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Conserved domains on  [gi|1140176920|ref|NP_001335380|]
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chromodomain-helicase-DNA-binding protein 1-like isoform 6 [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
1-627 8.12e-151

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: 468.90  E-value: 8.12e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920    1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQDLKQESRFHVLLTT 80
Cdd:PLN03142   197 MGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTS 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   81 YEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGD 160
Cdd:PLN03142   277 FEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFD 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  161 FIQRYQDIEKESESASELHKLLQPFLLRRVKAEVATELPKKTEVVIYHGMSALQKKYYKAILMKDLDAFeNETAKKVKLQ 240
Cdd:PLN03142   357 EWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVV-NAGGERKRLL 435
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  241 NILSQLRKCVDHPYLFDGVEP-EPFEVGDHLTEASGKLHLLDKLLAFLYSGGHRVLLFSQMTQMLDILQDYMDYRGYSYE 319
Cdd:PLN03142   436 NIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYC 515
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  320 RVDGSVRGEERHLAIKNFGQ--QPIFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRL 397
Cdd:PLN03142   516 RIDGNTGGEDRDASIDAFNKpgSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRF 595
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  398 IGRDTVEEIVYRKAASKLQLTNMIIEGGHFtlgAQKPAADADlQLSEILKFGLDKLLASEGSTMDEIDLESIL--GE--- 472
Cdd:PLN03142   596 CTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD-ELLQMVRYGAEMVFSSKDSTITDEDIDRIIakGEeat 671
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  473 ----TKDGQWVSDALPAAEGGS---------RDQEEGKNHMYLFEGKDYSKEPSKEDRKSFEQLVNLQKTLLEKASQEGR 539
Cdd:PLN03142   672 aeldAKMKKFTEDAIKFKMDDTaelydfddeDDKDENKLDFKKIVSDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPK 751
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  540 SLRnkgsvlIPGLVEGS------TKRKRVLSPEELEDRQKKRQEAAAKRRRLIEEKKRQ-----KEEAEHKKKM-----A 603
Cdd:PLN03142   752 EPR------IPRMPQLHdfqffnVQRLTELYEKEVRYLMQAHQKGQLKDTIDVAEPEEPgdpltAEEQEEKEQLleegfS 825
                          650       660
                   ....*....|....*....|....
gi 1140176920  604 WWESNNYQSFCLPSEESEPEDLEN 627
Cdd:PLN03142   826 TWSRRDFNAFIRACEKYGRNDIKS 849
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
644-794 6.39e-94

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


:

Pssm-ID: 394880  Cd Length: 152  Bit Score: 290.70  E-value: 6.39e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 644 SLKYVSGDVTHPQA-GAEDALIVHCVDDSGHWGRGGLFTALEKRSAEPRKIYELAGKMKDLSLGGVLLFPVDDKESRNKG 722
Cdd:cd03331     1 DINYVSGDVTHPQTtSTEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1140176920 723 QDLLALIVAQHRDRSNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAAR 794
Cdd:cd03331    81 RDYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
1-627 8.12e-151

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 468.90  E-value: 8.12e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920    1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQDLKQESRFHVLLTT 80
Cdd:PLN03142   197 MGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTS 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   81 YEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGD 160
Cdd:PLN03142   277 FEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFD 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  161 FIQRYQDIEKESESASELHKLLQPFLLRRVKAEVATELPKKTEVVIYHGMSALQKKYYKAILMKDLDAFeNETAKKVKLQ 240
Cdd:PLN03142   357 EWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVV-NAGGERKRLL 435
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  241 NILSQLRKCVDHPYLFDGVEP-EPFEVGDHLTEASGKLHLLDKLLAFLYSGGHRVLLFSQMTQMLDILQDYMDYRGYSYE 319
Cdd:PLN03142   436 NIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYC 515
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  320 RVDGSVRGEERHLAIKNFGQ--QPIFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRL 397
Cdd:PLN03142   516 RIDGNTGGEDRDASIDAFNKpgSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRF 595
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  398 IGRDTVEEIVYRKAASKLQLTNMIIEGGHFtlgAQKPAADADlQLSEILKFGLDKLLASEGSTMDEIDLESIL--GE--- 472
Cdd:PLN03142   596 CTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD-ELLQMVRYGAEMVFSSKDSTITDEDIDRIIakGEeat 671
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  473 ----TKDGQWVSDALPAAEGGS---------RDQEEGKNHMYLFEGKDYSKEPSKEDRKSFEQLVNLQKTLLEKASQEGR 539
Cdd:PLN03142   672 aeldAKMKKFTEDAIKFKMDDTaelydfddeDDKDENKLDFKKIVSDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPK 751
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  540 SLRnkgsvlIPGLVEGS------TKRKRVLSPEELEDRQKKRQEAAAKRRRLIEEKKRQ-----KEEAEHKKKM-----A 603
Cdd:PLN03142   752 EPR------IPRMPQLHdfqffnVQRLTELYEKEVRYLMQAHQKGQLKDTIDVAEPEEPgdpltAEEQEEKEQLleegfS 825
                          650       660
                   ....*....|....*....|....
gi 1140176920  604 WWESNNYQSFCLPSEESEPEDLEN 627
Cdd:PLN03142   826 TWSRRDFNAFIRACEKYGRNDIKS 849
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
1-423 6.31e-124

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 388.04  E-value: 6.31e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRlNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEEraclQQDLKQESRFHVLLTT 80
Cdd:COG0553   269 MGLGKTIQALALLLELKER-GLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRER----AKGANPFEDADLVITS 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  81 YEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgD 160
Cdd:COG0553   344 YGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLK--A 421
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 161 FIQRYQD-IEKESESASE-LHKLLQPFLLRRVKAEVATELPKKTEVVIYHGMSALQKKYYKAIL---MKDLDAFENETAK 235
Cdd:COG0553   422 FRERFARpIEKGDEEALErLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLeylRRELEGAEGIRRR 501
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 236 KVKLQnILSQLRKCVDHPYLFDgvepepfEVGDHLTEASGKLHLLDKLLAFLYSGGHRVLLFSQMTQMLDILQDYMDYRG 315
Cdd:COG0553   502 GLILA-ALTRLRQICSHPALLL-------EEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERG 573
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 316 YSYERVDGSVRGEERHLAIKNFGQQP-IFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKV 394
Cdd:COG0553   574 IEYAYLHGGTSAEERDELVDRFQEGPeAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQV 653
                         410       420
                  ....*....|....*....|....*....
gi 1140176920 395 IRLIGRDTVEEIVYRKAASKLQLTNMIIE 423
Cdd:COG0553   654 YKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
1-189 1.04e-118

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: 357.52  E-value: 1.04e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQDLKQESRFHVLLTT 80
Cdd:cd18006    28 MGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVITYMGDKEKRLDLQQDIKSTNRFHVLLTT 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  81 YEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGD 160
Cdd:cd18006   108 YEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKLDD 187
                         170       180
                  ....*....|....*....|....*....
gi 1140176920 161 FIQRYQDIEKESESASELHKLLQPFLLRR 189
Cdd:cd18006   188 FIKAYSETDDESETVEELHLLLQPFLLRR 216
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
644-794 6.39e-94

