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Conserved domains on  [gi|767951847|ref|XP_011515862|]
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chromodomain-helicase-DNA-binding protein 7 isoform X7 [Homo sapiens]

Protein Classification

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
967-1566 1.10e-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: 513.19  E-value: 1.10e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  967 KLREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTE-LNVV 1044
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLgYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPvLRAV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1045 VYHGSQASRRTIQLYEMyfkdpqgrvIKGsyKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMM 1124
Cdd:PLN03142  249 KFHGNPEERAHQREELL---------VAG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLF 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1125 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF---GDLKTEEQVQKLQAILKPMMLRRLKEDVEKNLAPK 1201
Cdd:PLN03142  318 STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPK 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1202 EETIIEVELTNIQKKYYRAILEKNFTFLSKGGGQANvpnLLNTMMELRKCCNHPYLINGAEEKileefkethnaeSPDFQ 1281
Cdd:PLN03142  398 KETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAEPG------------PPYTT 462
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1282 LQAMIQAAGKLVLIDKLLPKLKAGGHRVLIFSQMVRCLDILEDYLIQRRYPYERIDGRVRGNLRQAAIDRFSKPDSDRFV 1361
Cdd:PLN03142  463 GEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFV 542
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1362 FLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKSVKIYRLITRNSYEREMFDKASLKLGLDKAVLQS 1441
Cdd:PLN03142  543 FLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ 622
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1442 MSGRENATngvqqLSKKEIEDLLRkgaYGALMDEEDEGSKFCEEDIDQILLR-RTHTITIESEGKGSTFAKASFVASGNR 1520
Cdd:PLN03142  623 GRLAEQKT-----VNKDELLQMVR---YGAEMVFSSKDSTITDEDIDRIIAKgEEATAELDAKMKKFTEDAIKFKMDDTA 694
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*.
gi 767951847 1521 TDISLDDpnfwQKWAKKAELDIDALNGRNnlVIDTPRvRKQTRLYS 1566
Cdd:PLN03142  695 ELYDFDD----EDDKDENKLDFKKIVSDN--WIDPPK-RERKRNYS 733
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
879-936 5.25e-35

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD5, CHD6, CHD7, CHD8, and CHD9. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. CHD6, CHD7, and CHD8 enzymes have been demonstrated to have different substrate specificities and remodeling activities. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


:

Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 127.79  E-value: 5.25e-35
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767951847  879 PDYVEVDRIMDFARSTD-DRGEPVTHYLVKWCSLPYEDSTWERRQDIDQAKIEEFEKLM 936
Cdd:cd18663     1 PDYVEVDRILDVSVSTDpNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
796-861 9.94e-25

repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, and similar proteins; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD5, CHD6, CHD7, CHD8, and CHD9. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. CHD6, CHD7, and CHD8 enzymes have been demonstrated to have different substrate specificities and remodeling activities. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


:

Pssm-ID: 349315 [Multi-domain]  Cd Length: 68  Bit Score: 98.56  E-value: 9.94e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767951847  796 DAEGPVVEKIMSSRSVKKQKESGEEVEI-EEFYVKYKNFSYLHCQWASIEDLEK-DKRIQQKIKRFKA 861
Cdd:cd18668     1 EEDTMIIEKILASRKKKKEKEEGAEEIEvEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFKQ 68
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
197-578 2.47e-11

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 69.03  E-value: 2.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   197 DFSMQQhgQPQQRMSQFSQGQEGL-------NQGNPFIATSGP--GHLSHVPQQSPSMAPSLRHsvQQFHHHPSTALHGE 267
Cdd:pfam03154  159 DSSAQQ--QILQTQPPVLQAQSGAasppsppPPGTTQAATAGPtpSAPSVPPQGSPATSQPPNQ--TQSTAAPHTLIQQT 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   268 SVAHSPRF-SPNPPQQGAVRPQTLNFSSrSQTVPSPTINNSGQYSRYPysnLNQGlvnntgmnqnlgltnntPMNQSVPR 346
Cdd:pfam03154  235 PTLHPQRLpSPHPPLQPMTQPPPPSQVS-PQPLPQPSLHGQMPPMPHS---LQTG-----------------PSHMQHPV 293
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   347 YPNAVGFPSNSGQGlmhQQPIHPSGSLNQMNTQTMH--PSQPQGTYASPPPMSPMKamsnPAGTPPPQVRPG-SAGIPme 423
Cdd:pfam03154  294 PPQPFPLTPQSSQS---QVPPGPSPAAPGQSQQRIHtpPSQSQLQSQQPPREQPLP----PAPLSMPHIKPPpTTPIP-- 364
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   424 vgsypnmphpqpshqppgAMGIGQRNMGPRNMQQSRPFigmssapreltgHMRPNGCPGVGLGDPQAIQERLIPGQQHPG 503
Cdd:pfam03154  365 ------------------QLPNPQSHKHPPHLSGPSPF------------QMNSNLPPPPALKPLSSLSTHHPPSAHPPP 414
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767951847   504 QQ--PSFQQLPTcPPLQPhPGLHHQSS--PPHPHHQPWAQLHPSPQNTPqkvpvhqhSPSEPFLEKPVPDMTQVSGPNA 578
Cdd:pfam03154  415 LQlmPQSQQLPP-PPAQP-PVLTQSQSlpPPAASHPPTSGLHQVPSQSP--------FPQHPFVPGGPPPITPPSGPPT 483
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
967-1566 1.10e-159

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 513.19  E-value: 1.10e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  967 KLREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTE-LNVV 1044
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLgYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPvLRAV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1045 VYHGSQASRRTIQLYEMyfkdpqgrvIKGsyKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMM 1124
Cdd:PLN03142  249 KFHGNPEERAHQREELL---------VAG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLF 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1125 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF---GDLKTEEQVQKLQAILKPMMLRRLKEDVEKNLAPK 1201
Cdd:PLN03142  318 STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPK 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1202 EETIIEVELTNIQKKYYRAILEKNFTFLSKGGGQANvpnLLNTMMELRKCCNHPYLINGAEEKileefkethnaeSPDFQ 1281
Cdd:PLN03142  398 KETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAEPG------------PPYTT 462
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1282 LQAMIQAAGKLVLIDKLLPKLKAGGHRVLIFSQMVRCLDILEDYLIQRRYPYERIDGRVRGNLRQAAIDRFSKPDSDRFV 1361
Cdd:PLN03142  463 GEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFV 542
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1362 FLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKSVKIYRLITRNSYEREMFDKASLKLGLDKAVLQS 1441
Cdd:PLN03142  543 FLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ 622
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1442 MSGRENATngvqqLSKKEIEDLLRkgaYGALMDEEDEGSKFCEEDIDQILLR-RTHTITIESEGKGSTFAKASFVASGNR 1520
Cdd:PLN03142  623 GRLAEQKT-----VNKDELLQMVR---YGAEMVFSSKDSTITDEDIDRIIAKgEEATAELDAKMKKFTEDAIKFKMDDTA 694
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*.
gi 767951847 1521 TDISLDDpnfwQKWAKKAELDIDALNGRNnlVIDTPRvRKQTRLYS 1566
Cdd:PLN03142  695 ELYDFDD----EDDKDENKLDFKKIVSDN--WIDPPK-RERKRNYS 733
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
968-1189 3.54e-154

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: 468.36  E-value: 3.54e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVYH 1047
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1048 GSQASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLE 1127
Cdd:cd18059    81 GSQASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767951847 1128 HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 1189
Cdd:cd18059   161 HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
917-1440 1.85e-130

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 422.33  E-value: 1.85e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  917 TWERRQDIDQAKIEEFEKLMSREPETERVERPPADDWKKSESSREYKNNNKLREYQLEGVNWLLFNWYNMRNCILADEMG 996
Cdd:COG0553   191 ELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMG 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  997 LGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVVYHGSQASRRTIQLYEmyfkdpqgrvikgsy 1075
Cdd:COG0553   271 LGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFApGLRVLVLDGTRERAKGANPFE--------------- 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1076 KFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSR 1155
Cdd:COG0553   336 DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGL 415
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1156 FPSETTFMQEFGDLKT---EEQVQKLQAILKPMMLRRLKEDVEKNLAPKEETIIEVELTNIQKKYYRAILEKNFTFLSKG 1232
Cdd:COG0553   416 LGSLKAFRERFARPIEkgdEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGA 495
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1233 GGQANVPNLLNTMMELRKCCNHPYLingaeekILEEFKEtHNAESpdfqlqamiqaaGKLVLIDKLLPKLKAGGHRVLIF 1312
Cdd:COG0553   496 EGIRRRGLILAALTRLRQICSHPAL-------LLEEGAE-LSGRS------------AKLEALLELLEELLAEGEKVLVF 555
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1313 SQMVRCLDILEDYLIQRRYPYERIDGRVRGNLRQAAIDRFSKpDSDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQN 1392
Cdd:COG0553   556 SQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAV 634
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 767951847 1393 DLQAQARCHRIGQSKSVKIYRLITRNSYEREMFDKASLKLGLDKAVLQ 1440
Cdd:COG0553   635 EEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
971-1258 3.34e-87

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: 286.50  E-value: 3.34e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   971 YQLEGVNWLLFNWYNM-RNCILADEMGLGKTIQSITFLYeiYLKGIH----GPFLVIAPLSTIPNWEREFRTWT---ELN 1042
Cdd:pfam00176    1 YQIEGVNWMLSLENNLgRGGILADEMGLGKTLQTISLLL--YLKHVDknwgGPTLIVVPLSLLHNWMNEFERWVsppALR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  1043 VVVYHGSQASRRTIQLYEMYFKDpqgrvikgsykFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLK 1122
Cdd:pfam00176   79 VVVLHGNKRPQERWKNDPNFLAD-----------FDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  1123 MMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG----DLKTEEQVQKLQAILKPMMLRRLKEDVEKNL 1198
Cdd:pfam00176  148 SLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpieRGGGKKGVSRLHKLLKPFLLRRTKKDVEKSL 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767951847  1199 APKEETIIEVELTNIQKKYY-RAILEKNFTFLSKG-GGQANVPNLLNTMMELRKCCNHPYLI 1258
Cdd:pfam00176  228 PPKVEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGeGGREIKASLLNILMRLRKICNHPGLI 289
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
879-936 5.25e-35

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD5, CHD6, CHD7, CHD8, and CHD9. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. CHD6, CHD7, and CHD8 enzymes have been demonstrated to have different substrate specificities and remodeling activities. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 127.79  E-value: 5.25e-35
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767951847  879 PDYVEVDRIMDFARSTD-DRGEPVTHYLVKWCSLPYEDSTWERRQDIDQAKIEEFEKLM 936
Cdd:cd18663     1 PDYVEVDRILDVSVSTDpNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
DEXDc smart00487
DEAD-like helicases superfamily;
961-1159 1.37e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 123.37  E-value: 1.37e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847    961 EYKNNNKLREYQLEGVNWLLFNWynmRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPL-STIPNWEREFRTWT 1039
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTrELAEQWAEELKKLG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   1040 E---LNVVVYHGSQASRRTIQlyemyfkdpqgRVIKGsyKFHAIITTFEMILTDCPE--LRNIPWRCVVIDEAHRLKN-- 1112
Cdd:smart00487   79 PslgLKVVGLYGGDSKREQLR-----------KLESG--KTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDgg 145
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 767951847   1113 RNCKLLEGLKMMDLE-HKVLLTGTP---LQNTVEELFSLLHFLEPSRFPSE 1159
Cdd:smart00487  146 FGDQLEKLLKLLPKNvQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLE 196
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
796-861 9.94e-25

repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, and similar proteins; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD5, CHD6, CHD7, CHD8, and CHD9. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. CHD6, CHD7, and CHD8 enzymes have been demonstrated to have different substrate specificities and remodeling activities. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349315 [Multi-domain]  Cd Length: 68  Bit Score: 98.56  E-value: 9.94e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767951847  796 DAEGPVVEKIMSSRSVKKQKESGEEVEI-EEFYVKYKNFSYLHCQWASIEDLEK-DKRIQQKIKRFKA 861
Cdd:cd18668     1 EEDTMIIEKILASRKKKKEKEEGAEEIEvEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFKQ 68
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
990-1438 3.26e-22

DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component of class 1 DISARM (Defence Island System Associated with Restriction Modification), which contains a DNA adenine N6 methyltransferase. This HMM describes a distinct form that is somewhat shorter than the majority of DrmD proteins.


