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Conserved domains on  [gi|1222443606|ref|WP_090495020|]
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DEAD/DEAH box helicase [Pseudoalteromonas sp. DSM 26666]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 11425670)

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

CATH:  1.20.1320.20|3.40.50.300
EC:  3.6.4.-
Gene Ontology:  GO:0016887|GO:0003676|GO:0004386|GO:0005524
PubMed:  20206133|20225155

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 588-1027 0e+00

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 587.58  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  588 VVLREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQAGPTLIVCPTSLVSNWQNEITKFAKSLKVT 667
Cdd:COG0553    240 ATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFAPGLRVL 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  668 TIFGA-HRNDSLQHLAQAQCILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNADFKLCLSGTPIEN 746
Cdd:COG0553    320 VLDGTrERAKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVEN 399

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  747 NLFELKSLLDFAMPSLLGSQAHFKQHFQGPIEREsNIERAEQLKALIMPFILRRTKAQVAQELPQKTELIKEFEFEPKQK 826
Cdd:COG0553    400 RLEELWSLLDFLNPGLLGSLKAFRERFARPIEKG-DEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQR 478

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  827 DMYQGITRALEEKLIDLFAEqgvqKSKLAFLEALLKLRQICCHPKLIEPETE---AASAKLEWLSSHLPLMLSLGRKVII 903
Cdd:COG0553    479 ALYEAVLEYLRRELEGAEGI----RRRGLILAALTRLRQICSHPALLLEEGAelsGRSAKLEALLELLEELLAEGEKVLV 554

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  904 FSQFTSALDLIAERLNTLNIKFSMLTGQT--RHRDKVIDEFTSGT-TSVFLISLKAGGTGLNLTQADTVIHFDPWWNPAV 980
Cdd:COG0553    555 FSQFTDTLDLLEERLEERGIEYAYLHGGTsaEERDELVDRFQEGPeAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAV 634

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1222443606  981 EKQATDRAYRIGQTNPVFVYKLIMANSIEQKVFQMQQDKQALVDALF 1027
Cdd:COG0553    635 EEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 588-1027 0e+00

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 587.58  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  588 VVLREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQAGPTLIVCPTSLVSNWQNEITKFAKSLKVT 667
Cdd:COG0553    240 ATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFAPGLRVL 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  668 TIFGA-HRNDSLQHLAQAQCILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNADFKLCLSGTPIEN 746
Cdd:COG0553    320 VLDGTrERAKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVEN 399

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  747 NLFELKSLLDFAMPSLLGSQAHFKQHFQGPIEREsNIERAEQLKALIMPFILRRTKAQVAQELPQKTELIKEFEFEPKQK 826
Cdd:COG0553    400 RLEELWSLLDFLNPGLLGSLKAFRERFARPIEKG-DEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQR 478

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  827 DMYQGITRALEEKLIDLFAEqgvqKSKLAFLEALLKLRQICCHPKLIEPETE---AASAKLEWLSSHLPLMLSLGRKVII 903
Cdd:COG0553    479 ALYEAVLEYLRRELEGAEGI----RRRGLILAALTRLRQICSHPALLLEEGAelsGRSAKLEALLELLEELLAEGEKVLV 554

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  904 FSQFTSALDLIAERLNTLNIKFSMLTGQT--RHRDKVIDEFTSGT-TSVFLISLKAGGTGLNLTQADTVIHFDPWWNPAV 980
Cdd:COG0553    555 FSQFTDTLDLLEERLEERGIEYAYLHGGTsaEERDELVDRFQEGPeAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAV 634

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1222443606  981 EKQATDRAYRIGQTNPVFVYKLIMANSIEQKVFQMQQDKQALVDALF 1027
Cdd:COG0553    635 EEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
 590-802 1.36e-99

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: 312.58  E-value: 1.36e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQAGPTLIVCPTSLVSNWQNEITKFAKSLKVTTI 669
Cdd:cd18012      5 LRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKVLVI 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  670 FGAHRNDS-LQHLAQAQCILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNADFKLCLSGTPIENNL 748
Cdd:cd18012     85 HGTKRKREkLRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTPIENHL 164

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1222443606  749 FELKSLLDFAMPSLLGSQAHFKQHFQGPIERESNIERAEQLKALIMPFILRRTK 802
Cdd:cd18012    165 GELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEEALEELKKLISPFILRRLK 218
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 590-1026 1.39e-77

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 275.91  E-value: 1.39e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQ-AGPTLIVCPTSLVSNWQNEITKFAKSLKVTT 668
Cdd:PLN03142   170 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGiTGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  669 IFG-----AHRNDSLQHLAQAQCILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNADFKLCLSGTP 743
Cdd:PLN03142   250 FHGnpeerAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTP 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  744 IENNLFELKSLLDFAMPSLLGSQAHFKQHFQGPIErESNIERAEQLKALIMPFILRRTKAQVAQELPQKTELIKEFEFEP 823
Cdd:PLN03142   330 LQNNLHELWALLNFLLPEIFSSAETFDEWFQISGE-NDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQ 408

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  824 KQKDMYqgitRALEEKLIDLFaEQGVQKSKLafLEALLKLRQICCHPKLIE------PETEA-----ASAKLEWLSSHLP 892
Cdd:PLN03142   409 MQKQYY----KALLQKDLDVV-NAGGERKRL--LNIAMQLRKCCNHPYLFQgaepgpPYTTGehlveNSGKMVLLDKLLP 481

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  893 LMLSLGRKVIIFSQFTSALDLIAERLNTLNIKFSMLTGQT--RHRDKVIDEFTSGTTS--VFLISLKAGGTGLNLTQADT 968
Cdd:PLN03142   482 KLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTggEDRDASIDAFNKPGSEkfVFLLSTRAGGLGINLATADI 561

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1222443606  969 VIHFDPWWNPAVEKQATDRAYRIGQTNPVFVYKLIMANSIEQKVFQMQQDKQALvDAL 1026
Cdd:PLN03142   562 VILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL-DAL 618
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 593-873 3.50e-68

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: 230.26  E-value: 3.50e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  593 YQQEGVAWLNFLKRN-QLGGILADDMGLGKTLQVIAYLASSYN-TPQAG-PTLIVCPTSLVSNWQNEITKFAK--SLKVT 667
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHvDKNWGgPTLIVVPLSLLHNWMNEFERWVSppALRVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  668 TIFG--AHRNDSLQHLAQAQC---ILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNADFKLCLSGT 742
Cdd:pfam00176   81 VLHGnkRPQERWKNDPNFLADfdvVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  743 PIENNLFELKSLLDFAMPSLLGSQAHFKQHFQGPIERESNIERAEQLKALIMPFILRRTKAQVAQELPQKTELIKEFEFE 822
Cdd:pfam00176  161 PLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLS 240

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1222443606  823 PKQKDMYQGITRALEEKLIDLfaEQGVQKSKLAFLEALLKLRQICCHPKLI 873
Cdd:pfam00176  241 KLQRKLYQTFLLKKDLNAIKT--GEGGREIKASLLNILMRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
590-755 1.50e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 99.49  E-value: 1.50e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606   590 LREYQQEGVAWLNFLKRNqlgGILADDMGLGKTLQVIAYLASSYNTPQAGPTLIVCPT-SLVSNWQNEITKFAKSLKVTT 668
Cdd:smart00487    9 LRPYQKEAIEALLSGLRD---VILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTrELAEQWAEELKKLGPSLGLKV 85

