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Conserved domains on  [gi|334187075|ref|NP_001190884|]
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chromatin remodeling factor [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
72-633 1.07e-138

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 435.81  E-value: 1.07e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075   72 ASLVWFNAAMDVFIAENGAHEFIAIRPEWKTVDRIIACREGDDGEEYLVKYKELSYRNSY--WESESDISDFQNEIQRFK 149
Cdd:COG0553   128 LLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLalLELALLAAEAELLLLLEL 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  150 DINSSSRRDKYVENERNREEFKQFDLTPEFLTGTLHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEE 229
Cdd:COG0553   208 LLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKER 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  230 NLS-PHLVVAPLSTIRNWEREFATWAPHMNVVMYTGDSEARDVIWEHEfyfsegrksKFDVLLTTYEMVHPGISVLSPIK 308
Cdd:COG0553   288 GLArPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRERAKGANPFE---------DADLVITSYGLLRRDIELLAAVD 358
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  309 WTCMIIDEGHRLKNQKSKLYSSLSQFTSKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQD-----INK--EEQI 381
Cdd:COG0553   359 WDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRErfarpIEKgdEEAL 438
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  382 SRLHQMLAPHLLRRLKKDVLKDkVPPKKELILRVDMSSQQKEVYKAVITN-----NYQVLTKKRDAKISnVLMKLRQVCS 456
Cdd:COG0553   439 ERLRRLLRPFLLRRTKEDVLKD-LPEKTEETLYVELTPEQRALYEAVLEYlrrelEGAEGIRRRGLILA-ALTRLRQICS 516
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  457 HPYLLPDFEPRFEdaneaftkllEASGKLQLLDKMMVKLKEQGHRVLIYTQFQHTLYLLEDYFTFKNWNYERIDGKISGP 536
Cdd:COG0553   517 HPALLLEEGAELS----------GRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAE 586
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  537 ERQVRIDRFNAENSNRFcFLLSTRAGGIGINLATADTVIIYDSDWNPHADLQAMARVHRLGQTNKVMIYRLIHKGTVEER 616
Cdd:COG0553   587 ERDELVDRFQEGPEAPV-FLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEK 665
                         570
                  ....*....|....*..
gi 334187075  617 MMEITKNKMLLEHLVVG 633
Cdd:COG0553   666 ILELLEEKRALAESVLG 682
CHDII_SANT-like pfam06461
CHD subfamily II, SANT-like domain; CHD proteins (name derived from the presence of a ...
815-958 1.17e-70

CHD subfamily II, SANT-like domain; CHD proteins (name derived from the presence of a Chromodomain, SWI2/SNF2 ATPase/Helicase and a motif with sequence similarity to a DNA)binding domain) are ATP-dependent chromatin remodelers found in plant and animals. In eukaryotes, there are three subfamilies, I, II and III. This domain is found in members of subfamily II which play a role in repression of genes involved in developmental regulation, including Mi-2 from Drosophila melanogaster, CHD3/4/5 from animals and PICKLE (a CHD3/4-related protein) from Arabidopsis. Sequence analysis revealed that this domain has a considerable similarity to SANT domains suggesting that it fold into this type of domain and it is integral to the DNA binding domain of CHD remodelers in subfamily II.


:

Pssm-ID: 461920  Cd Length: 137  Bit Score: 231.87  E-value: 1.17e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075   815 PRTVTRPYRKRAR-DNSEEIPLMEGEGRYLMVLGFNETERDIFLRTFKRYGAGNFDWKEFVNPLYMKTYDEINKYGILFL 893
Cdd:pfam06461    1 PQTGRRPYRRRARvDKDEPLPLMEGEGGSIEVLGFNARQRKAFLNALMRYGMGNFDWKEFVRDLRGKTEKEIKAYGSLFL 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187075   894 KHIAENPTDNSTNFkvitamvyADGVPKEGISSDELLVSMTFMMLVKEKCQFLDNHPTAPVFSNY 958
Cdd:pfam06461   81 RHICEPGADNSETF--------ADGVPKEGLSRQDVLTRIGVMSLIRKKVQEFEHIPGKPSFPDL 137
DUF1087 super family cl05792
CHD subfamily II, DUF1087; This domain is found in chromatin remodelling factors (CHDs) from ...
733-775 6.96e-15

CHD subfamily II, DUF1087; This domain is found in chromatin remodelling factors (CHDs) from subfamily II including CHD3/4/5 from animals and PICKLE. from Arabidopsis. The exact function is, as yet, unknown.