Pssm-ID: 468472 [Multi-domain]  Cd Length: 868  Bit Score: 104.38  E-value: 3.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  990 ILADEMGLGKTIQS---ITFLYEIYLKGIhgpfLVIAPLSTIPNWEREFRTWTELNVVVyhgsqASRRTiqlYEMYFKDP 1066
Cdd:NF038318   51 ILADEVGLGKTIEAglvLKYVLESGAKKI----LIILPANLRKQWEIELEEKFDLESLI-----LDSLT---VEKDAKKW 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1067 QGRvIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKN--RNCKLLEGLkmMDLEH---KVLLTGTPLQNTV 1141
Cdd:NF038318  119 NKR-LTDNKKVRIVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRNvhKGGKRAKNL--YELTKgipKILLTATPLQNSL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1142 EELFSLLHFLEPSRFPSETTFM------QEFGDLKTEeqvqklqaiLKPMMLRRLKEDVEKNLAPKEETII--------- 1206
Cdd:NF038318  196 LDLYGLVSFIDPRIFGSEKVFSkryikdEDYSDLKRE---------LSPVLYRTLRKDVADYMQFKKRKCItvdfelspd 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1207 EVELTN-----IQKKYYRAI-----------------------------LEKNFTFLSKGGGQANVPNLLNtmmelrkcc 1252
Cdd:NF038318  267 EIELYVrvnnfLKRDILYSIptsnrtliilvirkllasssfalaetfevLKKRLEKLKEGTRSANAQEGFD--------- 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1253 nhpYLINGAEEKILEEFKETHNAESPDFQLQaMIQAAGKLV--LIDK------------LLPKLKAG---------GHRV 1309
Cdd:NF038318  338 ---LFWSFVEDEIDESGFEEKQDELYTRQKE-FIQHEIDEVdaIIDVakriktnakvtaLKTALEIAfeyqreegiAQKV 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1310 LIFSQMVRCLDILEDYLIQRRYPYERI---DG--------------RVR--GN--------LRQAAIDRFSkpdsDRFVF 1362
Cdd:NF038318  414 VVFTESKRTQKYIAEELRKSGYEGEDIllfNGdfddamtkeiyrawQVKnyGKanygrsveYKHAIVDYFK----NNAKI 489
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767951847 1363 LLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKSVKIYRLI-TRNSYEREMFDKASLKLGLDKAV 1438
Cdd:NF038318  490 LIVTDAGSEGLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYEILSEKFELFEGV 566
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
883-934 3.24e-12

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 62.59  E-value: 3.24e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767951847   883 EVDRIMDfaRSTDDRGepVTHYLVKWCSLPYEDSTWERRQDID--QAKIEEFEK 934
Cdd:pfam00385    2 EVERILD--HRKDKGG--KEEYLVKWKGYPYDENTWEPEENLSkcPELIEEFKD 51
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
197-578 2.47e-11

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 69.03  E-value: 2.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   197 DFSMQQhgQPQQRMSQFSQGQEGL-------NQGNPFIATSGP--GHLSHVPQQSPSMAPSLRHsvQQFHHHPSTALHGE 267
Cdd:pfam03154  159 DSSAQQ--QILQTQPPVLQAQSGAasppsppPPGTTQAATAGPtpSAPSVPPQGSPATSQPPNQ--TQSTAAPHTLIQQT 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   268 SVAHSPRF-SPNPPQQGAVRPQTLNFSSrSQTVPSPTINNSGQYSRYPysnLNQGlvnntgmnqnlgltnntPMNQSVPR 346
Cdd:pfam03154  235 PTLHPQRLpSPHPPLQPMTQPPPPSQVS-PQPLPQPSLHGQMPPMPHS---LQTG-----------------PSHMQHPV 293
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   347 YPNAVGFPSNSGQGlmhQQPIHPSGSLNQMNTQTMH--PSQPQGTYASPPPMSPMKamsnPAGTPPPQVRPG-SAGIPme 423
Cdd:pfam03154  294 PPQPFPLTPQSSQS---QVPPGPSPAAPGQSQQRIHtpPSQSQLQSQQPPREQPLP----PAPLSMPHIKPPpTTPIP-- 364
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   424 vgsypnmphpqpshqppgAMGIGQRNMGPRNMQQSRPFigmssapreltgHMRPNGCPGVGLGDPQAIQERLIPGQQHPG 503
Cdd:pfam03154  365 ------------------QLPNPQSHKHPPHLSGPSPF------------QMNSNLPPPPALKPLSSLSTHHPPSAHPPP 414
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767951847   504 QQ--PSFQQLPTcPPLQPhPGLHHQSS--PPHPHHQPWAQLHPSPQNTPqkvpvhqhSPSEPFLEKPVPDMTQVSGPNA 578
Cdd:pfam03154  415 LQlmPQSQQLPP-PPAQP-PVLTQSQSlpPPAASHPPTSGLHQVPSQSP--------FPQHPFVPGGPPPITPPSGPPT 483
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
801-862 4.00e-09

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 53.74  E-value: 4.00e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767951847   801 VVEKIMSSRSVKKQKESgeeveieeFYVKYKNFSYLHCQWASIEDLEKDKRIqqkIKRFKAK 862
Cdd:pfam00385    2 EVERILDHRKDKGGKEE--------YLVKWKGYPYDENTWEPEENLSKCPEL---IEEFKDR 52
CHROMO smart00298
Chromatin organization modifier domain;
801-863 2.93e-07

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 48.75  E-value: 2.93e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767951847    801 VVEKIMSSRSVKKqkesgeevEIEEFYVKYKNFSYLHCQWASIEDLEKDKRiqqKIKRFKAKQ 863
Cdd:smart00298    3 EVEKILDHRWKKK--------GELEYLVKWKGYSYSEDTWEPEENLLNCSK---KLDNYKKKE 54
CHROMO smart00298
Chromatin organization modifier domain;
883-934 7.51e-07

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 47.59  E-value: 7.51e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 767951847    883 EVDRIMDfaRSTDDRGEpvTHYLVKWCSLPYEDSTWERRQDI--DQAKIEEFEK 934
Cdd:smart00298    3 EVEKILD--HRWKKKGE--LEYLVKWKGYSYSEDTWEPEENLlnCSKKLDNYKK 52
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
446-577 8.35e-06

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 50.58  E-value: 8.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   446 GQRNMGPRNMQQSRPFIGMSSAP--RELTGHMRPNGCPGVGLGDPQaiqerlIPGQQHPGQQPSFQQLPT-----CPPLQ 518
Cdd:TIGR01628  376 MQLQPRMRQLPMGSPMGGAMGQPpyYGQGPQQQFNGQPLGWPRMSM------MPTPMGPGGPLRPNGLAPmnavrAPSRN 449
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767951847   519 PHPGLHHQSSPPHPhHQPWAQLHPSPQNTPQKVPVHQHSPSEPFLEK-----PVPDMTQVSGPN 577
Cdd:TIGR01628  450 AQNAAQKPPMQPVM-YPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQvlasaTPQMQKQVLGER 512
KLF1_2_4_N-like cd22056
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ...
497-564 7.91e-04

N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of Kruppel-like factor (KLF)1, KLF2, and KLF4; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domains of an unknown subfamily of KLFs, predominantly found in fish, related to the N-terminal domains of KLF1, KLF2, and KLF4.


Pssm-ID: 409231 [Multi-domain]  Cd Length: 339  Bit Score: 43.49  E-value: 7.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  497 PGQQHPGQQPSFQQLPTCPPLQPHPGLHHQSSPPHPHHQPWAQL------HPSPQNTPQ----------KVPVHQH---- 556
Cdd:cd22056   220 AFTHHQAAGPGALQGRGGRGGPDCHLLHSSHHHHHHHHLQYQYMnapyppHYAHQGAPQfhgqysvfrePMRVHHQghpg 299
                          90
                  ....*....|....*.
gi 767951847  557 --------SPSEPFLE 564
Cdd:cd22056   300 smltppssPPLLEFYA 315
ARG80 COG5068
Regulator of arginine metabolism and related MADS box-containing transcription factors ...
201-409 7.87e-03

Regulator of arginine metabolism and related MADS box-containing transcription factors [Transcription];


Pssm-ID: 227400 [Multi-domain]  Cd Length: 412  Bit Score: 40.77  E-value: 7.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  201 QQHGQPQQRMSQFSQGQEGLNQGNPFIATSGPG-HLSHVPQQSPSMAPSLRHSVQQFH--HHPSTALHGESVahSPRFSP 277
Cdd:COG5068   208 QQYQQHSSRKDHPTVPHSNTNNGRPPAKFMIPElHSSHSTLDLPSDFISDSGFPNQSStsIFPLDSAIIQIT--PPHLPN 285
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  278 NPPQQGAVRPQtLNFSSRSQTVPSPTINNSGQYSRYPYSNLNQGLvnntgmnqnlgltnntpmnqsvPRYPNAVGFPSNS 357
Cdd:COG5068   286 NPPQENRHELY-SNDSSMVSETPPPKNLPNGSPNQSPLNNLSRGN----------------------PASPNSIIRENNQ 342
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767951847  358 GQGLMHQ----QPIHPSG-SLNQMNTQTMHPSqpQGTYASPPPMSPMK-AMSNPAGTP 409
Cdd:COG5068   343 VEDESFNgrqgSAIWNALiSTTQPNSGLHTEA--STAPSSTIPADPLKnAAQTNSGTR 398
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
967-1566 1.10e-159

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 513.19  E-value: 1.10e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  967 KLREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTE-LNVV 1044
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLgYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPvLRAV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1045 VYHGSQASRRTIQLYEMyfkdpqgrvIKGsyKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMM 1124
Cdd:PLN03142  249 KFHGNPEERAHQREELL---------VAG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLF 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1125 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF---GDLKTEEQVQKLQAILKPMMLRRLKEDVEKNLAPK 1201
Cdd:PLN03142  318 STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPK 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1202 EETIIEVELTNIQKKYYRAILEKNFTFLSKGGGQANvpnLLNTMMELRKCCNHPYLINGAEEKileefkethnaeSPDFQ 1281
Cdd:PLN03142  398 KETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAEPG------------PPYTT 462
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1282 LQAMIQAAGKLVLIDKLLPKLKAGGHRVLIFSQMVRCLDILEDYLIQRRYPYERIDGRVRGNLRQAAIDRFSKPDSDRFV 1361
Cdd:PLN03142  463 GEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFV 542
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1362 FLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKSVKIYRLITRNSYEREMFDKASLKLGLDKAVLQS 1441
Cdd:PLN03142  543 FLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ 622
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1442 MSGRENATngvqqLSKKEIEDLLRkgaYGALMDEEDEGSKFCEEDIDQILLR-RTHTITIESEGKGSTFAKASFVASGNR 1520
Cdd:PLN03142  623 GRLAEQKT-----VNKDELLQMVR---YGAEMVFSSKDSTITDEDIDRIIAKgEEATAELDAKMKKFTEDAIKFKMDDTA 694
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*.
gi 767951847 1521 TDISLDDpnfwQKWAKKAELDIDALNGRNnlVIDTPRvRKQTRLYS 1566
Cdd:PLN03142  695 ELYDFDD----EDDKDENKLDFKKIVSDN--WIDPPK-RERKRNYS 733
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
968-1189 3.54e-154

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: 468.36  E-value: 3.54e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVYH 1047
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1048 GSQASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLE 1127
Cdd:cd18059    81 GSQASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767951847 1128 HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 1189
Cdd:cd18059   161 HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
968-1189 2.71e-151

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: 460.56  E-value: 2.71e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFLYEIYLK-GIHGPFLVIAPLSTIPNWEREFRTWTELNVVVY 1046
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVeGIRGPFLVIAPLSTIPNWQREFETWTDMNVVVY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1047 HGSQASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDL 1126
Cdd:cd17995    81 HGSGESRQIIQQYEMYFKDAQGRKKKGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767951847 1127 EHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 1189
Cdd:cd17995   161 EHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEQVEKLQALLKPYMLRR 223
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
968-1189 6.36e-138

