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Conserved domains on  [gi|373428660|ref|NP_004275|]
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chromodomain-helicase-DNA-binding protein 1-like isoform 1 [Homo sapiens]

Protein Classification

DEXHc_CHD1L and Macro_Poa1p-like_SNF2 domain-containing protein( domain architecture ID 13327344)

DEXHc_CHD1L and Macro_Poa1p-like_SNF2 domain-containing protein

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
46-699 3.88e-160

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: 495.47  E-value: 3.88e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660   46 LRSYQLEGVNWLAQRF-HCQNGcILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCV 124
Cdd:PLN03142  170 MRDYQLAGLNWLIRLYeNGING-ILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  125 TYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGT 204
Cdd:PLN03142  249 KFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGT 328
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  205 PIQNSLQELYSLLSFVEPDLFSKEEVGDFIQRYQDIEKESESASELHKLLQPFLLRRVKAEVATELPKKTEVVIYHGMSA 284
Cdd:PLN03142  329 PLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQ 408
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  285 LQKKYYKAILMKDLDAFeNETAKKVKLQNILSQLRKCVDHPYLFDGVEP-EPFEVGDHLTEASGKLHLLDKLLAFLYSGG 363
Cdd:PLN03142  409 MQKQYYKALLQKDLDVV-NAGGERKRLLNIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKMVLLDKLLPKLKERD 487
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  364 HRVLLFSQMTQMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGQ--QPIFVFLLSTRAGGVGMNLTAADTVIFVDS 441
Cdd:PLN03142  488 SRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKpgSEKFVFLLSTRAGGLGINLATADIVILYDS 567
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  442 DFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIEGGHFtlgAQKPAADADlQLSEILKFG 521
Cdd:PLN03142  568 DWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD-ELLQMVRYG 643
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  522 LDKLLASEGSTMDEIDLESIL--GE-------TKDGQWVSDALPAAEGGS---------RDQEEGKNHMYLFEGKDYSKE 583
Cdd:PLN03142  644 AEMVFSSKDSTITDEDIDRIIakGEeataeldAKMKKFTEDAIKFKMDDTaelydfddeDDKDENKLDFKKIVSDNWIDP 723
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  584 PSKEDRKSFEQLVNLQKTLLEKASQEGRSLRnkgsvlIPGLVEGS------TKRKRVLSPEELEDRQKKRQEAAAKRRRL 657
Cdd:PLN03142  724 PKRERKRNYSESEYFKQAMRQGAPAKPKEPR------IPRMPQLHdfqffnVQRLTELYEKEVRYLMQAHQKGQLKDTID 797
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|..
gi 373428660  658 IEEKKRQ-----KEEAEHKKKM-----AWWESNNYQSFCLPSEESEPEDLEN 699
Cdd:PLN03142  798 VAEPEEPgdpltAEEQEEKEQLleegfSTWSRRDFNAFIRACEKYGRNDIKS 849
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
716-866 4.00e-93

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: 4.00e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 716 SLKYVSGDVTHPQA-GAEDALIVHCVDDSGHWGRGGLFTALEKRSAEPRKIYELAGKMKDLSLGGVLLFPVDDKESRNKG 794
Cdd:cd03331    1 DINYVSGDVTHPQTtSTEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 373428660 795 QDLLALIVAQHRDRSNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAAR 866
Cdd:cd03331   81 RDYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
46-699 3.88e-160

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 495.47  E-value: 3.88e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660   46 LRSYQLEGVNWLAQRF-HCQNGcILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCV 124
Cdd:PLN03142  170 MRDYQLAGLNWLIRLYeNGING-ILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  125 TYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGT 204
Cdd:PLN03142  249 KFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGT 328
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  205 PIQNSLQELYSLLSFVEPDLFSKEEVGDFIQRYQDIEKESESASELHKLLQPFLLRRVKAEVATELPKKTEVVIYHGMSA 284
Cdd:PLN03142  329 PLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQ 408
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  285 LQKKYYKAILMKDLDAFeNETAKKVKLQNILSQLRKCVDHPYLFDGVEP-EPFEVGDHLTEASGKLHLLDKLLAFLYSGG 363
Cdd:PLN03142  409 MQKQYYKALLQKDLDVV-NAGGERKRLLNIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKMVLLDKLLPKLKERD 487
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  364 HRVLLFSQMTQMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGQ--QPIFVFLLSTRAGGVGMNLTAADTVIFVDS 441
Cdd:PLN03142  488 SRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKpgSEKFVFLLSTRAGGLGINLATADIVILYDS 567
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  442 DFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIEGGHFtlgAQKPAADADlQLSEILKFG 521
Cdd:PLN03142  568 DWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD-ELLQMVRYG 643
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  522 LDKLLASEGSTMDEIDLESIL--GE-------TKDGQWVSDALPAAEGGS---------RDQEEGKNHMYLFEGKDYSKE 583
Cdd:PLN03142  644 AEMVFSSKDSTITDEDIDRIIakGEeataeldAKMKKFTEDAIKFKMDDTaelydfddeDDKDENKLDFKKIVSDNWIDP 723
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  584 PSKEDRKSFEQLVNLQKTLLEKASQEGRSLRnkgsvlIPGLVEGS------TKRKRVLSPEELEDRQKKRQEAAAKRRRL 657
Cdd:PLN03142  724 PKRERKRNYSESEYFKQAMRQGAPAKPKEPR------IPRMPQLHdfqffnVQRLTELYEKEVRYLMQAHQKGQLKDTID 797
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|..
gi 373428660  658 IEEKKRQ-----KEEAEHKKKM-----AWWESNNYQSFCLPSEESEPEDLEN 699
Cdd:PLN03142  798 VAEPEEPgdpltAEEQEEKEQLleegfSTWSRRDFNAFIRACEKYGRNDIKS 849
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
46-261 2.26e-138

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: 410.68  E-value: 2.26e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVT 125
Cdd:cd18006    1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 126 YAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTP 205
Cdd:cd18006   81 YMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 373428660 206 IQNSLQELYSLLSFVEPDLFSKEEVGDFIQRYQDIEKESESASELHKLLQPFLLRR 261
Cdd:cd18006  161 IQNSLQELYALLSFIEPNVFPKDKLDDFIKAYSETDDESETVEELHLLLQPFLLRR 216
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
2-495 2.20e-135

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 420.02  E-value: 2.20e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660   2 ERAGATSRGGQAPGFLLRLHTEGRAEAARVQEQDLRQWGLTGIH-------------LRSYQLEGVNWLAQRFHCQNGCI 68
Cdd:COG0553  185 ALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLRealeslpaglkatLRPYQLEGAAWLLFLRRLGLGGL 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  69 LGDEMGLGKTCQTIALFIYLAGRlNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEEraclQQDLKQESRFHV 148
Cdd:COG0553  265 LADDMGLGKTIQALALLLELKER-GLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRER----AKGANPFEDADL 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 149 LLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKE 228
Cdd:COG0553  340 VITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSL 419
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 229 EvgDFIQRYQD-IEKESESASE-LHKLLQPFLLRRVKAEVATELPKKTEVVIYHGMSALQKKYYKAIL---MKDLDAFEN 303
Cdd:COG0553  420 K--AFRERFARpIEKGDEEALErLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLeylRRELEGAEG 497
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 304 ETAKKVKLQnILSQLRKCVDHPYLFDgvepepfEVGDHLTEASGKLHLLDKLLAFLYSGGHRVLLFSQMTQMLDILQDYM 383
Cdd:COG0553  498 IRRRGLILA-ALTRLRQICSHPALLL-------EEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERL 569
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 384 DYRGYSYERVDGSVRGEERHLAIKNFGQQP-IFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNK 462
Cdd:COG0553  570 EERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTR 649
                        490       500       510
                 ....*....|....*....|....*....|...
gi 373428660 463 SVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIE 495
Cdd:COG0553  650 DVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
716-866 4.00e-93

