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Conserved domains on  [gi|373432615|ref|NP_001243265|]
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chromodomain-helicase-DNA-binding protein 1-like isoform 2 [Homo sapiens]

Protein Classification

DEAD/DEAH box helicase; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1( domain architecture ID 13327344)

DEAD/DEAH box containing ATP-dependent helicase, similar to ISWI chromatin-remodeling complex ATPases, which are catalytic components of ISW1-type complexes, which act by remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 (SMARCAD1) is a DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
16-599 5.81e-135

Probable chromatin-remodeling complex ATPase chain; Provisional


The actual alignment was detected with superfamily member PLN03142:

Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 426.14  E-value: 5.81e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615   16 RFAPGLSCVTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSV 95
Cdd:PLN03142  240 RFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFST 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615   96 VFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGDFIQRYQDIEKESESASELHKLLQPFLLRRVKAEVATELPKKTE 175
Cdd:PLN03142  320 NYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKE 399
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  176 VVIYHGMSALQKKYYKAILMKDLDAFeNETAKKVKLQNILSQLRKCVDHPYLFDGVEP-EPFEVGDHLTEASGKLHLLDK 254
Cdd:PLN03142  400 TILKVGMSQMQKQYYKALLQKDLDVV-NAGGERKRLLNIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKMVLLDK 478
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  255 LLAFLYSGGHRVLLFSQMTQMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGQ--QPIFVFLLSTRAGGVGMNLTA 332
Cdd:PLN03142  479 LLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKpgSEKFVFLLSTRAGGLGINLAT 558
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  333 ADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIEGGHFtlgAQKPAADADl 412
Cdd:PLN03142  559 ADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD- 634
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  413 QLSEILKFGLDKLLASEGSTMDEIDLESIL--GE-------TKDGQWVSDALPAAEGGS---------RDQEEGKNHMYL 474
Cdd:PLN03142  635 ELLQMVRYGAEMVFSSKDSTITDEDIDRIIakGEeataeldAKMKKFTEDAIKFKMDDTaelydfddeDDKDENKLDFKK 714
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  475 FEGKDYSKEPSKEDRKSFEQLVNLQKTLLEKASQEGRSLRnkgsvlIPGLVEGS------TKRKRVLSPEELEDRQKKRQ 548
Cdd:PLN03142  715 IVSDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPR------IPRMPQLHdfqffnVQRLTELYEKEVRYLMQAHQ 788
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 373432615  549 EAAAKRRRLIEEKKRQ-----KEEAEHKKKM-----AWWESNNYQSFCLPSEESEPEDLEN 599
Cdd:PLN03142  789 KGQLKDTIDVAEPEEPgdpltAEEQEEKEQLleegfSTWSRRDFNAFIRACEKYGRNDIKS 849
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
616-766 7.60e-94

macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this subfamily contain a C-terminal macrodomain that show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. In addition, they also contain an SNF2 domain, defined by the presence of seven motifs with sequence similarity to DNA helicases. SNF2 proteins have the capacity to use the energy released by their DNA-dependent ATPase activity to stabilize or perturb protein-DNA interactions and play important roles in transcriptional regulation, maintenance of chromosome integrity and DNA repair.


:

Pssm-ID: 394880  Cd Length: 152  Bit Score: 289.93  E-value: 7.60e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615 616 SLKYVSGDVTHPQA-GAEDALIVHCVDDSGHWGRGGLFTALEKRSAEPRKIYELAGKMKDLSLGGVLLFPVDDKESRNKG 694
Cdd:cd03331    1 DINYVSGDVTHPQTtSTEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 373432615 695 QDLLALIVAQHRDRSNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAAR 766
Cdd:cd03331   81 RDYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
16-599 5.81e-135

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 426.14  E-value: 5.81e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615   16 RFAPGLSCVTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSV 95
Cdd:PLN03142  240 RFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFST 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615   96 VFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGDFIQRYQDIEKESESASELHKLLQPFLLRRVKAEVATELPKKTE 175
Cdd:PLN03142  320 NYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKE 399
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  176 VVIYHGMSALQKKYYKAILMKDLDAFeNETAKKVKLQNILSQLRKCVDHPYLFDGVEP-EPFEVGDHLTEASGKLHLLDK 254
Cdd:PLN03142  400 TILKVGMSQMQKQYYKALLQKDLDVV-NAGGERKRLLNIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKMVLLDK 478
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  255 LLAFLYSGGHRVLLFSQMTQMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGQ--QPIFVFLLSTRAGGVGMNLTA 332
Cdd:PLN03142  479 LLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKpgSEKFVFLLSTRAGGLGINLAT 558
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  333 ADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIEGGHFtlgAQKPAADADl 412
Cdd:PLN03142  559 ADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD- 634
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  413 QLSEILKFGLDKLLASEGSTMDEIDLESIL--GE-------TKDGQWVSDALPAAEGGS---------RDQEEGKNHMYL 474
Cdd:PLN03142  635 ELLQMVRYGAEMVFSSKDSTITDEDIDRIIakGEeataeldAKMKKFTEDAIKFKMDDTaelydfddeDDKDENKLDFKK 714
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  475 FEGKDYSKEPSKEDRKSFEQLVNLQKTLLEKASQEGRSLRnkgsvlIPGLVEGS------TKRKRVLSPEELEDRQKKRQ 548
Cdd:PLN03142  715 IVSDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPR------IPRMPQLHdfqffnVQRLTELYEKEVRYLMQAHQ 788
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 373432615  549 EAAAKRRRLIEEKKRQ-----KEEAEHKKKM-----AWWESNNYQSFCLPSEESEPEDLEN 599
Cdd:PLN03142  789 KGQLKDTIDVAEPEEPgdpltAEEQEEKEQLleegfSTWSRRDFNAFIRACEKYGRNDIKS 849
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
15-395 2.57e-103