The actual alignment was detected with superfamily member pfam06465:

Pssm-ID: 461922  Cd Length: 60  Bit Score: 70.14  E-value: 6.96e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 334187075   733 NADRTSHWKDLLKDKYEVQQAEELSALGKRKRNGKQVMYAEDD 775
Cdd:pfam06465   17 ESEDPNYWEKLLKHHYEQQQEEEFNALGKGKRSRKQVVSVEED 59
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
72-633 1.07e-138

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 435.81  E-value: 1.07e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075   72 ASLVWFNAAMDVFIAENGAHEFIAIRPEWKTVDRIIACREGDDGEEYLVKYKELSYRNSY--WESESDISDFQNEIQRFK 149
Cdd:COG0553   128 LLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLalLELALLAAEAELLLLLEL 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  150 DINSSSRRDKYVENERNREEFKQFDLTPEFLTGTLHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEE 229
Cdd:COG0553   208 LLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKER 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  230 NLS-PHLVVAPLSTIRNWEREFATWAPHMNVVMYTGDSEARDVIWEHEfyfsegrksKFDVLLTTYEMVHPGISVLSPIK 308
Cdd:COG0553   288 GLArPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRERAKGANPFE---------DADLVITSYGLLRRDIELLAAVD 358
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  309 WTCMIIDEGHRLKNQKSKLYSSLSQFTSKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQD-----INK--EEQI 381
Cdd:COG0553   359 WDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRErfarpIEKgdEEAL 438
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  382 SRLHQMLAPHLLRRLKKDVLKDkVPPKKELILRVDMSSQQKEVYKAVITN-----NYQVLTKKRDAKISnVLMKLRQVCS 456
Cdd:COG0553   439 ERLRRLLRPFLLRRTKEDVLKD-LPEKTEETLYVELTPEQRALYEAVLEYlrrelEGAEGIRRRGLILA-ALTRLRQICS 516
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  457 HPYLLPDFEPRFEdaneaftkllEASGKLQLLDKMMVKLKEQGHRVLIYTQFQHTLYLLEDYFTFKNWNYERIDGKISGP 536
Cdd:COG0553   517 HPALLLEEGAELS----------GRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAE 586
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  537 ERQVRIDRFNAENSNRFcFLLSTRAGGIGINLATADTVIIYDSDWNPHADLQAMARVHRLGQTNKVMIYRLIHKGTVEER 616
Cdd:COG0553   587 ERDELVDRFQEGPEAPV-FLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEK 665
                         570
                  ....*....|....*..
gi 334187075  617 MMEITKNKMLLEHLVVG 633
Cdd:COG0553   666 ILELLEEKRALAESVLG 682
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
177-658 2.34e-137

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 443.09  E-value: 2.34e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  177 PEFLTGTLHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEEN--LSPHLVVAPLSTIRNWEREFATWA 254
Cdd:PLN03142  163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRgiTGPHMVVAPKSTLGNWMNEIRRFC 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  255 PHMNVVMYTGDSEARDVIweHEFYFSEGrksKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQF 334
Cdd:PLN03142  243 PVLRAVKFHGNPEERAHQ--REELLVAG---KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLF 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  335 TSKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQDI-------NKEEQISRLHQMLAPHLLRRLKKDVLKDkVPP 407
Cdd:PLN03142  318 STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWfqisgenDQQEVVQQLHKVLRPFLLRRLKSDVEKG-LPP 396
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  408 KKELILRVDMSSQQKEVYKAVITNNYQVLTKKRD-AKISNVLMKLRQVCSHPYLLPDFEPrfedaNEAFTK---LLEASG 483
Cdd:PLN03142  397 KKETILKVGMSQMQKQYYKALLQKDLDVVNAGGErKRLLNIAMQLRKCCNHPYLFQGAEP-----GPPYTTgehLVENSG 471
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  484 KLQLLDKMMVKLKEQGHRVLIYTQFQHTLYLLEDYFTFKNWNYERIDGKISGPERQVRIDRFNAENSNRFCFLLSTRAGG 563
Cdd:PLN03142  472 KMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGG 551
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  564 IGINLATADTVIIYDSDWNPHADLQAMARVHRLGQTNKVMIYRLIHKGTVEERMMEITKNKMLLEHLVVGKQHLCQ---- 639
Cdd:PLN03142  552 LGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEqktv 631
                         490       500
                  ....*....|....*....|.
gi 334187075  640 --DELDDIIKYGSKELFSEEN 658
Cdd:PLN03142  632 nkDELLQMVRYGAEMVFSSKD 652
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
183-395 1.79e-96

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: 306.20  E-value: 1.79e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  183 TLHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLF--EENLSPHLVVAPLSTIRNWEREFATWAPHMNVV 260
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFhsQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  261 MYTGDSEARDVIWEHEFYFSEGRKSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQFTSKHIV 340
Cdd:cd17993    81 VYLGDIKSRDTIREYEFYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 334187075  341 LLTGTPLQNNLNELFALMHFLDADKFGSLEKF---QDINKEEQISRLHQMLAPHLLRR 395
Cdd:cd17993   161 LITGTPLQNSLKELWALLHFLMPGKFDIWEEFeeeHDEEQEKGIADLHKELEPFILRR 218
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
187-461 9.43e-83