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: 4.00e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 716 SLKYVSGDVTHPQA-GAEDALIVHCVDDSGHWGRGGLFTALEKRSAEPRKIYELAGKMKDLSLGGVLLFPVDDKESRNKG 794
Cdd:cd03331    1 DINYVSGDVTHPQTtSTEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 373428660 795 QDLLALIVAQHRDRSNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAAR 866
Cdd:cd03331   81 RDYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
49-328 7.00e-89

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: 284.19  E-value: 7.00e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660   49 YQLEGVNWLAQRfHCQ--NGCILGDEMGLGKTCQTIALFIYL-AGRLNDEGPFLILCPLSVLSNWKEEMQRFA--PGLSC 123
Cdd:pfam00176   1 YQIEGVNWMLSL-ENNlgRGGILADEMGLGKTLQTISLLLYLkHVDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  124 VTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTG 203
Cdd:pfam00176  80 VVLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  204 TPIQNSLQELYSLLSFVEPDLFSkeEVGDFIQRY-QDIE--KESESASELHKLLQPFLLRRVKAEVATELPKKTEVVIYH 280
Cdd:pfam00176 160 TPLQNNLEELWALLNFLRPGPFG--SLSTFRNWFdRPIErgGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFC 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 373428660  281 GMSALQKKYYKA-ILMKDLDAFENETA---KKVKLQNILSQLRKCVDHPYLF 328
Cdd:pfam00176 238 RLSKLQRKLYQTfLLKKDLNAIKTGEGgreIKASLLNILMRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
41-230 2.52e-27

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 110.27  E-value: 2.52e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660    41 LTGIHLRSYQLEGVNWLAQRFHcqnGCILGDEMGLGKTCQtIALFIYLAGRLNDEGPFLILCPLSVL-SNWKEEMQRFAP 119
Cdd:smart00487   4 FGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLA-ALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660   120 ---GLSCVTYAGDKEERaclQQDLKQESRFHVLLTTYEICLKDAS--FLKSFPWSVLVVDEAHRLKNQS--SLLHKTLSE 192
Cdd:smart00487  80 slgLKVVGLYGGDSKRE---QLRKLESGKTDILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLKL 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 373428660   193 F-SVVFSLLLTGTP---IQNSLQELYSLLSFVEPDLFSKEEV 230
Cdd:smart00487 157 LpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPI 198
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
46-699 3.88e-160

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 495.47  E-value: 3.88e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660   46 LRSYQLEGVNWLAQRF-HCQNGcILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCV 124
Cdd:PLN03142  170 MRDYQLAGLNWLIRLYeNGING-ILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  125 TYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGT 204
Cdd:PLN03142  249 KFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGT 328
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  205 PIQNSLQELYSLLSFVEPDLFSKEEVGDFIQRYQDIEKESESASELHKLLQPFLLRRVKAEVATELPKKTEVVIYHGMSA 284
Cdd:PLN03142  329 PLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQ 408
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  285 LQKKYYKAILMKDLDAFeNETAKKVKLQNILSQLRKCVDHPYLFDGVEP-EPFEVGDHLTEASGKLHLLDKLLAFLYSGG 363
Cdd:PLN03142  409 MQKQYYKALLQKDLDVV-NAGGERKRLLNIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKMVLLDKLLPKLKERD 487
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  364 HRVLLFSQMTQMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGQ--QPIFVFLLSTRAGGVGMNLTAADTVIFVDS 441
Cdd:PLN03142  488 SRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKpgSEKFVFLLSTRAGGLGINLATADIVILYDS 567
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  442 DFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIEGGHFtlgAQKPAADADlQLSEILKFG 521
Cdd:PLN03142  568 DWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD-ELLQMVRYG 643
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  522 LDKLLASEGSTMDEIDLESIL--GE-------TKDGQWVSDALPAAEGGS---------RDQEEGKNHMYLFEGKDYSKE 583
Cdd:PLN03142  644 AEMVFSSKDSTITDEDIDRIIakGEeataeldAKMKKFTEDAIKFKMDDTaelydfddeDDKDENKLDFKKIVSDNWIDP 723
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  584 PSKEDRKSFEQLVNLQKTLLEKASQEGRSLRnkgsvlIPGLVEGS------TKRKRVLSPEELEDRQKKRQEAAAKRRRL 657
Cdd:PLN03142  724 PKRERKRNYSESEYFKQAMRQGAPAKPKEPR------IPRMPQLHdfqffnVQRLTELYEKEVRYLMQAHQKGQLKDTID 797
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|..
gi 373428660  658 IEEKKRQ-----KEEAEHKKKM-----AWWESNNYQSFCLPSEESEPEDLEN 699
Cdd:PLN03142  798 VAEPEEPgdpltAEEQEEKEQLleegfSTWSRRDFNAFIRACEKYGRNDIKS 849
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
46-261 2.26e-138

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: 410.68  E-value: 2.26e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVT 125
Cdd:cd18006    1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 126 YAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTP 205
Cdd:cd18006   81 YMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 373428660 206 IQNSLQELYSLLSFVEPDLFSKEEVGDFIQRYQDIEKESESASELHKLLQPFLLRR 261
Cdd:cd18006  161 IQNSLQELYALLSFIEPNVFPKDKLDDFIKAYSETDDESETVEELHLLLQPFLLRR 216
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
2-495 2.20e-135

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 420.02  E-value: 2.20e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660   2 ERAGATSRGGQAPGFLLRLHTEGRAEAARVQEQDLRQWGLTGIH-------------LRSYQLEGVNWLAQRFHCQNGCI 68
Cdd:COG0553  185 ALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLRealeslpaglkatLRPYQLEGAAWLLFLRRLGLGGL 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  69 LGDEMGLGKTCQTIALFIYLAGRlNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEEraclQQDLKQESRFHV 148
Cdd:COG0553  265 LADDMGLGKTIQALALLLELKER-GLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRER----AKGANPFEDADL 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 149 LLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKE 228
Cdd:COG0553  340 VITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSL 419
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 229 EvgDFIQRYQD-IEKESESASE-LHKLLQPFLLRRVKAEVATELPKKTEVVIYHGMSALQKKYYKAIL---MKDLDAFEN 303
Cdd:COG0553  420 K--AFRERFARpIEKGDEEALErLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLeylRRELEGAEG 497
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 304 ETAKKVKLQnILSQLRKCVDHPYLFDgvepepfEVGDHLTEASGKLHLLDKLLAFLYSGGHRVLLFSQMTQMLDILQDYM 383
Cdd:COG0553  498 IRRRGLILA-ALTRLRQICSHPALLL-------EEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERL 569
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 384 DYRGYSYERVDGSVRGEERHLAIKNFGQQP-IFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNK 462
Cdd:COG0553  570 EERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTR 649
                        490       500       510
                 ....*....|....*....|....*....|...
gi 373428660 463 SVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIE 495
Cdd:COG0553  650 DVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
716-866 4.00e-93

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: 4.00e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 716 SLKYVSGDVTHPQA-GAEDALIVHCVDDSGHWGRGGLFTALEKRSAEPRKIYELAGKMKDLSLGGVLLFPVDDKESRNKG 794
Cdd:cd03331    1 DINYVSGDVTHPQTtSTEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 373428660 795 QDLLALIVAQHRDRSNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAAR 866
Cdd:cd03331   81 RDYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
49-328 7.00e-89

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: 284.19  E-value: 7.00e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660   49 YQLEGVNWLAQRfHCQ--NGCILGDEMGLGKTCQTIALFIYL-AGRLNDEGPFLILCPLSVLSNWKEEMQRFA--PGLSC 123
Cdd:pfam00176   1 YQIEGVNWMLSL-ENNlgRGGILADEMGLGKTLQTISLLLYLkHVDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  124 VTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTG 203
Cdd:pfam00176  80 VVLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  204 TPIQNSLQELYSLLSFVEPDLFSkeEVGDFIQRY-QDIE--KESESASELHKLLQPFLLRRVKAEVATELPKKTEVVIYH 280
Cdd:pfam00176 160 TPLQNNLEELWALLNFLRPGPFG--SLSTFRNWFdRPIErgGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFC 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 373428660  281 GMSALQKKYYKA-ILMKDLDAFENETA---KKVKLQNILSQLRKCVDHPYLF 328
Cdd:pfam00176 238 RLSKLQRKLYQTfLLKKDLNAIKTGEGgreIKASLLNILMRLRKICNHPGLI 289
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
45-261 1.50e-78