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606   669 IF---GAHRNDSLQHLA--QAQCILTTYPLLKRDIA--YYSPLYFENIILDEAQYIKND--TAQVSRLVKRLNADFK-LC 738
Cdd:smart00487   86 VGlygGDSKREQLRKLEsgKTDILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKLLPKNVQlLL 165

                           170
                    ....*....|....*..
gi 1222443606   739 LSGTPIENNLFELKSLL 755
Cdd:smart00487  166 LSATPPEEIENLLELFL 182
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 588-1027 0e+00

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 587.58  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  588 VVLREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQAGPTLIVCPTSLVSNWQNEITKFAKSLKVT 667
Cdd:COG0553    240 ATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFAPGLRVL 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  668 TIFGA-HRNDSLQHLAQAQCILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNADFKLCLSGTPIEN 746
Cdd:COG0553    320 VLDGTrERAKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVEN 399

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  747 NLFELKSLLDFAMPSLLGSQAHFKQHFQGPIEREsNIERAEQLKALIMPFILRRTKAQVAQELPQKTELIKEFEFEPKQK 826
Cdd:COG0553    400 RLEELWSLLDFLNPGLLGSLKAFRERFARPIEKG-DEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQR 478

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  827 DMYQGITRALEEKLIDLFAEqgvqKSKLAFLEALLKLRQICCHPKLIEPETE---AASAKLEWLSSHLPLMLSLGRKVII 903
Cdd:COG0553    479 ALYEAVLEYLRRELEGAEGI----RRRGLILAALTRLRQICSHPALLLEEGAelsGRSAKLEALLELLEELLAEGEKVLV 554

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  904 FSQFTSALDLIAERLNTLNIKFSMLTGQT--RHRDKVIDEFTSGT-TSVFLISLKAGGTGLNLTQADTVIHFDPWWNPAV 980
Cdd:COG0553    555 FSQFTDTLDLLEERLEERGIEYAYLHGGTsaEERDELVDRFQEGPeAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAV 634

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1222443606  981 EKQATDRAYRIGQTNPVFVYKLIMANSIEQKVFQMQQDKQALVDALF 1027
Cdd:COG0553    635 EEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVL 681
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
 590-802 1.36e-99

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: 312.58  E-value: 1.36e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQAGPTLIVCPTSLVSNWQNEITKFAKSLKVTTI 669
Cdd:cd18012      5 LRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKVLVI 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  670 FGAHRNDS-LQHLAQAQCILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNADFKLCLSGTPIENNL 748
Cdd:cd18012     85 HGTKRKREkLRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTPIENHL 164

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1222443606  749 FELKSLLDFAMPSLLGSQAHFKQHFQGPIERESNIERAEQLKALIMPFILRRTK 802
Cdd:cd18012    165 GELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEEALEELKKLISPFILRRLK 218
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 590-1026 1.39e-77

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 275.91  E-value: 1.39e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQ-AGPTLIVCPTSLVSNWQNEITKFAKSLKVTT 668
Cdd:PLN03142   170 MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGiTGPHMVVAPKSTLGNWMNEIRRFCPVLRAVK 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  669 IFG-----AHRNDSLQHLAQAQCILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNADFKLCLSGTP 743
Cdd:PLN03142   250 FHGnpeerAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTP 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  744 IENNLFELKSLLDFAMPSLLGSQAHFKQHFQGPIErESNIERAEQLKALIMPFILRRTKAQVAQELPQKTELIKEFEFEP 823
Cdd:PLN03142   330 LQNNLHELWALLNFLLPEIFSSAETFDEWFQISGE-NDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQ 408

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  824 KQKDMYqgitRALEEKLIDLFaEQGVQKSKLafLEALLKLRQICCHPKLIE------PETEA-----ASAKLEWLSSHLP 892
Cdd:PLN03142   409 MQKQYY----KALLQKDLDVV-NAGGERKRL--LNIAMQLRKCCNHPYLFQgaepgpPYTTGehlveNSGKMVLLDKLLP 481

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  893 LMLSLGRKVIIFSQFTSALDLIAERLNTLNIKFSMLTGQT--RHRDKVIDEFTSGTTS--VFLISLKAGGTGLNLTQADT 968
Cdd:PLN03142   482 KLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTggEDRDASIDAFNKPGSEkfVFLLSTRAGGLGINLATADI 561

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1222443606  969 VIHFDPWWNPAVEKQATDRAYRIGQTNPVFVYKLIMANSIEQKVFQMQQDKQALvDAL 1026
Cdd:PLN03142   562 VILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLAL-DAL 618
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 593-873 3.50e-68

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: 230.26  E-value: 3.50e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  593 YQQEGVAWLNFLKRN-QLGGILADDMGLGKTLQVIAYLASSYN-TPQAG-PTLIVCPTSLVSNWQNEITKFAK--SLKVT 667
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHvDKNWGgPTLIVVPLSLLHNWMNEFERWVSppALRVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  668 TIFG--AHRNDSLQHLAQAQC---ILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNADFKLCLSGT 742
Cdd:pfam00176   81 VLHGnkRPQERWKNDPNFLADfdvVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  743 PIENNLFELKSLLDFAMPSLLGSQAHFKQHFQGPIERESNIERAEQLKALIMPFILRRTKAQVAQELPQKTELIKEFEFE 822
Cdd:pfam00176  161 PLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLS 240

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1222443606  823 PKQKDMYQGITRALEEKLIDLfaEQGVQKSKLAFLEALLKLRQICCHPKLI 873
Cdd:pfam00176  241 KLQRKLYQTFLLKKDLNAIKT--GEGGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
 590-800 6.77e-61

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: 207.59  E-value: 6.77e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSY------NTPQAGPTLIVCPTSLVSNWQNEITKFAKS 663
Cdd:cd17999      1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHhkransFNSENLPSLVVCPPTLVGHWVAEIKKYFPN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  664 LKVTTI----FGAHRNDSLQHLAQAQCILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNADFKLCL 739
Cdd:cd17999     81 AFLKPLayvgPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHRLIL 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222443606  740 SGTPIENNLFELKSLLDFAMPSLLGSQAHFKQHFQGPI-----------ERESNIERAEQLKALIMPFILRR 800
Cdd:cd17999    161 SGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPIlasrdskasakEQEAGALALEALHKQVLPFLLRR 232
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
 590-763 9.61e-60

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: 202.41  E-value: 9.61e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLAS-SYNTPQAGPTLIVCPTSLVSNWQNEITKFAKSLKVTT 668
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYlLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  669 IFGA--HRNDSLQHLAQAQC--ILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNADFKLCLSGTPI 744
Cdd:cd17919     81 YHGSqrERAQIRAKEKLDKFdvVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPL 160

                          170
                   ....*....|....*....
gi 1222443606  745 ENNLFELKSLLDFAMPSLL 763
Cdd:cd17919    161 QNNLEELWALLDFLDPPFL 179
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
 590-800 3.43e-55