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: 424.84  E-value: 6.36e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVYH 1047
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1048 GSQASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLE 1127
Cdd:cd18058    81 GSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767951847 1128 HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 1189
Cdd:cd18058   161 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
968-1189 1.70e-133

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: 412.86  E-value: 1.70e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVYH 1047
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDLNVVVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1048 GSQASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLE 1127
Cdd:cd18061    81 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767951847 1128 HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 1189
Cdd:cd18061   161 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
968-1189 3.71e-133

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: 411.75  E-value: 3.71e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVYH 1047
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1048 GSQASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLE 1127
Cdd:cd18060    81 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767951847 1128 HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 1189
Cdd:cd18060   161 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 222
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
917-1440 1.85e-130

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 422.33  E-value: 1.85e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  917 TWERRQDIDQAKIEEFEKLMSREPETERVERPPADDWKKSESSREYKNNNKLREYQLEGVNWLLFNWYNMRNCILADEMG 996
Cdd:COG0553   191 ELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMG 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  997 LGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVVYHGSQASRRTIQLYEmyfkdpqgrvikgsy 1075
Cdd:COG0553   271 LGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFApGLRVLVLDGTRERAKGANPFE--------------- 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1076 KFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSR 1155
Cdd:COG0553   336 DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGL 415
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1156 FPSETTFMQEFGDLKT---EEQVQKLQAILKPMMLRRLKEDVEKNLAPKEETIIEVELTNIQKKYYRAILEKNFTFLSKG 1232
Cdd:COG0553   416 LGSLKAFRERFARPIEkgdEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGA 495
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1233 GGQANVPNLLNTMMELRKCCNHPYLingaeekILEEFKEtHNAESpdfqlqamiqaaGKLVLIDKLLPKLKAGGHRVLIF 1312
Cdd:COG0553   496 EGIRRRGLILAALTRLRQICSHPAL-------LLEEGAE-LSGRS------------AKLEALLELLEELLAEGEKVLVF 555
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1313 SQMVRCLDILEDYLIQRRYPYERIDGRVRGNLRQAAIDRFSKpDSDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQN 1392
Cdd:COG0553   556 SQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAV 634
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 767951847 1393 DLQAQARCHRIGQSKSVKIYRLITRNSYEREMFDKASLKLGLDKAVLQ 1440
Cdd:COG0553   635 EEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
971-1258 3.34e-87

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: 286.50  E-value: 3.34e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   971 YQLEGVNWLLFNWYNM-RNCILADEMGLGKTIQSITFLYeiYLKGIH----GPFLVIAPLSTIPNWEREFRTWT---ELN 1042
Cdd:pfam00176    1 YQIEGVNWMLSLENNLgRGGILADEMGLGKTLQTISLLL--YLKHVDknwgGPTLIVVPLSLLHNWMNEFERWVsppALR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  1043 VVVYHGSQASRRTIQLYEMYFKDpqgrvikgsykFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLK 1122
Cdd:pfam00176   79 VVVLHGNKRPQERWKNDPNFLAD-----------FDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  1123 MMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG----DLKTEEQVQKLQAILKPMMLRRLKEDVEKNL 1198
Cdd:pfam00176  148 SLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpieRGGGKKGVSRLHKLLKPFLLRRTKKDVEKSL 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767951847  1199 APKEETIIEVELTNIQKKYY-RAILEKNFTFLSKG-GGQANVPNLLNTMMELRKCCNHPYLI 1258
Cdd:pfam00176  228 PPKVEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGeGGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
967-1189 2.71e-84

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: 275.00  E-value: 2.71e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  967 KLREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFLYeiYL---KGIHGPFLVIAPLSTIPNWEREFRTWT-ELN 1042
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLS--YLfhsQQQYGPFLVVVPLSTMPAWQREFAKWApDMN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1043 VVVYHGSQASRRTIQLYEMYFkdPQGRVIKgsykFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLK 1122
Cdd:cd17993    79 VIVYLGDIKSRDTIREYEFYF--SQTKKLK----FNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALK 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767951847 1123 MMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFmQEFGDLKTEEQVQKLQAILKPMMLRR 1189
Cdd:cd17993   153 EFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEF-EEEHDEEQEKGIADLHKELEPFILRR 218
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
968-1153 3.18e-79

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: 259.04  E-value: 3.18e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVV 1045
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLaYLLKEGKERGPVLVVCPLSVLENWEREFEKWTpDLRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1046 YHGSQASRRTIQLYEmyfkdpqgrvikGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 1125
Cdd:cd17919    81 YHGSQRERAQIRAKE------------KLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR 148
                         170       180
                  ....*....|....*....|....*...
gi 767951847 1126 LEHKVLLTGTPLQNTVEELFSLLHFLEP 1153
Cdd:cd17919   149 AKRRLLLTGTPLQNNLEELWALLDFLDP 176
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
965-1191 6.21e-74

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: 246.14  E-value: 6.21e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  965 NNKLREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNV 1043
Cdd:cd18009     1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTpSVPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1044 VVYHGSQASRRTIQlYEMYFKDPQGRvikgsyKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKM 1123
Cdd:cd18009    81 LLYHGTKEERERLR-KKIMKREGTLQ------DFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1124 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG-----------DLKTEEQ----VQKLQAILKPMMLR 1188
Cdd:cd18009   154 FNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDfsslsdnaadiSNLSEEReqniVHMLHAILKPFLLR 233

                  ...
gi 767951847 1189 RLK 1191
Cdd:cd18009   234 RLK 236
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
968-1189 9.88e-73

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: 241.19  E-value: 9.88e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFLYEIYLKG-IHGPFLVIAPLSTIPNWEREFRTWT-ELNVVV 1045
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWApDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1046 YHGSqasrrtiqlyemyfkdpqgrvikgsykfHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 1125
Cdd:cd17994    81 YVGD----------------------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYK 132
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767951847 1126 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 1189
Cdd:cd17994   133 IGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQIKKLHDLLGPHMLRR 196
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
968-1189 8.07e-69

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: 231.44  E-value: 8.07e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFLYEIYLKG-IHGPFLVIAPLSTIPNWEREFRTWT-ELNVVV 1045
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhTKGPFLVSAPLSTIINWEREFQMWApDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1046 YHGSQASRRTIQLYEMYFKDpqgRVIKGS-----------YKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRN 1114
Cdd:cd18055    81 YTGDKDSRAIIRENEFSFDD---NAVKGGkkafkmkreaqVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQ 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767951847 1115 CKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 1189
Cdd:cd18055   158 SKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
965-1191 1.12e-68

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: 230.67  E-value: 1.12e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  965 NNKLREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELN 1042
Cdd:cd17997     1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLgYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCpSLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1043 VVVYHGSQASRRTIQlyemyfkdpQGRVIKGsyKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLK 1122
Cdd:cd17997    81 VVVLIGDKEERADII---------RDVLLPG--KFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVR 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767951847 1123 MMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF----GDLKTEEQVQKLQAILKPMMLRRLK 1191
Cdd:cd17997   150 LFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFnvnnCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
965-1191 6.77e-67

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: 6.77e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  965 NNKLREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSI---TFLYEIylKGIHGPFLVIAPLSTIPNWEREFRTWT-E 1040
Cdd:cd17996     1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTIsliTYLMEK--KKNNGPYLVIVPLSTLSNWVSEFEKWApS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1041 LNVVVYHGSQASRRTIQlyemyfkdPQGRvikgSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEG 1120
Cdd:cd17996    79 VSKIVYKGTPDVRKKLQ--------SQIR----AGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQT 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1121 LK-MMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG------------DLKTEEQV---QKLQAILKP 1184
Cdd:cd17996   147 LNtYYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNtpfantgeqvkiELNEEETLliiRRLHKVLRP 226

                  ....*..
gi 767951847 1185 MMLRRLK 1191
Cdd:cd17996   227 FLLRRLK 233
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
968-1189 7.73e-67

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: 225.71  E-value: 7.73e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFLYEIYLKG-IHGPFLVIAPLSTIPNWEREFRTWT-ELNVVV 1045
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWApDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1046 YHGSQASRRTIQLYEMYFKDPQGRVIKGSY--------KFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKL 1117
Cdd:cd18057    81 YTGDKESRSVIRENEFSFEDNAIRSGKKVFrmkkeaqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767951847 1118 LEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 1189
Cdd:cd18057   161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
968-1189 1.66e-66

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: 224.56  E-value: 1.66e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFLYEIYLKG-IHGPFLVIAPLSTIPNWEREFRTWT-ELNVVV 1045
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWApDMYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1046 YHGSQASRRTIQLYEMYFKDPQGRVIK--------GSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKL 1117
Cdd:cd18056    81 YVGDKDSRAIIRENEFSFEDNAIRGGKkasrmkkeASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767951847 1118 LEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 1189
Cdd:cd18056   161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQIKKLHDMLGPHMLRR 232
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
967-1189 1.20e-65

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. CHD2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350812 [Multi-domain]  Cd Length: 237  Bit Score: 222.57  E-value: 1.20e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  967 KLREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVV 1044
Cdd:cd18054    20 ELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLsYLFHQHQLYGPFLLVVPLSTLTSWQREFEIWApEINVV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1045 VYHGSQASRRTIQLYEmyFKDPQGRVIKgsykFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMM 1124
Cdd:cd18054   100 VYIGDLMSRNTIREYE--WIHSQTKRLK----FNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDF 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767951847 1125 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKtEEQVQKLQAILKPMMLRR 1189
Cdd:cd18054   174 KSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGR-ENGYQSLHKVLEPFLLRR 237
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
968-1189 3.75e-60

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: 205.75  E-value: 3.75e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFLyeIYLKG---IHGPFLVIAPLSTIPNWEREFRTWT-ELNV 1043
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLL--WYLAGrlkLLGPFLVLCPLSVLDNWKEELNRFApDLSV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1044 VVYHGSQASRRTIQlyemyfkdpqgRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKM 1123
Cdd:cd18006    79 ITYMGDKEKRLDLQ-----------QDIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSE 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767951847 1124 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETT--FMQEFGDLKTE-EQVQKLQAILKPMMLRR 1189
Cdd:cd18006   148 FSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKLddFIKAYSETDDEsETVEELHLLLQPFLLRR 216
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
965-1191 2.00e-59

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: 203.95  E-value: 2.00e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  965 NNKLREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNV 1043
Cdd:cd18012     2 KATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFApELKV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1044 VVYHGSQASRRTIQLYEMYFkdpqgrvikgsykfhAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKM 1123
Cdd:cd18012    82 LVIHGTKRKREKLRALEDYD---------------LVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKA 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767951847 1124 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG----DLKTEEQVQKLQAILKPMMLRRLK 1191
Cdd:cd18012   147 LKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAkpieKDGDEEALEELKKLISPFILRRLK 218
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
968-1189 1.00e-57

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: 199.12  E-value: 1.00e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTE-LNVVV 1045
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLaHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPgFKILT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1046 YHGSQASRRtiqlyemyfkdpqgRVIKGSYK---FHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLK 1122
Cdd:cd18003    81 YYGSAKERK--------------LKRQGWMKpnsFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLL 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767951847 1123 MMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTF----------MQEFGDLKTEEQVQKLQAILKPMMLRR 1189
Cdd:cd18003   147 NFNTQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFkewfsnpltaMSEGSQEENEELVRRLHKVLRPFLLRR 223
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1290-1415 1.58e-57