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: 253.82  E-value: 1.50e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  45 HLRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCV 124
Cdd:cd17993    1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 125 TYAGDKEERACLQQ-----DLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSL 199
Cdd:cd17993   81 VYLGDIKSRDTIREyefyfSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 373428660 200 LLTGTPIQNSLQELYSLLSFVEPDLF-SKEEvgdfIQRYQDIEKESESASeLHKLLQPFLLRR 261
Cdd:cd17993  161 LITGTPLQNSLKELWALLHFLMPGKFdIWEE----FEEEHDEEQEKGIAD-LHKELEPFILRR 218
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
46-225 3.80e-77

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: 248.63  E-value: 3.80e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVT 125
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 126 YAGDKEERACLQQDLKQESrFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTP 205
Cdd:cd17919   81 YHGSQRERAQIRAKEKLDK-FDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTP 159
                        170       180
                 ....*....|....*....|
gi 373428660 206 IQNSLQELYSLLSFVEPDLF 225
Cdd:cd17919  160 LQNNLEELWALLDFLDPPFL 179
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
46-261 1.65e-75

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: 246.01  E-value: 1.65e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPgLSCVT 125
Cdd:cd17995    1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 126 YAGDKEERACLQQ-----------DLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFS 194
Cdd:cd17995   80 YHGSGESRQIIQQyemyfkdaqgrKKKGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 373428660 195 VVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgDFIQRYQDIEKESEsASELHKLLQPFLLRR 261
Cdd:cd17995  160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSE--EFLEEFGDLKTAEQ-VEKLQALLKPYMLRR 223
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
46-263 4.89e-73

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: 239.15  E-value: 4.89e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRFHcqNGC--ILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSC 123
Cdd:cd17997    4 MRDYQIRGLNWLISLFE--NGIngILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLRV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 124 VTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTG 203
Cdd:cd17997   82 VVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTG 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 373428660 204 TPIQNSLQELYSLLSFVEPDLFSKEEVGD-FIQRYQDIEKESESASELHKLLQPFLLRRVK 263
Cdd:cd17997  162 TPLQNNLHELWALLNFLLPDVFTSSEDFDeWFNVNNCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
43-263 5.26e-69

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: 228.81  E-value: 5.26e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  43 GIHLRSYQLEGVNWLAQRFhcQNGC--ILGDEMGLGKTCQTIALFIYLAGRLNDeGPFLILCPLSVLSNWKEEMQRFAPG 120
Cdd:cd18009    1 GGVMRPYQLEGMEWLRMLW--ENGIngILADEMGLGKTIQTIALLAHLRERGVW-GPFLVIAPLSTLPNWVNEFARFTPS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 121 LSCVTYAGDKEERACLQQDLKQESR----FHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVV 196
Cdd:cd18009   78 VPVLLYHGTKEERERLRKKIMKREGtlqdFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSD 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 373428660 197 FSLLLTGTPIQNSLQELYSLLSFVEPDLFSK----EEVGDFIQRYQDIEKESESASE--------LHKLLQPFLLRRVK 263
Cdd:cd18009  158 NRLLLTGTPLQNNLSELWSLLNFLLPDVFDDlssfESWFDFSSLSDNAADISNLSEEreqnivhmLHAILKPFLLRRLK 236
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
46-263 3.20e-66

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: 220.51  E-value: 3.20e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIAlFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVT 125
Cdd:cd18012    5 LRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLA-LLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKVLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 126 YAGDKEERACLQQDLKQEsrfhVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTP 205
Cdd:cd18012   84 IHGTKRKREKLRALEDYD----LVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTP 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 373428660 206 IQNSLQELYSLLSFVEPDLFSKEEvgDFIQRYQ-DIEK--ESESASELHKLLQPFLLRRVK 263
Cdd:cd18012  160 IENHLGELWSIFDFLNPGLLGSYK--RFKKRFAkPIEKdgDEEALEELKKLISPFILRRLK 218
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
40-261 2.31e-65

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: 219.11  E-value: 2.31e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  40 GLTGIHLRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAP 119
Cdd:cd18054   15 GGENLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFEIWAP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 120 GLSCVTYAGDKEERACLQQ-----DLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFS 194
Cdd:cd18054   95 EINVVVYIGDLMSRNTIREyewihSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFK 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 373428660 195 VVFSLLLTGTPIQNSLQELYSLLSFVEPDLFskeevgdfiQRYQDIEKESESASE-----LHKLLQPFLLRR 261
Cdd:cd18054  175 SNHRLLITGTPLQNSLKELWSLLHFIMPEKF---------EFWEDFEEDHGKGREngyqsLHKVLEPFLLRR 237
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
46-263 2.85e-65

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: 218.39  E-value: 2.85e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRFHCQ-NGcILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCV 124
Cdd:cd17996    4 LKEYQLKGLQWMVSLYNNNlNG-ILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSKI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 125 TYAGDKEERACLQQDLKQeSRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSE-FSVVFSLLLTG 203
Cdd:cd17996   83 VYKGTPDVRKKLQSQIRA-GKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyYHARYRLLLTG 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 373428660 204 TPIQNSLQELYSLLSFVEPDLFSkeEVGDFIQRYQ----------DIEKESESA----SELHKLLQPFLLRRVK 263
Cdd:cd17996  162 TPLQNNLPELWALLNFLLPKIFK--SCKTFEQWFNtpfantgeqvKIELNEEETlliiRRLHKVLRPFLLRRLK 233
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
46-261 7.99e-62

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: 208.75  E-value: 7.99e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRFHCQ-NGcILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCV 124
Cdd:cd18003    1 LREYQHIGLDWLATLYEKNlNG-ILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 125 TYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGT 204
Cdd:cd18003   80 TYYGSAKERKLKRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGT 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 373428660 205 PIQNSLQELYSLLSFVEPDLFSKEEvgDFIQRYQDIEKE-SESASE--------LHKLLQPFLLRR 261
Cdd:cd18003  160 PLQNSLMELWSLMHFLMPHIFQSHQ--EFKEWFSNPLTAmSEGSQEeneelvrrLHKVLRPFLLRR 223
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
46-261 6.48e-60

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: 202.28  E-value: 6.48e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLaqRFHCQNG--CILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSC 123
Cdd:cd17994    1 LHPYQLEGLNWL--RFSWAQGtdTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 124 VTYAGDkeeraclqqdlkqesrfHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTG 203
Cdd:cd17994   79 VTYVGD-----------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTG 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 373428660 204 TPIQNSLQELYSLLSFVEPDLFSKEEvgDFIQRYQDIEKEsESASELHKLLQPFLLRR 261
Cdd:cd17994  142 TPLQNNLEELFHLLNFLTPERFNNLQ--GFLEEFADISKE-DQIKKLHDLLGPHMLRR 196
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
46-261 2.46e-58

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: 199.27  E-value: 2.46e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVT 125
Cdd:cd18002    1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 126 YAGDKEERACLQQ--DLK----QESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSL 199
Cdd:cd18002   81 YWGNPKDRKVLRKfwDRKnlytRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 373428660 200 LLTGTPIQNSLQELYSLLSFVEPDLF-SKEEVGDFIQRyqDIEKESESA--------SELHKLLQPFLLRR 261
Cdd:cd18002  161 LLTGTPIQNSMAELWALLHFIMPTLFdSHDEFNEWFSK--DIESHAENKtglnehqlKRLHMILKPFMLRR 229
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
40-261 4.25e-58