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: 191.43  E-value: 3.43e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQAGPTLIVCPTSLVSNWQNEITKFAKSLKVTTI 669
Cdd:cd18001      1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKVF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  670 FG---AHRNDSLQHLAQAQ-CILTTYPLLKRDIAYYSPlYFEN------IILDEAQYIKNDTAQVSRLVKRLNADFKLCL 739
Cdd:cd18001     81 HGtskKERERNLERIQRGGgVLLTTYGMVLSNTEQLSA-DDHDefkwdyVILDEGHKIKNSKTKSAKSLREIPAKNRIIL 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1222443606  740 SGTPIENNLFELKSLLDFAMP-SLLGSQAHFKQHFQGPIERESN-----------IERAEQLKALIMPFILRR 800
Cdd:cd18001    160 TGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENPITRGRDkdatqgekalgSEVAENLRQIIKPYFLRR 232
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 870-1003 1.31e-54

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 185.76  E-value: 1.31e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  870 PKLIEpetEAASAKLEWLSSHLPLMLSLGRKVIIFSQFTSALDLIAERLNTLNIKFSMLTGQTRH--RDKVIDEFTSGTT 947
Cdd:cd18793      2 PPKIE---EVVSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSkeRQKLVDRFNEDPD 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1222443606  948 S-VFLISLKAGGTGLNLTQADTVIHFDPWWNPAVEKQATDRAYRIGQTNPVFVYKLI 1003
Cdd:cd18793     79 IrVFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
 590-800 1.83e-50

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: 178.34  E-value: 1.83e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSY-----------NTPQ----------AGPTLIVCPTS 648
Cdd:cd18005      1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLgktgtrrdrenNRPRfkkkppassaKKPVLIVAPLS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  649 LVSNWQNEITKFAkSLKVTTIFGAHRNDSLQHLAQA---QCILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVS 725
Cdd:cd18005     81 VLYNWKDELDTWG-HFEVGVYHGSRKDDELEGRLKAgrlEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSKLT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  726 RLVKRLNADFKLCLSGTPIENNLFELKSLLDFAMPSLLGSQAHFKQHFQGPIER-------ESNIERAEQ----LKALIM 794
Cdd:cd18005    160 QAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRgqrhtatARELRLGRKrkqeLAVKLS 239


                   ....*.
gi 1222443606  795 PFILRR 800
Cdd:cd18005    240 KFFLRR 245
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
 590-802 1.96e-50

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: 177.51  E-value: 1.96e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLAS-SYNTPQAGPTLIVCPTSLVSNWQNEITKFAKSLKVTT 668
Cdd:cd17997      4 MRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYlKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLRVVV 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  669 IFGAH--RNDSLQHLAQAQ---CILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNADFKLCLSGTP 743
Cdd:cd17997     84 LIGDKeeRADIIRDVLLPGkfdVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGTP 163

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1222443606  744 IENNLFELKSLLDFAMPSLLGSQAHFKQHFQGPIERESNIERAEQLKALIMPFILRRTK 802
Cdd:cd17997    164 LQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
 590-800 5.48e-50

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: 176.39  E-value: 5.48e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLAS-SYNTPQAGPTLIVCPTSLVSNWQNEITKFAKSLKVTT 668
Cdd:cd18003      1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHlACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  669 IFGAHRNDSLQHLAQAQ------CIlTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNADFKLCLSGT 742
Cdd:cd18003     81 YYGSAKERKLKRQGWMKpnsfhvCI-TSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGT 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1222443606  743 PIENNLFELKSLLDFAMPSLLGSQAHFKQHFQGPIE------RESNIERAEQLKALIMPFILRR 800
Cdd:cd18003    160 PLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLTamsegsQEENEELVRRLHKVLRPFLLRR 223
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
 590-800 5.91e-50

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: 176.71  E-value: 5.91e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLnfLKRnqlGGILADDMGLGKTLQVIA------------------YLASSYNTPQAGPTLIVCPTSLVS 651
Cdd:cd18008      1 LLPYQKQGLAWM--LPR---GGILADEMGLGKTIQALAlilatrpqdpkipeeleeNSSDPKKLYLSKTTLIVVPLSLLS 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  652 NWQNEITKFAK--SLKVTTIFGAHRNDSLQHLAQAQCILTTYPLLKRDIA-------------YYSPLY---FENIILDE 713
Cdd:cd18008     76 QWKDEIEKHTKpgSLKVYVYHGSKRIKSIEELSDYDIVITTYGTLASEFPknkkgggrdskekEASPLHrirWYRVILDE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  714 AQYIKNDTAQVSRLVKRLNADFKLCLSGTPIENNLFELKSLLDFAMPSLLGSQAHFKQHFQGPIErESNIERAEQLKALI 793
Cdd:cd18008    156 AHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFS-KNDRKALERLQALL 234


                   ....*..
gi 1222443606  794 MPFILRR 800
Cdd:cd18008    235 KPILLRR 241
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
 588-802 6.14e-45

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: 162.17  E-value: 6.14e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  588 VVLREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQAGPTLIVCPTSLVSNWQNEITKFAKSLKVT 667
Cdd:cd18009      2 GVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPVL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  668 TIFGA--HRNDSLQHLAQAQC-------ILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNADFKLC 738
Cdd:cd18009     82 LYHGTkeERERLRKKIMKREGtlqdfpvVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLL 161

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222443606  739 LSGTPIENNLFELKSLLDFAMPSLLGSQAHFKQHF--------QGPIERESNiERAEQ----LKALIMPFILRRTK 802
Cdd:cd18009    162 LTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFdfsslsdnAADISNLSE-EREQNivhmLHAILKPFLLRRLK 236
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
 590-800 4.81e-44

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: 159.76  E-value: 4.81e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWL-NFLKRNQLGG----ILADDMGLGKTLQVIAYL-----ASSYNTPQAGPTLIVCPTSLVSNWQNEITK 659
Cdd:cd18004      1 LRPHQREGVQFLyDCLTGRRGYGgggaILADEMGLGKTLQAIALVwtllkQGPYGKPTAKKALIVCPSSLVGNWKAEFDK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  660 FAKS--LKVTTIFGAHRNDSLQHLAQA-----QCILTTYPLLKRDIA-YYSPLYFENIILDEAQYIKNDTAQVSRLVKRL 731
Cdd:cd18004     81 WLGLrrIKVVTADGNAKDVKASLDFFSsastyPVLIISYETLRRHAEkLSKKISIDLLICDEGHRLKNSESKTTKALNSL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  732 NADFKLCLSGTPIENNLFELKSLLDFAMPSLLGSQAHFKQHFQGPI-----------ERESNIERAEQLKALIMPFILRR 800
Cdd:cd18004    161 PCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPIlrsrdpdaseeDKELGAERSQELSELTSRFILRR 240
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
 590-761 1.45e-43

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: 156.39  E-value: 1.45e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQAGPTLIVCPTSLVSNWQNEITKFAKSLKVTTI 669
Cdd:cd17998      1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEPY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  670 FGAH------RNDSLQHLAQAQCILTTYPLL---KRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNADFKLCLS 740
Cdd:cd17998     81 YGSQeerkhlRYDILKGLEDFDVIVTTYNLAtsnPDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLLT 160

