070     1 LLPYQRRAVNWM-----LVPGGILADEMGLGKTVEVLaLILLhprpdndldaadddsdemvcCPDCLVAETPVSSKATLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1436 ICPPTLTGHWVYEVEKFLAQSpiLRPLHYFGFP-VGREKLRS-QIGTTCNLVVASYDTVRKDIDY--------------- 1498
Cdd:cd18070    76 VCPSAILAQWLDEINRHVPSS--LKVLTYQGVKkDGALASPApEILAEYDIVVTTYDVLRTELHYaeanrsnrrrrrqkr 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 195446151 1499 -------FSGIHFNYCVLDEGHIIKNGKTKSSKAIKQLKANHRLILSGTPIQNNVLELWSLFDFLMP 1558
Cdd:cd18070   154 yeappspLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGV 220
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
1377-1609 3.18e-22

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: 97.05  E-value: 3.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFlNKYNLHG-ILCDDMGLGKTLQTICILagdhiQRENTNQSNLPSLVICPPTLTGHWVYEVEKFLAQ 1455
Cdd:cd18060     1 LREYQLEGVNWLLF-NWYNRQNcILADEMGLGKTIQSIAFL-----QEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1456 SPILrplhYFGFPVGREKLRsQIGTTC--------------NLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTK 1521
Cdd:cd18060    75 NTIV----YHGSLASRQMIQ-QYEMYCkdsrgrlipgaykfDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1522 SSKAIKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSrpilasrDAKSSPKDQEagvlameaLHRQ 1601
Cdd:cd18060   150 LLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG-------DLKTEEQVQK--------LQAI 214

                  ....*...
gi 195446151 1602 VLPFLLRR 1609
Cdd:cd18060   215 LKPMMLRR 222
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
1377-1609 4.26e-22

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: 95.97  E-value: 4.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAGdhIQRENTNQSnlPSLVICPPTLTGHWVYEVEKFlaqS 1456
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYS--LYKEGHSKG--PFLVSAPLSTIINWEREFEMW---A 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1457 PILRPLHYFGFPVgreklrsqigttcnlVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKSSKAIKQLKANHRLI 1536
Cdd:cd17994    74 PDFYVVTYVGDHV---------------LLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLL 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 195446151 1537 LSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFsrpilasrdAKSSPKDQeagvlaMEALHRQVLPFLLRR 1609
Cdd:cd17994   139 LTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEF---------ADISKEDQ------IKKLHDLLGPHMLRR 196
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
1377-1609 2.57e-21

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: 95.08  E-value: 2.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAGdhIQRENTNQSnlPSLVICPPTLTGHWVYEVEKFlaqS 1456
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYS--LYKEGHTKG--PFLVSAPLSTIINWEREFQMW---A 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1457 PILRPLHYFGFPVGRE---------------------KLRSQIGTTCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHII 1515
Cdd:cd18055    74 PDFYVVTYTGDKDSRAiirenefsfddnavkggkkafKMKREAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1516 KNGKTKSSKAIKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFsrpilasrdAKSSPKDQeagvlaM 1595
Cdd:cd18055   154 KNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF---------ADISKEDQ------I 218
                         250
                  ....*....|....
gi 195446151 1596 EALHRQVLPFLLRR 1609
Cdd:cd18055   219 KKLHDLLGPHMLRR 232
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
1377-1609 8.83e-21

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: 93.17  E-value: 8.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFlNKYNLHG-ILCDDMGLGKTLQTICILAGDHIQRENTnqsnlPSLVICPPTLTGHWVYEVEKFLAQ 1455
Cdd:cd18059     1 LREYQLEGVNWLLF-NWYNTRNcILADEMGLGKTIQSITFLYEIYLKGIHG-----PFLVIAPLSTIPNWEREFRTWTEL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1456 SPILrplhYFGFPVGREKLRS-------------QIGTTCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTKS 1522
Cdd:cd18059    75 NVVV----YHGSQASRRTIQLyemyfkdpqgrviKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1523 SKAIKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFSrpilasrDAKSSPKDQEagvlameaLHRQV 1602
Cdd:cd18059   151 LEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG-------DLKTEEQVQK--------LQAIL 215