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: 199.12  E-value: 4.25e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  40 GLTGIHLRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAP 119
Cdd:cd18053   15 GHEGLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 120 GLSCVTYAGDKEERACLQ-----QDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFS 194
Cdd:cd18053   95 QMNAVVYLGDINSRNMIRthewmHPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFK 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 373428660 195 VVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKeevgdfiqrYQDIEKESESASE-----LHKLLQPFLLRR 261
Cdd:cd18053  175 SNHRLLITGTPLQNSLKELWSLLHFIMPEKFSS---------WEDFEEEHGKGREygyasLHKELEPFLLRR 237
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
38-273 1.68e-57

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: 197.58  E-value: 1.68e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  38 QWGltgiHLRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRF 117
Cdd:cd18064   12 KWG----KLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKRW 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 118 APGLSCVTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVF 197
Cdd:cd18064   88 VPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTN 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 373428660 198 SLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGDFIQRYQDIEKESESASELHKLLQPFLLRRVKAEVATELPKK 273
Cdd:cd18064  168 RLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSLPPK 243
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
46-261 1.27e-53

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: 186.37  E-value: 1.27e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLaqRFHCQNGC--ILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSC 123
Cdd:cd18055    1 LHMYQLEGLNWL--RFSWAQGTdtILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 124 VTYAGDKEERACLQQD-----------------LKQES--RFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSS 184
Cdd:cd18055   79 VTYTGDKDSRAIIRENefsfddnavkggkkafkMKREAqvKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQS 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 373428660 185 LLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgDFIQRYQDIEKESEsASELHKLLQPFLLRR 261
Cdd:cd18055  159 KFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLE--GFLEEFADISKEDQ-IKKLHDLLGPHMLRR 232
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
41-263 1.74e-53

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: 185.99  E-value: 1.74e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  41 LTGIHLRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPG 120
Cdd:cd18065   11 VKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 121 LSCVTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLL 200
Cdd:cd18065   91 LRAVCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLL 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 373428660 201 LTGTPIQNSLQELYSLLSFVEPDLFSKEEVGDFIQRYQDIEKESESASELHKLLQPFLLRRVK 263
Cdd:cd18065  171 LTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 233
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
346-470 1.75e-53

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 182.29  E-value: 1.75e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 346 SGKLHLLDKLLAFLYSGGHRVLLFSQMTQMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGQQP-IFVFLLSTRAG 424
Cdd:cd18793   10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdIRVFLLSTKAG 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 373428660 425 GVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLI 470
Cdd:cd18793   90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
46-225 5.50e-53

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: 182.97  E-value: 5.50e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIALFIYLAgRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVT 125
Cdd:cd17998    1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLK-EIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 126 YAGDKEERACLQQD-LKQESRFHVLLTTYEICL---KDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLL 201
Cdd:cd17998   80 YYGSQEERKHLRYDiLKGLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLL 159
                        170       180
                 ....*....|....*....|....
gi 373428660 202 TGTPIQNSLQELYSLLSFVEPDLF 225
Cdd:cd17998  160 TGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
46-261 6.53e-53

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: 184.50  E-value: 6.53e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLaqRFHCQNGC--ILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSC 123
Cdd:cd18057    1 LHPYQLEGLNWL--RFSWAQGTdtILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 124 VTYAGDKEERACLQQD-----------------LKQES--RFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSS 184
Cdd:cd18057   79 VTYTGDKESRSVIRENefsfednairsgkkvfrMKKEAqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQS 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 373428660 185 LLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgDFIQRYQDIEKESEsASELHKLLQPFLLRR 261
Cdd:cd18057  159 KFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLE--GFLEEFADISKEDQ-IKKLHDLLGPHMLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
46-261 6.73e-51

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: 178.72  E-value: 6.73e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLaqRFHCQNGC--ILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSC 123
Cdd:cd18056    1 LHPYQLEGLNWL--RFSWAQGTdtILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 124 VTYAGDKEERACLQQD-----------------LKQES--RFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSS 184
Cdd:cd18056   79 VTYVGDKDSRAIIRENefsfednairggkkasrMKKEAsvKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQS 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 373428660 185 LLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgDFIQRYQDIEKESEsASELHKLLQPFLLRR 261
Cdd:cd18056  159 KFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLE--GFLEEFADIAKEDQ-IKKLHDMLGPHMLRR 232
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
46-261 2.61e-50

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: 176.77  E-value: 2.61e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIALF--IYLAGRlndEGPFLILCPLSVLSNWKEEMQRFAPgLSC 123
Cdd:cd18058    1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLseIFLMGI---RGPFLIIAPLSTITNWEREFRTWTE-MNA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 124 VTYAGDKEERACLQQ-----------DLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSE 192
Cdd:cd18058   77 IVYHGSQISRQMIQQyemyyrdeqgnPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKL 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 373428660 193 FSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVgdFIQRYQDIEKEsESASELHKLLQPFLLRR 261
Cdd:cd18058  157 MALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETT--FLEEFGDLKTE-EQVKKLQSILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
46-261 6.51e-50

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: 175.61  E-value: 6.51e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIALF--IYLAGRlndEGPFLILCPLSVLSNWKEEMQRFAPgLSC 123
Cdd:cd18059    1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLyeIYLKGI---HGPFLVIAPLSTIPNWEREFRTWTE-LNV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 124 VTYAGDKEERACLQ-----------QDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSE 192
Cdd:cd18059   77 VVYHGSQASRRTIQlyemyfkdpqgRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKM 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 373428660 193 FSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVgdFIQRYQDIEKEsESASELHKLLQPFLLRR 261
Cdd:cd18059  157 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETT--FMQEFGDLKTE-EQVQKLQAILKPMMLRR 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
46-261 1.68e-48

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: 171.39  E-value: 1.68e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIALF--IYLAGRlndEGPFLILCPLSVLSNWKEEMQRFAPgLSC 123
Cdd:cd18060    1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLqeVYNVGI---HGPFLVIAPLSTITNWEREFNTWTE-MNT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 124 VTYAGDKEERACLQQ------DLKQE-----SRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSE 192
Cdd:cd18060   77 IVYHGSLASRQMIQQyemyckDSRGRlipgaYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKH 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 373428660 193 FSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEevGDFIQRYQDIEKEsESASELHKLLQPFLLRR 261
Cdd:cd18060  157 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSE--SEFLKDFGDLKTE-EQVQKLQAILKPMMLRR 222
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
46-261 1.79e-46

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: 166.79  E-value: 1.79e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIALFIYLAGRLNDE--------------------GPFLILCPLS 105
Cdd:cd18005    1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRrdrennrprfkkkppassakKPVLIVAPLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 106 VLSNWKEEMQRFAP-GLSCVTYAGDKEEracLQQDLKQeSRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSS 184
Cdd:cd18005   81 VLYNWKDELDTWGHfEVGVYHGSRKDDE---LEGRLKA-GRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 185 LLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFS-----KEEVGDFIQRYQ-------DIEKESESASELHK 252
Cdd:cd18005  157 KLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGsrsqfKKHFSEPIKRGQrhtatarELRLGRKRKQELAV 236

                 ....*....
gi 373428660 253 LLQPFLLRR 261
Cdd:cd18005  237 KLSKFFLRR 245
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
21-263 1.12e-45

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: 164.47  E-value: 1.12e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  21 HTEGRAEAARVQEQDLRqwgLTGIHLRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLI 100
Cdd:cd18063    2 YTVAHAITERVEKQSSL---LINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 101 LCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQDLKQeSRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLK 180
Cdd:cd18063   79 IVPLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRS-GKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 181 NQSSLLHKTLSEFSVV-FSLLLTGTPIQNSLQELYSLLSFVEPDLFskEEVGDFIQRYQ----------DIEKESE--SA 247
Cdd:cd18063  158 NHHCKLTQVLNTHYVApRRILLTGTPLQNKLPELWALLNFLLPTIF--KSCSTFEQWFNapfamtgervDLNEEETilII 235
                        250
                 ....*....|....*.
gi 373428660 248 SELHKLLQPFLLRRVK 263
Cdd:cd18063  236 RRLHKVLRPFLLRRLK 251
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
46-263 6.11e-45