                          170       180
                   ....*....|....*....|.
gi 1222443606  741 GTPIENNLFELKSLLDFAMPS 761
Cdd:cd17998    161 GTPLQNNLLELMSLLNFIMPK 181
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
 590-763 3.81e-42

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: 152.48  E-value: 3.81e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLAS-SYNTPQAGPTLIVCPTSLVSNWQNEITKFAKSLKVTT 668
Cdd:cd18000      1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAAlHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  669 I-----FGAHRNDSLQHLAQAQ----------CILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNA 733
Cdd:cd18000     81 LhssgsGTGSEEKLGSIERKSQlirkvvgdggILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRT 160

                          170       180       190
                   ....*....|....*....|....*....|
gi 1222443606  734 DFKLCLSGTPIENNLFELKSLLDFAMPSLL 763
Cdd:cd18000    161 PHRLILSGTPIQNNLKELWSLFDFVFPPYL 190
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
 590-800 6.44e-41

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: 149.90  E-value: 6.44e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIA---YLASSYNTPqaGPTLIVCPTSLVSNWQNEITKFAKSLKV 666
Cdd:cd18006      1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISllwYLAGRLKLL--GPFLVLCPLSVLDNWKEELNRFAPDLSV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  667 TTIFG--AHRNDSLQHLAQA---QCILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNADFKLCLSG 741
Cdd:cd18006     79 ITYMGdkEKRLDLQQDIKSTnrfHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTG 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222443606  742 TPIENNLFELKSLLDFAMPSLLGSQA--HFKQHFQgpiERESNIERAEQLKALIMPFILRR 800
Cdd:cd18006    159 TPIQNSLQELYALLSFIEPNVFPKDKldDFIKAYS---ETDDESETVEELHLLLQPFLLRR 216
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
 590-802 5.21e-40

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: 147.90  E-value: 5.21e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQ-AGPTLIVCPTSLVSNWQNEITKFAKSLKVTT 668
Cdd:cd17996      4 LKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKnNGPYLVIVPLSTLSNWVSEFEKWAPSVSKIV 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  669 IFG---AHRNDSLQHLAQA-QCILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKR-LNADFKLCLSGTP 743
Cdd:cd17996     84 YKGtpdVRKKLQSQIRAGKfNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyYHARYRLLLTGTP 163

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  744 IENNLFELKSLLDFAMPSLLGSQAHFKQHFQGPIERES---NIERAEQLKALIM--------PFILRRTK 802
Cdd:cd17996    164 LQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGeqvKIELNEEETLLIIrrlhkvlrPFLLRRLK 233
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
 590-800 5.33e-40

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: 147.65  E-value: 5.33e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQ---VIAYLASSYNTpqAGPTLIVCPTSLVSNWQNEITKFAKSLKV 666
Cdd:cd18002      1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQsiaVLAHLAEEHNI--WGPFLVIAPASTLHNWQQEISRFVPQFKV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  667 TTIFGA----------------HRNDSLQHLaqaqcILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKR 730
Cdd:cd18002     79 LPYWGNpkdrkvlrkfwdrknlYTRDAPFHV-----VITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLS 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222443606  731 LNADFKLCLSGTPIENNLFELKSLLDFAMPSLLGSQAHFKQHFQGPIERESNIERA---EQLKALIM---PFILRR 800
Cdd:cd18002    154 FHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENKTGlneHQLKRLHMilkPFMLRR 229
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
 590-800 1.48e-37

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: 140.57  E-value: 1.48e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNT-PQAGPTLIVCPTSLVSNWQNEITKFAKSLKVTT 668
Cdd:cd17993      2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSqQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  669 IFG--AHRNDSLQHLAQAQ--------CILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNADFKLC 738
Cdd:cd17993     82 YLGdiKSRDTIREYEFYFSqtkklkfnVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRLL 161

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1222443606  739 LSGTPIENNLFELKSLLDFAMPSllgsqahfKQHFQGPIERESNIERAEQLKAL---IMPFILRR 800
Cdd:cd17993    162 ITGTPLQNSLKELWALLHFLMPG--------KFDIWEEFEEEHDEEQEKGIADLhkeLEPFILRR 218
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
 590-800 6.25e-36

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: 135.84  E-value: 6.25e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQA-GPTLIVCPTSLVSNWQNEITKFAkSLKVTT 668
Cdd:cd17995      1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIrGPFLVIAPLSTIPNWQREFETWT-DMNVVV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  669 IFGAHRNDSLQHLAQAQC----------------ILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLN 732
Cdd:cd17995     80 YHGSGESRQIIQQYEMYFkdaqgrkkkgvykfdvLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1222443606  733 ADFKLCLSGTPIENNLFELKSLLDFAMPSLLGSQAHFKQHFqGPIERESNIERaeqLKALIMPFILRR 800
Cdd:cd17995    160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF-GDLKTAEQVEK---LQALLKPYMLRR 223
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
 590-812 3.21e-35

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: 134.79  E-value: 3.21e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIA---YLASSYNTPqaGPTLIVCPTSLVSNWQNEITKFAKSLKV 666
Cdd:cd18064     16 LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISllgYMKHYRNIP--GPHMVLVPKSTLHNWMAEFKRWVPTLRA 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  667 TTIFGahrnDSLQHLAQAQCIL---------TTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNADFKL 737
Cdd:cd18064     94 VCLIG----DKDQRAAFVRDVLlpgewdvcvTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRL 169

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1222443606  738 CLSGTPIENNLFELKSLLDFAMPSLLGSQAHFKQHFQGPiERESNIERAEQLKALIMPFILRRTKAQVAQELPQK 812
Cdd:cd18064    170 LLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTN-NCLGDQKLVERLHMVLRPFLLRRIKADVEKSLPPK 243
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
 600-800 9.31e-35

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: 132.98  E-value: 9.31e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  600 WLNFL------KRNQL--GGILADDMGLGKTLQVIAYLASSyntpqagPTLIVCPTSLVSNWQNEITKFAKS--LKVTTI 669
Cdd:cd18071     32 FLNTItnfsqkKRPELvrGGILADDMGLGKTLTTISLILAN-------FTLIVCPLSVLSNWETQFEEHVKPgqLKVYTY 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  670 FGAHRNDSLQHLAQAQCILTTYPLLKRDIAYY--SPLY---FENIILDEAQYIKNDTAQVSRLVKRLNADFKLCLSGTPI 744
Cdd:cd18071    105 HGGERNRDPKLLSKYDIVLTTYNTLASDFGAKgdSPLHtinWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPI 184

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1222443606  745 ENNLFELKSLLDFAMPSLLGSQAHFKQHFQGPIERESNIERAeQLKALIMPFILRR 800
Cdd:cd18071    185 QNSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPLTMGDPTGLK-RLQVLMKQITLRR 239
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
 590-800 2.15e-33