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: 195.00  E-value: 1.58e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1290 GKLVLIDKLLPKLKAGGHRVLIFSQMVRCLDILEDYLIQRRYPYERIDGRVRGNLRQAAIDRFSKPDSDrFVFLLCTRAG 1369
Cdd:cd18793    11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI-RVFLLSTKAG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767951847 1370 GLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKSVKIYRLI 1415
Cdd:cd18793    90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
968-1156 8.76e-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: 183.36  E-value: 8.76e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVVY 1046
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCpSLKVEPY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1047 HGSQASRRTIqlyemyfkdpQGRVIKGSYKFHAIITTFEMILTDCPE---LRNIPWRCVVIDEAHRLKNRNCKLLEGLKM 1123
Cdd:cd17998    81 YGSQEERKHL----------RYDILKGLEDFDVIVTTYNLATSNPDDrsfFKRLKLNYVVYDEGHMLKNMTSERYRHLMT 150
                         170       180       190
                  ....*....|....*....|....*....|...
gi 767951847 1124 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRF 1156
Cdd:cd17998   151 INANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
968-1189 1.01e-52

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: 185.66  E-value: 1.01e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLlFNWY-NMRNCILADEMGLGKTIQSITFLYEIYLK---------------------GIHGPFLVIAPL 1025
Cdd:cd18005     1 LRDYQREGVEFM-YDLYkNGRGGILGDDMGLGKTVQVIAFLAAVLGKtgtrrdrennrprfkkkppasSAKKPVLIVAPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1026 STIPNWEREFRTWTELNVVVYHGSqasRRTiqlyemyfKDPQGRVIKGSYKFhaIITTFEMILTDCPELRNIPWRCVVID 1105
Cdd:cd18005    80 SVLYNWKDELDTWGHFEVGVYHGS---RKD--------DELEGRLKAGRLEV--VVTTYDTLRRCIDSLNSINWSAVIAD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1106 EAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGD---------------LK 1170
Cdd:cd18005   147 EAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEpikrgqrhtatarelRL 226
                         250
                  ....*....|....*....
gi 767951847 1171 TEEQVQKLQAILKPMMLRR 1189
Cdd:cd18005   227 GRKRKQELAVKLSKFFLRR 245
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
967-1189 1.29e-52

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: 185.25  E-value: 1.29e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  967 KLREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVV 1044
Cdd:cd18053    20 ELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLnYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWApQMNAV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1045 VYHGSQASRRTIQLYEmyFKDPQGRVIKgsykFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMM 1124
Cdd:cd18053   100 VYLGDINSRNMIRTHE--WMHPQTKRLK----FNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDF 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767951847 1125 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKtEEQVQKLQAILKPMMLRR 1189
Cdd:cd18053   174 KSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGR-EYGYASLHKELEPFLLRR 237
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
968-1189 5.35e-51

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: 180.01  E-value: 5.35e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLfNWYNMR-NCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREF-RTWTELNVV 1044
Cdd:cd18002     1 LKEYQLKGLNWLA-NLYEQGiNGILADEMGLGKTVQSIAVLaHLAEEHNIWGPFLVIAPASTLHNWQQEIsRFVPQFKVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1045 VYHGSQASRRTIQLY----EMYFKDPqgrvikgsyKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEG 1120
Cdd:cd18002    80 PYWGNPKDRKVLRKFwdrkNLYTRDA---------PFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKT 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767951847 1121 LKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG-DLKT---------EEQVQKLQAILKPMMLRR 1189
Cdd:cd18002   151 LLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSkDIEShaenktglnEHQLKRLHMILKPFMLRR 229
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
965-1191 1.35e-49

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: 176.77  E-value: 1.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  965 NNKLREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNV 1043
Cdd:cd18062    21 NGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALItYLMEHKRINGPFLIIVPLSTLSNWVYEFDKWAPSVV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1044 -VVYHGSQASRRTIQlyemyfkdPQGRvikgSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLK 1122
Cdd:cd18062   101 kVSYKGSPAARRAFV--------PQLR----SGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLN 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1123 MMDLE-HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG----------DLKTEEQ---VQKLQAILKPMMLR 1188
Cdd:cd18062   169 THYVApRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLR 248

                  ...
gi 767951847 1189 RLK 1191
Cdd:cd18062   249 RLK 251
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
957-1202 4.00e-48

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: 172.54  E-value: 4.00e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  957 ESSREYKNNNKLREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREF 1035
Cdd:cd18064     5 EDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLgYMKHYRNIPGPHMVLVPKSTLHNWMAEF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1036 RTWT-ELNVVVYHGSQASRRTiqlyemYFKDPqgrVIKGSYKfhAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRN 1114
Cdd:cd18064    85 KRWVpTLRAVCLIGDKDQRAA------FVRDV---LLPGEWD--VCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1115 CKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGD---LKTEEQVQKLQAILKPMMLRRLK 1191
Cdd:cd18064   154 SKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTnncLGDQKLVERLHMVLRPFLLRRIK 233
                         250
                  ....*....|.
gi 767951847 1192 EDVEKNLAPKE 1202
Cdd:cd18064   234 ADVEKSLPPKK 244
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
965-1191 5.08e-48

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: 172.55  E-value: 5.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  965 NNKLREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNV 1043
Cdd:cd18063    21 NGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALItYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1044 -VVYHGSQASRRTIQlyemyfkdPQGRvikgSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLK 1122
Cdd:cd18063   101 kISYKGTPAMRRSLV--------PQLR----SGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLN 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1123 MMDLE-HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG----------DLKTEEQ---VQKLQAILKPMMLR 1188
Cdd:cd18063   169 THYVApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgervDLNEEETiliIRRLHKVLRPFLLR 248

                  ...
gi 767951847 1189 RLK 1191
Cdd:cd18063   249 RLK 251
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
968-1189 9.59e-46

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: 165.54  E-value: 9.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLFnwynmRNCILADEMGLGKTIQSI-------------TFLYEIYLKGIHGPF-----LVIAPLSTIP 1029
Cdd:cd18008     1 LLPYQKQGLAWMLP-----RGGILADEMGLGKTIQALalilatrpqdpkiPEELEENSSDPKKLYlskttLIVVPLSLLS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1030 NWEREFRTWTE---LNVVVYHGSQASRRTIQLYEmyfkdpqgrvikgsykFHAIITTFEMILTDCPE------------- 1093
Cdd:cd18008    76 QWKDEIEKHTKpgsLKVYVYHGSKRIKSIEELSD----------------YDIVITTYGTLASEFPKnkkgggrdskeke 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1094 ---LRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLK 1170
Cdd:cd18008   140 aspLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPF 219
                         250       260
                  ....*....|....*....|..
gi 767951847 1171 TE---EQVQKLQAILKPMMLRR 1189
Cdd:cd18008   220 SKndrKALERLQALLKPILLRR 241
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
957-1191 3.56e-44

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: 160.57  E-value: 3.56e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  957 ESSREYKNNNKLREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREF 1035
Cdd:cd18065     5 EESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLgYLKHYRNIPGPHMVLVPKSTLHNWMNEF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1036 RTWT-ELNVVVYHGSQASRRTIQLYEMyfkdpqgrvIKGSYKfhAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRN 1114
Cdd:cd18065    85 KRWVpSLRAVCLIGDKDARAAFIRDVM---------MPGEWD--VCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1115 CKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGD---LKTEEQVQKLQAILKPMMLRRLK 1191
Cdd:cd18065   154 SKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRRIK 233
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
968-1189 3.86e-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: 151.76  E-value: 3.86e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLFNWYNMRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTE-LNVVVY 1046
Cdd:cd18001     1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPgLRVKVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1047 HGSQASRRTIQLYemyfkdpqgRVIKGsykFHAIITTFEMILTDCPEL-----RNIPWRCVVIDEAHRLKNRNCKLLEGL 1121
Cdd:cd18001    81 HGTSKKERERNLE---------RIQRG---GGVLLTTYGMVLSNTEQLsaddhDEFKWDYVILDEGHKIKNSKTKSAKSL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1122 KMMDLEHKVLLTGTPLQNTVEELFSLLHFLEP-SRFPSETTFMQEF------GDLKTEEQVQK---------LQAILKPM 1185
Cdd:cd18001   149 REIPAKNRIILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFenpitrGRDKDATQGEKalgsevaenLRQIIKPY 228

                  ....
gi 767951847 1186 MLRR 1189
Cdd:cd18001   229 FLRR 232
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
968-1189 5.25e-40

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: 148.97  E-value: 5.25e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLL-----FNWYNMRNCILADEMGLGKTIQSITFLYeIYLKgiHGPF--------LVIAPLSTIPNWERE 1034
Cdd:cd18004     1 LRPHQREGVQFLYdcltgRRGYGGGGAILADEMGLGKTLQAIALVW-TLLK--QGPYgkptakkaLIVCPSSLVGNWKAE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1035 FRTWTELNVVVYHGSQASRRTIQLyEMYFKDPQGRvikgsykFHAIITTFEMILTDCPELrNIPWRC--VVIDEAHRLKN 1112
Cdd:cd18004    78 FDKWLGLRRIKVVTADGNAKDVKA-SLDFFSSAST-------YPVLIISYETLRRHAEKL-SKKISIdlLICDEGHRLKN 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1113 RNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGD--LK------TEEQV-------QK 1177
Cdd:cd18004   149 SESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEpiLRsrdpdaSEEDKelgaersQE 228
                         250
                  ....*....|..
gi 767951847 1178 LQAILKPMMLRR 1189
Cdd:cd18004   229 LSELTSRFILRR 240
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
968-1189 7.66e-39

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: 145.19  E-value: 7.66e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLF-NWYNMRNcILADEMGLGKTIQSITFLY------EIYLKGIHGPFLVIAPLSTIPNWEREFRTWTE 1040
Cdd:cd17999     1 LRPYQQEGINWLAFlNKYNLHG-ILCDDMGLGKTLQTLCILAsdhhkrANSFNSENLPSLVVCPPTLVGHWVAEIKKYFP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1041 ---LNVVVYHGSQASRRTIQlyemyfkdpqgrviKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKL 1117
Cdd:cd17999    80 nafLKPLAYVGPPQERRRLR--------------EQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1118 LEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG-------DLK-----TEEQVQKLQAILK-- 1183
Cdd:cd17999   146 SKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLkpilasrDSKasakeQEAGALALEALHKqv 225

                  ....*..
gi 767951847 1184 -PMMLRR 1189
Cdd:cd17999   226 lPFLLRR 232
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
968-1153 1.61e-37

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: 140.15  E-value: 1.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLfnWYNMRNC--ILADEMGLGKTIQSITFLYEI-YLKGIHGPFLVIAPLSTIPNWEREFRTW-TELNV 1043
Cdd:cd18000     1 LFKYQQTGVQWLW--ELHCQRVggILGDEMGLGKTIQIIAFLAALhHSKLGLGPSLIVCPATVLKQWVKEFHRWwPPFRV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1044 VVYHGSQASRRTIQLYEMYFKDPQgRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKM 1123
Cdd:cd18000    79 VVLHSSGSGTGSEEKLGSIERKSQ-LIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQ 157
                         170       180       190
                  ....*....|....*....|....*....|
gi 767951847 1124 MDLEHKVLLTGTPLQNTVEELFSLLHFLEP 1153
Cdd:cd18000   158 LRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
879-936 5.25e-35

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD5, CHD6, CHD7, CHD8, and CHD9. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. CHD6, CHD7, and CHD8 enzymes have been demonstrated to have different substrate specificities and remodeling activities. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 127.79  E-value: 5.25e-35
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767951847  879 PDYVEVDRIMDFARSTD-DRGEPVTHYLVKWCSLPYEDSTWERRQDIDQAKIEEFEKLM 936
Cdd:cd18663     1 PDYVEVDRILDVSVSTDpNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
968-1166 2.23e-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: 132.42  E-value: 2.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNwllFNWYNM----------RNCILADEMGLGKTIQSITFLYeIYLKgiHGP----FLVIAPLSTIPNWER 1033
Cdd:cd18007     1 LKPHQVEGVR---FLWSNLvgtdvgsdegGGCILAHTMGLGKTLQVITFLH-TYLA--AAPrrsrPLVLCPASTLYNWED 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1034 EFRTWT---ELNVVVYHGSQASRRTIQL-----------------YEMYFKDPQGRvIKGSYKFHAIITTfemILTDCPE 1093
Cdd:cd18007    75 EFKKWLppdLRPLLVLVSLSASKRADARlrkinkwhkeggvlligYELFRNLASNA-TTDPRLKQEFIAA---LLDPGPD 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767951847 1094 LrnipwrcVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF 1166
Cdd:cd18007   151 L-------LVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
DEXDc smart00487
DEAD-like helicases superfamily;
961-1159 1.37e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 123.37  E-value: 1.37e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847    961 EYKNNNKLREYQLEGVNWLLFNWynmRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPL-STIPNWEREFRTWT 1039
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTrELAEQWAEELKKLG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   1040 E---LNVVVYHGSQASRRTIQlyemyfkdpqgRVIKGsyKFHAIITTFEMILTDCPE--LRNIPWRCVVIDEAHRLKN-- 1112
Cdd:smart00487   79 PslgLKVVGLYGGDSKREQLR-----------KLESG--KTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDgg 145
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 767951847   1113 RNCKLLEGLKMMDLE-HKVLLTGTP---LQNTVEELFSLLHFLEPSRFPSE 1159
Cdd:smart00487  146 FGDQLEKLLKLLPKNvQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLE 196
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
968-1166 8.39e-30

