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Conserved domains on  [gi|13386044|ref|NP_080815|]
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chromodomain-helicase-DNA-binding protein 1-like isoform 1 [Mus musculus]

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
 39-549 1.66e-159

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: 493.93  E-value: 1.66e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044    39 RLRSYQLEGVNWLVQCF-HCQNGcILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAPGLSC 117
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYeNGING-ILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   118 VTYTGDKEERARLQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSAVFRLLLTG 197
Cdd:PLN03142  248 VKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITG 327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   198 TPIQNSLRELYSLLCVVEPDLFCR-EQVEDFVQryqdIEKESKSA---SELHRLLQPFLLRRVKAQVATELPKKTEVVVY 273
Cdd:PLN03142  328 TPLQNNLHELWALLNFLLPEIFSSaETFDEWFQ----ISGENDQQevvQQLHKVLRPFLLRRLKSDVEKGLPPKKETILK 403

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   274 HGMSALQKKYYKAILMKDLDAFeNETAKKVKLQNILTQLRKCVDHPYLFDGVEP-EPFEVGEHLIEASGKLHLLDRLLAF 352
Cdd:PLN03142  404 VGMSQMQKQYYKALLQKDLDVV-NAGGERKRLLNIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKMVLLDKLLPK 482

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   353 LYSGGHRVLLFSQMTHMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFgNQP---IFVFLLSTRAGGVGMNLTAADT 429
Cdd:PLN03142  483 LKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAF-NKPgseKFVFLLSTRAGGLGINLATADI 561

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   430 VIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMVIEGGHFtpgAQKPSAEADfQLS 509
Cdd:PLN03142  562 VILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD-ELL 637

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 13386044   510 EILKFGLDKLLSSEGSSMEDIDLKSIL--GE-------TKDGQWTPDAL 549
Cdd:PLN03142  638 QMVRYGAEMVFSSKDSTITDEDIDRIIakGEeataeldAKMKKFTEDAI 686
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
 721-871 4.99e-93

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


:

Pssm-ID: 394880  Cd Length: 152  Bit Score: 289.93  E-value: 4.99e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 721 SINYVSGDVTHPQAGE-EDAVIVHCVDDSGRWGRGGLFTALEVRSAEPRKIYELAGKMEDLSLGDVLLFPIDDKESRDKG 799
Cdd:cd03331   1 DINYVSGDVTHPQTTStEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13386044 800 QDLLALVVAQHRDRTNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLATR 871
Cdd:cd03331  81 RDYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 39-549 1.66e-159

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 493.93  E-value: 1.66e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044    39 RLRSYQLEGVNWLVQCF-HCQNGcILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAPGLSC 117
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYeNGING-ILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   118 VTYTGDKEERARLQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSAVFRLLLTG 197
Cdd:PLN03142  248 VKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITG 327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   198 TPIQNSLRELYSLLCVVEPDLFCR-EQVEDFVQryqdIEKESKSA---SELHRLLQPFLLRRVKAQVATELPKKTEVVVY 273
Cdd:PLN03142  328 TPLQNNLHELWALLNFLLPEIFSSaETFDEWFQ----ISGENDQQevvQQLHKVLRPFLLRRLKSDVEKGLPPKKETILK 403

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   274 HGMSALQKKYYKAILMKDLDAFeNETAKKVKLQNILTQLRKCVDHPYLFDGVEP-EPFEVGEHLIEASGKLHLLDRLLAF 352
Cdd:PLN03142  404 VGMSQMQKQYYKALLQKDLDVV-NAGGERKRLLNIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKMVLLDKLLPK 482

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   353 LYSGGHRVLLFSQMTHMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFgNQP---IFVFLLSTRAGGVGMNLTAADT 429
Cdd:PLN03142  483 LKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAF-NKPgseKFVFLLSTRAGGLGINLATADI 561

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   430 VIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMVIEGGHFtpgAQKPSAEADfQLS 509
Cdd:PLN03142  562 VILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD-ELL 637

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 13386044   510 EILKFGLDKLLSSEGSSMEDIDLKSIL--GE-------TKDGQWTPDAL 549
Cdd:PLN03142  638 QMVRYGAEMVFSSKDSTITDEDIDRIIakGEeataeldAKMKKFTEDAI 686
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 40-489 6.63e-136

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 421.56  E-value: 6.63e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALLIYLVGRlNDEGPFLVLCPLSVLSNWKEEMERFAPGLSCVT 119
Cdd:COG0553 242 LRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKER-GLARPVLIVAPTSLVGNWQRELAKFAPGLRVLV 320

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 120 YTGDKEeRARLQQDLRQesgFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSAVFRLLLTGTP 199
Cdd:COG0553 321 LDGTRE-RAKGANPFED---ADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTP 396

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 200 IQNSLRELYSLLCVVEPDLFcrEQVEDFVQRYQD-IEKESKSASE-LHRLLQPFLLRRVKAQVATELPKKTEVVVYHGMS 277
Cdd:COG0553 397 VENRLEELWSLLDFLNPGLL--GSLKAFRERFARpIEKGDEEALErLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELT 474

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 278 ALQKKYYKAIL---MKDLDAFENETAKKVKLQnILTQLRKCVDHPYLFDgvepepfEVGEHLIEASGKLHLLDRLLAFLY 354
Cdd:COG0553 475 PEQRALYEAVLeylRRELEGAEGIRRRGLILA-ALTRLRQICSHPALLL-------EEGAELSGRSAKLEALLELLEELL 546

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 355 SGGHRVLLFSQMTHMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGNQP-IFVFLLSTRAGGVGMNLTAADTVIFV 433
Cdd:COG0553 547 AEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVFLISLKAGGEGLNLTAADHVIHY 626

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13386044 434 DSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMVIE 489
Cdd:COG0553 627 DLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
 40-255 1.45e-128

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: 385.25  E-value: 1.45e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAPGLSCVT 119
Cdd:cd18006   1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 120 YTGDKEERARLQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSAVFRLLLTGTP 199
Cdd:cd18006  81 YMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13386044 200 IQNSLRELYSLLCVVEPDLFCREQVEDFVQRYQDIEKESKSASELHRLLQPFLLRR 255
Cdd:cd18006 161 IQNSLQELYALLSFIEPNVFPKDKLDDFIKAYSETDDESETVEELHLLLQPFLLRR 216
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
 721-871 4.99e-93

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


Pssm-ID: 394880  Cd Length: 152  Bit Score: 289.93  E-value: 4.99e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 721 SINYVSGDVTHPQAGE-EDAVIVHCVDDSGRWGRGGLFTALEVRSAEPRKIYELAGKMEDLSLGDVLLFPIDDKESRDKG 799
Cdd:cd03331   1 DINYVSGDVTHPQTTStEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13386044 800 QDLLALVVAQHRDRTNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLATR 871
Cdd:cd03331  81 RDYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 43-322 2.40e-86

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: 277.64  E-value: 2.40e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044    43 YQLEGVNWLVQCfHCQ--NGCILGDEMGLGKTCQTIALLIYLVG-RLNDEGPFLVLCPLSVLSNWKEEMERFA--PGLSC 117
Cdd:pfam00176   1 YQIEGVNWMLSL-ENNlgRGGILADEMGLGKTLQTISLLLYLKHvDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   118 VTYTGDKEERARLQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSAVFRLLLTG 197
Cdd:pfam00176  80 VVLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   198 TPIQNSLRELYSLLCVVEPDLFCreQVEDFVQRY-QDIE--KESKSASELHRLLQPFLLRRVKAQVATELPKKTEVVVYH 274
Cdd:pfam00176 160 TPLQNNLEELWALLNFLRPGPFG--SLSTFRNWFdRPIErgGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFC 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 13386044   275 GMSALQKKYYKA-ILMKDLDAFENETA---KKVKLQNILTQLRKCVDHPYLF 322
Cdd:pfam00176 238 RLSKLQRKLYQTfLLKKDLNAIKTGEGgreIKASLLNILMRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
35-227 3.62e-28

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 112.59  E-value: 3.62e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044     35 LTGIRLRSYQLEGVNWLVQCFHcqnGCILGDEMGLGKT-CQTIALLIYLvgRLNDEGPFLVLCPLSVL-SNWKEEMERFA 112
Cdd:smart00487   4 FGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTlAALLPALEAL--KRGKGGRVLVLVPTRELaEQWAEELKKLG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044    113 P--GLSCVTYTGDKEERARLQQDLRQEsgFHVLLTTYEICLKDAS--FLKSFSWSVLAVDEAHRLKNQS--SLLHRTLSE 186
Cdd:smart00487  79 PslGLKVVGLYGGDSKREQLRKLESGK--TDILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLKL 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 13386044    187 F-SAVFRLLLTGTP---IQNSLRELYSLLCVVEPDLFCREQVEDF 227
Cdd:smart00487 157 LpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPIEQF 201
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 722-869 7.57e-04