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 333.35  E-value: 2.57e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  15 ARFAPGLSCVTYAGDKEEraclQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFS 94
Cdd:COG0553  310 AKFAPGLRVLVLDGTRER----AKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  95 VVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgDFIQRYQD-IEKESESASE-LHKLLQPFLLRRVKAEVATELPK 172
Cdd:COG0553  386 ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLK--AFRERFARpIEKGDEEALErLRRLLRPFLLRRTKEDVLKDLPE 463
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615 173 KTEVVIYHGMSALQKKYYKAIL---MKDLDAFENETAKKVKLQnILSQLRKCVDHPYLFDgvepepfEVGDHLTEASGKL 249
Cdd:COG0553  464 KTEETLYVELTPEQRALYEAVLeylRRELEGAEGIRRRGLILA-ALTRLRQICSHPALLL-------EEGAELSGRSAKL 535
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615 250 HLLDKLLAFLYSGGHRVLLFSQMTQMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGQQP-IFVFLLSTRAGGVGM 328
Cdd:COG0553  536 EALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVFLISLKAGGEGL 615
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 373432615 329 NLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIE 395
Cdd:COG0553  616 NLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
616-766 7.60e-94

macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this subfamily contain a C-terminal macrodomain that show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. In addition, they also contain an SNF2 domain, defined by the presence of seven motifs with sequence similarity to DNA helicases. SNF2 proteins have the capacity to use the energy released by their DNA-dependent ATPase activity to stabilize or perturb protein-DNA interactions and play important roles in transcriptional regulation, maintenance of chromosome integrity and DNA repair.


Pssm-ID: 394880  Cd Length: 152  Bit Score: 289.93  E-value: 7.60e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615 616 SLKYVSGDVTHPQA-GAEDALIVHCVDDSGHWGRGGLFTALEKRSAEPRKIYELAGKMKDLSLGGVLLFPVDDKESRNKG 694
Cdd:cd03331    1 DINYVSGDVTHPQTtSTEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 373432615 695 QDLLALIVAQHRDRSNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAAR 766
Cdd:cd03331   81 RDYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
16-161 2.09e-86

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: 272.77  E-value: 2.09e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  16 RFAPGLSCVTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSV 95
Cdd:cd18006   71 RFAPDLSVITYMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSV 150
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 373432615  96 VFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGDFIQRYQDIEKESESASELHKLLQPFLLRR 161
Cdd:cd18006  151 DFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKLDDFIKAYSETDDESETVEELHLLLQPFLLRR 216
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
8-228 9.69e-58

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: 198.68  E-value: 9.69e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615    8 RWaWGRPArfapgLSCVTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLH 87
Cdd:pfam00176  70 RW-VSPPA-----LRVVVLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLS 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615   88 KTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSkeEVGDFIQRY-QDIE--KESESASELHKLLQPFLLRRVKA 164
Cdd:pfam00176 144 KALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFG--SLSTFRNWFdRPIErgGGKKGVSRLHKLLKPFLLRRTKK 221
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 373432615  165 EVATELPKKTEVVIYHGMSALQKKYYKA-ILMKDLDAFENETA---KKVKLQNILSQLRKCVDHPYLF 228
Cdd:pfam00176 222 DVEKSLPPKVEYILFCRLSKLQRKLYQTfLLKKDLNAIKTGEGgreIKASLLNILMRLRKICNHPGLI 289
HELICc smart00490
helicase superfamily c-terminal domain;
277-359 4.65e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 82.26  E-value: 4.65e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615   277 DILQDYMDYRGYSYERVDGSVRGEERHLAIKNFgQQPIFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAH 356
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKF-NNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79

                   ...
gi 373432615   357 RIG 359
Cdd:smart00490  80 RAG 82
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
16-599 5.81e-135

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 426.14  E-value: 5.81e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615   16 RFAPGLSCVTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSV 95
Cdd:PLN03142  240 RFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFST 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615   96 VFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGDFIQRYQDIEKESESASELHKLLQPFLLRRVKAEVATELPKKTE 175
Cdd:PLN03142  320 NYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKE 399
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  176 VVIYHGMSALQKKYYKAILMKDLDAFeNETAKKVKLQNILSQLRKCVDHPYLFDGVEP-EPFEVGDHLTEASGKLHLLDK 254
Cdd:PLN03142  400 TILKVGMSQMQKQYYKALLQKDLDVV-NAGGERKRLLNIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKMVLLDK 478
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  255 LLAFLYSGGHRVLLFSQMTQMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGQ--QPIFVFLLSTRAGGVGMNLTA 332
Cdd:PLN03142  479 LLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKpgSEKFVFLLSTRAGGLGINLAT 558
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  333 ADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIEGGHFtlgAQKPAADADl 412
Cdd:PLN03142  559 ADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD- 634
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  413 QLSEILKFGLDKLLASEGSTMDEIDLESIL--GE-------TKDGQWVSDALPAAEGGS---------RDQEEGKNHMYL 474
Cdd:PLN03142  635 ELLQMVRYGAEMVFSSKDSTITDEDIDRIIakGEeataeldAKMKKFTEDAIKFKMDDTaelydfddeDDKDENKLDFKK 714
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  475 FEGKDYSKEPSKEDRKSFEQLVNLQKTLLEKASQEGRSLRnkgsvlIPGLVEGS------TKRKRVLSPEELEDRQKKRQ 548
Cdd:PLN03142  715 IVSDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPKEPR------IPRMPQLHdfqffnVQRLTELYEKEVRYLMQAHQ 788
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 373432615  549 EAAAKRRRLIEEKKRQ-----KEEAEHKKKM-----AWWESNNYQSFCLPSEESEPEDLEN 599
Cdd:PLN03142  789 KGQLKDTIDVAEPEEPgdpltAEEQEEKEQLleegfSTWSRRDFNAFIRACEKYGRNDIKS 849
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
15-395 2.57e-103

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 333.35  E-value: 2.57e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  15 ARFAPGLSCVTYAGDKEEraclQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFS 94
Cdd:COG0553  310 AKFAPGLRVLVLDGTRER----AKGANPFEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  95 VVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgDFIQRYQD-IEKESESASE-LHKLLQPFLLRRVKAEVATELPK 172
Cdd:COG0553  386 ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLK--AFRERFARpIEKGDEEALErLRRLLRPFLLRRTKEDVLKDLPE 463
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615 173 KTEVVIYHGMSALQKKYYKAIL---MKDLDAFENETAKKVKLQnILSQLRKCVDHPYLFDgvepepfEVGDHLTEASGKL 249
Cdd:COG0553  464 KTEETLYVELTPEQRALYEAVLeylRRELEGAEGIRRRGLILA-ALTRLRQICSHPALLL-------EEGAELSGRSAKL 535
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615 250 HLLDKLLAFLYSGGHRVLLFSQMTQMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGQQP-IFVFLLSTRAGGVGM 328
Cdd:COG0553  536 EALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVFLISLKAGGEGL 615
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 373432615 329 NLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIE 395
Cdd:COG0553  616 NLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
616-766 7.60e-94

macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this subfamily contain a C-terminal macrodomain that show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. In addition, they also contain an SNF2 domain, defined by the presence of seven motifs with sequence similarity to DNA helicases. SNF2 proteins have the capacity to use the energy released by their DNA-dependent ATPase activity to stabilize or perturb protein-DNA interactions and play important roles in transcriptional regulation, maintenance of chromosome integrity and DNA repair.