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: 271.48  E-value: 9.43e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075   187 YQLEGLNFLRYSWSK-KTNVILADEMGLGKTIQSIAFLASLFEENL---SPHLVVAPLSTIRNWEREFATWA--PHMNVV 260
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKnwgGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075   261 MYTGDSEARdviweHEFYFSEGRKSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQFTSKHIV 340
Cdd:pfam00176   81 VLHGNKRPQ-----ERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRW 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075   341 LLTGTPLQNNLNELFALMHFLDADKFGSLEKFQD--------INKEEQISRLHQMLAPHLLRRLKKDVLKDkVPPKKELI 412
Cdd:pfam00176  156 ILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNwfdrpierGGGKKGVSRLHKLLKPFLLRRTKKDVEKS-LPPKVEYI 234
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 334187075   413 LRVDMSSQQKEVYKAVIT--NNYQVLT----KKRDAKISNVLMKLRQVCSHPYLL 461
Cdd:pfam00176  235 LFCRLSKLQRKLYQTFLLkkDLNAIKTgeggREIKASLLNILMRLRKICNHPGLI 289
CHDII_SANT-like pfam06461
CHD subfamily II, SANT-like domain; CHD proteins (name derived from the presence of a ...
815-958 1.17e-70

CHD subfamily II, SANT-like domain; CHD proteins (name derived from the presence of a Chromodomain, SWI2/SNF2 ATPase/Helicase and a motif with sequence similarity to a DNA)binding domain) are ATP-dependent chromatin remodelers found in plant and animals. In eukaryotes, there are three subfamilies, I, II and III. This domain is found in members of subfamily II which play a role in repression of genes involved in developmental regulation, including Mi-2 from Drosophila melanogaster, CHD3/4/5 from animals and PICKLE (a CHD3/4-related protein) from Arabidopsis. Sequence analysis revealed that this domain has a considerable similarity to SANT domains suggesting that it fold into this type of domain and it is integral to the DNA binding domain of CHD remodelers in subfamily II.


Pssm-ID: 461920  Cd Length: 137  Bit Score: 231.87  E-value: 1.17e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075   815 PRTVTRPYRKRAR-DNSEEIPLMEGEGRYLMVLGFNETERDIFLRTFKRYGAGNFDWKEFVNPLYMKTYDEINKYGILFL 893
Cdd:pfam06461    1 PQTGRRPYRRRARvDKDEPLPLMEGEGGSIEVLGFNARQRKAFLNALMRYGMGNFDWKEFVRDLRGKTEKEIKAYGSLFL 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187075   894 KHIAENPTDNSTNFkvitamvyADGVPKEGISSDELLVSMTFMMLVKEKCQFLDNHPTAPVFSNY 958
Cdd:pfam06461   81 RHICEPGADNSETF--------ADGVPKEGLSRQDVLTRIGVMSLIRKKVQEFEHIPGKPSFPDL 137
DEXDc smart00487
DEAD-like helicases superfamily;
176-359 6.79e-27

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 109.12  E-value: 6.79e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075    176 TPEFLTGTLHTYQLEGLNFLrysWSKKTNVILADEMGLGKTIQ-SIAFLASLFEENLSPHLVVAPL-STIRNWEREFATW 253
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAaLLPALEALKRGKGGRVLVLVPTrELAEQWAEELKKL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075    254 APHMN---VVMYTGDSEARDviwehefyFSEGRKSKFDVLLTTYEMV--HPGISVLSPIKWTCMIIDEGHRLKNQ--KSK 326
Cdd:smart00487   78 GPSLGlkvVGLYGGDSKREQ--------LRKLESGKTDILVTTPGRLldLLENDKLSLSNVDLVILDEAHRLLDGgfGDQ 149
                           170       180       190
                    ....*....|....*....|....*....|....
gi 334187075    327 LYSSLSQF-TSKHIVLLTGTPLQNNLNELFALMH 359
Cdd:smart00487  150 LEKLLKLLpKNVQLLLLSATPPEEIENLLELFLN 183
DUF1087 pfam06465
CHD subfamily II, DUF1087; This domain is found in chromatin remodelling factors (CHDs) from ...
733-775 6.96e-15

CHD subfamily II, DUF1087; This domain is found in chromatin remodelling factors (CHDs) from subfamily II including CHD3/4/5 from animals and PICKLE. from Arabidopsis. The exact function is, as yet, unknown.


Pssm-ID: 461922  Cd Length: 60  Bit Score: 70.14  E-value: 6.96e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 334187075   733 NADRTSHWKDLLKDKYEVQQAEELSALGKRKRNGKQVMYAEDD 775
Cdd:pfam06465   17 ESEDPNYWEKLLKHHYEQQQEEEFNALGKGKRSRKQVVSVEED 59
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
72-633 1.07e-138