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: 129.19  E-value: 2.15e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWL-----NFLKRNQLGGILADDMGLGKTLQVIAYLASSY------NTPQAGPTLIVCPTSLVSNWQNEIT 658
Cdd:cd18066      1 LRPHQREGIEFLyecvmGMRVNERFGAILADEMGLGKTLQCISLIWTLLrqgpygGKPVIKRALIVTPGSLVKNWKKEFQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  659 KFAKS--LKVTTIFGAHRNDSLQHLAQAQCILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNADFK 736
Cdd:cd18066     81 KWLGSerIKVFTVDQDHKVEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSCERR 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1222443606  737 LCLSGTPIENNLFELKSLLDFAMPSLLGSQAHFKQHFQGPI-----------ERESNIERAEQLKALIMPFILRR 800
Cdd:cd18066    161 IILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIvrsreptatpeEKKLGEARAAELTRLTGLFILRR 235
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
 590-802 2.30e-33

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: 128.98  E-value: 2.30e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIA---YLASSYNTPqaGPTLIVCPTSLVSNWQNEITKFAKSLKV 666
Cdd:cd18065     16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIAllgYLKHYRNIP--GPHMVLVPKSTLHNWMNEFKRWVPSLRA 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  667 TTIFG------AHRNDSLQHLAQAQCIlTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNADFKLCLS 740
Cdd:cd18065     94 VCLIGdkdaraAFIRDVMMPGEWDVCV-TSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLT 172

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222443606  741 GTPIENNLFELKSLLDFAMPSLLGSQAHFKQHFQGPiERESNIERAEQLKALIMPFILRRTK 802
Cdd:cd18065    173 GTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTK-NCLGDQKLVERLHAVLKPFLLRRIK 233
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
 590-757 4.33e-33

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: 128.37  E-value: 4.33e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFlKRNQL--GGILADDMGLGKTLQVIAYLASSYNT------------------------PQAGpTLI 643
Cdd:cd18072      1 LLLHQKQALAWLLW-RERQKprGGILADDMGLGKTLTMIALILAQKNTqnrkeeekekalteweskkdstlvPSAG-TLV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  644 VCPTSLVSNWQNEITKFAKS--LKVTTIFGAHRNDSLQHLAQAQCILTTYPLLKRDIAYY------SPL---YFENIILD 712
Cdd:cd18072     79 VCPASLVHQWKNEVESRVASnkLRVCLYHGPNRERIGEVLRDYDIVITTYSLVAKEIPTYkeesrsSPLfriAWARIILD 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1222443606  713 EAQYIKNDTAQVSRLVKRLNADFKLCLSGTPIENNLFELKSLLDF 757
Cdd:cd18072    159 EAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKF 203
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
 590-800 4.82e-33

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: 128.36  E-value: 4.82e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWL-----NFLKRNQLGGILADDMGLGKTLQVIAYLASSY-NTPQAGPTL----IVCPTSLVSNWQNEITK 659
Cdd:cd18067      1 LRPHQREGVKFLyrcvtGRRIRGSHGCIMADEMGLGKTLQCITLMWTLLrQSPQCKPEIdkaiVVSPSSLVKNWANELGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  660 F-AKSLKVTTIFGAHRNDSLQHL---AQAQCILTTYPLLkrdIAYYSPL--YFEN--------IILDEAQYIKNDTAQVS 725
Cdd:cd18067     81 WlGGRLQPLAIDGGSKKEIDRKLvqwASQQGRRVSTPVL---IISYETFrlHVEVlqkgevglVICDEGHRLKNSDNQTY 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  726 RLVKRLNADFKLCLSGTPIENNLFELKSLLDFAMPSLLGSQAHFKQHFQGPI-----------ERESNIERAEQLKALIM 794
Cdd:cd18067    158 QALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPIlkgrdadasekERQLGEEKLQELISIVN 237


                   ....*.
gi 1222443606  795 PFILRR 800
Cdd:cd18067    238 RCIIRR 243
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
 590-799 2.07e-32

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: 126.69  E-value: 2.07e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLnfLKRnqlGGILADDMGLGKTLQVIAYLA----------SSYNTPQ----------------AGPTLI 643
Cdd:cd18070      1 LLPYQRRAVNWM--LVP---GGILADEMGLGKTVEVLALILlhprpdndldAADDDSDemvccpdclvaetpvsSKATLI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  644 VCPTSLVSNWQNEITKFAK-SLKVTTIFGAHRNDSLQ-----HLAQAQCILTTYPLLKRDIAYY---------------- 701
Cdd:cd18070     76 VCPSAILAQWLDEINRHVPsSLKVLTYQGVKKDGALAspapeILAEYDIVVTTYDVLRTELHYAeanrsnrrrrrqkrye 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  702 ---SPLY---FENIILDEAQYIKNDTAQVSRLVKRLNADFKLCLSGTPIEN---NLFELKSLLDFAMPSLLGSQAHFKQH 772
Cdd:cd18070    156 appSPLVlveWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRgldDLFGLLSFLGVEPFCDSDWWARVLIR 235

                          250       260
                   ....*....|....*....|....*..
gi 1222443606  773 FQGPieresnIERAEQLKALIMPFILR 799
Cdd:cd18070    236 PQGR------NKAREPLAALLKELLWR 256
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
 590-800 4.74e-32

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: 124.78  E-value: 4.74e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQAGPTLIVCPTSLVSNWQNEITKFAK------- 662
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEmntivyh 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  663 ----SLKVTTIFGAHRNDSLQHLA----QAQCILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNAD 734
Cdd:cd18060     81 gslaSRQMIQQYEMYCKDSRGRLIpgayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222443606  735 FKLCLSGTPIENNLFELKSLLDFAMPSLLGSQAHFKQHFqGPIEREsniERAEQLKALIMPFILRR 800
Cdd:cd18060    161 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF-GDLKTE---EQVQKLQAILKPMMLRR 222
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
 586-800 4.93e-31

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: 122.42  E-value: 4.93e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  586 DSVVLREYQQEGVAWL--NFLKRNQLggILADDMGLGKTLQVIAYLASSYNTPQA-GPTLIVCPTSLVSNWQNEITKFAK 662
Cdd:cd18054     17 ENLELRDYQLEGLNWLahSWCKNNSV--ILADEMGLGKTIQTISFLSYLFHQHQLyGPFLLVVPLSTLTSWQREFEIWAP 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  663 SLKVTTIFG--AHRNDSLQH--------LAQAQCILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLN 732
Cdd:cd18054     95 EINVVVYIGdlMSRNTIREYewihsqtkRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFK 174

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1222443606  733 ADFKLCLSGTPIENNLFELKSLLDFAMPSLLGSQAHFK-QHFQGpieRESNIeraEQLKALIMPFILRR 800
Cdd:cd18054    175 SNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEeDHGKG---RENGY---QSLHKVLEPFLLRR 237
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
 590-800 5.26e-31

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: 120.62  E-value: 5.26e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQA-GPTLIVCPTSLVSNWQNEITKFAKSLKVTT 668
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSkGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  669 IFGAHrndslqhlaqaqCILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNADFKLCLSGTPIENNL 748
Cdd:cd17994     81 YVGDH------------VLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNL 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1222443606  749 FELKSLLDFAMPSLLGSQAHFKQHFQGpIERESNIERaeqLKALIMPFILRR 800
Cdd:cd17994    149 EELFHLLNFLTPERFNNLQGFLEEFAD-ISKEDQIKK---LHDLLGPHMLRR 196
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
 590-794 1.32e-30