                  ....*..
gi 195446151 1603 LPFLLRR 1609
Cdd:cd18059   216 KPMMLRR 222
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
1377-1609 1.93e-20

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: 92.44  E-value: 1.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAGDHIQrentNQSNLPSLVICPPTLTGHWVYEVEKFlaqS 1456
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKE----GHSKGPYLVSAPLSTIINWEREFEMW---A 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1457 PILRPLHYFGFPVGRE---------------------KLRSQIGTTCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHII 1515
Cdd:cd18057    74 PDFYVVTYTGDKESRSvirenefsfednairsgkkvfRMKKEAQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1516 KNGKTKSSKAIKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFsrpilasrdAKSSPKDQeagvlaM 1595
Cdd:cd18057   154 KNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF---------ADISKEDQ------I 218
                         250
                  ....*....|....
gi 195446151 1596 EALHRQVLPFLLRR 1609
Cdd:cd18057   219 KKLHDLLGPHMLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
1377-1609 1.01e-19

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: 90.12  E-value: 1.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFLNKYNLHGILCDDMGLGKTLQTICILAGDHIQrentNQSNLPSLVICPPTLTGHWVYEVEKFlaqS 1456
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKE----GHSKGPFLVSAPLSTIINWEREFEMW---A 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1457 PILRPLHYFGFPVGR---------------------EKLRSQIGTTCNLVVASYDTVRKDIDYFSGIHFNYCVLDEGHII 1515
Cdd:cd18056    74 PDMYVVTYVGDKDSRaiirenefsfednairggkkaSRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1516 KNGKTKSSKAIKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRFsrpilasrdAKSSPKDQeagvlaM 1595
Cdd:cd18056   154 KNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEF---------ADIAKEDQ------I 218
                         250
                  ....*....|....
gi 195446151 1596 EALHRQVLPFLLRR 1609
Cdd:cd18056   219 KKLHDMLGPHMLRR 232
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
1377-1571 7.91e-19

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: 87.37  E-value: 7.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLWFlNKYNLHG-ILCDDMGLGKTLQTICILagDHIQRENTNQsnlPSLVICPPTLTGHWVYEVEKFLAQ 1455
Cdd:cd18061     1 LREYQLEGLNWLLF-NWYNRRNcILADEMGLGKTIQSITFL--YEILLTGIRG---PFLIIAPLSTIANWEREFRTWTDL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1456 SPILrplhYFGFPVGREKLRsQIGTTC--------------NLVVASYDTVRKDIDYFSGIHFNYCVLDEGHIIKNGKTK 1521
Cdd:cd18061    75 NVVV----YHGSLISRQMIQ-QYEMYFrdsqgriirgayrfQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCK 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 195446151 1522 SSKAIKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGFLGTEKQFIQRF 1571
Cdd:cd18061   150 LLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF 199
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
1399-1560 3.22e-17

DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 82.34  E-value: 3.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1399 ILCDDMGLGKTLQTICILAgDHIQRENTNqsnlPSLVICPPTLTGHWVYEV-EKFLAQSPILRPLHYfgfpvgrEKLRSQ 1477
Cdd:cd18011    21 LLADEVGLGKTIEAGLIIK-ELLLRGDAK----RVLILCPASLVEQWQDELqDKFGLPFLILDRETA-------AQLRRL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1478 IG---TTCNLVVASYDTVRKDIDY---FSGIHFNYCVLDEGHIIKNG----KTKSSKAIKQL--KANHRLILSGTPIQNN 1545
Cdd:cd18011    89 IGnpfEEFPIVIVSLDLLKRSEERrglLLSEEWDLVVVDEAHKLRNSgggkETKRYKLGRLLakRARHVLLLTATPHNGK 168
                         170
                  ....*....|....*
gi 195446151 1546 VLELWSLFDFLMPGF 1560
Cdd:cd18011   169 EEDFRALLSLLDPGR 183
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1721-1844 1.61e-14