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: 119.18  E-value: 8.39e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLFNWYNMR-----NCILADEMGLGKTIQSITFLYEIYLKGIHGP------FLVIAPLSTIPNWEREFR 1036
Cdd:cd18066     1 LRPHQREGIEFLYECVMGMRvnerfGAILADEMGLGKTLQCISLIWTLLRQGPYGGkpvikrALIVTPGSLVKNWKKEFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1037 TWTelnvvvyhgsqaSRRTIQLYEMYFKDPQGRVIKGSYkFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCK 1116
Cdd:cd18066    81 KWL------------GSERIKVFTVDQDHKVEEFIASPL-YSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIK 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 767951847 1117 LLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF 1166
Cdd:cd18066   148 TTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVY 197
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
968-1189 2.28e-27

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: 111.53  E-value: 2.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLFNwyNMRnCILADEMGLGKTIQSITFLYeiYLKGiHGPFLVIAPLSTIPNWEREFRTW----TELNV 1043
Cdd:cd18010     1 LLPFQREGVCFALRR--GGR-VLIADEMGLGKTVQAIAIAA--YYRE-EWPLLIVCPSSLRLTWADEIERWlpslPPDDI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1044 VVYHGSQasrrtiqlyeMYFKDPQGRVikgsykfhaIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRN---CKLLEG 1120
Cdd:cd18010    75 QVIVKSK----------DGLRDGDAKV---------VIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKakrTKAALP 135
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767951847 1121 LkMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTF--------MQEFG-DLKTEEQVQKLQAIL-KPMMLRR 1189
Cdd:cd18010   136 L-LKRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFgrrycaakQGGFGwDYSGSSNLEELHLLLlATIMIRR 213
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1290-1404 1.14e-26

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: 105.76  E-value: 1.14e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  1290 GKLVLIDKLLPKLKagGHRVLIFSQMVRCLDilEDYLIQRR-YPYERIDGRVRGNLRQAAIDRFSKPDSDrfvFLLCTRA 1368
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 767951847  1369 GGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIG 1404
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
968-1189 2.32e-25

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: 106.79  E-value: 2.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLFNWYNMRN-----CILADEMGLGKTIQSITFLYEIYLKGIHGP-----FLVIAPLSTIPNWEREFRT 1037
Cdd:cd18067     1 LRPHQREGVKFLYRCVTGRRIrgshgCIMADEMGLGKTLQCITLMWTLLRQSPQCKpeidkAIVVSPSSLVKNWANELGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1038 WTELNVVVYHGSQASRRTIQLYEMYFKDPQGRVIKGSykfhAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKL 1117
Cdd:cd18067    81 WLGGRLQPLAIDGGSKKEIDRKLVQWASQQGRRVSTP----VLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1118 LEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF---------GD------LKTEEQVQKLQAIL 1182
Cdd:cd18067   157 YQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFelpilkgrdADasekerQLGEEKLQELISIV 236

                  ....*..
gi 767951847 1183 KPMMLRR 1189
Cdd:cd18067   237 NRCIIRR 243
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
796-861 9.94e-25

repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, and similar proteins; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD5, CHD6, CHD7, CHD8, and CHD9. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. CHD6, CHD7, and CHD8 enzymes have been demonstrated to have different substrate specificities and remodeling activities. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349315 [Multi-domain]  Cd Length: 68  Bit Score: 98.56  E-value: 9.94e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767951847  796 DAEGPVVEKIMSSRSVKKQKESGEEVEI-EEFYVKYKNFSYLHCQWASIEDLEK-DKRIQQKIKRFKA 861
Cdd:cd18668     1 EEDTMIIEKILASRKKKKEKEEGAEEIEvEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFKQ 68
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
985-1189 1.05e-23

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: 101.78  E-value: 1.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  985 NMRNCILADEMGLGKTIQSITFLyeiylkgIHGPFLVIAPLSTIPNWEREFRTWTE---LNVVVYHGSQASRRTIQLYem 1061
Cdd:cd18071    47 LVRGGILADDMGLGKTLTTISLI-------LANFTLIVCPLSVLSNWETQFEEHVKpgqLKVYTYHGGERNRDPKLLS-- 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1062 yfkdpqgrvikgsyKFHAIITTFEMILTD-----CPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTP 1136
Cdd:cd18071   118 --------------KYDIVLTTYNTLASDfgakgDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTP 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767951847 1137 LQNTVEELFSLLHFLEPSRFPSETTFMQEFG---DLKTEEQVQKLQAILKPMMLRR 1189
Cdd:cd18071   184 IQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQrplTMGDPTGLKRLQVLMKQITLRR 239
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
989-1166 3.27e-23

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: 100.35  E-value: 3.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  989 CILADEMGLGKTIQSITFLYEIYLKGIHGPF---LVIAPLSTIPNWEREFRTWTELNvvvyhgsqASRRTIQLYEM-YFK 1064
Cdd:cd18068    31 CILAHCMGLGKTLQVVTFLHTVLLCEKLENFsrvLVVCPLNTVLNWLNEFEKWQEGL--------KDEEKIEVNELaTYK 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1065 DPQGRVIKGSYKFH---AIITTFEM--ILT--DCPELR------------NIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 1125
Cdd:cd18068   103 RPQERSYKLQRWQEeggVMIIGYDMyrILAqeRNVKSReklkeifnkalvDPGPDFVVCDEGHILKNEASAVSKAMNSIR 182
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767951847 1126 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF 1166
Cdd:cd18068   183 TKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
968-1189 4.96e-23

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: 98.90  E-value: 4.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLFNWYNmrNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVyh 1047
Cdd:cd18011     1 PLPHQIDAVLRALRKPPV--RLLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQDKFGLPFLI-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1048 gsqASRRTIQLYEMYFKDPQGRvikgsykFHAIITTFEMILTDcPELR----NIPWRCVVIDEAHRLKNRNC-------K 1116
Cdd:cd18011    77 ---LDRETAAQLRRLIGNPFEE-------FPIVIVSLDLLKRS-EERRglllSEEWDLVVVDEAHKLRNSGGgketkryK 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767951847 1117 LLEGLKMMDlEHKVLLTGTPLQNTVEELFSLLHFLEPSRFpsetTFMQEFGDLKTEEQVqklqaiLKPMMLRR 1189
Cdd:cd18011   146 LGRLLAKRA-RHVLLLTATPHNGKEEDFRALLSLLDPGRF----AVLGRFLRLDGLREV------LAKVLLRR 207
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
990-1438 3.26e-22

DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component of class 1 DISARM (Defence Island System Associated with Restriction Modification), which contains a DNA adenine N6 methyltransferase. This HMM describes a distinct form that is somewhat shorter than the majority of DrmD proteins.


Pssm-ID: 468472 [Multi-domain]  Cd Length: 868  Bit Score: 104.38  E-value: 3.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  990 ILADEMGLGKTIQS---ITFLYEIYLKGIhgpfLVIAPLSTIPNWEREFRTWTELNVVVyhgsqASRRTiqlYEMYFKDP 1066
Cdd:NF038318   51 ILADEVGLGKTIEAglvLKYVLESGAKKI----LIILPANLRKQWEIELEEKFDLESLI-----LDSLT---VEKDAKKW 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1067 QGRvIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKN--RNCKLLEGLkmMDLEH---KVLLTGTPLQNTV 1141
Cdd:NF038318  119 NKR-LTDNKKVRIVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRNvhKGGKRAKNL--YELTKgipKILLTATPLQNSL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1142 EELFSLLHFLEPSRFPSETTFM------QEFGDLKTEeqvqklqaiLKPMMLRRLKEDVEKNLAPKEETII--------- 1206
Cdd:NF038318  196 LDLYGLVSFIDPRIFGSEKVFSkryikdEDYSDLKRE---------LSPVLYRTLRKDVADYMQFKKRKCItvdfelspd 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1207 EVELTN-----IQKKYYRAI-----------------------------LEKNFTFLSKGGGQANVPNLLNtmmelrkcc 1252
Cdd:NF038318  267 EIELYVrvnnfLKRDILYSIptsnrtliilvirkllasssfalaetfevLKKRLEKLKEGTRSANAQEGFD--------- 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1253 nhpYLINGAEEKILEEFKETHNAESPDFQLQaMIQAAGKLV--LIDK------------LLPKLKAG---------GHRV 1309
Cdd:NF038318  338 ---LFWSFVEDEIDESGFEEKQDELYTRQKE-FIQHEIDEVdaIIDVakriktnakvtaLKTALEIAfeyqreegiAQKV 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1310 LIFSQMVRCLDILEDYLIQRRYPYERI---DG--------------RVR--GN--------LRQAAIDRFSkpdsDRFVF 1362
Cdd:NF038318  414 VVFTESKRTQKYIAEELRKSGYEGEDIllfNGdfddamtkeiyrawQVKnyGKanygrsveYKHAIVDYFK----NNAKI 489
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767951847 1363 LLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKSVKIYRLI-TRNSYEREMFDKASLKLGLDKAV 1438
Cdd:NF038318  490 LIVTDAGSEGLNLQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYEILSEKFELFEGV 566
HELICc smart00490
helicase superfamily c-terminal domain;
1320-1404 1.95e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 89.96  E-value: 1.95e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   1320 DILEDYLIQRRYPYERIDGRVRGNLRQAAIDRFSKPDSDrfvFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQAR 1399
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 767951847   1400 CHRIG 1404
Cdd:smart00490   78 AGRAG 82
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
989-1166 1.17e-17

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: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  989 CILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVyhgSQASRRTIQLY----EMYFK 1064
Cdd:cd18069    31 CILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKWLPPPEAL---PNVRPRPFKVFilndEHKTT 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1065 DPQGRVI-KGSYKFHAIITTFEMI-LTDCPELrnipwrcVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVE 1142
Cdd:cd18069   108 AARAKVIeDWVKDGGVLLMGYEMFrLRPGPDV-------VICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLI 180
                         170       180
                  ....*....|....*....|....
gi 767951847 1143 ELFSLLHFLEPSRFPSETTFMQEF 1166
Cdd:cd18069   181 EYWCMVDFVRPDFLGTRQEFSNMF 204
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
880-934 1.62e-17

repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 to CHD9, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349306 [Multi-domain]  Cd Length: 54  Bit Score: 77.62  E-value: 1.62e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767951847  880 DYVEVDRIMdfARSTDDRGepVTHYLVKWCSLPYEDSTWERRQDI---DQAKIEEFEK 934
Cdd:cd18659     1 EYTIVERII--AHREDDEG--VTEYLVKWKGLPYDECTWESEEDIsdiFQEAIDEYKK 54
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
968-1189 4.20e-17