Pssm-ID: 394880  Cd Length: 152  Bit Score: 289.93  E-value: 7.60e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615 616 SLKYVSGDVTHPQA-GAEDALIVHCVDDSGHWGRGGLFTALEKRSAEPRKIYELAGKMKDLSLGGVLLFPVDDKESRNKG 694
Cdd:cd03331    1 DINYVSGDVTHPQTtSTEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 373432615 695 QDLLALIVAQHRDRSNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAAR 766
Cdd:cd03331   81 RDYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
16-161 2.09e-86

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: 272.77  E-value: 2.09e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  16 RFAPGLSCVTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSV 95
Cdd:cd18006   71 RFAPDLSVITYMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSV 150
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 373432615  96 VFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGDFIQRYQDIEKESESASELHKLLQPFLLRR 161
Cdd:cd18006  151 DFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKLDDFIKAYSETDDESETVEELHLLLQPFLLRR 216
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
8-228 9.69e-58

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: 198.68  E-value: 9.69e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615    8 RWaWGRPArfapgLSCVTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLH 87
Cdd:pfam00176  70 RW-VSPPA-----LRVVVLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLS 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615   88 KTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSkeEVGDFIQRY-QDIE--KESESASELHKLLQPFLLRRVKA 164
Cdd:pfam00176 144 KALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFG--SLSTFRNWFdRPIErgGGKKGVSRLHKLLKPFLLRRTKK 221
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 373432615  165 EVATELPKKTEVVIYHGMSALQKKYYKA-ILMKDLDAFENETA---KKVKLQNILSQLRKCVDHPYLF 228
Cdd:pfam00176 222 DVEKSLPPKVEYILFCRLSKLQRKLYQTfLLKKDLNAIKTGEGgreIKASLLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
246-370 8.26e-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: 182.29  E-value: 8.26e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615 246 SGKLHLLDKLLAFLYSGGHRVLLFSQMTQMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGQQP-IFVFLLSTRAG 324
Cdd:cd18793   10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdIRVFLLSTKAG 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 373432615 325 GVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLI 370
Cdd:cd18793   90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
10-161 1.29e-45

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: 162.53  E-value: 1.29e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  10 AWGRP-ARFAPGLSCVTYAGDKEERACLQQ-----DLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQS 83
Cdd:cd17993   65 AWQREfAKWAPDMNVIVYLGDIKSRDTIREyefyfSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDE 144
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 373432615  84 SLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLF-SKEEvgdfIQRYQDIEKESESASeLHKLLQPFLLRR 161
Cdd:cd17993  145 SLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFdIWEE----FEEEHDEEQEKGIAD-LHKELEPFILRR 218
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
16-163 5.50e-43

DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 and 5 (SMARCA1 and SMARCA5) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350755 [Multi-domain]  Cd Length: 222  Bit Score: 155.56  E-value: 5.50e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  16 RFAPGLSCVTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSV 95
Cdd:cd17997   74 RWCPSLRVVVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNS 153
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 373432615  96 VFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGD-FIQRYQDIEKESESASELHKLLQPFLLRRVK 163
Cdd:cd17997  154 RNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDeWFNVNNCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
21-161 1.09e-42

DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; Chromodomain-helicase-DNA-binding protein 6-9 (CHD6, CHD7, CHD8, and CHD9) are members of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350753 [Multi-domain]  Cd Length: 223  Bit Score: 154.71  E-value: 1.09e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  21 LSCVTYAGDKEERACLQQ-----------DLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKT 89
Cdd:cd17995   75 MNVVVYHGSGESRQIIQQyemyfkdaqgrKKKGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQG 154
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 373432615  90 LSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgDFIQRYQDIEKESEsASELHKLLQPFLLRR 161
Cdd:cd17995  155 LKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSE--EFLEEFGDLKTAEQ-VEKLQALLKPYMLRR 223
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
15-163 6.19e-39

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: 144.45  E-value: 6.19e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  15 ARFAPGLSCVTYAGDKEERACLQQDLKQESR----FHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTL 90
Cdd:cd18009   72 ARFTPSVPVLLYHGTKEERERLRKKIMKREGtlqdFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQEL 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  91 SEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSK----EEVGDFIQRYQDIEKESESASE--------LHKLLQPFL 158
Cdd:cd18009  152 KTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDlssfESWFDFSSLSDNAADISNLSEEreqnivhmLHAILKPFL 231

                 ....*
gi 373432615 159 LRRVK 163
Cdd:cd18009  232 LRRLK 236
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
15-125 4.30e-37

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: 137.31  E-value: 4.30e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  15 ARFAPGLSCVTYAGDKEERACLQQDLKQESrFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFS 94
Cdd:cd17919   70 EKWTPDLRVVVYHGSQRERAQIRAKEKLDK-FDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR 148
                         90       100       110
                 ....*....|....*....|....*....|.
gi 373432615  95 VVFSLLLTGTPIQNSLQELYSLLSFVEPDLF 125
Cdd:cd17919  149 AKRRLLLTGTPLQNNLEELWALLDFLDPPFL 179
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
10-161 5.85e-36

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: 135.90  E-value: 5.85e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  10 AWGRPAR-FAPGLSCVTYAGDKEERACLQQ-----DLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQS 83
Cdd:cd18054   84 SWQREFEiWAPEINVVVYIGDLMSRNTIREyewihSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDD 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  84 SLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFskeevgdfiQRYQDIEKESESASE-----LHKLLQPFL 158
Cdd:cd18054  164 SLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKF---------EFWEDFEEDHGKGREngyqsLHKVLEPFL 234