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


Pssm-ID: 394880  Cd Length: 152  Bit Score: 290.70  E-value: 6.39e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 644 SLKYVSGDVTHPQA-GAEDALIVHCVDDSGHWGRGGLFTALEKRSAEPRKIYELAGKMKDLSLGGVLLFPVDDKESRNKG 722
Cdd:cd03331     1 DINYVSGDVTHPQTtSTEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1140176920 723 QDLLALIVAQHRDRSNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAAR 794
Cdd:cd03331    81 RDYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
1-256 8.03e-77

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: 250.68  E-value: 8.03e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYL-AGRLNDEGPFLILCPLSVLSNWKEEMQRFA--PGLSCVTYAGDKEERACLQQDLKQESRFHVL 77
Cdd:pfam00176  26 MGLGKTLQTISLLLYLkHVDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVVVLHGNKRPQERWKNDPNFLADFDVV 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  78 LTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSkeE 157
Cdd:pfam00176 106 ITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFG--S 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 158 VGDFIQRY-QDIE--KESESASELHKLLQPFLLRRVKAEVATELPKKTEVVIYHGMSALQKKYYKA-ILMKDLDAFENET 233
Cdd:pfam00176 184 LSTFRNWFdRPIErgGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTfLLKKDLNAIKTGE 263
                         250       260
                  ....*....|....*....|....*.
gi 1140176920 234 A---KKVKLQNILSQLRKCVDHPYLF 256
Cdd:pfam00176 264 GgreIKASLLNILMRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
1-158 2.33e-20

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 89.86  E-value: 2.33e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920    1 MGLGKTCQtIALFIYLAGRLNDEGPFLILCPLSVL-SNWKEEMQRFAP---GLSCVTYAGDKEERaclQQDLKQESRFHV 76
Cdd:smart00487  33 TGSGKTLA-ALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKLGPslgLKVVGLYGGDSKRE---QLRKLESGKTDI 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   77 LLTTYEICLKDAS--FLKSFPWSVLVVDEAHRLKNQS--SLLHKTLSEF-SVVFSLLLTGTP---IQNSLQELYSLLSFV 148
Cdd:smart00487 109 LVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLKLLpKNVQLLLLSATPpeeIENLLELFLNDPVFI 188
                          170
                   ....*....|
gi 1140176920  149 EPDLFSKEEV 158
Cdd:smart00487 189 DVGFTPLEPI 198
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
1-627 8.12e-151

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 468.90  E-value: 8.12e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920    1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQDLKQESRFHVLLTT 80
Cdd:PLN03142   197 MGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREELLVAGKFDVCVTS 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   81 YEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGD 160
Cdd:PLN03142   277 FEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFD 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  161 FIQRYQDIEKESESASELHKLLQPFLLRRVKAEVATELPKKTEVVIYHGMSALQKKYYKAILMKDLDAFeNETAKKVKLQ 240
Cdd:PLN03142   357 EWFQISGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVV-NAGGERKRLL 435
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  241 NILSQLRKCVDHPYLFDGVEP-EPFEVGDHLTEASGKLHLLDKLLAFLYSGGHRVLLFSQMTQMLDILQDYMDYRGYSYE 319
Cdd:PLN03142   436 NIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYC 515
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  320 RVDGSVRGEERHLAIKNFGQ--QPIFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRL 397
Cdd:PLN03142   516 RIDGNTGGEDRDASIDAFNKpgSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRF 595
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  398 IGRDTVEEIVYRKAASKLQLTNMIIEGGHFtlgAQKPAADADlQLSEILKFGLDKLLASEGSTMDEIDLESIL--GE--- 472
Cdd:PLN03142   596 CTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD-ELLQMVRYGAEMVFSSKDSTITDEDIDRIIakGEeat 671
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  473 ----TKDGQWVSDALPAAEGGS---------RDQEEGKNHMYLFEGKDYSKEPSKEDRKSFEQLVNLQKTLLEKASQEGR 539
Cdd:PLN03142   672 aeldAKMKKFTEDAIKFKMDDTaelydfddeDDKDENKLDFKKIVSDNWIDPPKRERKRNYSESEYFKQAMRQGAPAKPK 751
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  540 SLRnkgsvlIPGLVEGS------TKRKRVLSPEELEDRQKKRQEAAAKRRRLIEEKKRQ-----KEEAEHKKKM-----A 603
Cdd:PLN03142   752 EPR------IPRMPQLHdfqffnVQRLTELYEKEVRYLMQAHQKGQLKDTIDVAEPEEPgdpltAEEQEEKEQLleegfS 825
                          650       660
                   ....*....|....*....|....
gi 1140176920  604 WWESNNYQSFCLPSEESEPEDLEN 627
Cdd:PLN03142   826 TWSRRDFNAFIRACEKYGRNDIKS 849
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
1-423 6.31e-124

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 388.04  E-value: 6.31e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRlNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEEraclQQDLKQESRFHVLLTT 80
Cdd:COG0553   269 MGLGKTIQALALLLELKER-GLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRER----AKGANPFEDADLVITS 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  81 YEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgD 160
Cdd:COG0553   344 YGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLK--A 421
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 161 FIQRYQD-IEKESESASE-LHKLLQPFLLRRVKAEVATELPKKTEVVIYHGMSALQKKYYKAIL---MKDLDAFENETAK 235
Cdd:COG0553   422 FRERFARpIEKGDEEALErLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLeylRRELEGAEGIRRR 501
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 236 KVKLQnILSQLRKCVDHPYLFDgvepepfEVGDHLTEASGKLHLLDKLLAFLYSGGHRVLLFSQMTQMLDILQDYMDYRG 315
Cdd:COG0553   502 GLILA-ALTRLRQICSHPALLL-------EEGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERG 573
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 316 YSYERVDGSVRGEERHLAIKNFGQQP-IFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKV 394
Cdd:COG0553   574 IEYAYLHGGTSAEERDELVDRFQEGPeAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQV 653
                         410       420
                  ....*....|....*....|....*....
gi 1140176920 395 IRLIGRDTVEEIVYRKAASKLQLTNMIIE 423
Cdd:COG0553   654 YKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
1-189 1.04e-118

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: 357.52  E-value: 1.04e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQDLKQESRFHVLLTT 80
Cdd:cd18006    28 MGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVITYMGDKEKRLDLQQDIKSTNRFHVLLTT 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  81 YEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGD 160
Cdd:cd18006   108 YEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKLDD 187
                         170       180
                  ....*....|....*....|....*....
gi 1140176920 161 FIQRYQDIEKESESASELHKLLQPFLLRR 189
Cdd:cd18006   188 FIKAYSETDDESETVEELHLLLQPFLLRR 216
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
644-794 6.39e-94

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


Pssm-ID: 394880  Cd Length: 152  Bit Score: 290.70  E-value: 6.39e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 644 SLKYVSGDVTHPQA-GAEDALIVHCVDDSGHWGRGGLFTALEKRSAEPRKIYELAGKMKDLSLGGVLLFPVDDKESRNKG 722
Cdd:cd03331     1 DINYVSGDVTHPQTtSTEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1140176920 723 QDLLALIVAQHRDRSNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAAR 794
Cdd:cd03331    81 RDYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
1-256 8.03e-77