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: 82.53  E-value: 4.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLFNW-YNMRNCILADEMGLGKTIQSITF------------------LYEIYLKGIHGPF-----LVIA 1023
Cdd:cd18072     1 LLLHQKQALAWLLWRErQKPRGGILADDMGLGKTLTMIALilaqkntqnrkeeekekaLTEWESKKDSTLVpsagtLVVC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1024 PLSTIPNWEREFRTWT---ELNVVVYHGsqASRRTIqlyemyfkdpqGRVIKgsyKFHAIITTFEMILTDCPELRN---- 1096
Cdd:cd18072    81 PASLVHQWKNEVESRVasnKLRVCLYHG--PNRERI-----------GEVLR---DYDIVITTYSLVAKEIPTYKEesrs 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1097 -----IPWRCVVIDEAHRLKNRN-------CKLLEGLKMMdlehkvlLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQ 1164
Cdd:cd18072   145 splfrIAWARIILDEAHNIKNPKvqasiavCKLRAHARWA-------LTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKK 217
                         250       260
                  ....*....|....*....|....*
gi 767951847 1165 EFgDLKTEEQVQKLQAILKPMMLRR 1189
Cdd:cd18072   218 QV-DNKSRKGGERLNILTKSLLLRR 241
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
883-934 3.24e-12

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 62.59  E-value: 3.24e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767951847   883 EVDRIMDfaRSTDDRGepVTHYLVKWCSLPYEDSTWERRQDID--QAKIEEFEK 934
Cdd:pfam00385    2 EVERILD--HRKDKGG--KEEYLVKWKGYPYDENTWEPEENLSkcPELIEEFKD 51
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
968-1152 6.60e-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: 66.60  E-value: 6.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLfnwYNMRNCILADeMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPN-WEREFRTWTELN---V 1043
Cdd:cd18013     1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARStWPDEVEKWNHLRnltV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1044 VVYHGSQASRRTI-----QLYemyfkdpqgrvikgsykfhaiITTFEMiLTDCPELRNIPW--RCVVIDEAHRLKNRNCK 1116
Cdd:cd18013    77 SVAVGTERQRSKAantpaDLY---------------------VINREN-LKWLVNKSGDPWpfDMVVIDELSSFKSPRSK 134
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767951847 1117 LLEGLKMMD--LEHKVLLTGTPLQNTVEELFSLLHFLE 1152
Cdd:cd18013   135 RFKALRKVRpvIKRLIGLTGTPSPNGLMDLWAQIALLD 172
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
798-860 1.25e-11

repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 to CHD9, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349307 [Multi-domain]  Cd Length: 70  Bit Score: 61.61  E-value: 1.25e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  798 EGPVVEKIMSSRSVKKQKESGEEVEIEE-------FYVKYKNFSYLHCQWASIEDLEKDkRIQQKIKRFK 860
Cdd:cd18660     1 DEDKIEKILDHRPKGPVEEASLDLTDPDepwdereFLVKWKGKSYLHCTWVTEETLEQL-RGKKKLKNYI 69
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
968-1156 1.43e-11

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: 66.60  E-value: 1.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  968 LREYQLEGVNWLLfnwynMRNCILADEMGLGKTIQSI----------------------TFLYEIYLKGIH----GPFLV 1021
Cdd:cd18070     1 LLPYQRRAVNWML-----VPGGILADEMGLGKTVEVLalillhprpdndldaadddsdeMVCCPDCLVAETpvssKATLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1022 IAPLSTIPNWEREFRTWTELNVVVYHgsqasrrtiqlYEMYFKDPQgrVIKGSYKFHA----IITTFEMILTD------- 1090
Cdd:cd18070    76 VCPSAILAQWLDEINRHVPSSLKVLT-----------YQGVKKDGA--LASPAPEILAeydiVVTTYDVLRTElhyaean 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1091 ----------------CPELRnIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLEHKVLLTGTPLQNTVEELFSLLHFLEPS 1154
Cdd:cd18070   143 rsnrrrrrqkryeappSPLVL-VEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVE 221

                  ..
gi 767951847 1155 RF 1156
Cdd:cd18070   222 PF 223
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
197-578 2.47e-11

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 69.03  E-value: 2.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   197 DFSMQQhgQPQQRMSQFSQGQEGL-------NQGNPFIATSGP--GHLSHVPQQSPSMAPSLRHsvQQFHHHPSTALHGE 267
Cdd:pfam03154  159 DSSAQQ--QILQTQPPVLQAQSGAasppsppPPGTTQAATAGPtpSAPSVPPQGSPATSQPPNQ--TQSTAAPHTLIQQT 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   268 SVAHSPRF-SPNPPQQGAVRPQTLNFSSrSQTVPSPTINNSGQYSRYPysnLNQGlvnntgmnqnlgltnntPMNQSVPR 346
Cdd:pfam03154  235 PTLHPQRLpSPHPPLQPMTQPPPPSQVS-PQPLPQPSLHGQMPPMPHS---LQTG-----------------PSHMQHPV 293
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   347 YPNAVGFPSNSGQGlmhQQPIHPSGSLNQMNTQTMH--PSQPQGTYASPPPMSPMKamsnPAGTPPPQVRPG-SAGIPme 423
Cdd:pfam03154  294 PPQPFPLTPQSSQS---QVPPGPSPAAPGQSQQRIHtpPSQSQLQSQQPPREQPLP----PAPLSMPHIKPPpTTPIP-- 364
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   424 vgsypnmphpqpshqppgAMGIGQRNMGPRNMQQSRPFigmssapreltgHMRPNGCPGVGLGDPQAIQERLIPGQQHPG 503
Cdd:pfam03154  365 ------------------QLPNPQSHKHPPHLSGPSPF------------QMNSNLPPPPALKPLSSLSTHHPPSAHPPP 414
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767951847   504 QQ--PSFQQLPTcPPLQPhPGLHHQSS--PPHPHHQPWAQLHPSPQNTPqkvpvhqhSPSEPFLEKPVPDMTQVSGPNA 578
Cdd:pfam03154  415 LQlmPQSQQLPP-PPAQP-PVLTQSQSlpPPAASHPPTSGLHQVPSQSP--------FPQHPFVPGGPPPITPPSGPPT 483
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
914-1488 8.21e-11

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 66.59  E-value: 8.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  914 EDSTWERRQDIDQAKIEEFEKLMSREPETERVERPPADDWKK---SESSREYKNNNKLREYQLEGVN-WLLFNWYNMRNC 989
Cdd:COG1061    24 ERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAealEAGDEASGTSFELRPYQQEALEaLLAALERGGGRG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  990 ILADEMGLGKTIQSITFLYEIYLKGihgPFLVIAPLSTIPN-WEREFRTWteLNVVVYHGSQasrrtiqlyemyfKDPQG 1068
Cdd:COG1061   104 LVVAPTGTGKTVLALALAAELLRGK---RVLVLVPRRELLEqWAEELRRF--LGDPLAGGGK-------------KDSDA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1069 RVIkgsykfhaiITTFEmILTDCPELRNIP--WRCVVIDEAHRLKNRncKLLEGLKMMDLEHKVLLTGTPLqntveelfs 1146
Cdd:COG1061   166 PIT---------VATYQ-SLARRAHLDELGdrFGLVIIDEAHHAGAP--SYRRILEAFPAAYRLGLTATPF--------- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1147 llhflepsRFPSETTFMQEFGDLKTEEQVQKLQAilkpmmlrrlkedvEKNLAPKEETIIEVELTNIQKKYyrAILEKNF 1226
Cdd:COG1061   225 --------RSDGREILLFLFDGIVYEYSLKEAIE--------------DGYLAPPEYYGIRVDLTDERAEY--DALSERL 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1227 TFLskgggqanvpnllntmmelrkccnhpyLINGAEEK--ILEEFKETHnaespdfqlqamiqaagklvlidkllpklkA 1304
Cdd:COG1061   281 REA---------------------------LAADAERKdkILRELLREH------------------------------P 303
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1305 GGHRVLIFSQMVRCLDILEDYLIQRRYPYERIDGRVRGNLRQAAIDRFSkpdSDRFVFLLCTRAGGLGINLTAADTCIIF 1384
Cdd:COG1061   304 DDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFR---DGELRILVTVDVLNEGVDVPRLDVAILL 380
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1385 DSDWNPQNDLQAQARCHRIGQSKS-VKIYRLITRNSYEREMFDKASLKLGLDKAVLQSMSGRENATNGVQQLSKKEIEDL 1463
Cdd:COG1061   381 RPTGSPREFIQRLGRGLRPAPGKEdALVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGE 460
                         570       580
                  ....*....|....*....|....*
gi 767951847 1464 LRKGAYGALMDEEDEGSKFCEEDID 1488
Cdd:COG1061   461 LEEELLEELELLEDALLLVLAELLL 485
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
879-934 4.59e-10

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and 4, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD3 and CHD4, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. Human CHD3 (also named Mi-2 alpha) and CHD4 (also named Mi-2 beta) are coexpressed in many cell lines and tissues and may act as the motor subunit of the NuRD complex (nucleosome remodeling and deacetylase activities). The proteins form distinct CHD3- and CHD4-NuRD complexes that repress, as well as activate gene transcription of overlapping and specific target genes. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349309 [Multi-domain]  Cd Length: 55  Bit Score: 56.50  E-value: 4.59e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767951847  879 PDYVEVDRIMDfaRSTDDRGEpvTHYLVKWCSLPYEDSTWERRQDidqaKIEEFEK 934
Cdd:cd18662     1 PEWLQIHRIIN--HRVDKDGN--TWYLVKWRDLPYDQSTWESEDD----DIPDYEK 48
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
204-576 1.64e-09

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 62.72  E-value: 1.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   204 GQPQQRMSQ-FSQGQEGLNQGN--PFIATSGPGHLSHVPQQ--SPSMAPSLRHSVQQfhhhPSTALHGESVAHsPRFSPN 278
Cdd:pfam09606   73 GGGQQGMPDpINALQNLAGQGTrpQMMGPMGPGPGGPMGQQmgGPGTASNLLASLGR----PQMPMGGAGFPS-QMSRVG 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   279 PPQQGAVRPQTLNFSSRSQTVPSPTINNSGQYSRYPYS-NLNQGLVNNTG------MNQNLGLTNNTPMNQSVPRYPNAV 351
Cdd:pfam09606  148 RMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQAgGMNGGQQGPMGgqmppqMGVPGMPGPADAGAQMGQQAQANG 227
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   352 GFPSNSGQG-----LMHQQPIHPSGSLNQMNTQTMHPSQ-PQGTYASPPPMSPMKAMsnpagtPPPQVRPGSAGIPMEVG 425
Cdd:pfam09606  228 GMNPQQMGGapnqvAMQQQQPQQQGQQSQLGMGINQMQQmPQGVGGGAGQGGPGQPM------GPPGQQPGAMPNVMSIG 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   426 SYPNMPHPQPSHQPPGAMGIGQRNMGPRNMQQSRPFIGMSSAPrelTGHMRPNGCPG--VGLGDPQAIQERL-------- 495
Cdd:pfam09606  302 DQNNYQQQQTRQQQQQQGGNHPAAHQQQMNQSVGQGGQVVALG---GLNHLETWNPGnfGGLGANPMQRGQPgmmsspsp 378
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   496 IPGQQHPGQQPSFQQLPTCPPLQP---HPGLHHQSSP-----PHPHHQPWAQLHPSpQNTPQKVPVHQHSPSEpflekPV 567
Cdd:pfam09606  379 VPGQQVRQVTPNQFMRQSPQPSVPspqGPGSQPPQSHpggmiPSPALIPSPSPQMS-QQPAQQRTIGQDSPGG-----SL 452

                   ....*....
gi 767951847   568 PDMTQVSGP 576
Cdd:pfam09606  453 NTPGQSAVN 461
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
801-862 4.00e-09

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 53.74  E-value: 4.00e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767951847   801 VVEKIMSSRSVKKQKESgeeveieeFYVKYKNFSYLHCQWASIEDLEKDKRIqqkIKRFKAK 862
Cdd:pfam00385    2 EVERILDHRKDKGGKEE--------YLVKWKGYPYDENTWEPEENLSKCPEL---IEEFKDR 52
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
15-416 1.30e-07