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 435.81  E-value: 1.07e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075   72 ASLVWFNAAMDVFIAENGAHEFIAIRPEWKTVDRIIACREGDDGEEYLVKYKELSYRNSY--WESESDISDFQNEIQRFK 149
Cdd:COG0553   128 LLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLalLELALLAAEAELLLLLEL 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  150 DINSSSRRDKYVENERNREEFKQFDLTPEFLTGTLHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEE 229
Cdd:COG0553   208 LLELELLAEAAVDAFRLRRLREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKER 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  230 NLS-PHLVVAPLSTIRNWEREFATWAPHMNVVMYTGDSEARDVIWEHEfyfsegrksKFDVLLTTYEMVHPGISVLSPIK 308
Cdd:COG0553   288 GLArPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRERAKGANPFE---------DADLVITSYGLLRRDIELLAAVD 358
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  309 WTCMIIDEGHRLKNQKSKLYSSLSQFTSKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQD-----INK--EEQI 381
Cdd:COG0553   359 WDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRErfarpIEKgdEEAL 438
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  382 SRLHQMLAPHLLRRLKKDVLKDkVPPKKELILRVDMSSQQKEVYKAVITN-----NYQVLTKKRDAKISnVLMKLRQVCS 456
Cdd:COG0553   439 ERLRRLLRPFLLRRTKEDVLKD-LPEKTEETLYVELTPEQRALYEAVLEYlrrelEGAEGIRRRGLILA-ALTRLRQICS 516
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  457 HPYLLPDFEPRFEdaneaftkllEASGKLQLLDKMMVKLKEQGHRVLIYTQFQHTLYLLEDYFTFKNWNYERIDGKISGP 536
Cdd:COG0553   517 HPALLLEEGAELS----------GRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAE 586
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  537 ERQVRIDRFNAENSNRFcFLLSTRAGGIGINLATADTVIIYDSDWNPHADLQAMARVHRLGQTNKVMIYRLIHKGTVEER 616
Cdd:COG0553   587 ERDELVDRFQEGPEAPV-FLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEK 665
                         570
                  ....*....|....*..
gi 334187075  617 MMEITKNKMLLEHLVVG 633
Cdd:COG0553   666 ILELLEEKRALAESVLG 682
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
177-658 2.34e-137

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 443.09  E-value: 2.34e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  177 PEFLTGTLHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEEN--LSPHLVVAPLSTIRNWEREFATWA 254
Cdd:PLN03142  163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRgiTGPHMVVAPKSTLGNWMNEIRRFC 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  255 PHMNVVMYTGDSEARDVIweHEFYFSEGrksKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQF 334
Cdd:PLN03142  243 PVLRAVKFHGNPEERAHQ--REELLVAG---KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLF 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  335 TSKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQDI-------NKEEQISRLHQMLAPHLLRRLKKDVLKDkVPP 407
Cdd:PLN03142  318 STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWfqisgenDQQEVVQQLHKVLRPFLLRRLKSDVEKG-LPP 396
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  408 KKELILRVDMSSQQKEVYKAVITNNYQVLTKKRD-AKISNVLMKLRQVCSHPYLLPDFEPrfedaNEAFTK---LLEASG 483
Cdd:PLN03142  397 KKETILKVGMSQMQKQYYKALLQKDLDVVNAGGErKRLLNIAMQLRKCCNHPYLFQGAEP-----GPPYTTgehLVENSG 471
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  484 KLQLLDKMMVKLKEQGHRVLIYTQFQHTLYLLEDYFTFKNWNYERIDGKISGPERQVRIDRFNAENSNRFCFLLSTRAGG 563
Cdd:PLN03142  472 KMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGG 551
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  564 IGINLATADTVIIYDSDWNPHADLQAMARVHRLGQTNKVMIYRLIHKGTVEERMMEITKNKMLLEHLVVGKQHLCQ---- 639
Cdd:PLN03142  552 LGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEqktv 631
                         490       500
                  ....*....|....*....|.
gi 334187075  640 --DELDDIIKYGSKELFSEEN 658
Cdd:PLN03142  632 nkDELLQMVRYGAEMVFSSKD 652
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
183-395 1.79e-96

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: 306.20  E-value: 1.79e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  183 TLHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLF--EENLSPHLVVAPLSTIRNWEREFATWAPHMNVV 260
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFhsQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  261 MYTGDSEARDVIWEHEFYFSEGRKSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQFTSKHIV 340
Cdd:cd17993    81 VYLGDIKSRDTIREYEFYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 334187075  341 LLTGTPLQNNLNELFALMHFLDADKFGSLEKF---QDINKEEQISRLHQMLAPHLLRR 395
Cdd:cd17993   161 LITGTPLQNSLKELWALLHFLMPGKFDIWEEFeeeHDEEQEKGIADLHKELEPFILRR 218
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
184-395 6.63e-89

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: 285.68  E-value: 6.63e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLF--EENLSPHLVVAPLSTIRNWEREFATWAPhMNVVM 261
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYqvEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  262 YTGDSEARDVIWEHEFYF--SEGRKS----KFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQFT 335
Cdd:cd17995    80 YHGSGESRQIIQQYEMYFkdAQGRKKkgvyKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334187075  336 SKHIVLLTGTPLQNNLNELFALMHFLDADKFGS----LEKFQDINKEEQISRLHQMLAPHLLRR 395
Cdd:cd17995   160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSseefLEEFGDLKTAEQVEKLQALLKPYMLRR 223
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
187-461 9.43e-83