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: 121.24  E-value: 1.32e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVawlNFLKRNQLGG----------ILADDMGLGKTLQVIAYLaSSY--NTPQAGPTLIVCPTSLVSNWQNEI 657
Cdd:cd18007      1 LKPHQVEGV---RFLWSNLVGTdvgsdegggcILAHTMGLGKTLQVITFL-HTYlaAAPRRSRPLVLCPASTLYNWEDEF 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  658 TK----FAKSLKVTTIFGAHRN----------------------DSLQHLaqAQCILTTYPLLKRDIAYYSPLYFENIIL 711
Cdd:cd18007     77 KKwlppDLRPLLVLVSLSASKRadarlrkinkwhkeggvlligyELFRNL--ASNATTDPRLKQEFIAALLDPGPDLLVL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  712 DEAQYIKNDTAQVSRLVKRLNADFKLCLSGTPIENNLFELKSLLDFAMPSLLGSQAHFKQHFQGPIERESNIERAEQLKA 791
Cdd:cd18007    155 DEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDSTEEDVR 234


                   ...
gi 1222443606  792 LIM 794
Cdd:cd18007    235 LML 237
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
 590-800 3.62e-30

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: 119.38  E-value: 3.62e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQAGPTLIVCPTSLVSNWQNEITKFAKsLKVTTI 669
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTE-MNAIVY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  670 FGA-------------HRNDS---LQHLAQAQCILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNA 733
Cdd:cd18058     80 HGSqisrqmiqqyemyYRDEQgnpLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMAL 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222443606  734 DFKLCLSGTPIENNLFELKSLLDFAMPSLLGSQAHFKQHFqGPIEREsniERAEQLKALIMPFILRR 800
Cdd:cd18058    160 EHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF-GDLKTE---EQVKKLQSILKPMMLRR 222
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 590-800 1.64e-29

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: 116.92  E-value: 1.64e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLnfLKRNqlGGIL-ADDMGLGKTLQVIAyLASSYntPQAGPTLIVCPTSLVSNWQNEITKFAKSLKVT- 667
Cdd:cd18010      1 LLPFQREGVCFA--LRRG--GRVLiADEMGLGKTVQAIA-IAAYY--REEWPLLIVCPSSLRLTWADEIERWLPSLPPDd 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  668 --TIFGAHrnDSLQHLAQAQCIlTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRL--NADFKLCLSGTP 743
Cdd:cd18010     74 iqVIVKSK--DGLRDGDAKVVI-VSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLlkRAKRVILLSGTP 150

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222443606  744 IENNLFELKSLLDFAMPSLLGSQAHFKQHFQGPIER---------ESNIERAEQLKALIMpfiLRR 800
Cdd:cd18010    151 ALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQGgfgwdysgsSNLEELHLLLLATIM---IRR 213
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
 590-800 1.98e-28

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: 114.33  E-value: 1.98e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQAGPTLIVCPTSLVSNWQNEITKFAK------- 662
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDlnvvvyh 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  663 ----SLKVTTIFGAHRNDSLQHLAQA----QCILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNAD 734
Cdd:cd18061     81 gsliSRQMIQQYEMYFRDSQGRIIRGayrfQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222443606  735 FKLCLSGTPIENNLFELKSLLDFAMPSLLGSQAHFKQHFqGPIEREsniERAEQLKALIMPFILRR 800
Cdd:cd18061    161 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF-GDLKTE---EQVQKLQAILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
 590-800 3.53e-28

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: 113.59  E-value: 3.53e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQAGPTLIVCPTSLVSNWQNEITKFAK------- 662
Cdd:cd18059      1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTElnvvvyh 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  663 ----SLKVTTIFGAHRNDSLQHLAQA----QCILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVKRLNAD 734
Cdd:cd18059     81 gsqaSRRTIQLYEMYFKDPQGRVIKGsykfHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLE 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222443606  735 FKLCLSGTPIENNLFELKSLLDFAMPSLLGSQAHFKQHFqGPIEREsniERAEQLKALIMPFILRR 800
Cdd:cd18059    161 HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF-GDLKTE---EQVQKLQAILKPMMLRR 222
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
 589-802 3.99e-28

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: 114.37  E-value: 3.99e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  589 VLREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQA-GPTLIVCPTSLVSNWQNEITKFAKSLKVT 667
Cdd:cd18062     23 VLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRInGPFLIIVPLSTLSNWVYEFDKWAPSVVKV 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  668 TIFG--AHRNDSLQHLAQAQ--CILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVK-RLNADFKLCLSGT 742
Cdd:cd18062    103 SYKGspAARRAFVPQLRSGKfnVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPRRLLLTGT 182

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1222443606  743 PIENNLFELKSLLDFAMPSLLGSQAHFKQHFQGP---------IERESNIERAEQLKALIMPFILRRTK 802
Cdd:cd18062    183 PLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPfamtgekvdLNEEETILIIRRLHKVLRPFLLRRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
 590-802 4.54e-28

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: 114.00  E-value: 4.54e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQA-GPTLIVCPTSLVSNWQNEITKFAKSLKVTT 668
Cdd:cd18063     24 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLnGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  669 IFG--AHRNDSLQHLAQAQ--CILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVK-RLNADFKLCLSGTP 743
Cdd:cd18063    104 YKGtpAMRRSLVPQLRSGKfnVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPRRILLTGTP 183

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1222443606  744 IENNLFELKSLLDFAMPSLLGSQAHFKQHFQGP---------IERESNIERAEQLKALIMPFILRRTK 802
Cdd:cd18063    184 LQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPfamtgervdLNEEETILIIRRLHKVLRPFLLRRLK 251
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
 590-800 1.38e-26

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: 109.38  E-value: 1.38e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQA-GPTLIVCPTSLVSNWQNEITKFAKSLKVTT 668
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSkGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  669 IFGAHRNDS----------------------LQHLAQAQ--CILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQV 724
Cdd:cd18057     81 YTGDKESRSvirenefsfednairsgkkvfrMKKEAQIKfhVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222443606  725 SRLVKRLNADFKLCLSGTPIENNLFELKSLLDFAMPSLLGSQAHFKQHFqGPIERESNIERaeqLKALIMPFILRR 800
Cdd:cd18057    161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF-ADISKEDQIKK---LHDLLGPHMLRR 232
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
 583-800 2.69e-26

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: 108.60  E-value: 2.69e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  583 GLHDSVVLREYQQEGVAWL--NFLKRNQLggILADDMGLGKTLQVIAYLASSYNTPQA-GPTLIVCPTSLVSNWQNEITK 659
Cdd:cd18053     14 GGHEGLELRDYQLNGLNWLahSWCKGNSC--ILADEMGLGKTIQTISFLNYLFHEHQLyGPFLLVVPLSTLTSWQREIQT 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  660 FAKSLKVTTIFG--AHRNDSLQH--------LAQAQCILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQVSRLVK 729
Cdd:cd18053     92 WAPQMNAVVYLGdiNSRNMIRTHewmhpqtkRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLI 171

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222443606  730 RLNADFKLCLSGTPIENNLFELKSLLDFAMPSLLGSQAHF-KQHFQGpieRESNIeraEQLKALIMPFILRR 800
Cdd:cd18053    172 DFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFeEEHGKG---REYGY---ASLHKELEPFLLRR 237
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
 590-800 3.74e-25