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: 162.52  E-value: 6.11e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVT 125
Cdd:cd18062   24 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 126 YAGDKEERACLQQDLKQeSRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTL-SEFSVVFSLLLTGT 204
Cdd:cd18062  104 YKGSPAARRAFVPQLRS-GKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRRLLLTGT 182
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 373428660 205 PIQNSLQELYSLLSFVEPDLFSKEEV------GDFIQRYQDIEKESESA----SELHKLLQPFLLRRVK 263
Cdd:cd18062  183 PLQNKLPELWALLNFLLPTIFKSCSTfeqwfnAPFAMTGEKVDLNEEETiliiRRLHKVLRPFLLRRLK 251
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
46-261 1.20e-44

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: 160.56  E-value: 1.20e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIAlFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFApGLSCVT 125
Cdd:cd18061    1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSIT-FLYEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 126 YAGDKEERACLQQD-----------LKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFS 194
Cdd:cd18061   79 YHGSLISRQMIQQYemyfrdsqgriIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 373428660 195 VVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVgdFIQRYQDIEKEsESASELHKLLQPFLLRR 261
Cdd:cd18061  159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSEST--FMQEFGDLKTE-EQVQKLQAILKPMMLRR 222
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
46-261 1.61e-43

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: 157.83  E-value: 1.61e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRFH-----CQNGCILGDEMGLGKTCQTIALFIYLAGRLNDEGP----FLILCPLSVLSNWKEEMQR 116
Cdd:cd18004    1 LRPHQREGVQFLYDCLTgrrgyGGGGAILADEMGLGKTLQAIALVWTLLKQGPYGKPtakkALIVCPSSLVGNWKAEFDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 117 FAPG--LSCVTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFL---KSFpwSVLVVDEAHRLKNQSSLLHKTLS 191
Cdd:cd18004   81 WLGLrrIKVVTADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLskkISI--DLLICDEGHRLKNSESKTTKALN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 192 EFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSkeEVGDFIQRYQ--------------DIEKESESASELHKLLQPF 257
Cdd:cd18004  159 SLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILG--SLASFRKVFEepilrsrdpdaseeDKELGAERSQELSELTSRF 236

                 ....
gi 373428660 258 LLRR 261
Cdd:cd18004  237 ILRR 240
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
46-222 6.45e-42

DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, also known Cockayne syndrome group B (CSB), Rad26 in Saccharomyces cerevisiae, and Rhp26 in Schizosaccharomyces pombe) is a DNA-binding protein that is important in transcription-coupled excision repair. ERCC6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350758 [Multi-domain]  Cd Length: 193  Bit Score: 151.71  E-value: 6.45e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLaQRFHCQN-GCILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGL--- 121
Cdd:cd18000    1 LFKYQQTGVQWL-WELHCQRvGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFrvv 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 122 ---SCVTYAGDKEERACLQQDLKQESRF----HVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFS 194
Cdd:cd18000   80 vlhSSGSGTGSEEKLGSIERKSQLIRKVvgdgGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLR 159
                        170       180
                 ....*....|....*....|....*...
gi 373428660 195 VVFSLLLTGTPIQNSLQELYSLLSFVEP 222
Cdd:cd18000  160 TPHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
46-261 1.62e-41

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: 152.12  E-value: 1.62e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLA--QRFHCQNgcILGDEMGLGKTCQTIALfIYL--AGRLNDEGPF----LILCPLSVLSNWKEEMQRF 117
Cdd:cd17999    1 LRPYQQEGINWLAflNKYNLHG--ILCDDMGLGKTLQTLCI-LASdhHKRANSFNSEnlpsLVVCPPTLVGHWVAEIKKY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 118 AP--GLSCVTYAGDKEERACLQQdlkQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSV 195
Cdd:cd17999   78 FPnaFLKPLAYVGPPQERRRLRE---QGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 196 VFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVgdFIQRY----------QDIEKESESA----SELHKLLQPFLLRR 261
Cdd:cd17999  155 NHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQ--FQRRFlkpilasrdsKASAKEQEAGalalEALHKQVLPFLLRR 232
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
46-261 2.39e-39

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: 145.98  E-value: 2.39e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIAlfiYLAGrLNDEGPF---LILCPLSVLSNWKEEMQRFAPGLS 122
Cdd:cd18001    1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICA---FLSG-MFDSGLIksvLVVMPTSLIPHWVKEFAKWTPGLR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 123 CVTYAG-DKEERACLQQDLKQesRFHVLLTTYEICLKDASFLKS-----FPWSVLVVDEAHRLKNQSSLLHKTLSEFSVV 196
Cdd:cd18001   77 VKVFHGtSKKERERNLERIQR--GGGVLLTTYGMVLSNTEQLSAddhdeFKWDYVILDEGHKIKNSKTKSAKSLREIPAK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 197 FSLLLTGTPIQNSLQELYSLLSFVEPD--LFSKEEvgdFIQRY-------------QDIEKESESASE-LHKLLQPFLLR 260
Cdd:cd18001  155 NRIILTGTPIQNNLKELWALFDFACNGslLGTRKT---FKMEFenpitrgrdkdatQGEKALGSEVAEnLRQIIKPYFLR 231

                 .
gi 373428660 261 R 261
Cdd:cd18001  232 R 232
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
46-261 1.96e-37

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: 140.50  E-value: 1.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRfhcqnGCILGDEMGLGKTCQTIAL-----------------FIYLAGRLNDEGPFLILCPLSVLS 108
Cdd:cd18008    1 LLPYQKQGLAWMLPR-----GGILADEMGLGKTIQALALilatrpqdpkipeeleeNSSDPKKLYLSKTTLIVVPLSLLS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 109 NWKEEMQRF--APGLSCVTYAGDKEERaclqqDLKQESRFHVLLTTYEI----------------CLKDASFLKSFPWSV 170
Cdd:cd18008   76 QWKDEIEKHtkPGSLKVYVYHGSKRIK-----SIEELSDYDIVITTYGTlasefpknkkgggrdsKEKEASPLHRIRWYR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 171 LVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGD-FIQRYQDiEKESESASE 249
Cdd:cd18008  151 VILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNsDISKPFS-KNDRKALER 229
                        250
                 ....*....|..
gi 373428660 250 LHKLLQPFLLRR 261
Cdd:cd18008  230 LQALLKPILLRR 241
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
46-252 2.96e-33

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: 128.56  E-value: 2.96e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVnwlaqRFHCQN------------GCILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEE 113
Cdd:cd18007    1 LKPHQVEGV-----RFLWSNlvgtdvgsdeggGCILAHTMGLGKTLQVITFLHTYLAAAPRRSRPLVLCPASTLYNWEDE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 114 MQRFA-----PGLSCVTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWS--------------VLVVD 174
Cdd:cd18007   76 FKKWLppdlrPLLVLVSLSASKRADARLRKINKWHKEGGVLLIGYELFRNLASNATTDPRLkqefiaalldpgpdLLVLD 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 373428660 175 EAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgDFIQRY-QDIEKESESASELHK 252
Cdd:cd18007  156 EGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLK--EFKKKFvKPIEAGQCVDSTEED 232
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
46-261 1.63e-31

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: 123.73  E-value: 1.63e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWL-----AQRFHCQNGCILGDEMGLGKTCQTIALFIYLAGRLNDEGPFL----ILCPLSVLSNWKEEMQR 116
Cdd:cd18067    1 LRPHQREGVKFLyrcvtGRRIRGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaiVVSPSSLVKNWANELGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 117 F-APGLSCVTYAG---DKEERACLQQDLKQESRFH--VLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTL 190
Cdd:cd18067   81 WlGGRLQPLAIDGgskKEIDRKLVQWASQQGRRVStpVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 191 SEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVgdFIQRY--------------QDIEKESESASELHKLLQP 256
Cdd:cd18067  161 DSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAE--FKKNFelpilkgrdadaseKERQLGEEKLQELISIVNR 238