                 ...
gi 373432615 159 LRR 161
Cdd:cd18054  235 LRR 237
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
11-161 6.38e-36

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: 134.49  E-value: 6.38e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  11 WGRPARF-APGLSCVTYAGDkeeraclqqdlkqesrfHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKT 89
Cdd:cd17994   65 WEREFEMwAPDFYVVTYVGD-----------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRI 127
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 373432615  90 LSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgDFIQRYQDIEKEsESASELHKLLQPFLLRR 161
Cdd:cd17994  128 LNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQ--GFLEEFADISKE-DQIKKLHDLLGPHMLRR 196
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
15-163 1.77e-35

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: 134.42  E-value: 1.77e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  15 ARFAPGLSCVTYAGDKEERACLQQDLKQeSRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSE-F 93
Cdd:cd17996   73 EKWAPSVSKIVYKGTPDVRKKLQSQIRA-GKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyY 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  94 SVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSkeEVGDFIQRYQ----------DIEKESESA----SELHKLLQPFLL 159
Cdd:cd17996  152 HARYRLLLTGTPLQNNLPELWALLNFLLPKIFK--SCKTFEQWFNtpfantgeqvKIELNEEETlliiRRLHKVLRPFLL 229

                 ....
gi 373432615 160 RRVK 163
Cdd:cd17996  230 RRLK 233
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
16-173 1.00e-34

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: 132.87  E-value: 1.00e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  16 RFAPGLSCVTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSV 95
Cdd:cd18064   86 RWVPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKT 165
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 373432615  96 VFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGDFIQRYQDIEKESESASELHKLLQPFLLRRVKAEVATELPKK 173
Cdd:cd18064  166 TNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSLPPK 243
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
3-161 1.22e-33

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: 129.01  E-value: 1.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615   3 VSWEMRWAwgrpaRFAPGLSCVTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQ 82
Cdd:cd18003   63 LNWEMEFK-----RWCPGFKILTYYGSAKERKLKRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNF 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  83 SSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgDFIQRYQDIEKE-SESASE--------LHKL 153
Cdd:cd18003  138 KSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQ--EFKEWFSNPLTAmSEGSQEeneelvrrLHKV 215

                 ....*...
gi 373432615 154 LQPFLLRR 161
Cdd:cd18003  216 LRPFLLRR 223
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
15-163 1.34e-32

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: 125.76  E-value: 1.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  15 ARFAPGLSCVTYAGDKEERACLQQDLKQEsrfhVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFS 94
Cdd:cd18012   73 AKFAPELKVLVIHGTKRKREKLRALEDYD----LVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALK 148
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 373432615  95 VVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgDFIQRYQ-DIEK--ESESASELHKLLQPFLLRRVK 163
Cdd:cd18012  149 ADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYK--RFKKRFAkPIEKdgDEEALEELKKLISPFILRRLK 218
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
3-161 1.39e-31

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: 123.25  E-value: 1.39e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615   3 VSWEMRWAwgrpaRFAPGLSCVTYAGDKEERACLQQD-----------------LKQES--RFHVLLTTYEICLKDASFL 63
Cdd:cd18057   63 INWEREFE-----MWAPDFYVVTYTGDKESRSVIRENefsfednairsgkkvfrMKKEAqiKFHVLLTSYELITIDQAIL 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  64 KSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgDFIQRYQDIEKE 143
Cdd:cd18057  138 GSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLE--GFLEEFADISKE 215
                        170
                 ....*....|....*...
gi 373432615 144 SEsASELHKLLQPFLLRR 161
Cdd:cd18057  216 DQ-IKKLHDLLGPHMLRR 232
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
3-161 1.93e-31

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: 122.81  E-value: 1.93e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615   3 VSWEMRWAwgrpaRFAPGLSCVTYAGDKEERACLQQD-----------------LKQES--RFHVLLTTYEICLKDASFL 63
Cdd:cd18055   63 INWEREFQ-----MWAPDFYVVTYTGDKDSRAIIRENefsfddnavkggkkafkMKREAqvKFHVLLTSYELVTIDQAAL 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  64 KSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgDFIQRYQDIEKE 143
Cdd:cd18055  138 GSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLE--GFLEEFADISKE 215
                        170
                 ....*....|....*...
gi 373432615 144 SEsASELHKLLQPFLLRR 161
Cdd:cd18055  216 DQ-IKKLHDLLGPHMLRR 232
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
10-161 6.71e-31

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: 121.31  E-value: 6.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  10 AWGRPAR-FAPGLSCVTYAGDKEERACLQ-----QDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQS 83
Cdd:cd18053   84 SWQREIQtWAPQMNAVVYLGDINSRNMIRthewmHPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDD 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  84 SLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKeevgdfiqrYQDIEKESESASE-----LHKLLQPFL 158
Cdd:cd18053  164 SLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSS---------WEDFEEEHGKGREygyasLHKELEPFL 234

                 ...
gi 373432615 159 LRR 161
Cdd:cd18053  235 LRR 237
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
15-161 7.59e-31

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: 121.07  E-value: 7.59e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  15 ARFAPGLSCVTYAGDKEERACLQQ--DLK----QESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHK 88
Cdd:cd18002   70 SRFVPQFKVLPYWGNPKDRKVLRKfwDRKnlytRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWK 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  89 TLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLF-SKEEVGDFIQRyqDIEKESESA--------SELHKLLQPFLL 159
Cdd:cd18002  150 TLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFdSHDEFNEWFSK--DIESHAENKtglnehqlKRLHMILKPFML 227

                 ..
gi 373432615 160 RR 161
Cdd:cd18002  228 RR 229
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
16-163 9.73e-31

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: 120.89  E-value: 9.73e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  16 RFAPGLSCVTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSV 95
Cdd:cd18065   86 RWVPSLRAVCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKT 165
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 373432615  96 VFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGDFIQRYQDIEKESESASELHKLLQPFLLRRVK 163
Cdd:cd18065  166 TNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 233
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
3-161 2.88e-30