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: 250.68  E-value: 8.03e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYL-AGRLNDEGPFLILCPLSVLSNWKEEMQRFA--PGLSCVTYAGDKEERACLQQDLKQESRFHVL 77
Cdd:pfam00176  26 MGLGKTLQTISLLLYLkHVDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVVVLHGNKRPQERWKNDPNFLADFDVV 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  78 LTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSkeE 157
Cdd:pfam00176 106 ITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFG--S 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 158 VGDFIQRY-QDIE--KESESASELHKLLQPFLLRRVKAEVATELPKKTEVVIYHGMSALQKKYYKA-ILMKDLDAFENET 233
Cdd:pfam00176 184 LSTFRNWFdRPIErgGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQTfLLKKDLNAIKTGE 263
                         250       260
                  ....*....|....*....|....*.
gi 1140176920 234 A---KKVKLQNILSQLRKCVDHPYLF 256
Cdd:pfam00176 264 GgreIKASLLNILMRLRKICNHPGLI 289
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
1-189 3.71e-64

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: 214.14  E-value: 3.71e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQ-----DLKQESRFH 75
Cdd:cd17993    29 MGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIVYLGDIKSRDTIREyefyfSQTKKLKFN 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  76 VLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLF-S 154
Cdd:cd17993   109 VLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFdI 188
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1140176920 155 KEEvgdfIQRYQDIEKESESASeLHKLLQPFLLRR 189
Cdd:cd17993   189 WEE----FEEEHDEEQEKGIAD-LHKELEPFILRR 218
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
1-191 4.97e-62

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: 208.33  E-value: 4.97e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQDLKQESRFHVLLTT 80
Cdd:cd17997    31 MGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLRVVVLIGDKEERADIIRDVLLPGKFDVCITS 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  81 YEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGD 160
Cdd:cd17997   111 YEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFD 190
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1140176920 161 -FIQRYQDIEKESESASELHKLLQPFLLRRVK 191
Cdd:cd17997   191 eWFNVNNCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
1-153 1.62e-61

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: 205.49  E-value: 1.62e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQDLKQESrFHVLLTT 80
Cdd:cd17919    28 MGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVVYHGSQRERAQIRAKEKLDK-FDVVLTT 106
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1140176920  81 YEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLF 153
Cdd:cd17919   107 YETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFLDPPFL 179
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
1-189 3.87e-60

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: 203.25  E-value: 3.87e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPgLSCVTYAGDKEERACLQQ-----------DLK 69
Cdd:cd17995    28 MGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVVYHGSGESRQIIQQyemyfkdaqgrKKK 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  70 QESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVE 149
Cdd:cd17995   107 GVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLE 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1140176920 150 PDLFSKEEvgDFIQRYQDIEKESEsASELHKLLQPFLLRR 189
Cdd:cd17995   187 PEKFPSSE--EFLEEFGDLKTAEQ-VEKLQALLKPYMLRR 223
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
1-191 1.50e-57

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: 196.84  E-value: 1.50e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDeGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQDLKQESR----FHV 76
Cdd:cd18009    31 MGLGKTIQTIALLAHLRERGVW-GPFLVIAPLSTLPNWVNEFARFTPSVPVLLYHGTKEERERLRKKIMKREGtlqdFPV 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  77 LLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSK- 155
Cdd:cd18009   110 VVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDl 189
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1140176920 156 ---EEVGDFIQRYQDIEKESESASE--------LHKLLQPFLLRRVK 191
Cdd:cd18009   190 ssfESWFDFSSLSDNAADISNLSEEreqnivhmLHAILKPFLLRRLK 236
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
1-191 2.32e-57

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: 196.05  E-value: 2.32e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQDLKQeSRFHVLLTT 80
Cdd:cd17996    31 MGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSKIVYKGTPDVRKKLQSQIRA-GKFNVLLTT 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  81 YEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSE-FSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSkeEVG 159
Cdd:cd17996   110 YEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFK--SCK 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1140176920 160 DFIQRYQ----------DIEKESESA----SELHKLLQPFLLRRVK 191
Cdd:cd17996   188 TFEQWFNtpfantgeqvKIELNEEETlliiRRLHKVLRPFLLRRLK 233
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
274-398 1.00e-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: 1.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 274 SGKLHLLDKLLAFLYSGGHRVLLFSQMTQMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGQQP-IFVFLLSTRAG 352
Cdd:cd18793    10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdIRVFLLSTKAG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1140176920 353 GVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLI 398
Cdd:cd18793    90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
1-189 1.09e-52

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: 182.94  E-value: 1.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQDLKQESRFHVLLTT 80
Cdd:cd18003    28 MGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILTYYGSAKERKLKRQGWMKPNSFHVCITS 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  81 YEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgD 160
Cdd:cd18003   108 YQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQ--E 185
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1140176920 161 FIQRYQDIEKE-SESASE--------LHKLLQPFLLRR 189
Cdd:cd18003   186 FKEWFSNPLTAmSEGSQEeneelvrrLHKVLRPFLLRR 223
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
1-189 6.12e-52

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: 181.36  E-value: 6.12e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQ-----DLKQESRFH 75
Cdd:cd18054    48 MGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVVVYIGDLMSRNTIREyewihSQTKRLKFN 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  76 VLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFsk 155
Cdd:cd18054   128 ALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKF-- 205
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1140176920 156 eevgdfiQRYQDIEKESESASE-----LHKLLQPFLLRR 189
Cdd:cd18054   206 -------EFWEDFEEDHGKGREngyqsLHKVLEPFLLRR 237
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
1-191 7.70e-52

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: 180.07  E-value: 7.70e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIAlFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQDLKQEsrfhVLLTT 80
Cdd:cd18012    32 MGLGKTLQTLA-LLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKVLVIHGTKRKREKLRALEDYD----LVITS 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  81 YEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgD 160
Cdd:cd18012   107 YGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYK--R 184
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1140176920 161 FIQRYQ-DIEK--ESESASELHKLLQPFLLRRVK 191
Cdd:cd18012   185 FKKRFAkPIEKdgDEEALEELKKLISPFILRRLK 218
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
1-189 4.58e-50

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: 174.55  E-value: 4.58e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDkeeraclqqdlkqesrfHVLLTT 80
Cdd:cd17994    28 MGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVTYVGD-----------------HVLLTS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  81 YEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgD 160
Cdd:cd17994    91 YELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQ--G 168
                         170       180
                  ....*....|....*....|....*....
gi 1140176920 161 FIQRYQDIEKEsESASELHKLLQPFLLRR 189
Cdd:cd17994   169 FLEEFADISKE-DQIKKLHDLLGPHMLRR 196
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
1-189 1.43e-49