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: 271.48  E-value: 9.43e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075   187 YQLEGLNFLRYSWSK-KTNVILADEMGLGKTIQSIAFLASLFEENL---SPHLVVAPLSTIRNWEREFATWA--PHMNVV 260
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKnwgGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075   261 MYTGDSEARdviweHEFYFSEGRKSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQFTSKHIV 340
Cdd:pfam00176   81 VLHGNKRPQ-----ERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRW 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075   341 LLTGTPLQNNLNELFALMHFLDADKFGSLEKFQD--------INKEEQISRLHQMLAPHLLRRLKKDVLKDkVPPKKELI 412
Cdd:pfam00176  156 ILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNwfdrpierGGGKKGVSRLHKLLKPFLLRRTKKDVEKS-LPPKVEYI 234
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 334187075   413 LRVDMSSQQKEVYKAVIT--NNYQVLT----KKRDAKISNVLMKLRQVCSHPYLL 461
Cdd:pfam00176  235 LFCRLSKLQRKLYQTFLLkkDLNAIKTgeggREIKASLLNILMRLRKICNHPGLI 289
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
184-395 9.48e-81

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: 262.38  E-value: 9.48e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEENLS--PHLVVAPLSTIRNWEREFATWAPHMNVVM 261
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSkgPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  262 YTGDSeardviwehefyfsegrkskfdVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQFTSKHIVL 341
Cdd:cd17994    81 YVGDH----------------------VLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLL 138
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 334187075  342 LTGTPLQNNLNELFALMHFLDADKF----GSLEKFQDINKEEQISRLHQMLAPHLLRR 395
Cdd:cd17994   139 LTGTPLQNNLEELFHLLNFLTPERFnnlqGFLEEFADISKEDQIKKLHDLLGPHMLRR 196
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
167-395 6.79e-76

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: 250.69  E-value: 6.79e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  167 REEFKQFDLTPEFLTGT---LHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEENL--SPHLVVAPLS 241
Cdd:cd18054     1 RPRFVALKKQPSYIGGEnleLRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQlyGPFLLVVPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  242 TIRNWEREFATWAPHMNVVMYTGDSEARDVIWEHEFYFSEGRKSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLK 321
Cdd:cd18054    81 TLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLK 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334187075  322 NQKSKLYSSLSQFTSKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQDIN---KEEQISRLHQMLAPHLLRR 395
Cdd:cd18054   161 NDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHgkgRENGYQSLHKVLEPFLLRR 237
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
184-362 1.41e-75

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: 247.48  E-value: 1.41e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEENLS--PHLVVAPLSTIRNWEREFATWAPHMNVVM 261
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKErgPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  262 YTGDSEARDVIWEHEfyfsegRKSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQFTSKHIVL 341
Cdd:cd17919    81 YHGSQRERAQIRAKE------KLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLL 154
                         170       180
                  ....*....|....*....|.
gi 334187075  342 LTGTPLQNNLNELFALMHFLD 362
Cdd:cd17919   155 LTGTPLQNNLEELWALLDFLD 175
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
184-395 2.18e-74

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: 246.08  E-value: 2.18e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEENLS--PHLVVAPLSTIRNWEREFATWAPHMNVVM 261
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTkgPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  262 YTGDSEARDVIWEHEFYFSE-----GRKS---------KFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKL 327
Cdd:cd18055    81 YTGDKDSRAIIRENEFSFDDnavkgGKKAfkmkreaqvKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334187075  328 YSSLSQFTSKHIVLLTGTPLQNNLNELFALMHFLDADKF----GSLEKFQDINKEEQISRLHQMLAPHLLRR 395
Cdd:cd18055   161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFnnleGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
184-395 4.77e-73

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: 242.28  E-value: 4.77e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEENLS--PHLVVAPLSTIRNWEREFATWAPHMNVVM 261
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSkgPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  262 YTGDSEARDVIWEHEFYFSE-----GRKS---------KFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKL 327
Cdd:cd18056    81 YVGDKDSRAIIRENEFSFEDnairgGKKAsrmkkeasvKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334187075  328 YSSLSQFTSKHIVLLTGTPLQNNLNELFALMHFLDADKF----GSLEKFQDINKEEQISRLHQMLAPHLLRR 395
Cdd:cd18056   161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFhnleGFLEEFADIAKEDQIKKLHDMLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
184-395 1.14e-72

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: 241.51  E-value: 1.14e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEENLS--PHLVVAPLSTIRNWEREFATWAPHMNVVM 261
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSkgPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  262 YTGDSEARDVIWEHEFYFSE-----GRKS---------KFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKL 327
Cdd:cd18057    81 YTGDKESRSVIRENEFSFEDnairsGKKVfrmkkeaqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334187075  328 YSSLSQFTSKHIVLLTGTPLQNNLNELFALMHFLDADKF----GSLEKFQDINKEEQISRLHQMLAPHLLRR 395
Cdd:cd18057   161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFnnleGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
CHDII_SANT-like pfam06461
CHD subfamily II, SANT-like domain; CHD proteins (name derived from the presence of a ...
815-958 1.17e-70

CHD subfamily II, SANT-like domain; CHD proteins (name derived from the presence of a Chromodomain, SWI2/SNF2 ATPase/Helicase and a motif with sequence similarity to a DNA)binding domain) are ATP-dependent chromatin remodelers found in plant and animals. In eukaryotes, there are three subfamilies, I, II and III. This domain is found in members of subfamily II which play a role in repression of genes involved in developmental regulation, including Mi-2 from Drosophila melanogaster, CHD3/4/5 from animals and PICKLE (a CHD3/4-related protein) from Arabidopsis. Sequence analysis revealed that this domain has a considerable similarity to SANT domains suggesting that it fold into this type of domain and it is integral to the DNA binding domain of CHD remodelers in subfamily II.