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: 119.40  E-value: 2.88e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615   3 VSWEMRWAwgrpaRFAPGLSCVTYAGDKEERACLQQD-----------------LKQES--RFHVLLTTYEICLKDASFL 63
Cdd:cd18056   63 INWEREFE-----MWAPDMYVVTYVGDKDSRAIIRENefsfednairggkkasrMKKEAsvKFHVLLTSYELITIDMAIL 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  64 KSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgDFIQRYQDIEKE 143
Cdd:cd18056  138 GSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLE--GFLEEFADIAKE 215
                        170
                 ....*....|....*...
gi 373432615 144 SEsASELHKLLQPFLLRR 161
Cdd:cd18056  216 DQ-IKKLHDMLGPHMLRR 232
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
11-161 8.10e-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: 112.05  E-value: 8.10e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  11 WGRPARFAPGLSCVTYAGDKEERACLQ-----------QDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRL 79
Cdd:cd18059   64 WEREFRTWTELNVVVYHGSQASRRTIQlyemyfkdpqgRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRL 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  80 KNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVgdFIQRYQDIEKEsESASELHKLLQPFLL 159
Cdd:cd18059  144 KNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETT--FMQEFGDLKTE-EQVQKLQAILKPMML 220

                 ..
gi 373432615 160 RR 161
Cdd:cd18059  221 RR 222
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
11-161 1.67e-27

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: 111.29  E-value: 1.67e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  11 WGRPARFAPGLSCVTYAGDKEERACLQQ-----------DLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRL 79
Cdd:cd18058   64 WEREFRTWTEMNAIVYHGSQISRQMIQQyemyyrdeqgnPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRL 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  80 KNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVgdFIQRYQDIEKEsESASELHKLLQPFLL 159
Cdd:cd18058  144 KNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETT--FLEEFGDLKTE-EQVKKLQSILKPMML 220

                 ..
gi 373432615 160 RR 161
Cdd:cd18058  221 RR 222
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
616-766 2.42e-26

macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Members of this family show similarity to the yeast protein Poa1p, reported to be a phosphatase specific for Appr-1"-p, a tRNA splicing metabolite. Poa1p may play a role in tRNA splicing regulation.


Pssm-ID: 394873  Cd Length: 135  Bit Score: 105.03  E-value: 2.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615 616 SLKYVSGDVTHPQagaEDALIVHCVDDSGHWGRGGLFTALEK--RSAEPRKIYELAGkmkdlsLGGVLLFPVDDKesrnk 693
Cdd:cd02901    1 KITYVKGDLFACP---ETKSLAHCCNCDGVMGKGIALQFKKKpgRVEELRAQCKKKL------LGGVAVLKRDGV----- 66
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 373432615 694 gQDLLALIVAQHRDRSNvlsgIKMAALEEGLKKIF-LAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAAR 766
Cdd:cd02901   67 -KRYIYYLITKKSYGPK----PTYEALRSSLEELReHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
11-125 3.62e-26

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: 106.32  E-value: 3.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  11 WGRP-ARFAPGLSCVTYAGDKEERACLQQD-LKQESRFHVLLTTYEICL---KDASFLKSFPWSVLVVDEAHRLKNQSSL 85
Cdd:cd17998   64 WLREfKRWCPSLKVEPYYGSQEERKHLRYDiLKGLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSE 143
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 373432615  86 LHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLF 125
Cdd:cd17998  144 RYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
11-161 1.89e-24

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: 102.44  E-value: 1.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  11 WGRPARFAPGLSCVTYAGDKEERACLQQ------DLKQE-----SRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRL 79
Cdd:cd18060   64 WEREFNTWTEMNTIVYHGSLASRQMIQQyemyckDSRGRlipgaYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRL 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  80 KNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEevGDFIQRYQDIEKEsESASELHKLLQPFLL 159
Cdd:cd18060  144 KNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSE--SEFLKDFGDLKTE-EQVQKLQAILKPMML 220

                 ..
gi 373432615 160 RR 161
Cdd:cd18060  221 RR 222
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
247-359 1.85e-23

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: 95.74  E-value: 1.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  247 GKLHLLDKLLAFlySGGHRVLLFSQMTQMLDIlQDYMDYRGYSYERVDGSVRGEERHLAIKNFGQQPIFVfLLSTRAGGV 326
Cdd:pfam00271   1 EKLEALLELLKK--ERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDV-LVATDVAER 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 373432615  327 GMNLTAADTVIFVDSDFNPQNDLQAAARAHRIG 359
Cdd:pfam00271  77 GLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
24-161 8.25e-23

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: 98.13  E-value: 8.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  24 VTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFL---KSFpwSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLL 100
Cdd:cd18004   90 VTADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLskkISI--DLLICDEGHRLKNSESKTTKALNSLPCRRRLL 167
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 373432615 101 LTGTPIQNSLQELYSLLSFVEPDLFSkeEVGDFIQRYQ--------------DIEKESESASELHKLLQPFLLRR 161
Cdd:cd18004  168 LTGTPIQNDLDEFFALVDFVNPGILG--SLASFRKVFEepilrsrdpdaseeDKELGAERSQELSELTSRFILRR 240
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
11-161 1.13e-22

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; Chromodomain-helicase-DNA-binding protein 9 (CHD9) acts as a transcriptional coactivator for PPARA and possibly other nuclear receptors. It is proposed to be a ATP-dependent chromatin remodeling protein. CHD9 has DNA-dependent ATPase activity and binds to A/T-rich DNA. It also associates with A/T-rich regulatory regions in promoters of genes that participate in the differentiation of progenitors during osteogenesis. CHD9 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350819 [Multi-domain]  Cd Length: 222  Bit Score: 97.38  E-value: 1.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  11 WGRPARFAPGLSCVTYAGDKEERACLQQD-----------LKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRL 79
Cdd:cd18061   64 WEREFRTWTDLNVVVYHGSLISRQMIQQYemyfrdsqgriIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRL 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  80 KNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVgdFIQRYQDIEKEsESASELHKLLQPFLL 159
Cdd:cd18061  144 KNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSEST--FMQEFGDLKTE-EQVQKLQAILKPMML 220

                 ..
gi 373432615 160 RR 161
Cdd:cd18061  221 RR 222
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
16-161 1.02e-21