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 56.56  E-value: 1.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847    15 NIFSEGLEGLGECGYPENPVNPMGQQMPIDQGFASLQPSLHHPstnqnqtklthfdhynqyeQQKMHLMDQPNRMM---S 91
Cdd:pfam09606   88 NLAGQGTRPQMMGPMGPGPGGPMGQQMGGPGTASNLLASLGRP-------------------QMPMGGAGFPSQMSrvgR 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847    92 NTPGNGLASPHSQYHTPPVPQVPHGGSgggqmgvypGMQNERHGQSFVDSSSMWGPRAVQVPDQIRAPYQQQQPQPQPPQ 171
Cdd:pfam09606  149 MQPGGQAGGMMQPSSGQPGSGTPNQMG---------PNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPADAGAQM 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   172 PAPSGPPAQGHPQHMQQMGSYMARGDFSMQQHGQPQQRMSQFSQGQEgLNQGNPFIATSG-PGHLSHVPQQSPSMAPslr 250
Cdd:pfam09606  220 GQQAQANGGMNPQQMGGAPNQVAMQQQQPQQQGQQSQLGMGINQMQQ-MPQGVGGGAGQGgPGQPMGPPGQQPGAMP--- 295
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   251 hsvqqfhhhPSTALHGESVAHSPRFSPNPPQQGAVRPQTLnfssrsQTVPSPTINNSGQYSRYPYSNL--NQGLVNNTGM 328
Cdd:pfam09606  296 ---------NVMSIGDQNNYQQQQTRQQQQQQGGNHPAAH------QQQMNQSVGQGGQVVALGGLNHleTWNPGNFGGL 360
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   329 NQNLGLTNNTPMNQSVPRYPNAVGFPSNSGQGLMHQ-QPIHPSGSLNQMNTQTMHPSQPQGTYASPPPMSPMKAMSNPAG 407
Cdd:pfam09606  361 GANPMQRGQPGMMSSPSPVPGQQVRQVTPNQFMRQSpQPSVPSPQGPGSQPPQSHPGGMIPSPALIPSPSPQMSQQPAQQ 440

                   ....*....
gi 767951847   408 TPPPQVRPG 416
Cdd:pfam09606  441 RTIGQDSPG 449
CD2_tandem_ScCHD1_like cd18664
repeat 2 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
880-938 2.49e-07

repeat 2 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein 1, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349311  Cd Length: 59  Bit Score: 49.19  E-value: 2.49e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767951847  880 DYVEVDRIMDFARSTDDRGEPVTHYLVKWCSLPYEDSTWERRQDIDQAKIEEFEKLMSR 938
Cdd:cd18664     1 EFHVVERIIASQRASLEDGTSQLQYLVKWRRLNYDECTWEDATLIAKLAPEQVDHFQNR 59
CHROMO smart00298
Chromatin organization modifier domain;
801-863 2.93e-07

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 48.75  E-value: 2.93e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767951847    801 VVEKIMSSRSVKKqkesgeevEIEEFYVKYKNFSYLHCQWASIEDLEKDKRiqqKIKRFKAKQ 863
Cdd:smart00298    3 EVEKILDHRWKKK--------GELEYLVKWKGYSYSEDTWEPEENLLNCSK---KLDNYKKKE 54
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
354-581 4.44e-07

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 55.04  E-value: 4.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   354 PSNSGQGLMHQQPIHPSGSLNQMNTQTMHPSQPQGT----YASPPPMSPMKAMSNPAGTPPPQvRPGSAGIPmEVGSYPN 429
Cdd:pfam09770  107 PAARAAQSSAQPPASSLPQYQYASQQSQQPSKPVRTgyekYKEPEPIPDLQVDASLWGVAPKK-AAAPAPAP-QPAAQPA 184
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   430 MPHPQPSHQPP-----GAMGIGQRNMGPRNMQQSRPFIGMSSAPRELTGHMRPNGCPGvglgdPQAIQERLIPGQQHPGQ 504
Cdd:pfam09770  185 SLPAPSRKMMSleeveAAMRAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQ-----QQQPQQQPQQPQQHPGQ 259
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   505 QPSFQQL--PTCPPLQPHPGLHHQSSPPHPHHQPWAQLHPSP--QN----TPQKVPVHQH--SPSEPFLEKPVPDMTQVS 574
Cdd:pfam09770  260 GHPVTILqrPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQilQNpnrlSAARVGYPQNpqPGVQPAPAHQAHRQQGSF 339

                   ....*..
gi 767951847   575 GPNAQLV 581
Cdd:pfam09770  340 GRQAPII 346
CHROMO smart00298
Chromatin organization modifier domain;
883-934 7.51e-07

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 47.59  E-value: 7.51e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 767951847    883 EVDRIMDfaRSTDDRGEpvTHYLVKWCSLPYEDSTWERRQDI--DQAKIEEFEK 934
Cdd:smart00298    3 EVEKILD--HRWKKKGE--LEYLVKWKGYSYSEDTWEPEENLlnCSKKLDNYKK 52
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
988-1135 2.16e-06

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 48.94  E-value: 2.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  988 NCILADEMGLGKTIQSITFLYEiYLKGIHGPFLVIAPLSTI-PNWEREFRTWTELNVVV---YHGSQASRRTiqlyemyf 1063
Cdd:cd00046     3 NVLITAPTGSGKTLAALLAALL-LLLKKGKKVLVLVPTKALaLQTAERLRELFGPGIRVavlVGGSSAEERE-------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847 1064 kdpqgRVIKGSYKFhaIITTFEMILTDCPELRNI---PWRCVVIDEAHRLKN-----RNCKLLEGLKMMDLEHKVLLTGT 1135
Cdd:cd00046    74 -----KNKLGDADI--IIATPDMLLNLLLREDRLflkDLKLIIVDEAHALLIdsrgaLILDLAVRKAGLKNAQVILLSAT 146
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
883-934 2.90e-06

CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this group are chromodomains or chromo shadow domains; these are SH3-fold-beta-barrel domains of the chromo-like superfamily. Chromodomains lack the first strand of the SH3-fold-beta-barrel, this first strand is altered by insertion in the chromo shadow domains. The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. Chromodomain-containing proteins include: i) those having an N-terminal chromodomain followed by a related chromo shadow domain, such as Drosophila and human heterochromatin protein Su(var)205 (HP1), and mammalian modifier 1 and 2; ii) those having a single chromodomain, such as Drosophila protein Polycomb (Pc), mammalian modifier 3, human Mi-2 autoantigen, and several yeast and Caenorhabditis elegans proteins of unknown function; iii) those having paired tandem chromodomains, such as mammalian DNA-binding/helicase proteins CHD-1 to CHD-4 and yeast protein CHD1; (iv) and elongation factor eEF3, a member of the ATP-binding cassette (ABC) family of proteins, that serves an essential function in the translation cycle of fungi. eEF3 is a soluble factor lacking a transmembrane domain and having two ABC domains arranged in tandem, with a unique chromodomain inserted within the ABC2 domain.


Pssm-ID: 349274 [Multi-domain]  Cd Length: 50  Bit Score: 45.55  E-value: 2.90e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767951847  883 EVDRIMDfarSTDDRGEpvTHYLVKWCSLPYEDSTWERRQDIDQAK--IEEFEK 934
Cdd:cd00024     2 EVEKILD---HRVRKGK--LEYLVKWKGYPPEENTWEPEENLTNAPelIKEYEK 50
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
260-589 3.24e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 52.08  E-value: 3.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   260 PSTALHGESVAHSPRfSPNppQQGAVRPQTLNFSSRSQT--VPSPTINNSGQYSRYPYSNLN-QGLV----NNTGMNQNL 332
Cdd:pfam03154  110 PNSPSEGEGESSDGR-SVN--DEGSSDPKDIDQDNRSTSpsIPSPQDNESDSDSSAQQQILQtQPPVlqaqSGAASPPSP 186
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   333 GLTNNTPMNQSVPRyPNAVGFPSN----SGQGLMHQQPIHPSGSLNQmNTQTMHPSQpqgtyaSPPPMSPMKAMSNPAgt 408
Cdd:pfam03154  187 PPPGTTQAATAGPT-PSAPSVPPQgspaTSQPPNQTQSTAAPHTLIQ-QTPTLHPQR------LPSPHPPLQPMTQPP-- 256
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   409 PPPQVRPGSAGIPmevgsypnmphpqpSHQPPGAMGIGQRNMGPRNMQQSRPFIGMSSAPRELTGHMRPNGCPGVGLGDP 488
Cdd:pfam03154  257 PPSQVSPQPLPQP--------------SLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQ 322
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   489 QAIQERLIPGQQHPGQQPSFQQLPTCPPLQPH---PglhhQSSPPHPHHQPWAQLHPSPQNTPQKVPVHQHSPSEPFLeK 565
Cdd:pfam03154  323 QRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHikpP----PTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPPPPAL-K 397
                          330       340
                   ....*....|....*....|....*....
gi 767951847   566 PVPDMTQVSGPNA-----QLVKSDDYLPS 589
Cdd:pfam03154  398 PLSSLSTHHPPSAhppplQLMPQSQQLPP 426
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
22-420 8.28e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 50.92  E-value: 8.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847    22 EGLGECGyPENPVNPMGQQMP--IDQGFASLQPSLHHPSTNQNQTklthfdhyNQYEQQKMhLMDQPNRMMSNTPgngla 99
Cdd:pfam03154  115 EGEGESS-DGRSVNDEGSSDPkdIDQDNRSTSPSIPSPQDNESDS--------DSSAQQQI-LQTQPPVLQAQSG----- 179
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   100 sphsqyhTPPVPQVPHGGSGGGQMGVYPgmqnerhgQSFVDSSSMWGPRAVQVPDQirapyqqqqPQPQPPQPAPSGPPA 179
Cdd:pfam03154  180 -------AASPPSPPPPGTTQAATAGPT--------PSAPSVPPQGSPATSQPPNQ---------TQSTAAPHTLIQQTP 235
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   180 QGHPQH-------MQQMGSYMARGDFSMQQHGQPqqrmSQFSQGQEGlnqgnPFIATSGPGHLSH-VPQQSPSMAPSLRH 251
Cdd:pfam03154  236 TLHPQRlpsphppLQPMTQPPPPSQVSPQPLPQP----SLHGQMPPM-----PHSLQTGPSHMQHpVPPQPFPLTPQSSQ 306
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   252 SVQQFHHHPSTALHGESVAHSPRFSPNPPQQGAVRPQTLNFSSRSQ-------TVPSPTINNSGQYSRYPYSNLNQGLvn 324
Cdd:pfam03154  307 SQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMphikpppTTPIPQLPNPQSHKHPPHLSGPSPF-- 384
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   325 ntGMNQNL----------GLTNNTPMNQSVPR---YPNAVGFPSNSGQG-LMHQQPIHPSGSLNQMNTQTMHPSQPQGTY 390
Cdd:pfam03154  385 --QMNSNLppppalkplsSLSTHHPPSAHPPPlqlMPQSQQLPPPPAQPpVLTQSQSLPPPAASHPPTSGLHQVPSQSPF 462
                          410       420       430
                   ....*....|....*....|....*....|
gi 767951847   391 ASPPPMSPMKAMSNPAGTPPPQVRPGSAGI 420
Cdd:pfam03154  463 PQHPFVPGGPPPITPPSGPPTSTSSAMPGI 492
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
446-577 8.35e-06

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 50.58  E-value: 8.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   446 GQRNMGPRNMQQSRPFIGMSSAP--RELTGHMRPNGCPGVGLGDPQaiqerlIPGQQHPGQQPSFQQLPT-----CPPLQ 518
Cdd:TIGR01628  376 MQLQPRMRQLPMGSPMGGAMGQPpyYGQGPQQQFNGQPLGWPRMSM------MPTPMGPGGPLRPNGLAPmnavrAPSRN 449
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767951847   519 PHPGLHHQSSPPHPhHQPWAQLHPSPQNTPQKVPVHQHSPSEPFLEK-----PVPDMTQVSGPN 577
Cdd:TIGR01628  450 AQNAAQKPPMQPVM-YPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQvlasaTPQMQKQVLGER 512
ResIII pfam04851
Type III restriction enzyme, res subunit;
967-1136 3.38e-05