Pssm-ID: 461920  Cd Length: 137  Bit Score: 231.87  E-value: 1.17e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075   815 PRTVTRPYRKRAR-DNSEEIPLMEGEGRYLMVLGFNETERDIFLRTFKRYGAGNFDWKEFVNPLYMKTYDEINKYGILFL 893
Cdd:pfam06461    1 PQTGRRPYRRRARvDKDEPLPLMEGEGGSIEVLGFNARQRKAFLNALMRYGMGNFDWKEFVRDLRGKTEKEIKAYGSLFL 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187075   894 KHIAENPTDNSTNFkvitamvyADGVPKEGISSDELLVSMTFMMLVKEKCQFLDNHPTAPVFSNY 958
Cdd:pfam06461   81 RHICEPGADNSETF--------ADGVPKEGLSRQDVLTRIGVMSLIRKKVQEFEHIPGKPSFPDL 137
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
182-397 2.06e-70

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: 234.96  E-value: 2.06e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  182 GTLHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFE--ENLSPHLVVAPLSTIRNWEREFATWAPHMNV 259
Cdd:cd17996     2 GTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEkkKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  260 VMYTGDSEARDVIwehefyFSEGRKSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQ-FTSKH 338
Cdd:cd17996    82 IVYKGTPDVRKKL------QSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyYHARY 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334187075  339 IVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQD----------------INKEEQ---ISRLHQMLAPHLLRRLK 397
Cdd:cd17996   156 RLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQwfntpfantgeqvkieLNEEETlliIRRLHKVLRPFLLRRLK 233
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
182-397 1.24e-67

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: 227.27  E-value: 1.24e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  182 GTLHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEENL-SPHLVVAPLSTIRNWEREFATWAPHMNVV 260
Cdd:cd18009     2 GVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVwGPFLVIAPLSTLPNWVNEFARFTPSVPVL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  261 MYTGDSEARDVIwEHEFYFSEGRKSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQFTSKHIV 340
Cdd:cd18009    82 LYHGTKEERERL-RKKIMKREGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334187075  341 LLTGTPLQNNLNELFALMHFLDADKFGSLEKFQ----------------DINKEEQ---ISRLHQMLAPHLLRRLK 397
Cdd:cd18009   161 LLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFEswfdfsslsdnaadisNLSEEREqniVHMLHAILKPFLLRRLK 236
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
182-397 6.90e-66

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: 221.81  E-value: 6.90e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  182 GTLHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASL--FEENLSPHLVVAPLSTIRNWEREFATWAPHMNV 259
Cdd:cd17997     2 GTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLkhYKNINGPHLIIVPKSTLDNWMREFKRWCPSLRV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  260 VMYTGDSEARDVIWEHEFyfsegRKSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQFTSKHI 339
Cdd:cd17997    82 VVLIGDKEERADIIRDVL-----LPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNR 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334187075  340 VLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQ---DINKEEQ-----ISRLHQMLAPHLLRRLK 397
Cdd:cd17997   157 LLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDewfNVNNCDDdnqevVQRLHKVLRPFLLRRIK 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
184-395 9.44e-66

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: 221.47  E-value: 9.44e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEENL-SPHLVVAPLSTIRNWEREFATWApHMNVVMY 262
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIhGPFLVIAPLSTITNWEREFNTWT-EMNTIVY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  263 TGDSEARDVIWEHEFYF--SEGR----KSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQFTS 336
Cdd:cd18060    80 HGSLASRQMIQQYEMYCkdSRGRlipgAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334187075  337 KHIVLLTGTPLQNNLNELFALMHFLDADKFGS----LEKFQDINKEEQISRLHQMLAPHLLRR 395
Cdd:cd18060   160 EHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSesefLKDFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
184-395 1.50e-64

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: 217.99  E-value: 1.50e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEENL-SPHLVVAPLSTIRNWEREFATWApHMNVVMY 262
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIrGPFLIIAPLSTITNWEREFRTWT-EMNAIVY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  263 TGDSEARDVIWEHEFYFSEGRKS------KFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQFTS 336
Cdd:cd18058    80 HGSQISRQMIQQYEMYYRDEQGNplsgifKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMAL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334187075  337 KHIVLLTGTPLQNNLNELFALMHFLDADKFGS----LEKFQDINKEEQISRLHQMLAPHLLRR 395
Cdd:cd18058   160 EHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSettfLEEFGDLKTEEQVKKLQSILKPMMLRR 222
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
184-395 2.93e-61