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: 94.73  E-value: 1.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  16 RFAP--GLSCVTYAGDKEERACLQQdlkQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEF 93
Cdd:cd17999   76 KYFPnaFLKPLAYVGPPQERRRLRE---QGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQL 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  94 SVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVgdFIQRY----------QDIEKESESA----SELHKLLQPFLL 159
Cdd:cd17999  153 KANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQ--FQRRFlkpilasrdsKASAKEQEAGalalEALHKQVLPFLL 230

                 ..
gi 373432615 160 RR 161
Cdd:cd17999  231 RR 232
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
16-163 1.24e-21

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: 95.13  E-value: 1.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  16 RFAPGLSCVTYAGDKEERACLQQDLKQeSRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSV 95
Cdd:cd18063   94 KWAPSVVKISYKGTPAMRRSLVPQLRS-GKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYV 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  96 V-FSLLLTGTPIQNSLQELYSLLSFVEPDLFskEEVGDFIQRYQ----------DIEKESE--SASELHKLLQPFLLRRV 162
Cdd:cd18063  173 ApRRILLTGTPLQNKLPELWALLNFLLPTIF--KSCSTFEQWFNapfamtgervDLNEEETilIIRRLHKVLRPFLLRRL 250

                 .
gi 373432615 163 K 163
Cdd:cd18063  251 K 251
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
16-163 4.20e-21

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: 93.57  E-value: 4.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  16 RFAPGLSCVTYAGDKEERACLQQDLKQeSRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTL-SEFS 94
Cdd:cd18062   94 KWAPSVVKVSYKGSPAARRAFVPQLRS-GKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYV 172
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 373432615  95 VVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEV------GDFIQRYQDIEKESESA----SELHKLLQPFLLRRVK 163
Cdd:cd18062  173 APRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTfeqwfnAPFAMTGEKVDLNEEETiliiRRLHKVLRPFLLRRLK 251
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
8-161 4.00e-20

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: 90.52  E-value: 4.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615   8 RWAWGRparfapgLSCVTYAGDKEEracLQQDLKQeSRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLH 87
Cdd:cd18005   91 TWGHFE-------VGVYHGSRKDDE---LEGRLKA-GRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSKLT 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  88 KTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFS-----KEEVGDFIQRYQ-------DIEKESESASELHKLLQ 155
Cdd:cd18005  160 QAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGsrsqfKKHFSEPIKRGQrhtatarELRLGRKRKQELAVKLS 239

                 ....*.
gi 373432615 156 PFLLRR 161
Cdd:cd18005  240 KFFLRR 245
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
15-161 3.96e-19

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: 87.04  E-value: 3.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  15 ARFAPGLSCVTYAG-DKEERACLQQDLKQesRFHVLLTTYEICLKDASFLKS-----FPWSVLVVDEAHRLKNQSSLLHK 88
Cdd:cd18001   69 AKWTPGLRVKVFHGtSKKERERNLERIQR--GGGVLLTTYGMVLSNTEQLSAddhdeFKWDYVILDEGHKIKNSKTKSAK 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  89 TLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPD--LFSKEEvgdFIQRY-------------QDIEKESESASE-LHK 152
Cdd:cd18001  147 SLREIPAKNRIILTGTPIQNNLKELWALFDFACNGslLGTRKT---FKMEFenpitrgrdkdatQGEKALGSEVAEnLRQ 223

                 ....*....
gi 373432615 153 LLQPFLLRR 161
Cdd:cd18001  224 IIKPYFLRR 232
HELICc smart00490
helicase superfamily c-terminal domain;
277-359 4.65e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 82.26  E-value: 4.65e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615   277 DILQDYMDYRGYSYERVDGSVRGEERHLAIKNFgQQPIFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAH 356
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKF-NNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79

                   ...
gi 373432615   357 RIG 359
Cdd:smart00490  80 RAG 82
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
44-161 2.10e-17

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: 82.34  E-value: 2.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  44 SRFHVLLTTYEI----------------CLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQ 107
Cdd:cd18008  108 SDYDIVITTYGTlasefpknkkgggrdsKEKEASPLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQ 187
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 373432615 108 NSLQELYSLLSFVEPDLFSKEEVGD-FIQRYQDiEKESESASELHKLLQPFLLRR 161
Cdd:cd18008  188 NSLDDLYSLLRFLRVEPFGDYPWFNsDISKPFS-KNDRKALERLQALLKPILLRR 241
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
11-122 1.06e-16

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: 78.90  E-value: 1.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  11 WGRPARFAPGLSCVTYAGDKEERACLQQDLKQESRF----HVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLL 86
Cdd:cd18000   72 WWPPFRVVVLHSSGSGTGSEEKLGSIERKSQLIRKVvgdgGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEI 151
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 373432615  87 HKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEP 122
Cdd:cd18000  152 TLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
70-152 2.64e-15

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: 76.18  E-value: 2.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  70 VLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgDFIQRY-QDIEKESESAS 148
Cdd:cd18007  151 LLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLK--EFKKKFvKPIEAGQCVDS 228

                 ....
gi 373432615 149 ELHK 152
Cdd:cd18007  229 TEED 232
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
48-161 1.68e-14

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: 74.04  E-value: 1.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  48 VLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSK 127
Cdd:cd18067  118 VLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGT 197
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 373432615 128 EEVgdFIQRY--------------QDIEKESESASELHKLLQPFLLRR 161
Cdd:cd18067  198 AAE--FKKNFelpilkgrdadaseKERQLGEEKLQELISIVNRCIIRR 243
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
46-161 5.74e-14

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: 72.19  E-value: 5.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  46 FHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLF 125
Cdd:cd18066  108 YSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGIL 187
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 373432615 126 SkeEVGDFIQRYQD------------IEKE--SESASELHKLLQPFLLRR 161
Cdd:cd18066  188 G--SLSTYRKVYEEpivrsreptatpEEKKlgEARAAELTRLTGLFILRR 235
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
38-161 1.20e-13

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: 71.35  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  38 QDLKQESRFHVLLTTYEICL-----KDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQE 112
Cdd:cd18071  111 RDPKLLSKYDIVLTTYNTLAsdfgaKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKD 190
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 373432615 113 LYSLLSFVEPDLFSKEEV-GDFIQRyqDIEKESESASE-LHKLLQPFLLRR 161
Cdd:cd18071  191 LGSLLSFLHLKPFSNPEYwRRLIQR--PLTMGDPTGLKrLQVLMKQITLRR 239
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
21-161 2.53e-10