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: 174.23  E-value: 1.43e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQ--DLK----QESRF 74
Cdd:cd18002    28 MGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLPYWGNPKDRKVLRKfwDRKnlytRDAPF 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  75 HVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLF- 153
Cdd:cd18002   108 HVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFd 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1140176920 154 SKEEVGDFIQRyqDIEKESESA--------SELHKLLQPFLLRR 189
Cdd:cd18002   188 SHDEFNEWFSK--DIESHAENKtglnehqlKRLHMILKPFMLRR 229
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
1-201 4.50e-49

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: 173.70  E-value: 4.50e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQDLKQESRFHVLLTT 80
Cdd:cd18064    43 MGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTS 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  81 YEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGD 160
Cdd:cd18064   123 YEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFD 202
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1140176920 161 FIQRYQDIEKESESASELHKLLQPFLLRRVKAEVATELPKK 201
Cdd:cd18064   203 SWFDTNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSLPPK 243
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
1-191 1.56e-45

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: 163.26  E-value: 1.56e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQDLKQESRFHVLLTT 80
Cdd:cd18065    43 MGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPSLRAVCLIGDKDARAAFIRDVMMPGEWDVCVTS 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  81 YEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGD 160
Cdd:cd18065   123 YEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFD 202
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1140176920 161 FIQRYQDIEKESESASELHKLLQPFLLRRVK 191
Cdd:cd18065   203 SWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 233
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
1-189 1.76e-45

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: 162.87  E-value: 1.76e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQD------------- 67
Cdd:cd18055    28 MGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVTYTGDKDSRAIIRENefsfddnavkggk 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  68 ----LKQES--RFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQEL 141
Cdd:cd18055   108 kafkMKREAqvKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEEL 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1140176920 142 YSLLSFVEPDLFSKEEvgDFIQRYQDIEKESEsASELHKLLQPFLLRR 189
Cdd:cd18055   188 FHLLNFLTPERFNNLE--GFLEEFADISKEDQ-IKKLHDLLGPHMLRR 232
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
1-189 1.87e-45

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: 163.30  E-value: 1.87e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQ-----QDLKQESRFH 75
Cdd:cd18053    48 MGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAVVYLGDINSRNMIRthewmHPQTKRLKFN 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  76 VLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSK 155
Cdd:cd18053   128 ILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSS 207
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1140176920 156 eevgdfiqrYQDIEKESESASE-----LHKLLQPFLLRR 189
Cdd:cd18053   208 ---------WEDFEEEHGKGREygyasLHKELEPFLLRR 237
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
1-189 8.41e-45

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: 161.00  E-value: 8.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQD------------- 67
Cdd:cd18057    28 MGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVTYTGDKESRSVIRENefsfednairsgk 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  68 ----LKQES--RFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQEL 141
Cdd:cd18057   108 kvfrMKKEAqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEEL 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1140176920 142 YSLLSFVEPDLFSKEEvgDFIQRYQDIEKESEsASELHKLLQPFLLRR 189
Cdd:cd18057   188 FHLLNFLTPERFNNLE--GFLEEFADISKEDQ-IKKLHDLLGPHMLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
1-189 2.57e-43

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: 156.76  E-value: 2.57e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQD------------- 67
Cdd:cd18056    28 MGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVTYVGDKDSRAIIRENefsfednairggk 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  68 ----LKQES--RFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQEL 141
Cdd:cd18056   108 kasrMKKEAsvKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEEL 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1140176920 142 YSLLSFVEPDLFSKEEvgDFIQRYQDIEKESEsASELHKLLQPFLLRR 189
Cdd:cd18056   188 FHLLNFLTPERFHNLE--GFLEEFADIAKEDQ-IKKLHDMLGPHMLRR 232
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
1-153 2.66e-42

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: 152.54  E-value: 2.66e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAgRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQD-LKQESRFHVLLT 79
Cdd:cd17998    28 MGLGKTIQVIAFLAYLK-EIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEPYYGSQEERKHLRYDiLKGLEDFDVIVT 106
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1140176920  80 TYEICL---KDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLF 153
Cdd:cd17998   107 TYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
1-189 1.27e-38

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: 143.26  E-value: 1.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALF--IYLAGRlndEGPFLILCPLSVLSNWKEEMQRFAPgLSCVTYAGDKEERACLQQ-----------D 67
Cdd:cd18058    28 MGLGKTIQSITFLseIFLMGI---RGPFLIIAPLSTITNWEREFRTWTE-MNAIVYHGSQISRQMIQQyemyyrdeqgnP 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  68 LKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSF 147
Cdd:cd18058   104 LSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNF 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1140176920 148 VEPDLFSKEEVgdFIQRYQDIEKEsESASELHKLLQPFLLRR 189
Cdd:cd18058   184 LEPSQFPSETT--FLEEFGDLKTE-EQVKKLQSILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
1-189 1.79e-38

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: 142.86  E-value: 1.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALF--IYLAGRlndEGPFLILCPLSVLSNWKEEMQRFAPgLSCVTYAGDKEERACLQ-----------QD 67
Cdd:cd18059    28 MGLGKTIQSITFLyeIYLKGI---HGPFLVIAPLSTIPNWEREFRTWTE-LNVVVYHGSQASRRTIQlyemyfkdpqgRV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  68 LKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSF 147
Cdd:cd18059   104 IKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHF 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1140176920 148 VEPDLFSKEEVgdFIQRYQDIEKEsESASELHKLLQPFLLRR 189
Cdd:cd18059   184 LEPSRFPSETT--FMQEFGDLKTE-EQVQKLQAILKPMMLRR 222
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
1-191 6.83e-38

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: 142.12  E-value: 6.83e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQDLKQeSRFHVLLTT 80
Cdd:cd18063    51 MGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRS-GKFNVLLTT 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  81 YEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVV-FSLLLTGTPIQNSLQELYSLLSFVEPDLFskEEVG 159
Cdd:cd18063   130 YEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVApRRILLTGTPLQNKLPELWALLNFLLPTIF--KSCS 207
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1140176920 160 DFIQRYQ----------DIEKESE--SASELHKLLQPFLLRRVK 191
Cdd:cd18063   208 TFEQWFNapfamtgervDLNEEETilIIRRLHKVLRPFLLRRLK 251
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
1-191 1.60e-37

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: 140.95  E-value: 1.60e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQDLKQeSRFHVLLTT 80
Cdd:cd18062    51 MGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRS-GKFNVLLTT 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  81 YEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTL-SEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEV- 158
Cdd:cd18062   130 YEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTf 209
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1140176920 159 -----GDFIQRYQDIEKESESA----SELHKLLQPFLLRRVK 191
Cdd:cd18062   210 eqwfnAPFAMTGEKVDLNEEETiliiRRLHKVLRPFLLRRLK 251
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
1-189 2.13e-36

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: 136.72  E-value: 2.13e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALF--IYLAGRlndEGPFLILCPLSVLSNWKEEMQRFAPgLSCVTYAGDKEERACLQQ------DLKQE- 71
Cdd:cd18060    28 MGLGKTIQSIAFLqeVYNVGI---HGPFLVIAPLSTITNWEREFNTWTE-MNTIVYHGSLASRQMIQQyemyckDSRGRl 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  72 ----SRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSF 147
Cdd:cd18060   104 ipgaYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHF 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1140176920 148 VEPDLFSKEevGDFIQRYQDIEKEsESASELHKLLQPFLLRR 189
Cdd:cd18060   184 LEPSQFPSE--SEFLKDFGDLKTE-EQVQKLQAILKPMMLRR 222
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
1-189 1.50e-34