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: 208.71  E-value: 2.93e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEENL-SPHLVVAPLSTIRNWEREFATWApHMNVVMY 262
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIrGPFLIIAPLSTIANWEREFRTWT-DLNVVVY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  263 TGDSEARDVIWEHEFYF--SEGR----KSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQFTS 336
Cdd:cd18061    80 HGSLISRQMIQQYEMYFrdSQGRiirgAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334187075  337 KHIVLLTGTPLQNNLNELFALMHFLDADKFGS----LEKFQDINKEEQISRLHQMLAPHLLRR 395
Cdd:cd18061   160 EHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSestfMQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
177-395 6.08e-61

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: 208.37  E-value: 6.08e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  177 PEFLTGT----LHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEEN--LSPHLVVAPLSTIRNWEREF 250
Cdd:cd18053    10 PSYIGGHegleLRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHqlYGPFLLVVPLSTLTSWQREI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  251 ATWAPHMNVVMYTGDSEARDVIWEHEFYFSEGRKSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSS 330
Cdd:cd18053    90 QTWAPQMNAVVYLGDINSRNMIRTHEWMHPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKT 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334187075  331 LSQFTSKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQDIN---KEEQISRLHQMLAPHLLRR 395
Cdd:cd18053   170 LIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHgkgREYGYASLHKELEPFLLRR 237
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
184-395 5.08e-60

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: 205.27  E-value: 5.08e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEENL-SPHLVVAPLSTIRNWEREFATWApHMNVVMY 262
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIhGPFLVIAPLSTIPNWEREFRTWT-ELNVVVY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  263 TGDSEARDVIWEHEFYF--SEGR----KSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQFTS 336
Cdd:cd18059    80 HGSQASRRTIQLYEMYFkdPQGRvikgSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334187075  337 KHIVLLTGTPLQNNLNELFALMHFLDADKFGS----LEKFQDINKEEQISRLHQMLAPHLLRR 395
Cdd:cd18059   160 EHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSettfMQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
184-395 2.55e-59

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: 203.05  E-value: 2.55e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASL-FEENL-SPHLVVAPLSTIRNWEREFATWAPHMNVVM 261
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLaGRLKLlGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  262 YTGDSEARDVIWEHEFYFSegrksKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQFTSKHIVL 341
Cdd:cd18006    81 YMGDKEKRLDLQQDIKSTN-----RFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334187075  342 LTGTPLQNNLNELFALMHFLDADKFGS------LEKFQDINKE-EQISRLHQMLAPHLLRR 395
Cdd:cd18006   156 LTGTPIQNSLQELYALLSFIEPNVFPKdklddfIKAYSETDDEsETVEELHLLLQPFLLRR 216
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
184-395 8.09e-59

DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or DOMO1) is the core catalytic component of the multiprotein chromatin-remodeling SRCAP complex, that is necessary for the incorporation of the histone variant H2A.Z into nucleosomes. SRCAP is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350761 [Multi-domain]  Cd Length: 223  Bit Score: 201.81  E-value: 8.09e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASL--FEENLSPHLVVAPLSTIRNWEREFATWAPHMNVVM 261
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLacEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  262 YTGDSEARdviweHEFYFSEGRKSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQFTSKHIVL 341
Cdd:cd18003    81 YYGSAKER-----KLKRQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334187075  342 LTGTPLQNNLNELFALMHFLDADKFGSLEKF---------------QDINkEEQISRLHQMLAPHLLRR 395
Cdd:cd18003   156 LTGTPLQNSLMELWSLMHFLMPHIFQSHQEFkewfsnpltamsegsQEEN-EELVRRLHKVLRPFLLRR 223
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
180-397 5.55e-55

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: 190.47  E-value: 5.55e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  180 LTGTLHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEENLS-PHLVVAPLSTIRNWEREFATWAPHMN 258
Cdd:cd18012     1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKgPSLVVAPTSLIYNWEEEAAKFAPELK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  259 VVMYTGDSEARDVIWEHEFYfsegrkskfDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQFTSKH 338
Cdd:cd18012    81 VLVIHGTKRKREKLRALEDY---------DLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADH 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334187075  339 IVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQD-----INK---EEQISRLHQMLAPHLLRRLK 397
Cdd:cd18012   152 RLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKrfakpIEKdgdEEALEELKKLISPFILRRLK 218
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
184-361 1.68e-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: 185.28  E-value: 1.68e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEENLS-PHLVVAPLSTIRNWEREFATWAPHMNVVMY 262
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPgPHLVVVPSSTLDNWLREFKRWCPSLKVEPY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  263 TGDSEARdviwEHEFYFSEGRKSKFDVLLTTYEMVHPG---ISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQFTSKHI 339
Cdd:cd17998    81 YGSQEER----KHLRYDILKGLEDFDVIVTTYNLATSNpddRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANFR 156
                         170       180
                  ....*....|....*....|..
gi 334187075  340 VLLTGTPLQNNLNELFALMHFL 361
Cdd:cd17998   157 LLLTGTPLQNNLLELMSLLNFI 178
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
482-608 2.54e-53

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 182.29  E-value: 2.54e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  482 SGKLQLLDKMMVKLKEQGHRVLIYTQFQHTLYLLEDYFTFKNWNYERIDGKISGPERQVRIDRFNaENSNRFCFLLSTRA 561
Cdd:cd18793    10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFN-EDPDIRVFLLSTKA 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 334187075  562 GGIGINLATADTVIIYDSDWNPHADLQAMARVHRLGQTNKVMIYRLI 608
Cdd:cd18793    89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
184-395 1.24e-50