                 ....*
gi 373428660 257 FLLRR 261
Cdd:cd18067  239 CIIRR 243
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
46-261 2.91e-31

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: 121.93  E-value: 2.91e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRfhcqNG-CILGDEMGLGKTCQTIALfiylAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLS-- 122
Cdd:cd18010    1 LLPFQREGVCFALRR----GGrVLIADEMGLGKTVQAIAI----AAYYREEWPLLIVCPSSLRLTWADEIERWLPSLPpd 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 123 ---CVTYAGDKEERaclqqdlkqeSRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEfsVVFS- 198
Cdd:cd18010   73 diqVIVKSKDGLRD----------GDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALP--LLKRa 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 373428660 199 ---LLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgDFIQRYQDIE--------KESESASELHKLL-QPFLLRR 261
Cdd:cd18010  141 krvILLSGTPALSRPIELFTQLDALDPKLFGRFH--DFGRRYCAAKqggfgwdySGSSNLEELHLLLlATIMIRR 213
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
46-261 1.01e-29

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: 118.02  E-value: 1.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLaqrFHC--------QNGCILGDEMGLGKTCQTIALfIYLAGRLNDEGP------FLILCPLSVLSNWK 111
Cdd:cd18066    1 LRPHQREGIEFL---YECvmgmrvneRFGAILADEMGLGKTLQCISL-IWTLLRQGPYGGkpvikrALIVTPGSLVKNWK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 112 EEMQRFAPGLSCVTYAGDKEERAclqQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLS 191
Cdd:cd18066   77 KEFQKWLGSERIKVFTVDQDHKV---EEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 192 EFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSkeEVGDFIQRYQD------------IEKE--SESASELHKLLQPF 257
Cdd:cd18066  154 SLSCERRIILTGTPIQNDLQEFFALIDFVNPGILG--SLSTYRKVYEEpivrsreptatpEEKKlgEARAAELTRLTGLF 231

                 ....
gi 373428660 258 LLRR 261
Cdd:cd18066  232 ILRR 235
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
66-261 1.87e-28

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: 114.49  E-value: 1.87e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  66 GCILGDEMGLGKTCQTIALFIYlagrlndeGPFLILCPLSVLSNWKEEM-QRFAPG-LSCVTYAGDkeERAclqQDLKQE 143
Cdd:cd18071   50 GGILADDMGLGKTLTTISLILA--------NFTLIVCPLSVLSNWETQFeEHVKPGqLKVYTYHGG--ERN---RDPKLL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 144 SRFHVLLTTYEICL-----KDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLS 218
Cdd:cd18071  117 SKYDIVLTTYNTLAsdfgaKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLS 196
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 373428660 219 FVEPDLFSKEEV-GDFIQRyqDIEKESESASE-LHKLLQPFLLRR 261
Cdd:cd18071  197 FLHLKPFSNPEYwRRLIQR--PLTMGDPTGLKrLQVLMKQITLRR 239
DEXDc smart00487
DEAD-like helicases superfamily;
41-230 2.52e-27

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 110.27  E-value: 2.52e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660    41 LTGIHLRSYQLEGVNWLAQRFHcqnGCILGDEMGLGKTCQtIALFIYLAGRLNDEGPFLILCPLSVL-SNWKEEMQRFAP 119
Cdd:smart00487   4 FGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTLA-ALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKLGP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660   120 ---GLSCVTYAGDKEERaclQQDLKQESRFHVLLTTYEICLKDAS--FLKSFPWSVLVVDEAHRLKNQS--SLLHKTLSE 192
Cdd:smart00487  80 slgLKVVGLYGGDSKRE---QLRKLESGKTDILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLKL 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 373428660   193 F-SVVFSLLLTGTP---IQNSLQELYSLLSFVEPDLFSKEEV 230
Cdd:smart00487 157 LpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPI 198
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
716-866 3.34e-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: 104.64  E-value: 3.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 716 SLKYVSGDVTHPQagaEDALIVHCVDDSGHWGRGGLFTALEK--RSAEPRKIYELAGkmkdlsLGGVLLFPVDDKesrnk 793
Cdd:cd02901    1 KITYVKGDLFACP---ETKSLAHCCNCDGVMGKGIALQFKKKpgRVEELRAQCKKKL------LGGVAVLKRDGV----- 66
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 373428660 794 gQDLLALIVAQHRDRSNvlsgIKMAALEEGLKKIF-LAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAAR 866
Cdd:cd02901   67 -KRYIYYLITKKSYGPK----PTYEALRSSLEELReHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
46-226 7.07e-24

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: 100.44  E-value: 7.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRFHcqNGCILGDEMGLGKTCQTIALFIYLAGRlNDEGPFLILCPLSVLSNWKEEMQ-RFAPGLSCV 124
Cdd:cd18011    1 PLPHQIDAVLRALRKPP--VRLLLADEVGLGKTIEAGLIIKELLLR-GDAKRVLILCPASLVEQWQDELQdKFGLPFLIL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 125 TyagDKEERACLQQDLKQESRFHVLLTTYEIcLKD----ASFLKSFPWSVLVVDEAHRLKN----QSSLLHKTLSEFSVV 196
Cdd:cd18011   78 D---RETAAQLRRLIGNPFEEFPIVIVSLDL-LKRseerRGLLLSEEWDLVVVDEAHKLRNsgggKETKRYKLGRLLAKR 153
                        170       180       190
                 ....*....|....*....|....*....|..
gi 373428660 197 FS--LLLTGTPIQNSLQELYSLLSFVEPDLFS 226
Cdd:cd18011  154 ARhvLLLTATPHNGKEEDFRALLSLLDPGRFA 185
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
46-260 1.99e-23

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: 100.50  E-value: 1.99e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRfhcqnGCILGDEMGLGKTCQTIALFiyLAGRLNDE---------------------------GPF 98
Cdd:cd18070    1 LLPYQRRAVNWMLVP-----GGILADEMGLGKTVEVLALI--LLHPRPDNdldaadddsdemvccpdclvaetpvssKAT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  99 LILCPLSVLSNWKEEMQRFAPG-LSCVTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFP---------- 167
Cdd:cd18070   74 LIVCPSAILAQWLDEINRHVPSsLKVLTYQGVKKDGALASPAPEILAEYDIVVTTYDVLRTELHYAEANRsnrrrrrqkr 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 168 ------------WSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgDFIQ 235
Cdd:cd18070  154 yeappsplvlveWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCDSD--WWAR 231
                        250       260
                 ....*....|....*....|....*
gi 373428660 236 RYQDIEKESESASELHKLLQPFLLR 260
Cdd:cd18070  232 VLIRPQGRNKAREPLAALLKELLWR 256
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
347-459 2.42e-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: 95.36  E-value: 2.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  347 GKLHLLDKLLAFlySGGHRVLLFSQMTQMLDIlQDYMDYRGYSYERVDGSVRGEERHLAIKNFGQQPIFVfLLSTRAGGV 426
Cdd:pfam00271   1 EKLEALLELLKK--ERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDV-LVATDVAER 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 373428660  427 GMNLTAADTVIFVDSDFNPQNDLQAAARAHRIG 459
Cdd:pfam00271  77 GLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
46-261 5.82e-21