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: 132.02  E-value: 1.50e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGP----FLILCPLSVLSNWKEEMQRFAPG--LSCVTYAGDKEERACLQQDLKQESRF 74
Cdd:cd18004    33 MGLGKTLQAIALVWTLLKQGPYGKPtakkALIVCPSSLVGNWKAEFDKWLGLrrIKVVTADGNAKDVKASLDFFSSASTY 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  75 HVLLTTYEICLKDASFL---KSFpwSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPD 151
Cdd:cd18004   113 PVLIISYETLRRHAEKLskkISI--DLLICDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPG 190
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1140176920 152 LFSkeEVGDFIQRYQ--------------DIEKESESASELHKLLQPFLLRR 189
Cdd:cd18004   191 ILG--SLASFRKVFEepilrsrdpdaseeDKELGAERSQELSELTSRFILRR 240
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
1-189 4.76e-34

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: 130.96  E-value: 4.76e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDE--------------------GPFLILCPLSVLSNWKEEMQRFAP-GLSCVTYAGDKE 59
Cdd:cd18005    28 MGLGKTVQVIAFLAAVLGKTGTRrdrennrprfkkkppassakKPVLIVAPLSVLYNWKDELDTWGHfEVGVYHGSRKDD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  60 EracLQQDLKQeSRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQ 139
Cdd:cd18005   108 E---LEGRLKA-GRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMK 183
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1140176920 140 ELYSLLSFVEPDLFS-----KEEVGDFIQRYQ-------DIEKESESASELHKLLQPFLLRR 189
Cdd:cd18005   184 ELWCLLDWAVPGALGsrsqfKKHFSEPIKRGQrhtatarELRLGRKRKQELAVKLSKFFLRR 245
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
1-189 1.51e-33

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: 128.58  E-value: 1.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIAlFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFApGLSCVTYAGDKEERACLQQD-----------LK 69
Cdd:cd18061    28 MGLGKTIQSIT-FLYEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVVVYHGSLISRQMIQQYemyfrdsqgriIR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  70 QESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVE 149
Cdd:cd18061   106 GAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLEHKVLLTGTPLQNTVEELFSLLHFLE 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1140176920 150 PDLFSKEEVgdFIQRYQDIEKEsESASELHKLLQPFLLRR 189
Cdd:cd18061   186 PLRFPSEST--FMQEFGDLKTE-EQVQKLQAILKPMMLRR 222
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
1-189 1.62e-32

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: 125.93  E-value: 1.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALfIYL--AGRLNDEGPF----LILCPLSVLSNWKEEMQRFAP--GLSCVTYAGDKEERACLQQdlkQES 72
Cdd:cd17999    28 MGLGKTLQTLCI-LASdhHKRANSFNSEnlpsLVVCPPTLVGHWVAEIKKYFPnaFLKPLAYVGPPQERRRLRE---QGE 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  73 RFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDL 152
Cdd:cd17999   104 KHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGY 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1140176920 153 FSKEEVgdFIQRY----------QDIEKESESA----SELHKLLQPFLLRR 189
Cdd:cd17999   184 LGTEKQ--FQRRFlkpilasrdsKASAKEQEAGalalEALHKQVLPFLLRR 232
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
1-150 1.30e-31

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: 122.05  E-value: 1.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGL------SCVTYAGDKEERACLQQDLKQESRF 74
Cdd:cd18000    28 MGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFrvvvlhSSGSGTGSEEKLGSIERKSQLIRKV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  75 ----HVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEP 150
Cdd:cd18000   108 vgdgGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
1-189 1.16e-30

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: 120.55  E-value: 1.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIAlfiYLAGrLNDEGPF---LILCPLSVLSNWKEEMQRFAPGLSCVTYAG-DKEERACLQQDLKQesRFHV 76
Cdd:cd18001    28 MGLGKTVQICA---FLSG-MFDSGLIksvLVVMPTSLIPHWVKEFAKWTPGLRVKVFHGtSKKERERNLERIQR--GGGV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  77 LLTTYEICLKDASFLKS-----FPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPD 151
Cdd:cd18001   102 LLTTYGMVLSNTEQLSAddhdeFKWDYVILDEGHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFACNG 181
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1140176920 152 --LFSKEEvgdFIQRY-------------QDIEKESESASE-LHKLLQPFLLRR 189
Cdd:cd18001   182 slLGTRKT---FKMEFenpitrgrdkdatQGEKALGSEVAEnLRQIIKPYFLRR 232
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
1-189 2.46e-30

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: 120.08  E-value: 2.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIAL-----------------FIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRF--APGLSCVTYAGDKEER 61
Cdd:cd18008    23 MGLGKTIQALALilatrpqdpkipeeleeNSSDPKKLYLSKTTLIVVPLSLLSQWKDEIEKHtkPGSLKVYVYHGSKRIK 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  62 aclqqDLKQESRFHVLLTTYEI----------------CLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVF 125
Cdd:cd18008   103 -----SIEELSDYDIVITTYGTlasefpknkkgggrdsKEKEASPLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAER 177
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1140176920 126 SLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGD-FIQRYQDiEKESESASELHKLLQPFLLRR 189
Cdd:cd18008   178 RWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNsDISKPFS-KNDRKALERLQALLKPILLRR 241
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
1-180 4.55e-28

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: 113.54  E-value: 4.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFA-----PGLSCVTYAGDKEERACLQQDLKQESRFH 75
Cdd:cd18007    35 MGLGKTLQVITFLHTYLAAAPRRSRPLVLCPASTLYNWEDEFKKWLppdlrPLLVLVSLSASKRADARLRKINKWHKEGG 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  76 VLLTTYEICLKDAS--------FLKSFPW------SVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQEL 141
Cdd:cd18007   115 VLLIGYELFRNLASnattdprlKQEFIAAlldpgpDLLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEY 194
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1140176920 142 YSLLSFVEPDLFSKEEvgDFIQRY-QDIEKESESASELHK 180
Cdd:cd18007   195 WTMVDFARPKYLGTLK--EFKKKFvKPIEAGQCVDSTEED 232
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
644-794 2.35e-26

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


Pssm-ID: 394873  Cd Length: 135  Bit Score: 105.03  E-value: 2.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 644 SLKYVSGDVTHPQagaEDALIVHCVDDSGHWGRGGLFTALEK--RSAEPRKIYELAGkmkdlsLGGVLLFPVDDKesrnk 721
Cdd:cd02901     1 KITYVKGDLFACP---ETKSLAHCCNCDGVMGKGIALQFKKKpgRVEELRAQCKKKL------LGGVAVLKRDGV----- 66
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1140176920 722 gQDLLALIVAQHRDRSNvlsgIKMAALEEGLKKIF-LAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAAR 794
Cdd:cd02901    67 -KRYIYYLITKKSYGPK----PTYEALRSSLEELReHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
1-189 5.79e-26

DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as HIP116 or SMARCA3) has both helicase and E3 ubiquitin ligase activities and ATP-dependent nucleosome-remodeling activity. HLTF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350829 [Multi-domain]  Cd Length: 239  Bit Score: 107.17  E-value: 5.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYlagrlndeGPFLILCPLSVLSNWKEEM-QRFAPG-LSCVTYAGDkeERAclqQDLKQESRFHVLL 78
Cdd:cd18071    57 MGLGKTLTTISLILA--------NFTLIVCPLSVLSNWETQFeEHVKPGqLKVYTYHGG--ERN---RDPKLLSKYDIVL 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  79 TTYEICL-----KDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLF 153
Cdd:cd18071   124 TTYNTLAsdfgaKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSFLHLKPF 203
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1140176920 154 SKEEV-GDFIQRyqDIEKESESASE-LHKLLQPFLLRR 189
Cdd:cd18071   204 SNPEYwRRLIQR--PLTMGDPTGLKrLQVLMKQITLRR 239
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
1-189 1.23e-24

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: 102.67  E-value: 1.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALfiylAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLS-----CVTYAGDKEERaclqqdlkqeSRFH 75
Cdd:cd18010    25 MGLGKTVQAIAI----AAYYREEWPLLIVCPSSLRLTWADEIERWLPSLPpddiqVIVKSKDGLRD----------GDAK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  76 VLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEfsVVFS----LLLTGTPIQNSLQELYSLLSFVEPD 151
Cdd:cd18010    91 VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALP--LLKRakrvILLSGTPALSRPIELFTQLDALDPK 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1140176920 152 LFSKEEvgDFIQRYQDIE--------KESESASELHKLL-QPFLLRR 189
Cdd:cd18010   169 LFGRFH--DFGRRYCAAKqggfgwdySGSSNLEELHLLLlATIMIRR 213
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
275-387 2.07e-23

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 95.74  E-value: 2.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 275 GKLHLLDKLLAFlySGGHRVLLFSQMTQMLDIlQDYMDYRGYSYERVDGSVRGEERHLAIKNFGQQPIFVfLLSTRAGGV 354
Cdd:pfam00271   1 EKLEALLELLKK--ERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDV-LVATDVAER 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1140176920 355 GMNLTAADTVIFVDSDFNPQNDLQAAARAHRIG 387
Cdd:pfam00271  77 GLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
1-189 7.32e-23

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: 98.38  E-value: 7.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALfIYLAGRLNDEGP------FLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERAclqQDLKQESRF 74
Cdd:cd18066    33 MGLGKTLQCISL-IWTLLRQGPYGGkpvikrALIVTPGSLVKNWKKEFQKWLGSERIKVFTVDQDHKV---EEFIASPLY 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  75 HVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFS 154
Cdd:cd18066   109 SVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILG 188
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1140176920 155 keEVGDFIQRYQD------------IEKE--SESASELHKLLQPFLLRR 189
Cdd:cd18066   189 --SLSTYRKVYEEpivrsreptatpEEKKlgEARAAELTRLTGLFILRR 235
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
1-189 2.75e-22

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: 96.77  E-value: 2.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLNDEGPFL----ILCPLSVLSNWKEEMQRF-APGLSCVTYAG---DKEERACLQQDLKQES 72
Cdd:cd18067    33 MGLGKTLQCITLMWTLLRQSPQCKPEIdkaiVVSPSSLVKNWANELGKWlGGRLQPLAIDGgskKEIDRKLVQWASQQGR 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  73 RFH--VLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEP 150
Cdd:cd18067   113 RVStpVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNP 192
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1140176920 151 DLFSKEEVgdFIQRY--------------QDIEKESESASELHKLLQPFLLRR 189
Cdd:cd18067   193 GILGTAAE--FKKNFelpilkgrdadaseKERQLGEEKLQELISIVNRCIIRR 243
DEXDc smart00487
DEAD-like helicases superfamily;
1-158 2.33e-20

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 89.86  E-value: 2.33e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920    1 MGLGKTCQtIALFIYLAGRLNDEGPFLILCPLSVL-SNWKEEMQRFAP---GLSCVTYAGDKEERaclQQDLKQESRFHV 76
Cdd:smart00487  33 TGSGKTLA-ALLPALEALKRGKGGRVLVLVPTRELaEQWAEELKKLGPslgLKVVGLYGGDSKRE---QLRKLESGKTDI 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   77 LLTTYEICLKDAS--FLKSFPWSVLVVDEAHRLKNQS--SLLHKTLSEF-SVVFSLLLTGTP---IQNSLQELYSLLSFV 148
Cdd:smart00487 109 LVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLKLLpKNVQLLLLSATPpeeIENLLELFLNDPVFI 188
                          170
                   ....*....|
gi 1140176920  149 EPDLFSKEEV 158
Cdd:smart00487 189 DVGFTPLEPI 198
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
2-154 9.63e-20

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: 88.50  E-value: 9.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   2 GLGKTCQTIALFIYLAGRlNDEGPFLILCPLSVLSNWKEEMQ-RFAPGLSCVTyagDKEERACLQQDLKQESRFHVLLTT 80
Cdd:cd18011    27 GLGKTIEAGLIIKELLLR-GDAKRVLILCPASLVEQWQDELQdKFGLPFLILD---RETAAQLRRLIGNPFEEFPIVIVS 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  81 YEIcLKD----ASFLKSFPWSVLVVDEAHRLKN----QSSLLHKTLSEFSVVFS--LLLTGTPIQNSLQELYSLLSFVEP 150
Cdd:cd18011   103 LDL-LKRseerRGLLLSEEWDLVVVDEAHKLRNsgggKETKRYKLGRLLAKRARhvLLLTATPHNGKEEDFRALLSLLDP 181

                  ....
gi 1140176920 151 DLFS 154
Cdd:cd18011   182 GRFA 185
HELICc smart00490
helicase superfamily c-terminal domain;
305-387 4.82e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 82.26  E-value: 4.82e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  305 DILQDYMDYRGYSYERVDGSVRGEERHLAIKNFgQQPIFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAH 384
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKF-NNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79

                   ...
gi 1140176920  385 RIG 387
Cdd:smart00490  80 RAG 82
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
1-189 4.77e-18

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: 84.45  E-value: 4.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLAGRLN-----------------DEGPF-----LILCPLSVLSNWKEEMQRFAPG--LSCVTYAG 56
Cdd:cd18072    29 MGLGKTLTMIALILAQKNTQNrkeeekekalteweskkDSTLVpsagtLVVCPASLVHQWKNEVESRVASnkLRVCLYHG 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  57 DKEERAClqqdlKQESRFHVLLTTYEICLKD---------ASFLKSFPWSVLVVDEAHRLKNqssllHKTLSEFSV---- 123
Cdd:cd18072   109 PNRERIG-----EVLRDYDIVITTYSLVAKEiptykeesrSSPLFRIAWARIILDEAHNIKN-----PKVQASIAVcklr 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1140176920 124 -VFSLLLTGTPIQNSLQELYSLLSFVEPDLFSkeevgDFIQRYQDIEKESESASE-LHKLLQPFLLRR 189
Cdd:cd18072   179 aHARWALTGTPIQNNLLDMYSLLKFLRCSPFD-----DLKVWKKQVDNKSRKGGErLNILTKSLLLRR 241
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
1-164 4.16e-16