O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441713  Cd Length: 168  Bit Score: 41.32  E-value: 7.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 722 INYVSGDVTHPQAgeeDAvIVHCVDDSGRWGrGGLftALEVRSA---EPRKIYELAGKMEDLSLGDVLLFPiddkesrdk 798
Cdd:COG2110   1 IEIVQGDITELDV---DA-IVNAANSSLLGG-GGV--AGAIHRAagpELLEECRRLCKQGGCPTGEAVITP--------- 64

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13386044 799 GQDLLALVVA-----QHRDRTNvlsgIKMAALEEGLKKIF-LAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLA 869
Cdd:COG2110  65 AGNLPAKYVIhtvgpVWRGGGP----SEEELLASCYRNSLeLAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLR 137
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
 39-549 1.66e-159

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 493.93  E-value: 1.66e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044    39 RLRSYQLEGVNWLVQCF-HCQNGcILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAPGLSC 117
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYeNGING-ILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   118 VTYTGDKEERARLQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSAVFRLLLTG 197
Cdd:PLN03142  248 VKFHGNPEERAHQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITG 327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   198 TPIQNSLRELYSLLCVVEPDLFCR-EQVEDFVQryqdIEKESKSA---SELHRLLQPFLLRRVKAQVATELPKKTEVVVY 273
Cdd:PLN03142  328 TPLQNNLHELWALLNFLLPEIFSSaETFDEWFQ----ISGENDQQevvQQLHKVLRPFLLRRLKSDVEKGLPPKKETILK 403

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   274 HGMSALQKKYYKAILMKDLDAFeNETAKKVKLQNILTQLRKCVDHPYLFDGVEP-EPFEVGEHLIEASGKLHLLDRLLAF 352
Cdd:PLN03142  404 VGMSQMQKQYYKALLQKDLDVV-NAGGERKRLLNIAMQLRKCCNHPYLFQGAEPgPPYTTGEHLVENSGKMVLLDKLLPK 482

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   353 LYSGGHRVLLFSQMTHMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFgNQP---IFVFLLSTRAGGVGMNLTAADT 429
Cdd:PLN03142  483 LKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAF-NKPgseKFVFLLSTRAGGLGINLATADI 561

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   430 VIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMVIEGGHFtpgAQKPSAEADfQLS 509
Cdd:PLN03142  562 VILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRL---AEQKTVNKD-ELL 637

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 13386044   510 EILKFGLDKLLSSEGSSMEDIDLKSIL--GE-------TKDGQWTPDAL 549
Cdd:PLN03142  638 QMVRYGAEMVFSSKDSTITDEDIDRIIakGEeataeldAKMKKFTEDAI 686
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
 40-489 6.63e-136

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 421.56  E-value: 6.63e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALLIYLVGRlNDEGPFLVLCPLSVLSNWKEEMERFAPGLSCVT 119
Cdd:COG0553 242 LRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKER-GLARPVLIVAPTSLVGNWQRELAKFAPGLRVLV 320

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 120 YTGDKEeRARLQQDLRQesgFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSAVFRLLLTGTP 199
Cdd:COG0553 321 LDGTRE-RAKGANPFED---ADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTP 396

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 200 IQNSLRELYSLLCVVEPDLFcrEQVEDFVQRYQD-IEKESKSASE-LHRLLQPFLLRRVKAQVATELPKKTEVVVYHGMS 277
Cdd:COG0553 397 VENRLEELWSLLDFLNPGLL--GSLKAFRERFARpIEKGDEEALErLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELT 474

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 278 ALQKKYYKAIL---MKDLDAFENETAKKVKLQnILTQLRKCVDHPYLFDgvepepfEVGEHLIEASGKLHLLDRLLAFLY 354
Cdd:COG0553 475 PEQRALYEAVLeylRRELEGAEGIRRRGLILA-ALTRLRQICSHPALLL-------EEGAELSGRSAKLEALLELLEELL 546

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 355 SGGHRVLLFSQMTHMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGNQP-IFVFLLSTRAGGVGMNLTAADTVIFV 433
Cdd:COG0553 547 AEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVFLISLKAGGEGLNLTAADHVIHY 626

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13386044 434 DSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMVIE 489
Cdd:COG0553 627 DLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
 40-255 1.45e-128

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: 385.25  E-value: 1.45e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAPGLSCVT 119
Cdd:cd18006   1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 120 YTGDKEERARLQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSAVFRLLLTGTP 199
Cdd:cd18006  81 YMGDKEKRLDLQQDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTP 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13386044 200 IQNSLRELYSLLCVVEPDLFCREQVEDFVQRYQDIEKESKSASELHRLLQPFLLRR 255
Cdd:cd18006 161 IQNSLQELYALLSFIEPNVFPKDKLDDFIKAYSETDDESETVEELHLLLQPFLLRR 216
Macro_Poa1p-like_SNF2 cd03331
macrodomain, Poa1p-like family, SNF2 subfamily; Macrodomains are found in a variety of ...
 721-871 4.99e-93

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


Pssm-ID: 394880  Cd Length: 152  Bit Score: 289.93  E-value: 4.99e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 721 SINYVSGDVTHPQAGE-EDAVIVHCVDDSGRWGRGGLFTALEVRSAEPRKIYELAGKMEDLSLGDVLLFPIDDKESRDKG 799
Cdd:cd03331   1 DINYVSGDVTHPQTTStEDAIIVHCVDDSGRWGRGGLFSALSSRSKQPKEQYELAGEMKDLHLGDVHLIPVDDKESRSGG 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13386044 800 QDLLALVVAQHRDRTNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLATR 871
Cdd:cd03331  81 RDYVALIVAQHRDRSNKLSGIKLSALETGLQKIATAAKQRNASVHLPRIGHGTPGFNWYGTERLIRKHLASR 152
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
 43-322 2.40e-86

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: 277.64  E-value: 2.40e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044    43 YQLEGVNWLVQCfHCQ--NGCILGDEMGLGKTCQTIALLIYLVG-RLNDEGPFLVLCPLSVLSNWKEEMERFA--PGLSC 117
Cdd:pfam00176   1 YQIEGVNWMLSL-ENNlgRGGILADEMGLGKTLQTISLLLYLKHvDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   118 VTYTGDKEERARLQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSAVFRLLLTG 197
Cdd:pfam00176  80 VVLHGNKRPQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   198 TPIQNSLRELYSLLCVVEPDLFCreQVEDFVQRY-QDIE--KESKSASELHRLLQPFLLRRVKAQVATELPKKTEVVVYH 274
Cdd:pfam00176 160 TPLQNNLEELWALLNFLRPGPFG--SLSTFRNWFdRPIErgGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFC 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 13386044   275 GMSALQKKYYKA-ILMKDLDAFENETA---KKVKLQNILTQLRKCVDHPYLF 322
Cdd:pfam00176 238 RLSKLQRKLYQTfLLKKDLNAIKTGEGgreIKASLLNILMRLRKICNHPGLI 289
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
 40-255 1.13e-79

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: 256.90  E-value: 1.13e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAPGLSCVT 119
Cdd:cd17993   2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 120 YTGDKEERARLQQ-----DLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSAVFRLL 194
Cdd:cd17993  82 YLGDIKSRDTIREyefyfSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRLL 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13386044 195 LTGTPIQNSLRELYSLLCVVEPDLF-CREQVEDfvqrYQDIEKESKSASeLHRLLQPFLLRR 255
Cdd:cd17993 162 ITGTPLQNSLKELWALLHFLMPGKFdIWEEFEE----EHDEEQEKGIAD-LHKELEPFILRR 218
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
 40-221 1.42e-77

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 249.79  E-value: 1.42e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAPGLSCVT 119
Cdd:cd17919   1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 120 YTGDKEERARLQQDLRQESgFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSAVFRLLLTGTP 199
Cdd:cd17919  81 YHGSQRERAQIRAKEKLDK-FDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTP 159

                       170       180
                ....*....|....*....|..
gi 13386044 200 IQNSLRELYSLLCVVEPDLFCR 221
Cdd:cd17919 160 LQNNLEELWALLDFLDPPFLLR 181
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
 40-255 1.02e-71