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: 92.93  E-value: 5.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRfHCQN--GCILGDEMGLGKTCQTIALFIYLAGRLN-----------------DEGPF-----LIL 101
Cdd:cd18072    1 LLLHQKQALAWLLWR-ERQKprGGILADDMGLGKTLTMIALILAQKNTQNrkeeekekalteweskkDSTLVpsagtLVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 102 CPLSVLSNWKEEMQRFAPG--LSCVTYAGDKEERAClqqdlKQESRFHVLLTTYEICLKD---------ASFLKSFPWSV 170
Cdd:cd18072   80 CPASLVHQWKNEVESRVASnkLRVCLYHGPNRERIG-----EVLRDYDIVITTYSLVAKEiptykeesrSSPLFRIAWAR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 171 LVVDEAHRLKNqssllHKTLSEFSV-----VFSLLLTGTPIQNSLQELYSLLSFVEPDLFSkeevgDFIQRYQDIEKESE 245
Cdd:cd18072  155 IILDEAHNIKN-----PKVQASIAVcklraHARWALTGTPIQNNLLDMYSLLKFLRCSPFD-----DLKVWKKQVDNKSR 224
                        250
                 ....*....|....*..
gi 373428660 246 SASE-LHKLLQPFLLRR 261
Cdd:cd18072  225 KGGErLNILTKSLLLRR 241
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
66-236 2.37e-19

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: 87.95  E-value: 2.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  66 GCILGDEMGLGKTCQTIAlFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQDLKQESR 145
Cdd:cd18069   30 GCILAHSMGLGKTLQVIS-FLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKWLPPPEALPNVRPRPFKVFILNDEHKTTA 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 146 FH------------VLLTTYEICLkdasfLKSFPwSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQEL 213
Cdd:cd18069  109 ARakviedwvkdggVLLMGYEMFR-----LRPGP-DVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEY 182
                        170       180
                 ....*....|....*....|....
gi 373428660 214 YSLLSFVEPD-LFSKEEVGDFIQR 236
Cdd:cd18069  183 WCMVDFVRPDfLGTRQEFSNMFER 206
HELICc smart00490
helicase superfamily c-terminal domain;
377-459 7.75e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 81.87  E-value: 7.75e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660   377 DILQDYMDYRGYSYERVDGSVRGEERHLAIKNFgQQPIFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAH 456
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKF-NNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79

                   ...
gi 373428660   457 RIG 459
Cdd:smart00490  80 RAG 82
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
65-234 2.53e-18

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: 85.32  E-value: 2.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  65 NGCILGDEMGLGKTCQTIALF--IYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGL--------SCVTYAGDKEERA 134
Cdd:cd18068   29 SGCILAHCMGLGKTLQVVTFLhtVLLCEKLENFSRVLVVCPLNTVLNWLNEFEKWQEGLkdeekievNELATYKRPQERS 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 135 CLQQDLKQESrfHVLLTTYEIC--------------LKDaSFLKSF--PWSVLVV-DEAHRLKNQSSLLHKTLSEFSVVF 197
Cdd:cd18068  109 YKLQRWQEEG--GVMIIGYDMYrilaqernvksrekLKE-IFNKALvdPGPDFVVcDEGHILKNEASAVSKAMNSIRTKR 185
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 373428660 198 SLLLTGTPIQNSLQELYSLLSFVEPDLFS--KEEVGDFI 234
Cdd:cd18068  186 RIVLTGTPLQNNLIEYHCMVNFVKPNLLGtiKEFRNRFV 224
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
42-606 5.16e-15

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 78.91  E-value: 5.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  42 TGIHLRSYQLEGVN-WLAQRFHCQNGCILgdEM--GLGKTcqTIALFIylAGRLNDEGPFLILCP-LSVLSNWKEEMQRF 117
Cdd:COG1061   77 TSFELRPYQQEALEaLLAALERGGGRGLV--VAptGTGKT--VLALAL--AAELLRGKRVLVLVPrRELLEQWAEELRRF 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 118 APGlscvtyagdkeeraCLQQDLKQESRFHVLLTTYEIcLKDASFLKSFP--WSVLVVDEAHRLknQSSLLHKTLSEFSV 195
Cdd:COG1061  151 LGD--------------PLAGGGKKDSDAPITVATYQS-LARRAHLDELGdrFGLVIIDEAHHA--GAPSYRRILEAFPA 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 196 VFSLLLTGTPiqnslqelysllsfvepdlFSKEEVGDFIQRYQDIEKEsESASEL--HKLLQPFLLRRVKAEVATELPKk 273
Cdd:COG1061  214 AYRLGLTATP-------------------FRSDGREILLFLFDGIVYE-YSLKEAieDGYLAPPEYYGIRVDLTDERAE- 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 274 tevviyhgMSALQKKYYKAILmkdldafENETAKKVKLQNILSQlrkcvdhpylfdgvepepfevgdhlteasgklhlld 353
Cdd:COG1061  273 --------YDALSERLREALA-------ADAERKDKILRELLRE------------------------------------ 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 354 kllaflYSGGHRVLLFSQMTQMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGQQPIfVFLLSTRAGGVGMNLTAA 433
Cdd:COG1061  302 ------HPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGEL-RILVTVDVLNEGVDVPRL 374
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 434 DTVIFVDSDFNPQNDLQAAARAHRIGQNKS-VKVIRLIGRDTVeeiVYRKAASKLQLTNMIIEGGHFTLGAQKPAADADL 512
Cdd:COG1061  375 DVAILLRPTGSPREFIQRLGRGLRPAPGKEdALVYDFVGNDVP---VLEELAKDLRDLAGYRVEFLDEEESEELALLIAV 451
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 513 QLSEILKFGLDKLLASEGSTMDEIDLESILGETKDGQWVSDALPAAEGGSRDQEEGKNHMYLFEGKDYSKEPSKEDRKSF 592
Cdd:COG1061  452 KPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLL 531
                        570
                 ....*....|....
gi 373428660 593 EQLVNLQKTLLEKA 606
Cdd:COG1061  532 LLLLLELLELLAAL 545
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
46-239 1.35e-13

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: 70.84  E-value: 1.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGVNWLAQRFHCqngCILGDeMGLGKTCQTIALFIYLagRLNDE-GPFLILCPLSVLSN-WKEEMQRFApGLSC 123
Cdd:cd18013    1 PHPYQKVAINFIIEHPYC---GLFLD-MGLGKTVTTLTALSDL--QLDDFtRRVLVIAPLRVARStWPDEVEKWN-HLRN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 124 VTYA---GDKEERACLQQdlkqeSRFHVLLTTYE----ICLKdasFLKSFPWSVLVVDEAHRLKNQSSllHKTLSEFSVV 196
Cdd:cd18013   74 LTVSvavGTERQRSKAAN-----TPADLYVINREnlkwLVNK---SGDPWPFDMVVIDELSSFKSPRS--KRFKALRKVR 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 373428660 197 FS----LLLTGTPIQNSLQELYSLLSFVEpdlfSKEEVGDFIQRYQD 239
Cdd:cd18013  144 PVikrlIGLTGTPSPNGLMDLWAQIALLD----QGERLGRSITAYRE 186
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
46-205 8.63e-10

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 58.09  E-value: 8.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  46 LRSYQLEGV-NWLAqrfHCQN--GCIlgdEM--GLGKTCQTIALFIYLAgrlndEGPFLILCP-LSVLSNWKEEMQRFAP 119
Cdd:cd17926    1 LRPYQEEALeAWLA---HKNNrrGIL---VLptGSGKTLTALALIAYLK-----ELRTLIVVPtDALLDQWKERFEDFLG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 120 GLS-CVTYAGDKEERAClqqdlkqesrFHVLLTTY---EICLKDASFLKSFpWSVLVVDEAHRLKnqSSLLHKTLSEFSV 195
Cdd:cd17926   70 DSSiGLIGGGKKKDFDD----------ANVVVATYqslSNLAEEEKDLFDQ-FGLLIVDEAHHLP--AKTFSEILKELNA 136
                        170
                 ....*....|
gi 373428660 196 VFSLLLTGTP 205
Cdd:cd17926  137 KYRLGLTATP 146
ResIII pfam04851
Type III restriction enzyme, res subunit;
44-206 1.18e-08