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: 78.32  E-value: 4.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIAlFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQDLKQESRFH----- 75
Cdd:cd18069    37 MGLGKTLQVIS-FLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKWLPPPEALPNVRPRPFKVFILNDEHKTTAARakvie 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  76 -------VLLTTYEICLkdasfLKSFPwSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFV 148
Cdd:cd18069   116 dwvkdggVLLMGYEMFR-----LRPGP-DVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFV 189
                         170
                  ....*....|....*..
gi 1140176920 149 EPD-LFSKEEVGDFIQR 164
Cdd:cd18069   190 RPDfLGTRQEFSNMFER 206
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
1-162 1.21e-15

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: 77.24  E-value: 1.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALF--IYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGL--------SCVTYAGDKEERACLQQDLKQ 70
Cdd:cd18068    37 MGLGKTLQVVTFLhtVLLCEKLENFSRVLVVCPLNTVLNWLNEFEKWQEGLkdeekievNELATYKRPQERSYKLQRWQE 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  71 ESrfHVLLTTYEIC--------------LKDaSFLKSF--PWSVLVV-DEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTP 133
Cdd:cd18068   117 EG--GVMIIGYDMYrilaqernvksrekLKE-IFNKALvdPGPDFVVcDEGHILKNEASAVSKAMNSIRTKRRIVLTGTP 193
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1140176920 134 IQNSLQELYSLLSFVEPDLFS--KEEVGDFI 162
Cdd:cd18068   194 LQNNLIEYHCMVNFVKPNLLGtiKEFRNRFV 224
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
1-188 3.42e-15

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: 76.23  E-value: 3.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFiyLAGRLNDE---------------------------GPFLILCPLSVLSNWKEEMQRFAPG-LSCV 52
Cdd:cd18070    23 MGLGKTVEVLALI--LLHPRPDNdldaadddsdemvccpdclvaetpvssKATLIVCPSAILAQWLDEINRHVPSsLKVL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  53 TYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFP----------------------WSVLVVDEAHRLKNQ 110
Cdd:cd18070   101 TYQGVKKDGALASPAPEILAEYDIVVTTYDVLRTELHYAEANRsnrrrrrqkryeappsplvlveWWRVCLDEAQMVESS 180
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1140176920 111 SSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEvgDFIQRYQDIEKESESASELHKLLQPFLLR 188
Cdd:cd18070   181 TSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCDSD--WWARVLIRPQGRNKAREPLAALLKELLWR 256
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
2-534 2.03e-12

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 70.44  E-value: 2.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   2 GLGKTcqTIALFIylAGRLNDEGPFLILCP-LSVLSNWKEEMQRFAPGlscvtyagdkeeraCLQQDLKQESRFHVLLTT 80
Cdd:COG1061   110 GTGKT--VLALAL--AAELLRGKRVLVLVPrRELLEQWAEELRRFLGD--------------PLAGGGKKDSDAPITVAT 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  81 YEIcLKDASFLKSFP--WSVLVVDEAHRLknQSSLLHKTLSEFSVVFSLLLTGTPiqnslqelysllsfvepdlFSKEEV 158
Cdd:COG1061   172 YQS-LARRAHLDELGdrFGLVIIDEAHHA--GAPSYRRILEAFPAAYRLGLTATP-------------------FRSDGR 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 159 GDFIQRYQDIEKEsESASEL--HKLLQPFLLRRVKAEVATELPKktevviyhgMSALQKKYYKAILmkdldafENETAKK 236
Cdd:COG1061   230 EILLFLFDGIVYE-YSLKEAieDGYLAPPEYYGIRVDLTDERAE---------YDALSERLREALA-------ADAERKD 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 237 VKLQNILSQlrkcvdhpylfdgvepepfevgdhlteasgklhlldkllaflYSGGHRVLLFSQMTQMLDILQDYMDYRGY 316
Cdd:COG1061   293 KILRELLRE------------------------------------------HPDDRKTLVFCSSVDHAEALAELLNEAGI 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 317 SYERVDGSVRGEERHLAIKNFGQQPIfVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKS-VKVI 395
Cdd:COG1061   331 RAAVVTGDTPKKEREEILEAFRDGEL-RILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGKEdALVY 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 396 RLIGRDTVeeiVYRKAASKLQLTNMIIEGGHFTLGAQKPAADADLQLSEILKFGLDKLLASEGSTMDEIDLESILGETKD 475
Cdd:COG1061   410 DFVGNDVP---VLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLL 486
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1140176920 476 GQWVSDALPAAEGGSRDQEEGKNHMYLFEGKDYSKEPSKEDRKSFEQLVNLQKTLLEKA 534
Cdd:COG1061   487 ELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAAL 545
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
1-167 1.20e-11

DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprise a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. The bacterial SNF2 present in this family are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 65.06  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTCQTIALFIYLagRLNDE-GPFLILCPLSVLSN-WKEEMQRFApGLSCVTYA---GDKEERACLQQdlkqeSRFH 75
Cdd:cd18013    24 MGLGKTVTTLTALSDL--QLDDFtRRVLVIAPLRVARStWPDEVEKWN-HLRNLTVSvavGTERQRSKAAN-----TPAD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920  76 VLLTTYE----ICLKdasFLKSFPWSVLVVDEAHRLKNQSSllHKTLSEFSVVFS----LLLTGTPIQNSLQELYSLLSF 147
Cdd:cd18013    96 LYVINREnlkwLVNK---SGDPWPFDMVVIDELSSFKSPRS--KRFKALRKVRPVikrlIGLTGTPSPNGLMDLWAQIAL 170
                         170       180
                  ....*....|....*....|
gi 1140176920 148 VEpdlfSKEEVGDFIQRYQD 167
Cdd:cd18013   171 LD----QGERLGRSITAYRE 186
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
2-133 2.80e-07

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 50.77  E-value: 2.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   2 GLGKTCQTIALFIYLAgrlndEGPFLILCP-LSVLSNWKEEMQRFAPGLS-CVTYAGDKEERAClqqdlkqesrFHVLLT 79
Cdd:cd17926    28 GSGKTLTALALIAYLK-----ELRTLIVVPtDALLDQWKERFEDFLGDSSiGLIGGGKKKDFDD----------ANVVVA 92
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1140176920  80 TY---EICLKDASFLKSFpWSVLVVDEAHRLKnqSSLLHKTLSEFSVVFSLLLTGTP 133
Cdd:cd17926    93 TYqslSNLAEEEKDLFDQ-FGLLIVDEAHHLP--AKTFSEILKELNAKYRLGLTATP 146
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
1-107 1.03e-05