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: 105.09  E-value: 3.74e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQA-GPTLIVCPTSLVSNWQNEITKFAKSLKVTT 668
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTkGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  669 ----------------------IFGAHRNDSLQHLAQAQ--CILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQV 724
Cdd:cd18055     81 ytgdkdsraiirenefsfddnaVKGGKKAFKMKREAQVKfhVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222443606  725 SRLVKRLNADFKLCLSGTPIENNLFELKSLLDFAMPSLLGSQAHFKQHFqGPIERESNIERaeqLKALIMPFILRR 800
Cdd:cd18055    161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF-ADISKEDQIKK---LHDLLGPHMLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
 590-800 5.75e-25

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: 104.76  E-value: 5.75e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVAWLNFLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQA-GPTLIVCPTSLVSNWQNEITKFAKSLKVTT 668
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSkGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  669 ----------------------IFGAHRNDSLQHLAQAQ--CILTTYPLLKRDIAYYSPLYFENIILDEAQYIKNDTAQV 724
Cdd:cd18056     81 yvgdkdsraiirenefsfednaIRGGKKASRMKKEASVKfhVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1222443606  725 SRLVKRLNADFKLCLSGTPIENNLFELKSLLDFAMPSLLgsqahfkQHFQGPIERESNIERAEQLKAL---IMPFILRR 800
Cdd:cd18056    161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERF-------HNLEGFLEEFADIAKEDQIKKLhdmLGPHMLRR 232
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 882-992 1.22e-24

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: 99.59  E-value: 1.22e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  882 AKLEWLSSHLPLmlSLGRKVIIFSQFTSALDlIAERLNTLNIKFSMLTGQT--RHRDKVIDEFTSGTTSVfLISLKAGGT 959
Cdd:pfam00271    1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLsqEEREEILEDFRKGKIDV-LVATDVAER 76

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1222443606  960 GLNLTQADTVIHFDPWWNPAVEKQATDRAYRIG 992
Cdd:pfam00271   77 GLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXDc smart00487
DEAD-like helicases superfamily;
590-755 1.50e-23

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 99.49  E-value: 1.50e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606   590 LREYQQEGVAWLNFLKRNqlgGILADDMGLGKTLQVIAYLASSYNTPQAGPTLIVCPT-SLVSNWQNEITKFAKSLKVTT 668
Cdd:smart00487    9 LRPYQKEAIEALLSGLRD---VILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTrELAEQWAEELKKLGPSLGLKV 85

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606   669 IF---GAHRNDSLQHLA--QAQCILTTYPLLKRDIA--YYSPLYFENIILDEAQYIKND--TAQVSRLVKRLNADFK-LC 738
Cdd:smart00487   86 VGlygGDSKREQLRKLEsgKTDILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKLLPKNVQlLL 165

                           170
                    ....*....|....*..
gi 1222443606   739 LSGTPIENNLFELKSLL 755
Cdd:smart00487  166 LSATPPEEIENLLELFL 182
HELICc smart00490
helicase superfamily c-terminal domain;
912-992 5.08e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 88.04  E-value: 5.08e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606   912 DLIAERLNTLNIKFSMLTGQT--RHRDKVIDEFTSGTtSVFLISLKAGGTGLNLTQADTVIHFDPWWNPAVEKQATDRAY 989
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLsqEEREEILDKFNNGK-IKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79


                    ...
gi 1222443606   990 RIG 992
Cdd:smart00490   80 RAG 82
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
 610-779 8.57e-21

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: 93.03  E-value: 8.57e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  610 GGILADDMGLGKTLQVIAYLASSY-NTPQAG--PTLIVCPTSLVSNWQNEITKFAK------SLKVTTIFGAHRNDSLQH 680
Cdd:cd18068     30 GCILAHCMGLGKTLQVVTFLHTVLlCEKLENfsRVLVVCPLNTVLNWLNEFEKWQEglkdeeKIEVNELATYKRPQERSY 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  681 LAQ------AQCIL--TTYPLL--KRDIAYYSPL------YFEN-----IILDEAQYIKNDTAQVSRLVKRLNADFKLCL 739
Cdd:cd18068    110 KLQrwqeegGVMIIgyDMYRILaqERNVKSREKLkeifnkALVDpgpdfVVCDEGHILKNEASAVSKAMNSIRTKRRIVL 189

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1222443606  740 SGTPIENNLFELKSLLDFAMPSLLGSQAHFKQHFQGPIER 779
Cdd:cd18068    190 TGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQN 229
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
 603-778 5.34e-20

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: 89.87  E-value: 5.34e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  603 FLKRNQLGGILADDMGLGKTLQVIAYLASSYNTPQAGPTLIVCPTSLVSNWQNEITKF-----------AKSLKVTTIfg 671
Cdd:cd18069     23 YKGSSGFGCILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKWlpppealpnvrPRPFKVFIL-- 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  672 ahrNDSLQHLAQAQCILTTYP------LLKRDIAYYSPLYfENIILDEAQYIKNDTAQVSRLVKRLNADFKLCLSGTPIE 745
Cdd:cd18069    101 ---NDEHKTTAARAKVIEDWVkdggvlLMGYEMFRLRPGP-DVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQ 176

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1222443606  746 NNLFELKSLLDFAMPSLLGSQAHFKQHFQGPIE 778
Cdd:cd18069    177 NNLIEYWCMVDFVRPDFLGTRQEFSNMFERPIL 209
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
527-974 8.59e-19

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 91.24  E-value: 8.59e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  527 RFEFIKTRDEFNIPLSYLPELVQHTAINVELHDPSLERYLDELNNDALLSPNTAIHGLhdSVVLREYQQEGV-AWLNFLK 605
Cdd:COG1061     20 LLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGT--SFELRPYQQEALeALLAALE 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  606 RNQLGGILADDMGLGKTLqVIAYLASSYNTPQagPTLIVCPT-SLVSNWQNEITKFakslkvttiFGAHRNDSLQHLAQA 684
Cdd:COG1061     98 RGGGRGLVVAPTGTGKTV-LALALAAELLRGK--RVLVLVPRrELLEQWAEELRRF---------LGDPLAGGGKKDSDA 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  685 QCILTTYPLLKRDIAYyspLYFEN----IILDEAQYIKNDTAQvsRLVKRLNADFKLCLSGTPIENNLFELkslldfamp 760
Cdd:COG1061    166 PITVATYQSLARRAHL---DELGDrfglVIIDEAHHAGAPSYR--RILEAFPAAYRLGLTATPFRSDGREI--------- 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  761 sllgsqahFKQHFQGPIERESnieraeqLKALImpfilrrtkaqvaqelpqKTELIKEFEfepkqkdmYQGITRALEEKL 840
Cdd:COG1061    232 --------LLFLFDGIVYEYS-------LKEAI------------------EDGYLAPPE--------YYGIRVDLTDER 270

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  841 IDLFAeqgvqksklafLEALLKlrqicchpKLIEPETEAASAKL-EWLSSHLPlmlslGRKVIIFSQFTSALDLIAERLN 919
Cdd:COG1061    271 AEYDA-----------LSERLR--------EALAADAERKDKILrELLREHPD-----DRKTLVFCSSVDHAEALAELLN 326