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: 235.61  E-value: 1.02e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAPgLSCVT 119
Cdd:cd17995   1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 120 YTGDKEERARLQQ-----------DLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFS 188
Cdd:cd17995  80 YHGSGESRQIIQQyemyfkdaqgrKKKGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13386044 189 AVFRLLLTGTPIQNSLRELYSLLCVVEPDLFCREqvEDFVQRYQDIEKESKsASELHRLLQPFLLRR 255
Cdd:cd17995 160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSS--EEFLEEFGDLKTAEQ-VEKLQALLKPYMLRR 223
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
 39-257 2.01e-71

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: 234.91  E-value: 2.01e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  39 RLRSYQLEGVNWLVQCFHcqNGC--ILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAPGLS 116
Cdd:cd17997   3 TMRDYQIRGLNWLISLFE--NGIngILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 117 CVTYTGDKEERARLQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSAVFRLLLT 196
Cdd:cd17997  81 VVVLIGDKEERADIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLT 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13386044 197 GTPIQNSLRELYSLLCVVEPDLFcrEQVEDFVQRY--QDIEKESKS-ASELHRLLQPFLLRRVK 257
Cdd:cd17997 161 GTPLQNNLHELWALLNFLLPDVF--TSSEDFDEWFnvNNCDDDNQEvVQRLHKVLRPFLLRRIK 222
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
 37-257 5.53e-70

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: 231.51  E-value: 5.53e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  37 GIRLRSYQLEGVNWLVQCFhcQNGC--ILGDEMGLGKTCQTIALLIYLVGRLNDeGPFLVLCPLSVLSNWKEEMERFAPG 114
Cdd:cd18009   1 GGVMRPYQLEGMEWLRMLW--ENGIngILADEMGLGKTIQTIALLAHLRERGVW-GPFLVIAPLSTLPNWVNEFARFTPS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 115 LSCVTYTGDKEERARLQQDLRQESG----FHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSAV 190
Cdd:cd18009  78 VPVLLYHGTKEERERLRKKIMKREGtlqdFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSD 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13386044 191 FRLLLTGTPIQNSLRELYSLLCVVEPDLFCR----EQVEDFVQRYQDIEKESKSASE--------LHRLLQPFLLRRVK 257
Cdd:cd18009 158 NRLLLTGTPLQNNLSELWSLLNFLLPDVFDDlssfESWFDFSSLSDNAADISNLSEEreqnivhmLHAILKPFLLRRLK 236
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
 40-257 7.28e-68

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: 225.71  E-value: 7.28e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQ-NGcILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAPGLSCV 118
Cdd:cd17996   4 LKEYQLKGLQWMVSLYNNNlNG-ILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSKI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 119 TYTGDKEERARLQQDLRQeSGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSE-FSAVFRLLLTG 197
Cdd:cd17996  83 VYKGTPDVRKKLQSQIRA-GKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyYHARYRLLLTG 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13386044 198 TPIQNSLRELYSLLCVVEPDLFcrEQVEDFVQRYQ-----DIEKESKSASE---------LHRLLQPFLLRRVK 257
Cdd:cd17996 162 TPLQNNLPELWALLNFLLPKIF--KSCKTFEQWFNtpfanTGEQVKIELNEeetlliirrLHKVLRPFLLRRLK 233
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
 34-255 9.45e-67

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: 222.96  E-value: 9.45e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  34 GLTGIRLRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAP 113
Cdd:cd18054  15 GGENLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFEIWAP 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 114 GLSCVTYTGDKEERARL-------QQDLRQEsgFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSE 186
Cdd:cd18054  95 EINVVVYIGDLMSRNTIreyewihSQTKRLK--FNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLID 172

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13386044 187 FSAVFRLLLTGTPIQNSLRELYSLLCVVEPDLFcrEQVEDFVQRYQdiEKESKSASELHRLLQPFLLRR 255
Cdd:cd18054 173 FKSNHRLLITGTPLQNSLKELWSLLHFIMPEKF--EFWEDFEEDHG--KGRENGYQSLHKVLEPFLLRR 237
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
 40-257 1.59e-62

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: 210.50  E-value: 1.59e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALLIYlVGRLNDEGPFLVLCPLSVLSNWKEEMERFAPGLSCVT 119
Cdd:cd18012   5 LRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLS-RKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKVLV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 120 YTGDKEERARLqqdlRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSAVFRLLLTGTP 199
Cdd:cd18012  84 IHGTKRKREKL----RALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTP 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13386044 200 IQNSLRELYSLLCVVEPDLFcrEQVEDFVQRYQ-DIEK--ESKSASELHRLLQPFLLRRVK 257
Cdd:cd18012 160 IENHLGELWSIFDFLNPGLL--GSYKRFKKRFAkPIEKdgDEEALEELKKLISPFILRRLK 218
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
 40-255 3.87e-59

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: 201.43  E-value: 3.87e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQ-NGcILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAPGLSCV 118
Cdd:cd18003   1 LREYQHIGLDWLATLYEKNlNG-ILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKIL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 119 TYTGDKEERARLQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSAVFRLLLTGT 198
Cdd:cd18003  80 TYYGSAKERKLKRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGT 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13386044 199 PIQNSLRELYSLLCVVEPDLFcrEQVEDFVQRYQDIEKESKSASE---------LHRLLQPFLLRR 255
Cdd:cd18003 160 PLQNSLMELWSLMHFLMPHIF--QSHQEFKEWFSNPLTAMSEGSQeeneelvrrLHKVLRPFLLRR 223
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
 40-255 1.09e-58

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: 199.20  E-value: 1.09e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAPGLSCVT 119
Cdd:cd17994   1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 120 YTGDkeerarlqqdlrqesgfHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSAVFRLLLTGTP 199
Cdd:cd17994  81 YVGD-----------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTP 143

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13386044 200 IQNSLRELYSLLCVVEPDLFcrEQVEDFVQRYQDIEKESKsASELHRLLQPFLLRR 255
Cdd:cd17994 144 LQNNLEELFHLLNFLTPERF--NNLQGFLEEFADISKEDQ-IKKLHDLLGPHMLRR 196
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
 23-267 6.71e-58

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: 198.74  E-value: 6.71e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  23 TRVQE-PDLQQWGltgiRLRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVL 101
Cdd:cd18064   2 TRFEDsPSYVKWG----KLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 102 SNWKEEMERFAPGLSCVTYTGDKEERARLQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLH 181
Cdd:cd18064  78 HNWMAEFKRWVPTLRAVCLIGDKDQRAAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLS 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 182 RTLSEFSAVFRLLLTGTPIQNSLRELYSLLCVVEPDLFcrEQVEDFVQRY--QDIEKESKSASELHRLLQPFLLRRVKAQ 259
Cdd:cd18064 158 EIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVF--NSAEDFDSWFdtNNCLGDQKLVERLHMVLRPFLLRRIKAD 235


                ....*...
gi 13386044 260 VATELPKK 267
Cdd:cd18064 236 VEKSLPPK 243
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
 34-255 3.29e-57

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: 196.42  E-value: 3.29e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  34 GLTGIRLRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAP 113
Cdd:cd18053  15 GHEGLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAP 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 114 GLSCVTYTGDKEER--ARLQQDLRQESG---FHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFS 188
Cdd:cd18053  95 QMNAVVYLGDINSRnmIRTHEWMHPQTKrlkFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFK 174

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13386044 189 AVFRLLLTGTPIQNSLRELYSLLCVVEPDLFcrEQVEDFVQRYQDiEKESKSASeLHRLLQPFLLRR 255
Cdd:cd18053 175 SNHRLLITGTPLQNSLKELWSLLHFIMPEKF--SSWEDFEEEHGK-GREYGYAS-LHKELEPFLLRR 237
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
 40-255 2.45e-56

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: 193.88  E-value: 2.45e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAPGLSCVT 119
Cdd:cd18002   1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 120 YTGDKEERARLQQDL------RQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSAVFRL 193
Cdd:cd18002  81 YWGNPKDRKVLRKFWdrknlyTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13386044 194 LLTGTPIQNSLRELYSLLCVVEPDLFcrEQVEDFVQRY-QDIEKESKSA--------SELHRLLQPFLLRR 255
Cdd:cd18002 161 LLTGTPIQNSMAELWALLHFIMPTLF--DSHDEFNEWFsKDIESHAENKtglnehqlKRLHMILKPFMLRR 229
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
 40-219 2.96e-53

DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 (SMARCAD1, also known as ATP-dependent helicase 1 or Hel1) possesses intrinsic ATP-dependent nucleosome-remodeling activity and is required for both DNA repair and heterochromatin organization. SMARCAD1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350756 [Multi-domain]  Cd Length: 187  Bit Score: 183.74  E-value: 2.96e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALLIYLVgRLNDEGPFLVLCPLSVLSNWKEEMERFAPGLSCVT 119
Cdd:cd17998   1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLK-EIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 120 YTGDKEERARLQQD-LRQESGFHVLLTTYEICL---KDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSAVFRLLL 195
Cdd:cd17998  80 YYGSQEERKHLRYDiLKGLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFRLLL 159

                       170       180
                ....*....|....*....|....
gi 13386044 196 TGTPIQNSLRELYSLLCVVEPDLF 219
Cdd:cd17998 160 TGTPLQNNLLELMSLLNFIMPKPF 183
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
 340-464 3.92e-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: 181.14  E-value: 3.92e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 340 SGKLHLLDRLLAFLYSGGHRVLLFSQMTHMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGNQP-IFVFLLSTRAG 418
Cdd:cd18793  10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdIRVFLLSTKAG 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 13386044 419 GVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLI 464
Cdd:cd18793  90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
 35-257 5.52e-53

DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 (SMARCA1, also called SNF2L) is a component of NURF (nucleosome-remodeling factor) and CERF (CECR2-containing-remodeling factor) complexes which promote the perturbation of chromatin structure in an ATP-dependent manner. SMARCA1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350823 [Multi-domain]  Cd Length: 233  Bit Score: 184.45  E-value: 5.52e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  35 LTGIRLRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAPG 114
Cdd:cd18065  11 VKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFKRWVPS 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 115 LSCVTYTGDKEERARLQQDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSAVFRLL 194
Cdd:cd18065  91 LRAVCLIGDKDARAAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLL 170

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13386044 195 LTGTPIQNSLRELYSLLCVVEPDLFcrEQVEDFVQRY--QDIEKESKSASELHRLLQPFLLRRVK 257
Cdd:cd18065 171 LTGTPLQNNLHELWALLNFLLPDVF--NSADDFDSWFdtKNCLGDQKLVERLHAVLKPFLLRRIK 233
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
 40-255 3.03e-52

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: 182.52  E-value: 3.03e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAPGLSCVT 119
Cdd:cd18055   1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 120 YTGDKEERARLQQD-----------------LRQES--GFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLL 180
Cdd:cd18055  81 YTGDKDSRAIIRENefsfddnavkggkkafkMKREAqvKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13386044 181 HRTLSEFSAVFRLLLTGTPIQNSLRELYSLLCVVEPDLFcrEQVEDFVQRYQDIEKESKsASELHRLLQPFLLRR 255
Cdd:cd18055 161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERF--NNLEGFLEEFADISKEDQ-IKKLHDLLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
 40-255 8.30e-52

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: 181.42  E-value: 8.30e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAPGLSCVT 119
Cdd:cd18057   1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 120 YTGDKEERARLQQD-----------------LRQES--GFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLL 180
Cdd:cd18057  81 YTGDKESRSVIRENefsfednairsgkkvfrMKKEAqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13386044 181 HRTLSEFSAVFRLLLTGTPIQNSLRELYSLLCVVEPDLFcrEQVEDFVQRYQDIEKESKsASELHRLLQPFLLRR 255
Cdd:cd18057 161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERF--NNLEGFLEEFADISKEDQ-IKKLHDLLGPHMLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
 40-255 6.74e-50

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: 176.02  E-value: 6.74e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAPGLSCVT 119
Cdd:cd18056   1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 120 YTGDKEERARLQQD-----------------LRQESG--FHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLL 180
Cdd:cd18056  81 YVGDKDSRAIIRENefsfednairggkkasrMKKEASvkFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13386044 181 HRTLSEFSAVFRLLLTGTPIQNSLRELYSLLCVVEPDLFcrEQVEDFVQRYQDIEKESKsASELHRLLQPFLLRR 255
Cdd:cd18056 161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERF--HNLEGFLEEFADIAKEDQ-IKKLHDMLGPHMLRR 232
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
 40-255 5.26e-47

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: 167.53  E-value: 5.26e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALL--IYLVGRlndEGPFLVLCPLSVLSNWKEEMERFAPgLSC 117
Cdd:cd18058   1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLseIFLMGI---RGPFLIIAPLSTITNWEREFRTWTE-MNA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 118 VTYTGDKEERARLQQD---LRQESG--------FHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSE 186
Cdd:cd18058  77 IVYHGSQISRQMIQQYemyYRDEQGnplsgifkFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKL 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13386044 187 FSAVFRLLLTGTPIQNSLRELYSLLCVVEPDLFCREQVedFVQRYQDIEKESKsASELHRLLQPFLLRR 255
Cdd:cd18058 157 MALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETT--FLEEFGDLKTEEQ-VKKLQSILKPMMLRR 222
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
 40-257 1.22e-45

DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (SMARCA2, also known as brahma homolog) is a component of the BAF complex. SMARCA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350821 [Multi-domain]  Cd Length: 251  Bit Score: 164.47  E-value: 1.22e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAPGLSCVT 119
Cdd:cd18063  24 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 120 YTGDKEERARLQQDLRQeSGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTL-SEFSAVFRLLLTGT 198
Cdd:cd18063 104 YKGTPAMRRSLVPQLRS-GKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRRILLTGT 182

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13386044 199 PIQNSLRELYSLLCVVEPDLFcrEQVEDFVQRYQ----------DIEKESK--SASELHRLLQPFLLRRVK 257
Cdd:cd18063 183 PLQNKLPELWALLNFLLPTIF--KSCSTFEQWFNapfamtgervDLNEEETilIIRRLHKVLRPFLLRRLK 251
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
 40-255 4.46e-45

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: 161.76  E-value: 4.46e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALL--IYLVGRlndEGPFLVLCPLSVLSNWKEEMERFAPgLSC 117
Cdd:cd18060   1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLqeVYNVGI---HGPFLVIAPLSTITNWEREFNTWTE-MNT 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 118 VTYTGDKEERARLQQD---LRQESG--------FHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSE 186
Cdd:cd18060  77 IVYHGSLASRQMIQQYemyCKDSRGrlipgaykFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKH 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13386044 187 FSAVFRLLLTGTPIQNSLRELYSLLCVVEPDLFCREQveDFVQRYQDIEKESKsASELHRLLQPFLLRR 255
Cdd:cd18060 157 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSES--EFLKDFGDLKTEEQ-VQKLQAILKPMMLRR 222
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
 40-255 4.92e-45

DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as RAD26L) may play a role in DNA repair and mitochondrial function. In humans, mutations in the ERCC6L2 gene are associated with bone marrow failure syndrome 2. ERCC6L2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350763 [Multi-domain]  Cd Length: 245  Bit Score: 162.55  E-value: 4.92e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALLIYLVGRLNDE--------------------GPFLVLCPLS 99
Cdd:cd18005   1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTGTRrdrennrprfkkkppassakKPVLIVAPLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 100 VLSNWKEEMERFApGLSCVTYTGDKEERArLQQDLRQeSGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSL 179
Cdd:cd18005  81 VLYNWKDELDTWG-HFEVGVYHGSRKDDE-LEGRLKA-GRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSK 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 180 LHRTLSEFSAVFRLLLTGTPIQNSLRELYSLLCVVEPDLF-----CREQVEDFVQRYQ-------DIEKESKSASELHRL 247
Cdd:cd18005 158 LTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALgsrsqFKKHFSEPIKRGQrhtatarELRLGRKRKQELAVK 237


                ....*...
gi 13386044 248 LQPFLLRR 255
Cdd:cd18005 238 LSKFFLRR 245
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
 40-257 5.53e-45

DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4, also known as transcription activator BRG1) is a component of the CREST-BRG1 complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. Mutation of SMARCA4 (BRG1), the ATPase of BAF (mSWI/SNF) and PBAF complexes, contributes to a range of malignancies and neurologic disorders. SMARCA4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350820 [Multi-domain]  Cd Length: 251  Bit Score: 162.52  E-value: 5.53e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAPGLSCVT 119
Cdd:cd18062  24 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVKVS 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 120 YTGDKEERARLQQDLRQeSGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTL-SEFSAVFRLLLTGT 198
Cdd:cd18062 104 YKGSPAARRAFVPQLRS-GKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRRLLLTGT 182