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: 61.34  E-value: 2.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  21 LSCVTYAGDKEERAClqqdlKQESRFHVLLTTYEICLKD---------ASFLKSFPWSVLVVDEAHRLKNqssllHKTLS 91
Cdd:cd18072  101 LRVCLYHGPNRERIG-----EVLRDYDIVITTYSLVAKEiptykeesrSSPLFRIAWARIILDEAHNIKN-----PKVQA 170
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 373432615  92 EFSV-----VFSLLLTGTPIQNSLQELYSLLSFVEPDLFSkeevgDFIQRYQDIEKESESASE-LHKLLQPFLLRR 161
Cdd:cd18072  171 SIAVcklraHARWALTGTPIQNNLLDMYSLLKFLRCSPFD-----DLKVWKKQVDNKSRKGGErLNILTKSLLLRR 241
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
38-161 4.57e-10

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: 60.30  E-value: 4.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  38 QDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEfsVVFS----LLLTGTPIQNSLQEL 113
Cdd:cd18010   81 KDGLRDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALP--LLKRakrvILLSGTPALSRPIEL 158
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 373432615 114 YSLLSFVEPDLFSKEEvgDFIQRYQDIE--------KESESASELHKLL-QPFLLRR 161
Cdd:cd18010  159 FTQLDALDPKLFGRFH--DFGRRYCAAKqggfgwdySGSSNLEELHLLLlATIMIRR 213
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
33-126 1.49e-09

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


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 58.45  E-value: 1.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  33 RACLQQDLKQESRFHVLLTTYEIcLKD----ASFLKSFPWSVLVVDEAHRLKN----QSSLLHKTLSEFSVVFS--LLLT 102
Cdd:cd18011   83 AQLRRLIGNPFEEFPIVIVSLDL-LKRseerRGLLLSEEWDLVVVDEAHKLRNsgggKETKRYKLGRLLAKRARhvLLLT 161
                         90       100
                 ....*....|....*....|....
gi 373432615 103 GTPIQNSLQELYSLLSFVEPDLFS 126
Cdd:cd18011  162 ATPHNGKEEDFRALLSLLDPGRFA 185
DEXDc smart00487
DEAD-like helicases superfamily;
2-130 3.58e-09

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 57.50  E-value: 3.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615     2 AVSWEMRWAwgRPARFAPGLSCVTYAGDKEERaclQQDLKQESRFHVLLTTYEICLKDAS--FLKSFPWSVLVVDEAHRL 79
Cdd:smart00487  67 AEQWAEELK--KLGPSLGLKVVGLYGGDSKRE---QLRKLESGKTDILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRL 141
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 373432615    80 KNQS--SLLHKTLSEF-SVVFSLLLTGTP---IQNSLQELYSLLSFVEPDLFSKEEV 130
Cdd:smart00487 142 LDGGfgDQLEKLLKLLpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPI 198
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
71-134 2.86e-08

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: 55.28  E-value: 2.86e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 373432615  71 LVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFS--KEEVGDFI 134
Cdd:cd18068  159 VVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGtiKEFRNRFV 224
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
41-506 1.37e-07

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 55.03  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  41 KQESRFHVLLTTYEIcLKDASFLKSFP--WSVLVVDEAHRLknQSSLLHKTLSEFSVVFSLLLTGTPiqnslqelyslls 118
Cdd:COG1061  160 KKDSDAPITVATYQS-LARRAHLDELGdrFGLVIIDEAHHA--GAPSYRRILEAFPAAYRLGLTATP------------- 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615 119 fvepdlFSKEEVGDFIQRYQDIEKEsESASEL--HKLLQPFLLRRVKAEVATELPKktevviyhgMSALQKKYYKAILmk 196
Cdd:COG1061  224 ------FRSDGREILLFLFDGIVYE-YSLKEAieDGYLAPPEYYGIRVDLTDERAE---------YDALSERLREALA-- 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615 197 dldafENETAKKVKLQNILSQlrkcvdhpylfdgvepepfevgdhlteasgklhlldkllaflYSGGHRVLLFSQMTQML 276
Cdd:COG1061  286 -----ADAERKDKILRELLRE------------------------------------------HPDDRKTLVFCSSVDHA 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615 277 DILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGQQPIfVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAH 356
Cdd:COG1061  319 EALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGEL-RILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGL 397
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615 357 RIGQNKS-VKVIRLIGRDTVeeiVYRKAASKLQLTNMIIEGGHFTLGAQKPAADADLQLSEILKFGLDKLLASEGSTMDE 435
Cdd:COG1061  398 RPAPGKEdALVYDFVGNDVP---VLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLED 474
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 373432615 436 IDLESILGETKDGQWVSDALPAAEGGSRDQEEGKNHMYLFEGKDYSKEPSKEDRKSFEQLVNLQKTLLEKA 506
Cdd:COG1061  475 ALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAAL 545
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
70-136 3.77e-07

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: 51.74  E-value: 3.77e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 373432615  70 VLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPD-LFSKEEVGDFIQR 136
Cdd:cd18069  139 VVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDfLGTRQEFSNMFER 206
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
16-160 5.72e-07

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: 51.58  E-value: 5.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  16 RFAPG-LSCVTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFP----------------------WSVLV 72
Cdd:cd18070   91 RHVPSsLKVLTYQGVKKDGALASPAPEILAEYDIVVTTYDVLRTELHYAEANRsnrrrrrqkryeappsplvlveWWRVC 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  73 VDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgDFIQRYQDIEKESESASELHK 152
Cdd:cd18070  171 LDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCDSD--WWARVLIRPQGRNKAREPLAA 248

                 ....*...
gi 373432615 153 LLQPFLLR 160
Cdd:cd18070  249 LLKELLWR 256
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
210-378 9.11e-06

Class II histone deacetylase complex subunits 2 and 3; This family of class II histone deacetylase complex subunits HDA2 and HDA3 is found in fungi, The member from S. pombe is referred to as Ccq1 in Swiss:Q10432. These proteins associate with HDA1 to generate the activity of the HDA1 histone deacetylase complex. HDA1 interacts with itself and with the HDA2-HDA3 subcomplex to form a probable tetramer and these interactions are necessary for catalytic activity. The HDA1 histone deacetylase complex is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. HDA2 and HDA3 have a conserved coiled-coil domain towards their C-terminus.