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: 71.47  E-value: 1.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151  1721 AKLPALKQLLldcgigvqtESVSQHRALIFCQLKAMLDIvehDLLRRHLpSVTYLRLDGSVPASQRQDIVNNFNSDP--- 1797
Cdd:pfam00271    1 EKLEALLELL---------KKERGGKVLIFSQTKKTLEA---ELLLEKE-GIKVARLHGDLSQEEREEILEDFRKGKidv 67
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 195446151  1798 ---------SIDvlllttlvgglglnLTGADTVIFVEHDWNPMKDLQAMDRAHRIG 1844
Cdd:pfam00271   68 lvatdvaerGLD--------------LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
1377-1580 2.43e-12

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: 68.15  E-value: 2.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINWLwflnKYNLHGILCDDMGLGKTLQTICILagDHIQRENTNQsnlPSLVICPPTLTGH-WVYEVEKFlaq 1455
Cdd:cd18013     1 PHPYQKVAINFI----IEHPYCGLFLDMGLGKTVTTLTAL--SDLQLDDFTR---RVLVIAPLRVARStWPDEVEKW--- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1456 sPILRPLHYFgFPVGREKLRSQIGTT-CNLVVASYDTVRKDIDYFsGIHFNY--CVLDEGHIIKNGKTKSSKAIKQL-KA 1531
Cdd:cd18013    69 -NHLRNLTVS-VAVGTERQRSKAANTpADLYVINRENLKWLVNKS-GDPWPFdmVVIDELSSFKSPRSKRFKALRKVrPV 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 195446151 1532 NHRLI-LSGTPIQNNVLELWSLFDFLMPGflgtekqfiQRFSRPILASRD 1580
Cdd:cd18013   146 IKRLIgLTGTPSPNGLMDLWAQIALLDQG---------ERLGRSITAYRE 186
HELICc smart00490
helicase superfamily c-terminal domain;
1758-1844 1.12e-09

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 56.45  E-value: 1.12e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151   1758 DIVEHDLLRRHLPsvtYLRLDGSVPASQRQDIVNNFNSDP------------SIDvlllttlvgglglnLTGADTVIFVE 1825
Cdd:smart00490    1 EELAELLKELGIK---VARLHGGLSQEEREEILDKFNNGKikvlvatdvaerGLD--------------LPGVDLVIIYD 63
                            90
                    ....*....|....*....
gi 195446151   1826 HDWNPMKDLQAMDRAHRIG 1844
Cdd:smart00490   64 LPWSPASYIQRIGRAGRAG 82
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
1377-1541 1.73e-09

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 58.09  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1377 LRGYQQAGINwLWFLNKYNLHGILCDDMGLGKTLQTICILAgdhiqrentNQSNLPSLVICPPT-LTGHWVYEVEKFLAQ 1455
Cdd:cd17926     1 LRPYQEEALE-AWLAHKNNRRGILVLPTGSGKTLTALALIA---------YLKELRTLIVVPTDaLLDQWKERFEDFLGD 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1456 SPILRplhyfgfpVGREKLRSQIGttCNLVVASYDTVRKDID--YFSGIHFNYCVLDEGHIIkNGKTkSSKAIKQLKANH 1533
Cdd:cd17926    71 SSIGL--------IGGGKKKDFDD--ANVVVATYQSLSNLAEeeKDLFDQFGLLIVDEAHHL-PAKT-FSEILKELNAKY 138

                  ....*...
gi 195446151 1534 RLILSGTP 1541
Cdd:cd17926   139 RLGLTATP 146
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
1337-1541 3.44e-06

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 51.95  E-value: 3.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1337 EQLKSEPLQARKSRDKEFLDYLFNPKTIPDYKVPVTLSVELRGYQQAGIN-WLWFLNKYNLHGILCDDMGLGKTLqTICI 1415
Cdd:COG1061    41 AIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTV-LALA 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195446151 1416 LAGDHIQRENTnqsnlpsLVICP-PTLTGHWVYEVEKFLAQSPILRPLHYFGFPVgreklrsqigttcnlVVASYDTV-- 1492
Cdd:COG1061   120 LAAELLRGKRV-------LVLVPrRELLEQWAEELRRFLGDPLAGGGKKDSDAPI---------------TVATYQSLar 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 195446151 1493 RKDIDYFSGiHFNYCVLDEGHiikNGKTKS-SKAIKQLKANHRLILSGTP 1541
Cdd:COG1061   178 RAHLDELGD-RFGLVIIDEAH---HAGAPSyRRILEAFPAAYRLGLTATP 223
 
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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