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13386044 199 PIQNSLRELYSLLCVVEPDLFcrEQVEDFVQRYQ----------DIEKESK--SASELHRLLQPFLLRRVK 257
Cdd:cd18062 183 PLQNKLPELWALLNFLLPTIF--KSCSTFEQWFNapfamtgekvDLNEEETilIIRRLHKVLRPFLLRRLK 251
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
 40-255 2.28e-44

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: 159.81  E-value: 2.28e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALL--IYLVGRlndEGPFLVLCPLSVLSNWKEEMERFAPgLSC 117
Cdd:cd18059   1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLyeIYLKGI---HGPFLVIAPLSTIPNWEREFRTWTE-LNV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 118 VTYTGDKEERARLQ-----------QDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSE 186
Cdd:cd18059  77 VVYHGSQASRRTIQlyemyfkdpqgRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKM 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13386044 187 FSAVFRLLLTGTPIQNSLRELYSLLCVVEPDLFCREQVedFVQRYQDIEKESKsASELHRLLQPFLLRR 255
Cdd:cd18059 157 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETT--FMQEFGDLKTEEQ-VQKLQAILKPMMLRR 222
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
 40-255 6.90e-44

DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350762 [Multi-domain]  Cd Length: 240  Bit Score: 158.99  E-value: 6.90e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFH-----CQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGP----FLVLCPLSVLSNWKEEMER 110
Cdd:cd18004   1 LRPHQREGVQFLYDCLTgrrgyGGGGAILADEMGLGKTLQAIALVWTLLKQGPYGKPtakkALIVCPSSLVGNWKAEFDK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 111 FAPG--LSCVTYTGDKEERARLQQDLRQESGFHVLLTTYEICLKDAS-FLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEF 187
Cdd:cd18004  81 WLGLrrIKVVTADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEkLSKKISIDLLICDEGHRLKNSESKTTKALNSL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 188 SAVFRLLLTGTPIQNSLRELYSLLCVVEPDLF-----CREQVEDFVQR-------YQDIEKESKSASELHRLLQPFLLRR 255
Cdd:cd18004 161 PCRRRLLLTGTPIQNDLDEFFALVDFVNPGILgslasFRKVFEEPILRsrdpdasEEDKELGAERSQELSELTSRFILRR 240
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
 40-255 2.87e-41

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: 151.37  E-value: 2.87e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIAlliYLVGrLNDEGPF---LVLCPLSVLSNWKEEMERFAPGLS 116
Cdd:cd18001   1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICA---FLSG-MFDSGLIksvLVVMPTSLIPHWVKEFAKWTPGLR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 117 CVTYTG-DKEERARLQQDLRQESGfhVLLTTYEICLKDASFLKS-----FSWSVLAVDEAHRLKNQSSLLHRTLSEFSAV 190
Cdd:cd18001  77 VKVFHGtSKKERERNLERIQRGGG--VLLTTYGMVLSNTEQLSAddhdeFKWDYVILDEGHKIKNSKTKSAKSLREIPAK 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 191 FRLLLTGTPIQNSLRELYSLLcvvepDLFCREQV----EDFVQRY-------------QDIEKESKSASE-LHRLLQPFL 252
Cdd:cd18001 155 NRIILTGTPIQNNLKELWALF-----DFACNGSLlgtrKTFKMEFenpitrgrdkdatQGEKALGSEVAEnLRQIIKPYF 229


                ...
gi 13386044 253 LRR 255
Cdd:cd18001 230 LRR 232
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
 40-255 1.44e-40

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: 149.42  E-value: 1.44e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALL---IYLVGRLNDEGPF--LVLCPLSVLSNWKEEMERFAP- 113
Cdd:cd17999   1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILasdHHKRANSFNSENLpsLVVCPPTLVGHWVAEIKKYFPn 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 114 -GLSCVTYTGDKEERARLQQdlrQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSAVFR 192
Cdd:cd17999  81 aFLKPLAYVGPPQERRRLRE---QGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHR 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13386044 193 LLLTGTPIQNSLRELYSLLCVVEPDLFCREQVedFVQRY--------------QDIEKESKSASELHRLLQPFLLRR 255
Cdd:cd17999 158 LILSGTPIQNNVLELWSLFDFLMPGYLGTEKQ--FQRRFlkpilasrdskasaKEQEAGALALEALHKQVLPFLLRR 232
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
 40-221 1.58e-40

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: 147.86  E-value: 1.58e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQcFHCQN-GCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAPGL--- 115
Cdd:cd18000   1 LFKYQQTGVQWLWE-LHCQRvGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFrvv 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 116 ---SCVTYTGDKE-----ERARLQQDLRQESGfHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEF 187
Cdd:cd18000  80 vlhSSGSGTGSEEklgsiERKSQLIRKVVGDG-GILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQL 158

                       170       180       190
                ....*....|....*....|....*....|....
gi 13386044 188 SAVFRLLLTGTPIQNSLRELYSLLCVVEPDLFCR 221
Cdd:cd18000 159 RTPHRLILSGTPIQNNLKELWSLFDFVFPPYLLR 192
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
 40-255 1.67e-40

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: 148.62  E-value: 1.67e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCILGDEMGLGKTCQTIALLiYLVGRLNDEGPFLVLCPLSVLSNWKEEMeRFAPGLSCVT 119
Cdd:cd18061   1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWEREF-RTWTDLNVVV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 120 YTGDKEERARLQQD-----------LRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFS 188
Cdd:cd18061  79 YHGSLISRQMIQQYemyfrdsqgriIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13386044 189 AVFRLLLTGTPIQNSLRELYSLLCVVEPDLFCREQVedFVQRYQDIEKESKsASELHRLLQPFLLRR 255
Cdd:cd18061 159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSEST--FMQEFGDLKTEEQ-VQKLQAILKPMMLRR 222
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
 40-255 2.12e-39

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: 146.28  E-value: 2.12e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCfhcqnGCILGDEMGLGKTCQTIALL-----------------IYLVGRLNDEGPFLVLCPLSVLS 102
Cdd:cd18008   1 LLPYQKQGLAWMLPR-----GGILADEMGLGKTIQALALIlatrpqdpkipeeleenSSDPKKLYLSKTTLIVVPLSLLS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 103 NWKEEMERF--APGLSCVTYTGDKeeRARLQQDLRQesgFHVLLTTYEI----------------CLKDASFLKSFSWSV 164
Cdd:cd18008  76 QWKDEIEKHtkPGSLKVYVYHGSK--RIKSIEELSD---YDIVITTYGTlasefpknkkgggrdsKEKEASPLHRIRWYR 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 165 LAVDEAHRLKNQSSLLHRTLSEFSAVFRLLLTGTPIQNSLRELYSLLCVVEPDLFC--REQVEDFVQRYQdiEKESKSAS 242
Cdd:cd18008 151 VILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGdyPWFNSDISKPFS--KNDRKALE 228

                       250
                ....*....|...
gi 13386044 243 ELHRLLQPFLLRR 255
Cdd:cd18008 229 RLQALLKPILLRR 241
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
 40-245 9.19e-34

DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) which is involved in transcriptional regulation and chromatin remodeling, and ARIP4 (also called androgen receptor-interacting protein 4, RAD54 like 2 or RAD54L2) which modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350765 [Multi-domain]  Cd Length: 239  Bit Score: 130.10  E-value: 9.19e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVN--W--LVQCFHCQ---NGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFA 112
Cdd:cd18007   1 LKPHQVEGVRflWsnLVGTDVGSdegGGCILAHTMGLGKTLQVITFLHTYLAAAPRRSRPLVLCPASTLYNWEDEFKKWL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 113 -----PGLSCVTYTGDKEERARLQ--QDLRQESGfhVLLTTYEICLKDAS--------FLKSFSW------SVLAVDEAH 171
Cdd:cd18007  81 ppdlrPLLVLVSLSASKRADARLRkiNKWHKEGG--VLLIGYELFRNLASnattdprlKQEFIAAlldpgpDLLVLDEGH 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13386044 172 RLKNQSSLLHRTLSEFSAVFRLLLTGTPIQNSLRELYSLLCVVEPDLFcrEQVEDFVQRY-QDIEKESKSASELH 245
Cdd:cd18007 159 RLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYL--GTLKEFKKKFvKPIEAGQCVDSTEE 231
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
 40-255 8.46e-31

DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as RAD54L or RAD54, plays a role in homologous recombination related repair of DNA double-strand breaks. RAD54A is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350825 [Multi-domain]  Cd Length: 243  Bit Score: 121.42  E-value: 8.46e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCF-----HCQNGCILGDEMGLGKTCQTIALLIYLVGRLNDEGPFL----VLCPLSVLSNWKEEMER 110
Cdd:cd18067   1 LRPHQREGVKFLYRCVtgrriRGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaiVVSPSSLVKNWANELGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 111 F-APGLSCVTYTG--DKEERARLQQDLRQES---GFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTL 184
Cdd:cd18067  81 WlGGRLQPLAIDGgsKKEIDRKLVQWASQQGrrvSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 185 SEFSAVFRLLLTGTPIQNSLRELYSLLCVVEPDLFCREQVedFVQRY--------------QDIEKESKSASELHRLLQP 250
Cdd:cd18067 161 DSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAE--FKKNFelpilkgrdadaseKERQLGEEKLQELISIVNR 238


                ....*
gi 13386044 251 FLLRR 255
Cdd:cd18067 239 CIIRR 243
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
 40-255 4.08e-30

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: 118.46  E-value: 4.08e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQcfhcQNG-CILGDEMGLGKTCQTIALLIYlvgrLNDEGPFLVLCPLSVLSNWKEEMERFAPGLS-- 116
Cdd:cd18010   1 LLPFQREGVCFALR----RGGrVLIADEMGLGKTVQAIAIAAY----YREEWPLLIVCPSSLRLTWADEIERWLPSLPpd 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 117 ---CVTYTGDKEERarlqqdlrqeSGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSllHRTlsefSAVFRL 193
Cdd:cd18010  73 diqVIVKSKDGLRD----------GDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKA--KRT----KAALPL 136

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13386044 194 --------LLTGTPIQNSLRELYSLLCVVEPDLFCREqvEDFVQRYQDIE--------KESKSASELH-RLLQPFLLRR 255
Cdd:cd18010 137 lkrakrviLLSGTPALSRPIELFTQLDALDPKLFGRF--HDFGRRYCAAKqggfgwdySGSSNLEELHlLLLATIMIRR 213
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
 40-255 5.86e-29

DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as RDH54, binds to double-stranded DNA, displays ATPase activity in the presence of DNA, and may have a role in meiotic and mitotic recombination. RAD54B is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350824 [Multi-domain]  Cd Length: 235  Bit Score: 116.10  E-value: 5.86e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQC-----FHCQNGCILGDEMGLGKTCQTIALlIYLVGRLNDEGP------FLVLCPLSVLSNWKEEM 108
Cdd:cd18066   1 LRPHQREGIEFLYECvmgmrVNERFGAILADEMGLGKTLQCISL-IWTLLRQGPYGGkpvikrALIVTPGSLVKNWKKEF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 109 ERFAPGLSCVTYTGDKEERARlqqDLRQESGFHVLLTTYEICLKDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFS 188
Cdd:cd18066  80 QKWLGSERIKVFTVDQDHKVE---EFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLS 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13386044 189 AVFRLLLTGTPIQNSLRELYSLLCVVEPDLF-----CREQVEDFVQRYQD-----IEKE--SKSASELHRLLQPFLLRR 255
Cdd:cd18066 157 CERRIILTGTPIQNDLQEFFALIDFVNPGILgslstYRKVYEEPIVRSREptatpEEKKlgEARAAELTRLTGLFILRR 235
DEXDc smart00487
DEAD-like helicases superfamily;
35-227 3.62e-28

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 112.59  E-value: 3.62e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044     35 LTGIRLRSYQLEGVNWLVQCFHcqnGCILGDEMGLGKT-CQTIALLIYLvgRLNDEGPFLVLCPLSVL-SNWKEEMERFA 112
Cdd:smart00487   4 FGFEPLRPYQKEAIEALLSGLR---DVILAAPTGSGKTlAALLPALEAL--KRGKGGRVLVLVPTRELaEQWAEELKKLG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044    113 P--GLSCVTYTGDKEERARLQQDLRQEsgFHVLLTTYEICLKDAS--FLKSFSWSVLAVDEAHRLKNQS--SLLHRTLSE 186
Cdd:smart00487  79 PslGLKVVGLYGGDSKREQLRKLESGK--TDILVTTPGRLLDLLEndKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLKL 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 13386044    187 F-SAVFRLLLTGTP---IQNSLRELYSLLCVVEPDLFCREQVEDF 227
Cdd:smart00487 157 LpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEPIEQF 201
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
 60-211 9.07e-27

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


Pssm-ID: 350829 [Multi-domain]  Cd Length: 239  Bit Score: 109.87  E-value: 9.07e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  60 GCILGDEMGLGKTCQTIALLIYlvgrlndeGPFLVLCPLSVLSNWKEEM-ERFAPG-LSCVTYTGDkeERARlqqDLRQE 137
Cdd:cd18071  50 GGILADDMGLGKTLTTISLILA--------NFTLIVCPLSVLSNWETQFeEHVKPGqLKVYTYHGG--ERNR---DPKLL 116

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13386044 138 SGFHVLLTTYEICL-----KDASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLSEFSAVFRLLLTGTPIQNSLRELYSLL 211
Cdd:cd18071 117 SKYDIVLTTYNTLAsdfgaKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLL 195
Macro_Poa1p-like cd02901
macrodomain, Poa1p-like family; Macrodomains are found in a variety of proteins with diverse ...
 721-871 8.58e-24

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: 97.71  E-value: 8.58e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 721 SINYVSGDVTHPQageEDAVIVHCVDDSGRWGRGGLFTALEV--RSAEPRKIYELAGkmedlsLGDVLLFPiddkesRDK 798
Cdd:cd02901   1 KITYVKGDLFACP---ETKSLAHCCNCDGVMGKGIALQFKKKpgRVEELRAQCKKKL------LGGVAVLK------RDG 65

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13386044 799 GQDLLALVVAQHRDRTNvlsgIKMAALEEGLKKIF-LAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLATR 871
Cdd:cd02901  66 VKRYIYYLITKKSYGPK----PTYEALRSSLEELReHCRENGVTSVAMPRIGCGLDGLDWEEVEPILKEVFDDR 135
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
 341-453 1.87e-23

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 95.74  E-value: 1.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   341 GKLHLLDRLLAFlySGGHRVLLFSQMTHMLDIlQDYMDYRGYSYERVDGSVRGEERHLAIKNFGNQPIFVfLLSTRAGGV 420
Cdd:pfam00271   1 EKLEALLELLKK--ERGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDV-LVATDVAER 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 13386044   421 GMNLTAADTVIFVDSDFNPQNDLQAAARAHRIG 453
Cdd:pfam00271  77 GLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
 40-254 1.01e-22

DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously expressed protein that contains motifs characteristic of several DNA repair proteins, transcription factors, and helicases. SHPRH is a functional homolog of S. cerevisiae RAD5 and is involved in DNA repair. SHPRH is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 98.57  E-value: 1.01e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVqcfhCQNGcILGDEMGLGKTCQTIALLI------------YLVGRLNDE-------------GPFLV 94
Cdd:cd18070   1 LLPYQRRAVNWML----VPGG-ILADEMGLGKTVEVLALILlhprpdndldaaDDDSDEMVCcpdclvaetpvssKATLI 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  95 LCPLSVLSNWKEEMERFAP-GLSCVTYTGDKEERARLQQDLRQESGFHVLLTTYEICLKDASFLKSFS------------ 161
Cdd:cd18070  76 VCPSAILAQWLDEINRHVPsSLKVLTYQGVKKDGALASPAPEILAEYDIVVTTYDVLRTELHYAEANRsnrrrrrqkrye 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 162 -----------WSVLaVDEAHRLKNQSSLLHRTLSEFSAVFRLLLTGTPIQNSLRELYSLLCVVEPDLFCreQVEDFVQR 230
Cdd:cd18070 156 appsplvlvewWRVC-LDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFC--DSDWWARV 232

                       250       260
                ....*....|....*....|....
gi 13386044 231 YQDIEKESKSASELHRLLQPFLLR 254
Cdd:cd18070 233 LIRPQGRNKAREPLAALLKELLWR 256
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
 40-219 1.11e-21

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: 93.89  E-value: 1.11e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHcqNGCILGDEMGLGKTCQTIALLIYLVGRlNDEGPFLVLCPLSVLSNWKEEM-ERFA-PGLSC 117
Cdd:cd18011   1 PLPHQIDAVLRALRKPP--VRLLLADEVGLGKTIEAGLIIKELLLR-GDAKRVLILCPASLVEQWQDELqDKFGlPFLIL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 118 VTYTGDKEERARLQQDLRqesgFHVLLTTYEIcLKD----ASFLKSFSWSVLAVDEAHRLKN----QSSLLHRTLSEFSA 189
Cdd:cd18011  78 DRETAAQLRRLIGNPFEE----FPIVIVSLDL-LKRseerRGLLLSEEWDLVVVDEAHKLRNsgggKETKRYKLGRLLAK 152