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: 46.24  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   1 MGLGKTcQTIALFIYLAGRLNdEGPFLILCPLSVLSN-WKEEMQ-RFAPGLSCVTYAGD--KEERACLQQDLKqesrfHV 76
Cdd:cd00046    10 TGSGKT-LAALLAALLLLLKK-GKKVLVLVPTKALALqTAERLReLFGPGIRVAVLVGGssAEEREKNKLGDA-----DI 82
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1140176920  77 LLTTYEICLKDASFLKSF---PWSVLVVDEAHRL 107
Cdd:cd00046    83 IIATPDMLLNLLLREDRLflkDLKLIIVDEAHAL 116
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
238-406 1.28e-05

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: 47.71  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 238 KLQNILSQLRKCVDHPYLF-DGVEPEPF---EVGDHLTEASGKLHLLDKLLAFL----YSGGHRVLLFSQMTQMLDILQD 309
Cdd:pfam11496  49 SMTLCLENLSLVATHPYLLvDHYMPKSLllkDEPEKLAYTSGKFLVLNDLVNLLierdRKEPINVAIVARSGKTLDLVEA 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 310 YMDYRGYSYERVDG-SVRGEERHLAIKNFGQQPIFVFLL------STRAGGVgMNLTAADTVIFVDSDFNPQNDLQAAAR 382
Cdd:pfam11496 129 LLLGKGLSYKRYSGeMLYGENKKVSDSGNKKIHSTTCHLlsstgqLTNDDSL-LENYKFDLIIAFDSSVDTSSPSVEHLR 207
                         170       180
                  ....*....|....*....|....
gi 1140176920 383 AHRIGQNKSVKVIRLIGRDTVEEI 406
Cdd:pfam11496 208 TQNRRKGNLAPIIRLVVINSIEHV 231
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
2-136 3.61e-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: 44.93  E-value: 3.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   2 GLGKT-CQTIALFIYLagRLNDEGP-FLILCPLSVL-----SNWKEEMQRFAPGLSCVtYAGDKeeracLQQDLKQESRF 74
Cdd:pfam00270  24 GSGKTlAFLLPALEAL--DKLDNGPqALVLAPTRELaeqiyEELKKLGKGLGLKVASL-LGGDS-----RKEQLEKLKGP 95
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1140176920  75 HVLLTTYEIC---LKDASFLKSFpwSVLVVDEAHRL--KNQSSLLHKTLSEFSVVF-SLLLTGTPIQN 136
Cdd:pfam00270  96 DILVGTPGRLldlLQERKLLKNL--KLLVLDEAHRLldMGFGPDLEEILRRLPKKRqILLLSATLPRN 161
ResIII pfam04851
Type III restriction enzyme, res subunit;
2-134 4.74e-05

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 44.59  E-value: 4.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   2 GLGKTcQTIALFIYLAGRLNDEGPFLILCP-LSVLSNWKEEMQRFAPG--LSCVTYAGDKEERaclqqdlkQESRFHVLL 78
Cdd:pfam04851  33 GSGKT-LTAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFLPNyvEIGEIISGDKKDE--------SVDDNKIVV 103
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1140176920  79 TTY-----EICLKDASFLKSFpWSVLVVDEAHRLknQSSLLHKTLSEFSVVFSLLLTGTPI 134
Cdd:pfam04851 104 TTIqslykALELASLELLPDF-FDVIIIDEAHRS--GASSYRNILEYFKPAFLLGLTATPE 161
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
491-602 5.62e-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: 5.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 491 RDQEEGKNHmylfegKDYSKEPSKEDRKSFEQLvnlQKTLLEKASQEGRSlrnkgsvlipGLVEgsTKRKRVLSPEELED 570
Cdd:pfam17380 466 RQQEEERKR------KKLELEKEKRDRKRAEEQ---RRKILEKELEERKQ----------AMIE--EERKRKLLEKEMEE 524
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1140176920 571 RQKKRQEaaAKRRRLIEEKKRQKEEAEHKKKM 602
Cdd:pfam17380 525 RQKAIYE--EERRREAEEERRKQQEMEERRRI 554
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
342-398 9.23e-05

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 41.54  E-value: 9.23e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1140176920 342 IFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQnKSVKVIRLI 398
Cdd:cd18785    22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILFV 77
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
663-789 9.45e-05

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


Pssm-ID: 394871  Cd Length: 121  Bit Score: 42.77  E-value: 9.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 663 LIVHCVDDSGHWGrGGLFTALEKRSAEPRKIYELAGKMKD-LSLGGVLLfpvddkesrNKGQDLLALIVAqHrdrSNVLS 741
Cdd:cd02749     2 AIVNPANNDLYLG-GGVAKAISKKAGGDLQEECEERKKNGyLKVGEVAV---------TKGGNLPARYII-H---VVGPV 67
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1140176920 742 GIKMAALEEGLKKIF-----LAAKKKKASVHLPRIGHATKGFNWYGTERLIRK 789
Cdd:cd02749    68 ASSKKKTYEPLKKCVknclsLADEKGLKSVAFPAIGTGIAGFPPEEAARIMLE 120
Caldesmon pfam02029
Caldesmon;
510-600 1.30e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.16  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920 510 KEPSKEDRKSFEQ-LVNLQKTLLEKASQEGRSLRNKGSVLIPGLVEGSTKRK---RVLSPEEledrQKKRQEAAAKRRRL 585
Cdd:pfam02029 236 REEEAEVFLEAEQkLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKKREerrKLLEEEE----QRRKQEEAERKLRE 311
                          90
                  ....*....|....*
gi 1140176920 586 IEEKKRQKEEAEHKK 600
Cdd:pfam02029 312 EEEKRRMKEEIERRR 326
Selenoprotein_S pfam06936
Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) ...
574-623 2.28e-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: 40.21  E-value: 2.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1140176920 574 KRQEA-AAKRRRLIE----------EKKRQKEEAEHKKKMAWWES----NNYQSFCLPSEESEPE 623
Cdd:pfam06936  80 KRQEAlEASRLRMQEeldaqaekfkEKQKQLEEEKRRQKIEMWESmqegKSYKGNAKLAQEETEE 144
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
4-111 4.22e-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: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1140176920   4 GKTcqTIALFIYLAGRLNDEGPFLILCPLSVLSN-----WKEEMQRFapGLSCVTYAGDKEEraclqqDLKQESRFHVLL 78
Cdd:cd17921    29 GKT--LIAELAILRALATSGGKAVYIAPTRALVNqkeadLRERFGPL--GKNVGLLTGDPSV------NKLLLAEADILV 98
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1140176920  79 TTYEIC---LKDASFLKSFPWSVLVVDEAHRLKNQS 111
Cdd:cd17921    99 ATPEKLdllLRNGGERLIQDVRLVVVDEAHLIGDGE 134
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
556-603 4.74e-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: 4.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1140176920 556 STKRKRVLSPEELEDR-----QKKRQEAAAKRRRLIEEKKRQKEEAEHKKKMA 603
Cdd:pfam13904 128 LAKPERKVSQEEAKEVlqeweRKKLEQQQRKREEEQREQLKKEEEEQERKQLA 180
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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