Pssm-ID: 402894  Cd Length: 281  Bit Score: 48.09  E-value: 9.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  210 KLQNILSQLRKCVDHPYLF-DGVEPEPF---EVGDHLTEASGKLHLLDKLLAFL----YSGGHRVLLFSQMTQMLDILQD 281
Cdd:pfam11496  49 SMTLCLENLSLVATHPYLLvDHYMPKSLllkDEPEKLAYTSGKFLVLNDLVNLLierdRKEPINVAIVARSGKTLDLVEA 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  282 YMDYRGYSYERVDG-SVRGEERHLAIKNFGQQPIFVFLL------STRAGGVgMNLTAADTVIFVDSDFNPQNDLQAAAR 354
Cdd:pfam11496 129 LLLGKGLSYKRYSGeMLYGENKKVSDSGNKKIHSTTCHLlsstgqLTNDDSL-LENYKFDLIIAFDSSVDTSSPSVEHLR 207
                         170       180
                  ....*....|....*....|....
gi 373432615  355 AHRIGQNKSVKVIRLIGRDTVEEI 378
Cdd:pfam11496 208 TQNRRKGNLAPIIRLVVINSIEHV 231
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
463-574 8.39e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 46.27  E-value: 8.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  463 RDQEEGKNHmylfegKDYSKEPSKEDRKSFEQLvnlQKTLLEKASQEGRSlrnkgsvlipGLVEgsTKRKRVLSPEELED 542
Cdd:pfam17380 466 RQQEEERKR------KKLELEKEKRDRKRAEEQ---RRKILEKELEERKQ----------AMIE--EERKRKLLEKEMEE 524
                          90       100       110
                  ....*....|....*....|....*....|..
gi 373432615  543 RQKKRQEaaAKRRRLIEEKKRQKEEAEHKKKM 574
Cdd:pfam17380 525 RQKAIYE--EERRREAEEERRKQQEMEERRRI 554
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
314-370 8.90e-05

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: 41.54  E-value: 8.90e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 373432615 314 IFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQnKSVKVIRLI 370
Cdd:cd18785   22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILFV 77
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
635-761 9.10e-05

macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. Macrodomains include the yeast macrodomain Poa1 which is a phosphatase of ADP-ribose-1"-phosphate, a by-product of tRNA splicing. Some macrodomains have ADPr-unrelated binding partners such as the coronavirus SUD-N (N-terminal subdomain) and SUD-M (middle subdomain) of the SARS-unique domain (SUD) which bind G-quadruplexes (unusual nucleic-acid structures formed by consecutive guanosine nucleotides). Macrodomains regulate a wide variety of cellular and organismal processes, including DNA damage repair, signal transduction, and immune response.


Pssm-ID: 394871  Cd Length: 121  Bit Score: 42.77  E-value: 9.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615 635 LIVHCVDDSGHWGrGGLFTALEKRSAEPRKIYELAGKMKD-LSLGGVLLfpvddkesrNKGQDLLALIVAqHrdrSNVLS 713
Cdd:cd02749    2 AIVNPANNDLYLG-GGVAKAISKKAGGDLQEECEERKKNGyLKVGEVAV---------TKGGNLPARYII-H---VVGPV 67
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 373432615 714 GIKMAALEEGLKKIF-----LAAKKKKASVHLPRIGHATKGFNWYGTERLIRK 761
Cdd:cd02749   68 ASSKKKTYEPLKKCVknclsLADEKGLKSVAFPAIGTGIAGFPPEEAARIMLE 120
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
62-139 1.33e-04

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: 43.88  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  62 FLKSFPWSVLVVDEAHRLKNQSSllHKTLSEFSVVFS----LLLTGTPIQNSLQELYSLLSFVEpdlfSKEEVGDFIQRY 137
Cdd:cd18013  111 SGDPWPFDMVVIDELSSFKSPRS--KRFKALRKVRPVikrlIGLTGTPSPNGLMDLWAQIALLD----QGERLGRSITAY 184

                 ..
gi 373432615 138 QD 139
Cdd:cd18013  185 RE 186
Caldesmon pfam02029
Caldesmon;
482-572 1.98e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.39  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373432615  482 KEPSKEDRKSFEQ-LVNLQKTLLEKASQEGRSLRNKGSVLIPGLVEGSTKRK---RVLSPEEledrQKKRQEAAAKRRRL 557
Cdd:pfam02029 236 REEEAEVFLEAEQkLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKKREerrKLLEEEE----QRRKQEEAERKLRE 311
                          90
                  ....*....|....*
gi 373432615  558 IEEKKRQKEEAEHKK 572
Cdd:pfam02029 312 EEEKRRMKEEIERRR 326
Selenoprotein_S pfam06936
Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) ...
546-595 2.94e-03

Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) sequences. SelS is a plasma membrane protein and is present in a variety of tissues and cell types. Selenoprotein S (SelS) is an intrinsically disordered protein. It formsa selenosulfide bond between cys 174 and Sec 188, that has a redox potential -234 mV. In vitro, SelS is an efficient reductase that depends on the presence of selenocysteine. Due to the high reactivity, SelS also has peroxidase activity that can catalyze the reduction of hydrogen peroxide. It is also resistant to inactivation by hydrogen peroxide which might provide evolutionary advantage compared to cysteine containing peroxidases.


Pssm-ID: 462043 [Multi-domain]  Cd Length: 192  Bit Score: 39.82  E-value: 2.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 373432615  546 KRQEA-AAKRRRLIE----------EKKRQKEEAEHKKKMAWWES----NNYQSFCLPSEESEPE 595
Cdd:pfam06936  80 KRQEAlEASRLRMQEeldaqaekfkEKQKQLEEEKRRQKIEMWESmqegKSYKGNAKLAQEETEE 144
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
528-575 6.54e-03

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 38.92  E-value: 6.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 373432615  528 STKRKRVLSPEELEDR-----QKKRQEAAAKRRRLIEEKKRQKEEAEHKKKMA 575
Cdd:pfam13904 128 LAKPERKVSQEEAKEVlqeweRKKLEQQQRKREEEQREQLKKEEEEQERKQLA 180
 
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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