                       170       180       190
                ....*....|....*....|....*....|..
gi 13386044 190 VFR--LLLTGTPIQNSLRELYSLLCVVEPDLF 219
Cdd:cd18011 153 RARhvLLLTATPHNGKEEDFRALLSLLDPGRF 184
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
 60-255 1.47e-20

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: 91.77  E-value: 1.47e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  60 GCILGDEMGLGKTCQTIALLIYLVGRLN-----------------DEGPF-----LVLCPLSVLSNWKEEMERFAPG--L 115
Cdd:cd18072  22 GGILADDMGLGKTLTMIALILAQKNTQNrkeeekekalteweskkDSTLVpsagtLVVCPASLVHQWKNEVESRVASnkL 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 116 SCVTYTG-DKEERARLQQDlrqesgFHVLLTTYEICLKD---------ASFLKSFSWSVLAVDEAHRLKNQSSLLHRTLS 185
Cdd:cd18072 102 RVCLYHGpNRERIGEVLRD------YDIVITTYSLVAKEiptykeesrSSPLFRIAWARIILDEAHNIKNPKVQASIAVC 175

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13386044 186 EFSAVFRLLLTGTPIQNSLRELYSLLcvvepdLFCR-EQVEDFVQRYQDIEKESKSASE-LHRLLQPFLLRR 255
Cdd:cd18072 176 KLRAHARWALTGTPIQNNLLDMYSLL------KFLRcSPFDDLKVWKKQVDNKSRKGGErLNILTKSLLLRR 241
HELICc smart00490
helicase superfamily c-terminal domain;
371-453 2.88e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 83.03  E-value: 2.88e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044    371 DILQDYMDYRGYSYERVDGSVRGEERHLAIKNFgNQPIFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAH 450
Cdd:smart00490   1 EELAELLKELGIKVARLHGGLSQEEREEILDKF-NNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79


                   ...
gi 13386044    451 RIG 453
Cdd:smart00490  80 RAG 82
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
 40-231 6.79e-19

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: 87.25  E-value: 6.79e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFhCQ----------NGCILGDEMGLGKTCQTIALL--IYLVGRLNDEGPFLVLCPLSVLSNWKEE 107
Cdd:cd18068   1 LKPHQVDGVQFMWDCC-CEslkktkkspgSGCILAHCMGLGKTLQVVTFLhtVLLCEKLENFSRVLVVCPLNTVLNWLNE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 108 MERFAPGL--------SCVTYTGDKEERARLQQDLRQESGfhVLLTTYEIC--------------LKDaSFLKSF---SW 162
Cdd:cd18068  80 FEKWQEGLkdeekievNELATYKRPQERSYKLQRWQEEGG--VMIIGYDMYrilaqernvksrekLKE-IFNKALvdpGP 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13386044 163 SVLAVDEAHRLKNQSSLLHRTLSEFSAVFRLLLTGTPIQNSLRELYSLLCVVEPDLFcrEQVEDFVQRY 231
Cdd:cd18068 157 DFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLL--GTIKEFRNRF 223
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
 60-232 6.55e-18

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: 83.71  E-value: 6.55e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  60 GCILGDEMGLGKTCQTIALlIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAPGLSC----------VTYTGDKEE--- 126
Cdd:cd18069  30 GCILAHSMGLGKTLQVISF-LDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKWLPPPEAlpnvrprpfkVFILNDEHKtta 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 127 -RARLQQDLRQESGfhVLLTTYEIC-LKDASflksfswSVLAVDEAHRLKNQSSLLHRTLSEFSAVFRLLLTGTPIQNSL 204
Cdd:cd18069 109 aRAKVIEDWVKDGG--VLLMGYEMFrLRPGP-------DVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNL 179

                       170       180
                ....*....|....*....|....*...
gi 13386044 205 RELYSLLCVVEPDLFCREQveDFVQRYQ 232
Cdd:cd18069 180 IEYWCMVDFVRPDFLGTRQ--EFSNMFE 205
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
36-467 3.00e-15

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 79.68  E-value: 3.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  36 TGIRLRSYQLEGVNWLVQCF--HCQNGCIlgdEM--GLGKTcqTIALLIylVGRLNDEGPFLVLCP-LSVLSNWKEEMER 110
Cdd:COG1061  77 TSFELRPYQQEALEALLAALerGGGRGLV---VAptGTGKT--VLALAL--AAELLRGKRVLVLVPrRELLEQWAEELRR 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 111 FapglscvtyTGDKEERARlqqdlRQESGFHVLLTTYEIcLKDASFLKSFS--WSVLAVDEAHRLknQSSLLHRTLSEFS 188
Cdd:COG1061 150 F---------LGDPLAGGG-----KKDSDAPITVATYQS-LARRAHLDELGdrFGLVIIDEAHHA--GAPSYRRILEAFP 212

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 189 AVFRLLLTGTPIQNSLRELYSLLC---VVEPDLfcREQVEDfvqryqdiekesksaselhRLLQPFLLRRVKaqvaTELP 265
Cdd:COG1061 213 AAYRLGLTATPFRSDGREILLFLFdgiVYEYSL--KEAIED-------------------GYLAPPEYYGIR----VDLT 267

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 266 KKTEvvvyhGMSALQKKYYKAILmkdldafENETAKKVKLQNILTQlrkcvdhpylfdgvepepfevgehlieasgklhl 345
Cdd:COG1061 268 DERA-----EYDALSERLREALA-------ADAERKDKILRELLRE---------------------------------- 301

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 346 ldrllaflYSGGHRVLLFSQMTHMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGNQPIfVFLLSTRAGGVGMNLT 425
Cdd:COG1061 302 --------HPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGEL-RILVTVDVLNEGVDVP 372

                       410       420       430       440
                ....*....|....*....|....*....|....*....|...
gi 13386044 426 AADTVIFVDSDFNPQNDLQAAARAHRIGQNKS-VKVIRLIGRD 467
Cdd:COG1061 373 RLDVAILLRPTGSPREFIQRLGRGLRPAPGKEdALVYDFVGND 415
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
 40-233 8.30e-12

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


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 65.45  E-value: 8.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQcfHCQNGCILgdEMGLGKTCQTIALLIYLVgRLNDEGPFLVLCPLSVLSN-WKEEMERFApGLSCV 118
Cdd:cd18013   1 PHPYQKVAINFIIE--HPYCGLFL--DMGLGKTVTTLTALSDLQ-LDDFTRRVLVIAPLRVARStWPDEVEKWN-HLRNL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 119 TY---TGDKEERARLQQdlrqeSGFHVLLTTYE----ICLKdasFLKSFSWSVLAVDEAHRLKNQSSllHRTLSEFSAVF 191
Cdd:cd18013  75 TVsvaVGTERQRSKAAN-----TPADLYVINREnlkwLVNK---SGDPWPFDMVVIDELSSFKSPRS--KRFKALRKVRP 144

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 13386044 192 R----LLLTGTPIQNSLRELYSLLCVVEPDlfcrEQVEDFVQRYQD 233
Cdd:cd18013 145 VikrlIGLTGTPSPNGLMDLWAQIALLDQG----ERLGRSITAYRE 186
ResIII pfam04851
Type III restriction enzyme, res subunit;
38-200 5.23e-11

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 61.92  E-value: 5.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044    38 IRLRSYQLEGVNWLVQCFHCQN--GCIlgdEM--GLGKTcQTIALLIYLVGRLNDEGPFLVLCP-LSVLSNWKEEMERFA 112
Cdd:pfam04851   2 LELRPYQIEAIENLLESIKNGQkrGLI---VMatGSGKT-LTAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   113 PG--LSCVTYTGDKEERARLQqdlrqesgFHVLLTTY-----EICLKDASFLKSFsWSVLAVDEAHRLknqSSLLHRTLS 185
Cdd:pfam04851  78 PNyvEIGEIISGDKKDESVDD--------NKIVVTTIqslykALELASLELLPDF-FDVIIIDEAHRS---GASSYRNIL 145

                         170
                  ....*....|....*.
gi 13386044   186 E-FSAVFRLLLTGTPI 200
Cdd:pfam04851 146 EyFKPAFLLGLTATPE 161
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 40-199 5.20e-10