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1222443606  920 TLNIKFSMLTGQTRH--RDKVIDEFTSGTTSVfLISLKAGGTGLNLTQADTVIHFDP 974
Cdd:COG1061    327 EAGIRAAVVTGDTPKkeREEILEAFRDGELRI-LVTVDVLNEGVDVPRLDVAILLRP 382
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
 590-772 1.07e-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: 82.72  E-value: 1.07e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVawLNFLKRNQLGGILADDMGLGKTLQ---VIAYLASSYNtpqAGPTLIVCPTSLVSNWQNEI-TKFAKSLK 665
Cdd:cd18011      1 PLPHQIDAV--LRALRKPPVRLLLADEVGLGKTIEaglIIKELLLRGD---AKRVLILCPASLVEQWQDELqDKFGLPFL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  666 VTTIFGAHRNDSLQH--LAQAQCILTTYPLLKRDIAYYSPLYFEN---IILDEAQYIKN----DTAQVSRLVKRLNADFK 736
Cdd:cd18011     76 ILDRETAAQLRRLIGnpFEEFPIVIVSLDLLKRSEERRGLLLSEEwdlVVVDEAHKLRNsgggKETKRYKLGRLLAKRAR 155

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1222443606  737 --LCLSGTPIENNLFELKSLLDFAMPSLLGSQAHFKQH 772
Cdd:cd18011    156 hvLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLRL 193
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 590-743 7.62e-13

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: 66.95  E-value: 7.62e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGV-AWLNflKRNQLGGILADDMGLGKT---LQVIAYLASsyntpqaGPTLIVCPT-SLVSNWQNEITKFAKSL 664
Cdd:cd17926      1 LRPYQEEALeAWLA--HKNNRRGILVLPTGSGKTltaLALIAYLKE-------LRTLIVVPTdALLDQWKERFEDFLGDS 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  665 KVTTIFGahrnDSLQHLAQAQCILTTYPLLKRDIAYYSPLY--FENIILDEAQYIKNDTAqvSRLVKRLNADFKLCLSGT 742
Cdd:cd17926     72 SIGLIGG----GKKKDFDDANVVVATYQSLSNLAEEEKDLFdqFGLLIVDEAHHLPAKTF--SEILKELNAKYRLGLTAT 145


                   .
gi 1222443606  743 P 743
Cdd:cd17926    146 P 146
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
 590-751 9.73e-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: 65.83  E-value: 9.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  590 LREYQQEGVawlNFLKRNQLGGILADdMGLGKTLQVIAYLASSYNTPQAGPTLIVCPTSLVSN-WQNEITKFA--KSLKV 666
Cdd:cd18013      1 PHPYQKVAI---NFIIEHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARStWPDEVEKWNhlRNLTV 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  667 TTIFGAHRNDSLQHLAQAQCILTTYPLLKRDIAYYSPLY-FENIILDEAQYIKNDTAQ-------VSRLVKRLnadfkLC 738
Cdd:cd18013     77 SVAVGTERQRSKAANTPADLYVINRENLKWLVNKSGDPWpFDMVVIDELSSFKSPRSKrfkalrkVRPVIKRL-----IG 151

                          170
                   ....*....|...
gi 1222443606  739 LSGTPIENNLFEL 751
Cdd:cd18013    152 LTGTPSPNGLMDL 164
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 899-1000 1.07e-06

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 47.31  E-value: 1.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  899 RKVIIFSQFTSALDLIAERLNtlnikfsmltgqtrhrdkvideftsgttsvFLISLKAGGTGLNLTQADTVIHFDPWWNP 978
Cdd:cd18785      4 VKIIVFTNSIEHAEEIASSLE------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSA 53

                           90       100
                   ....*....|....*....|..
gi 1222443606  979 AVEKQATDRAYRIGQTNPVFVY 1000
Cdd:cd18785     54 ASYIQRVGRAGRGGKDEGEVIL 75
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
 883-974 3.88e-06

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 47.12  E-value: 3.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  883 KLEWLSSHLPLMLSlGRKVIIFSQFTSALDLIAERLNTLNIKFSMLTG--QTRHRDKVIDEFTSGTTSVfLISlkaggT- 959
Cdd:cd18787     13 KKLLLLLLLLEKLK-PGKAIIFVNTKKRVDRLAELLEELGIKVAALHGdlSQEERERALKKFRSGKVRV-LVA-----Td 85

                           90
                   ....*....|....*....
gi 1222443606  960 ----GLNLTQADTVIHFDP 974
Cdd:cd18787     86 vaarGLDIPGVDHVINYDL 104
PRK13766 PRK13766
Hef nuclease; Provisional
 855-974 9.81e-04

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 43.32  E-value: 9.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  855 AFLEALLKLRQI-CCHPKLiepeteaaSAKLEWLSSHLPLmlSLGRKVIIFSQFTSALDLIAERLNTLNIKFSMLTGQ-T 932
Cdd:PRK13766   331 RFRKAVRKAKELdIEHPKL--------EKLREIVKEQLGK--NPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQaS 400

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1222443606  933 RHRDK---------VIDEFTSGTTSVfLISLKAGGTGLNLTQADTVIHFDP 974
Cdd:PRK13766   401 KDGDKgmsqkeqieILDKFRAGEFNV-LVSTSVAEEGLDIPSVDLVIFYEP 450
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
 898-970 1.49e-03

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 40.31  E-value: 1.49e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1222443606  898 GRKVIIFSQFTSALDLIAERLNTlnikfSMLTGQTRH--RDKVIDEFTSGTTSVFLISlKAGGTGLNLTQADTVI 970
Cdd:cd18789     49 GDKIIVFTDNVEALYRYAKRLLK-----PFITGETPQseREEILQNFREGEYNTLVVS-KVGDEGIDLPEANVAI 117
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 610-714 1.58e-03

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 40.08  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  610 GGILADDMGLGKTLqvIAYL-ASSYNTPQAGPTLIVCPT-SLVSNWQNEITKFAKSLKVTTIFGAHRNDSLQH---LAQA 684
Cdd:cd00046      3 NVLITAPTGSGKTL--AALLaALLLLLKKGKKVLVLVPTkALALQTAERLRELFGPGIRVAVLVGGSSAEEREknkLGDA 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1222443606  685 QCILTTYPLLKRDIAYYSPLYFEN---IILDEA 714
Cdd:cd00046     81 DIIIATPDMLLNLLLREDRLFLKDlklIIVDEA 113
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
 900-974 3.05e-03

C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 39.26  E-value: 3.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222443606  900 KVIIFSQFTSALDLIAERLNTL--NIKFSMLTGQTRHRD----------KVIDEFTSGTTSVfLISLKAGGTGLNLTQAD 967
Cdd:cd18801     32 RVIIFSEFRDSAEEIVNFLSKIrpGIRATRFIGQASGKSskgmsqkeqkEVIEQFRKGGYNV-LVATSIGEEGLDIGEVD 110


                   ....*..
gi 1222443606  968 TVIHFDP 974
Cdd:cd18801    111 LIICYDA 117
 
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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