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 45.74  E-value: 3.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   967 KLREYQLEGV-NWLLFNWYNMRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAP-LSTIPNWEREFRTWTElnvv 1044
Cdd:pfam04851    3 ELRPYQIEAIeNLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFLP---- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  1045 vyhgsqASRRTIQLYEMYFKDPQGRVIKgsYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRL----------KNRN 1114
Cdd:pfam04851   79 ------NYVEIGEIISGDKKDESVDDNK--IVVTTIQSLYKALELASLELLPDFFDVIIIDEAHRSgassyrnileYFKP 150
                          170       180
                   ....*....|....*....|..
gi 767951847  1115 CKLLEglkmmdlehkvlLTGTP 1136
Cdd:pfam04851  151 AFLLG------------LTATP 160
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
969-1144 1.17e-04

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 44.16  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   969 REYQLEGVNWLLFNwynmRNCILADEMGLGKT-IQSITFLYEIYLKGIHGPFLVIAPLST-IPNWEREFRTW---TELNV 1043
Cdd:pfam00270    1 TPIQAEAIPAILEG----RDVLVQAPTGSGKTlAFLLPALEALDKLDNGPQALVLAPTRElAEQIYEELKKLgkgLGLKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  1044 VVYHGSQAsrrtiqlyemyfKDPQGRVIKGSykfHAIITTFEMILTDCPE---LRNIpwRCVVIDEAHRL--KNRNCKLL 1118
Cdd:pfam00270   77 ASLLGGDS------------RKEQLEKLKGP---DILVGTPGRLLDLLQErklLKNL--KLLVLDEAHRLldMGFGPDLE 139
                          170       180
                   ....*....|....*....|....*..
gi 767951847  1119 EGLKMMDLEHK-VLLTGTPLQNtVEEL 1144
Cdd:pfam00270  140 EILRRLPKKRQiLLLSATLPRN-LEDL 165
CD_POL_like cd18974
chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the ...
883-934 2.31e-04

chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Penicillium solitum protein PENSOL_c198G03123 a putative polyprotein from a Ty3/Gypsy long terminal repeat (LTR) retroelement. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349330  Cd Length: 50  Bit Score: 40.54  E-value: 2.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767951847  883 EVDRIMDFARSTDDrgepvTHYLVKWCSLPYEDSTWERRQDIDQAK--IEEFEK 934
Cdd:cd18974     2 EVEEIVDEKMIDDE-----LHYLVKWKGWPAEYNQWEPEDDMENAPkaIQSYEK 50
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
212-428 3.01e-04

MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 44.21  E-value: 3.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   212 QFSQGQEGLN-QGNPFIATSGPGHLShvPQQSPSMAPslrHSVQQFHHHPSTALHGESVAHSPRFSPNPPQQgavrPQTl 290
Cdd:pfam15822   25 QPPQGWPGSNpWNNPSAPPAVPSGLP--PSTAPSTVP---FGPAPTGMYPSIPLTGPSPGPPAPFPPSGPSC----PPP- 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   291 nfssrSQTVPSPTINNSGQYSRYPysnlnqglvnntgmnqnlgltnntPMNQSVPRYPNAVGFPSNSGQGlmhqQPIHPS 370
Cdd:pfam15822   95 -----GGPYPAPTVPGPGPIGPYP------------------------TPNMPFPELPRPYGAPTDPAAA----APSGPW 141
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767951847   371 GSLNQ------MNTQTMHPSQP---QGTY-ASPPPMSPMKAMSNPAGTPPPQVRPGSAGIPMEVGSYP 428
Cdd:pfam15822  142 GSMSSgpwapgMGGQYPAPNMPypsPGPYpAVPPPQSPGAAPPVPWGTVPPGPWGPPAPYPDPTGSYP 209
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
1357-1412 4.59e-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: 40.38  E-value: 4.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767951847 1357 SDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKSVKIY 1412
Cdd:cd18785    20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVIL 75
CD3_cpSRP43_like cd18628
chromodomain 3 of chloroplast signal recognition particle 43 kDa protein, and similar proteins; ...
880-933 5.45e-04

chromodomain 3 of chloroplast signal recognition particle 43 kDa protein, and similar proteins; This subgroup includes the chromodomain 3 of chloroplast SRP43 (cpSRP43), and similar proteins. CpSRP43 is a component of the chloroplast signal recognition particle (SRP) pathway. It forms a stable complex with cpSRP54 (cpSRP complex) which is required for the efficient posttranslational transport of members of the nuclearly encoded light harvesting chlorophyll-a/b-binding proteins (LHCPs) to the thylakoid membrane. Chromatin organization modifier (chromo) domain is a conserved region of around 50 amino acids found in a variety of chromosomal proteins, which appear to play a role in the functional organization of the eukaryotic nucleus. Experimental evidence implicates the chromodomain in the binding activity of these proteins to methylated histone tails and maybe RNA. May occur as single instance, in a tandem arrangement or followed by a related chromo shadow domain.


Pssm-ID: 349278  Cd Length: 51  Bit Score: 39.29  E-value: 5.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767951847  880 DYVEVDRIMDfARSTDdrGEPVTHYLVKWcsLPYEDSTWERRQDIDQAKIEEFE 933
Cdd:cd18628     2 EYAVAESVIG-KRVGD--DGKTIEYLVKW--TDMSDATWEPQDNVDSTLVLLYQ 50
chromodomain cd18964
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
884-934 5.86e-04

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349320  Cd Length: 54  Bit Score: 39.24  E-value: 5.86e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767951847  884 VDRIMDfARSTDDRGEPVTHYLVKWCSLPYEDSTWERRQDI-DQAK-IEEFEK 934
Cdd:cd18964     3 VERIIG-RRPSARDGPGKFLWLVKWDGYPIEDATWEPPENLgEHAKlIEDFEK 54
CD2_tandem_CHD1-2_like cd18661
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
881-933 6.26e-04

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and 2, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 and CHD2. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349308  Cd Length: 58  Bit Score: 39.21  E-value: 6.26e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767951847  881 YVEVDRIMDFARSTD-DRGEPvtHYLVKWCSLPYEDSTWERRQDID---QAKIEEFE 933
Cdd:cd18661     2 YQIVERIIAHSPQKSaASGYP--DYLCKWQGLPYSECTWEDGALISkkfQACIDEYH 56
KLF1_2_4_N-like cd22056
N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of ...
497-564 7.91e-04

N-terminal domain of Kruppel-like factors with similarity to the N-terminal domains of Kruppel-like factor (KLF)1, KLF2, and KLF4; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specifity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domains of an unknown subfamily of KLFs, predominantly found in fish, related to the N-terminal domains of KLF1, KLF2, and KLF4.


Pssm-ID: 409231 [Multi-domain]  Cd Length: 339  Bit Score: 43.49  E-value: 7.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  497 PGQQHPGQQPSFQQLPTCPPLQPHPGLHHQSSPPHPHHQPWAQL------HPSPQNTPQ----------KVPVHQH---- 556
Cdd:cd22056   220 AFTHHQAAGPGALQGRGGRGGPDCHLLHSSHHHHHHHHLQYQYMnapyppHYAHQGAPQfhgqysvfrePMRVHHQghpg 299
                          90
                  ....*....|....*.
gi 767951847  557 --------SPSEPFLE 564
Cdd:cd22056   300 smltppssPPLLEFYA 315
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
801-861 1.13e-03

repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 to CHD9, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349306 [Multi-domain]  Cd Length: 54  Bit Score: 38.33  E-value: 1.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767951847  801 VVEKIMSSRSVKKQKESgeeveieeFYVKYKNFSYLHCQWASIEDLEkdKRIQQKIKRFKA 861
Cdd:cd18659     4 IVERIIAHREDDEGVTE--------YLVKWKGLPYDECTWESEEDIS--DIFQEAIDEYKK 54
chromodomain cd18965
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
902-924 1.74e-03

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349321  Cd Length: 53  Bit Score: 37.84  E-value: 1.74e-03
                          10        20
                  ....*....|....*....|...
gi 767951847  902 THYLVKWCSLPYEDSTWERRQDI 924
Cdd:cd18965    16 LEYLVKWHGLPESENTWEREKDI 38
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
352-576 1.78e-03

MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 41.90  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   352 GFPSNSGQGLMHQQPIHPSGsLNQMNTQTMHP--SQPQGTYASPPPMSPmkamsnPAGTPPPqVRPGSAGIPMEVGSYPn 429
Cdd:pfam15822   29 GWPGSNPWNNPSAPPAVPSG-LPPSTAPSTVPfgPAPTGMYPSIPLTGP------SPGPPAP-FPPSGPSCPPPGGPYP- 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847   430 mphpqpSHQPPGAMGIGQrnMGPRNM---QQSRPFIG----MSSAPRELTGHMrPNGCPGVGLGdpqaiqerlipgqqhp 502
Cdd:pfam15822  100 ------APTVPGPGPIGP--YPTPNMpfpELPRPYGAptdpAAAAPSGPWGSM-SSGPWAPGMG---------------- 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767951847   503 GQQPSfQQLPTCPPlQPHPGLHHQSSPPHPHHQPWAQLHPSPQNTPQKVPVHQHSPSEPFLEKPVPDMTQV-SGP 576
Cdd:pfam15822  155 GQYPA-PNMPYPSP-GPYPAVPPPQSPGAAPPVPWGTVPPGPWGPPAPYPDPTGSYPMPGLYPTPNNPFQVpSGP 227
CD_HP1_like cd18960
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
884-934 2.96e-03

chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; uncharacterized subgroup; CHRomatin Organization Modifier (chromo) domain of mammalian HP1alpha (Cbx5), HP1beta (Cbx1), HP1gamma (Cbx5), and similar proteins. HP1 has diverse functions in heterochromatin formation and impacts both gene expression and gene silencing. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3).


Pssm-ID: 349316  Cd Length: 51  Bit Score: 37.15  E-value: 2.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767951847  884 VDRIMDfARSTDDRGEpvtHYLVKWCSLPYEDSTWERRQDIDQAK-IEEFEK 934
Cdd:cd18960     4 VERILD-KRLGRNGGE---EFLIKWQGFPESDSSWEPRENLQCDEmLEEFEK 51
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
883-925 5.74e-03

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349322  Cd Length: 49  Bit Score: 36.49  E-value: 5.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 767951847  883 EVDRIMDfarSTDDRGEpvTHYLVKWCSLPYEDSTWERRQDID 925
Cdd:cd18966     2 EVERILA---ERRDDGG--KRYLVKWEGYPLEEATWEPEENIG 39
ARG80 COG5068
Regulator of arginine metabolism and related MADS box-containing transcription factors ...
201-409 7.87e-03

Regulator of arginine metabolism and related MADS box-containing transcription factors [Transcription];


Pssm-ID: 227400 [Multi-domain]  Cd Length: 412  Bit Score: 40.77  E-value: 7.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  201 QQHGQPQQRMSQFSQGQEGLNQGNPFIATSGPG-HLSHVPQQSPSMAPSLRHSVQQFH--HHPSTALHGESVahSPRFSP 277
Cdd:COG5068   208 QQYQQHSSRKDHPTVPHSNTNNGRPPAKFMIPElHSSHSTLDLPSDFISDSGFPNQSStsIFPLDSAIIQIT--PPHLPN 285
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951847  278 NPPQQGAVRPQtLNFSSRSQTVPSPTINNSGQYSRYPYSNLNQGLvnntgmnqnlgltnntpmnqsvPRYPNAVGFPSNS 357
Cdd:COG5068   286 NPPQENRHELY-SNDSSMVSETPPPKNLPNGSPNQSPLNNLSRGN----------------------PASPNSIIRENNQ 342
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767951847  358 GQGLMHQ----QPIHPSG-SLNQMNTQTMHPSqpQGTYASPPPMSPMK-AMSNPAGTP 409
Cdd:COG5068   343 VEDESFNgrqgSAIWNALiSTTQPNSGLHTEA--STAPSSTIPADPLKnAAQTNSGTR 398
CD1_tandem_CHD1-2_like cd18666
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
826-860 8.29e-03

repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and 2, and similar proteins; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 and CHD2. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349313  Cd Length: 85  Bit Score: 36.89  E-value: 8.29e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 767951847  826 FYVKYKNFSYLHCQWASIEDLEkdkriQQKIKRFK 860
Cdd:cd18666    49 YLIKWKGWSHIHNTWESEESLK-----DQNVKGMK 78
 
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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