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 58.47  E-value: 5.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  40 LRSYQLEGVNWLVQCFHCQNGCIlgdEM--GLGKTCQTIALLIYLVgrlndEGPFLVLCP-LSVLSNWKEEMERFAPGLS 116
Cdd:cd17926   1 LRPYQEEALEAWLAHKNNRRGIL---VLptGSGKTLTALALIAYLK-----ELRTLIVVPtDALLDQWKERFEDFLGDSS 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 117 CVTYTGDKEERARlqqdlrqesGFHVLLTTY---EICLKDASFLKSFsWSVLAVDEAHRLKnqSSLLHRTLSEFSAVFRL 193
Cdd:cd17926  73 IGLIGGGKKKDFD---------DANVVVATYqslSNLAEEEKDLFDQ-FGLLIVDEAHHLP--AKTFSEILKELNAKYRL 140


                ....*.
gi 13386044 194 LLTGTP 199
Cdd:cd17926 141 GLTATP 146
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
 59-200 1.18e-07

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: 51.64  E-value: 1.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  59 NGCILGDEMGLGKTcqTIALLIyLVGRLNDEGP-FLVLCPLSVLSN-WKEEM-ERFAPGLSCVTYTGDKEERARLQQDLR 135
Cdd:cd00046   2 ENVLITAPTGSGKT--LAALLA-ALLLLLKKGKkVLVLVPTKALALqTAERLrELFGPGIRVAVLVGGSSAEEREKNKLG 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13386044 136 QEsgfHVLLTTYEICLKDASFLKSFS---WSVLAVDEAHRLKNQSsllHRTLSEFSAVFRLLLTGTPI 200
Cdd:cd00046  79 DA---DIIIATPDMLLNLLLREDRLFlkdLKLIIVDEAHALLIDS---RGALILDLAVRKAGLKNAQV 140
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
 68-202 1.71e-06

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: 48.78  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044    68 GLGKTcqTIALL--IYLVGRLNDEGPFLVLCPLSVL-----SNWKEEMERFAPGLSCVtYTGDKeerarLQQDLRQESGF 140
Cdd:pfam00270  24 GSGKT--LAFLLpaLEALDKLDNGPQALVLAPTRELaeqiyEELKKLGKGLGLKVASL-LGGDS-----RKEQLEKLKGP 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13386044   141 HVLLTTYEIC---LKDASFLKSFSWsvLAVDEAHRL--KNQSSLLHRTLSEFSAVFR-LLLTGTPIQN 202
Cdd:pfam00270  96 DILVGTPGRLldlLQERKLLKNLKL--LVLDEAHRLldMGFGPDLEEILRRLPKKRQiLLLSATLPRN 161
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
 304-472 2.90e-06

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


Pssm-ID: 402894  Cd Length: 281  Bit Score: 50.02  E-value: 2.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   304 KLQNILTQLRKCVDHPYLF-DGVEPEPF---EVGEHLIEASGKLHLLDRLLAFL----YSGGHRVLLFSQMTHMLDILQD 375
Cdd:pfam11496  49 SMTLCLENLSLVATHPYLLvDHYMPKSLllkDEPEKLAYTSGKFLVLNDLVNLLierdRKEPINVAIVARSGKTLDLVEA 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044   376 YMDYRGYSYERVDG-SVRGEERHLAIKNFGNQPIFVFLL------STRAGGVgMNLTAADTVIFVDSDFNPQNDLQAAAR 448
Cdd:pfam11496 129 LLLGKGLSYKRYSGeMLYGENKKVSDSGNKKIHSTTCHLlsstgqLTNDDSL-LENYKFDLIIAFDSSVDTSSPSVEHLR 207

                         170       180
                  ....*....|....*....|....
gi 13386044   449 AHRIGQNKSVKVIRLIGRDTVEEI 472
Cdd:pfam11496 208 TQNRRKGNLAPIIRLVVINSIEHV 231
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
 408-464 1.01e-04

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 41.54  E-value: 1.01e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13386044 408 IFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQnKSVKVIRLI 464
Cdd:cd18785  22 SLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILFV 77
Macro_SF cd02749
macrodomain superfamily; Macrodomains are found in a variety of proteins with diverse cellular ...
 740-866 1.59e-04

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


Pssm-ID: 394871  Cd Length: 121  Bit Score: 42.00  E-value: 1.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 740 VIVHCVDDSGRWGrGGLFTALEVRSA-EPRKIYELAGKMEDLSLGDVLLFpiddkesrdKGQDLLALVVAqHrdrTNVLS 818
Cdd:cd02749   2 AIVNPANNDLYLG-GGVAKAISKKAGgDLQEECEERKKNGYLKVGEVAVT---------KGGNLPARYII-H---VVGPV 67

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 13386044 819 GIKMAALEEGLKKIF-----LAAKKKKASVHLPRIGHATKGFNWYGTERLIRK 866
Cdd:cd02749  68 ASSKKKTYEPLKKCVknclsLADEKGLKSVAFPAIGTGIAGFPPEEAARIMLE 120
YmdB COG2110
O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ...
 722-869 7.57e-04

O-acetyl-ADP-ribose deacetylase (regulator of RNase III), contains Macro domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441713  Cd Length: 168  Bit Score: 41.32  E-value: 7.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 722 INYVSGDVTHPQAgeeDAvIVHCVDDSGRWGrGGLftALEVRSA---EPRKIYELAGKMEDLSLGDVLLFPiddkesrdk 798
Cdd:COG2110   1 IEIVQGDITELDV---DA-IVNAANSSLLGG-GGV--AGAIHRAagpELLEECRRLCKQGGCPTGEAVITP--------- 64

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13386044 799 GQDLLALVVA-----QHRDRTNvlsgIKMAALEEGLKKIF-LAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLA 869
Cdd:COG2110  65 AGNLPAKYVIhtvgpVWRGGGP----SEEELLASCYRNSLeLAEELGIRSIAFPAIGTGVGGFPWEEAAPIAVETLR 137
AAA_22 pfam13401
AAA domain;
55-207 1.96e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.25  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044    55 FHCQNGCILGDEmGLGKTcqtiALLIYLVGRLNDEGPFLVLCPLSVLSNWKEEMERFAP--GLSCVTYTGDKEERARLQQ 132
Cdd:pfam13401   3 FGAGILVLTGES-GTGKT----TLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRALLRalGLPLSGRLSKEELLAALQQ 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13386044   133 DLRqesgfhvllttyeiclkdasflKSFSWSVLAVDEAHRLKNQS-SLLHRTLSEFSAVFRLLLTGTPiqnSLREL 207
Cdd:pfam13401  78 LLL----------------------ALAVAVVLIIDEAQHLSLEAlEELRDLLNLSSKLLQLILVGTP---ELREL 128
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
 38-212 2.12e-03

DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer 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: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 40.33  E-value: 2.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  38 IRLRSYQLEGVNWLVQcfhcQNG-CILGdeMGLGKTcqTIA-LLIYLVGRLNDEGP-------FLV-LCPL-----SVLS 102
Cdd:cd18034   1 FTPRSYQLELFEAALK----RNTiVVLP--TGSGKT--LIAvMLIKEMGELNRKEKnpkkravFLVpTVPLvaqqaEAIR 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044 103 NWKeemerfapGLSCVTYTG----DKEERARLQQDLRQesgFHVLLTTYEIcLKDA---SFLKSFSWSVLAVDEAHRLKN 175
Cdd:cd18034  73 SHT--------DLKVGEYSGemgvDKWTKERWKEELEK---YDVLVMTAQI-LLDAlrhGFLSLSDINLLIFDECHHATG 140

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 13386044 176 QSSlLHRTLSEF------SAVFRLL-LTGTPI---------QNSLRELYSLLC 212
Cdd:cd18034 141 DHP-YARIMKEFyhlegrTSRPRILgLTASPVngkgdpksvEKKIQQLEELLN 192
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
 70-177 9.77e-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: 38.01  E-value: 9.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13386044  70 GKTcqTIALLIYLVGRLNDEGPFLVLCPLSVLSNWKEE--MERFAP-GLSCVTYTGDKEErarlqqDLRQESGFHVLLTT 146
Cdd:cd17921  29 GKT--LIAELAILRALATSGGKAVYIAPTRALVNQKEAdlRERFGPlGKNVGLLTGDPSV------NKLLLAEADILVAT 100

                        90       100       110
                ....*....|....*....|....*....|....
gi 13386044 147 YEIC---LKDASFLKSFSWSVLAVDEAHRLKNQS 177
Cdd:cd17921 101 PEKLdllLRNGGERLIQDVRLVVVDEAHLIGDGE 134
 
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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