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 54.99  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660   44 IHLRSYQLEGV-NWLAQRFHCQ-NGCIlgdEM--GLGKTcQTIALFIYLAGRLNDEGPFLILCP-LSVLSNWKEEMQRFA 118
Cdd:pfam04851   2 LELRPYQIEAIeNLLESIKNGQkRGLI---VMatGSGKT-LTAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  119 PG--LSCVTYAGDKEERaclqqdlkQESRFHVLLTTY-----EICLKDASFLKSFpWSVLVVDEAHRL--KNQSSLLHKt 189
Cdd:pfam04851  78 PNyvEIGEIISGDKKDE--------SVDDNKIVVTTIqslykALELASLELLPDF-FDVIIIDEAHRSgaSSYRNILEY- 147
                         170
                  ....*....|....*..
gi 373428660  190 lseFSVVFSLLLTGTPI 206
Cdd:pfam04851 148 ---FKPAFLLGLTATPE 161
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
65-179 1.27e-06

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 48.94  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  65 NGCILGDEMGLGKTcQTIALFIYLAGRLNdEGPFLILCPLSVLSN-WKEEMQ-RFAPGLSCVTYAGD--KEERACLQQDL 140
Cdd:cd00046    2 ENVLITAPTGSGKT-LAALLAALLLLLKK-GKKVLVLVPTKALALqTAERLReLFGPGIRVAVLVGGssAEEREKNKLGD 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 373428660 141 KqesrfHVLLTTYEICLKDASFLKSF---PWSVLVVDEAHRL 179
Cdd:cd00046   80 A-----DIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHAL 116
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
310-478 8.71e-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: 48.48  E-value: 8.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  310 KLQNILSQLRKCVDHPYLF-DGVEPEPF---EVGDHLTEASGKLHLLDKLLAFL----YSGGHRVLLFSQMTQMLDILQD 381
Cdd:pfam11496  49 SMTLCLENLSLVATHPYLLvDHYMPKSLllkDEPEKLAYTSGKFLVLNDLVNLLierdRKEPINVAIVARSGKTLDLVEA 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  382 YMDYRGYSYERVDG-SVRGEERHLAIKNFGQQPIFVFLL------STRAGGVgMNLTAADTVIFVDSDFNPQNDLQAAAR 454
Cdd:pfam11496 129 LLLGKGLSYKRYSGeMLYGENKKVSDSGNKKIHSTTCHLlsstgqLTNDDSL-LENYKFDLIIAFDSSVDTSSPSVEHLR 207
                         170       180
                  ....*....|....*....|....
gi 373428660  455 AHRIGQNKSVKVIRLIGRDTVEEI 478
Cdd:pfam11496 208 TQNRRKGNLAPIIRLVVINSIEHV 231
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
74-208 3.07e-05

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 45.31  E-value: 3.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660   74 GLGKT-CQTIALFIYLagRLNDEGP-FLILCPLSVL-----SNWKEEMQRFAPGLSCVtYAGDKeeracLQQDLKQESRF 146
Cdd:pfam00270  24 GSGKTlAFLLPALEAL--DKLDNGPqALVLAPTRELaeqiyEELKKLGKGLGLKVASL-LGGDS-----RKEQLEKLKGP 95
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 373428660  147 HVLLTTYEIC---LKDASFLKSFpwSVLVVDEAHRL--KNQSSLLHKTLSEFSVVF-SLLLTGTPIQN 208
Cdd:pfam00270  96 DILVGTPGRLldlLQERKLLKNL--KLLVLDEAHRLldMGFGPDLEEILRRLPKKRqILLLSATLPRN 161
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
563-674 6.58e-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: 46.66  E-value: 6.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  563 RDQEEGKNHmylfegKDYSKEPSKEDRKSFEQLvnlQKTLLEKASQEGRSlrnkgsvlipGLVEgsTKRKRVLSPEELED 642
Cdd:pfam17380 466 RQQEEERKR------KKLELEKEKRDRKRAEEQ---RRKILEKELEERKQ----------AMIE--EERKRKLLEKEMEE 524
                          90       100       110
                  ....*....|....*....|....*....|..
gi 373428660  643 RQKKRQEaaAKRRRLIEEKKRQKEEAEHKKKM 674
Cdd:pfam17380 525 RQKAIYE--EERRREAEEERRKQQEMEERRRI 554
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
414-470 1.01e-04

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 41.54  E-value: 1.01e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 373428660 414 IFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQnKSVKVIRLI 470
Cdd:cd18785   22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILFV 77
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
735-861 1.03e-04

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: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660 735 LIVHCVDDSGHWGrGGLFTALEKRSAEPRKIYELAGKMKD-LSLGGVLLfpvddkesrNKGQDLLALIVAqHrdrSNVLS 813
Cdd:cd02749    2 AIVNPANNDLYLG-GGVAKAISKKAGGDLQEECEERKKNGyLKVGEVAV---------TKGGNLPARYII-H---VVGPV 67
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 373428660 814 GIKMAALEEGLKKIF-----LAAKKKKASVHLPRIGHATKGFNWYGTERLIRK 861
Cdd:cd02749   68 ASSKKKTYEPLKKCVknclsLADEKGLKSVAFPAIGTGIAGFPPEEAARIMLE 120
Caldesmon pfam02029
Caldesmon;
582-672 1.24e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.55  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  582 KEPSKEDRKSFEQ-LVNLQKTLLEKASQEGRSLRNKGSVLIPGLVEGSTKRK---RVLSPEEledrQKKRQEAAAKRRRL 657
Cdd:pfam02029 236 REEEAEVFLEAEQkLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKKREerrKLLEEEE----QRRKQEEAERKLRE 311
                          90
                  ....*....|....*
gi 373428660  658 IEEKKRQKEEAEHKK 672
Cdd:pfam02029 312 EEEKRRMKEEIERRR 326
Selenoprotein_S pfam06936
Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) ...
646-695 2.98e-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: 2.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 373428660  646 KRQEA-AAKRRRLIE----------EKKRQKEEAEHKKKMAWWES----NNYQSFCLPSEESEPE 695
Cdd:pfam06936  80 KRQEAlEASRLRMQEeldaqaekfkEKQKQLEEEKRRQKIEMWESmqegKSYKGNAKLAQEETEE 144
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
76-183 4.63e-03

DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 39.17  E-value: 4.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  76 GKTcqTIALFIYLAGRLNDEGPFLILCPLSVLSN-----WKEEMQRFapGLSCVTYAGDKEEraclqqDLKQESRFHVLL 150
Cdd:cd17921   29 GKT--LIAELAILRALATSGGKAVYIAPTRALVNqkeadLRERFGPL--GKNVGLLTGDPSV------NKLLLAEADILV 98
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 373428660 151 TTYEIC---LKDASFLKSFPWSVLVVDEAHRLKNQS 183
Cdd:cd17921   99 ATPEKLdllLRNGGERLIQDVRLVVVDEAHLIGDGE 134
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
628-683 4.85e-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: 39.30  E-value: 4.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 373428660  628 STKRKRVLSPEELEDR-----QKKRQEAAAKRRRLIEEKKRQKEEAEHKKKM---AW--WESNNYQ 683
Cdd:pfam13904 128 LAKPERKVSQEEAKEVlqeweRKKLEQQQRKREEEQREQLKKEEEEQERKQLaekAWqkWMKNVKN 193
AAA_22 pfam13401
AAA domain;
59-217 6.73e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 37.71  E-value: 6.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660   59 QRFHCQNGCILGDEmGLGKTcqtiALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLscvtyAGDKEERACLQQ 138
Cdd:pfam13401   1 IRFGAGILVLTGES-GTGKT----TLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRALLRAL-----GLPLSGRLSKEE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 373428660  139 DLkqeSRFHVLLTTYeiclkdasflksFPWSVLVVDEAHRLKNQS-SLLHKTLSEFSVVFSLLLTGTPiqnslqELYSLL 217
Cdd:pfam13401  71 LL---AALQQLLLAL------------AVAVVLIIDEAQHLSLEAlEELRDLLNLSSKLLQLILVGTP------ELRELL 129
 
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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