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: 178.47  E-value: 1.24e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEEN--LSPHLVVAPLSTIRNWEREFATWAPHMNVVM 261
Cdd:cd18002     1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHniWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  262 YTGDSEARDVI---WEHEFYFseGRKSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQFTSKH 338
Cdd:cd18002    81 YWGNPKDRKVLrkfWDRKNLY--TRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRN 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334187075  339 IVLLTGTPLQNNLNELFALMHFLDADKFGSLEKF-----QDIN---------KEEQISRLHQMLAPHLLRR 395
Cdd:cd18002   159 RLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFnewfsKDIEshaenktglNEHQLKRLHMILKPFMLRR 229
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
184-395 2.57e-50

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: 177.56  E-value: 2.57e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEENLSPH-LVVAPLSTIRNWEREFATWAPHMNVVMY 262
Cdd:cd18001     1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSvLVVMPTSLIPHWVKEFAKWTPGLRVKVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  263 TGDS-EARDVIWEHefyfsegRKSKFDVLLTTYEMVHPGISVLSP-----IKWTCMIIDEGHRLKNQKSKLYSSLSQFTS 336
Cdd:cd18001    81 HGTSkKERERNLER-------IQRGGGVLLTTYGMVLSNTEQLSAddhdeFKWDYVILDEGHKIKNSKTKSAKSLREIPA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  337 KHIVLLTGTPLQNNLNELFALMHFL-DADKFGSLEKFqDINKEEQISR--------------------LHQMLAPHLLRR 395
Cdd:cd18001   154 KNRIILTGTPIQNNLKELWALFDFAcNGSLLGTRKTF-KMEFENPITRgrdkdatqgekalgsevaenLRQIIKPYFLRR 232
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
172-397 8.00e-50

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: 176.36  E-value: 8.00e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  172 QFDLTPEFLTG-TLHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASL--FEENLSPHLVVAPLSTIRNWER 248
Cdd:cd18065     3 RFEESPSYVKGgTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLkhYRNIPGPHMVLVPKSTLHNWMN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  249 EFATWAPHMNVVMYTGDSEARDViweheFYFSEGRKSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLY 328
Cdd:cd18065    83 EFKRWVPSLRAVCLIGDKDARAA-----FIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLS 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334187075  329 SSLSQFTSKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQD-------INKEEQISRLHQMLAPHLLRRLK 397
Cdd:cd18065   158 EIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSwfdtkncLGDQKLVERLHAVLKPFLLRRIK 233
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
172-409 4.81e-49

DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 (SMARCA5, also called SNF2H) is the catalytic subunit of the four known chromatin-remodeling complexes: CHRAC, RSF, ACF/WCRF, and WICH. SMARCA5 plays a major role organising arrays of nucleosomes adjacent to the binding sites for the architectural transcription factor CTCF sites and acts to promote CTCF binding SMARCA5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350822 [Multi-domain]  Cd Length: 244  Bit Score: 174.47  E-value: 4.81e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  172 QFDLTPEFLT-GTLHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASL--FEENLSPHLVVAPLSTIRNWER 248
Cdd:cd18064     3 RFEDSPSYVKwGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMkhYRNIPGPHMVLVPKSTLHNWMA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  249 EFATWAPHMNVVMYTGDSEARDVIWEHEFYFSEgrkskFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLY 328
Cdd:cd18064    83 EFKRWVPTLRAVCLIGDKDQRAAFVRDVLLPGE-----WDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  329 SSLSQFTSKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQD-------INKEEQISRLHQMLAPHLLRRLKKDVL 401
Cdd:cd18064   158 EIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSwfdtnncLGDQKLVERLHMVLRPFLLRRIKADVE 237

                  ....*...
gi 334187075  402 KdKVPPKK 409
Cdd:cd18064   238 K-SLPPKK 244
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
179-397 2.20e-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: 172.94  E-value: 2.20e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  179 FLTGTLHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEENL--SPHLVVAPLSTIRNWEREFATWAPH 256
Cdd:cd18063    19 LINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRlnGPYLIIVPLSTLSNWTYEFDKWAPS 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  257 MNVVMYTGDSEARDVIwehefyFSEGRKSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSL-SQFT 335
Cdd:cd18063    99 VVKISYKGTPAMRRSL------VPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYV 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334187075  336 SKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQ--------------DINKEEQ---ISRLHQMLAPHLLRRLK 397
Cdd:cd18063   173 APRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEqwfnapfamtgervDLNEEETiliIRRLHKVLRPFLLRRLK 251
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
179-397 1.13e-47

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: 171.00  E-value: 1.13e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  179 FLTGTLHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEENL--SPHLVVAPLSTIRNWEREFATWAPH 256
Cdd:cd18062    19 LVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRinGPFLIIVPLSTLSNWVYEFDKWAPS 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  257 MNVVMYTGDSEARDViwehefYFSEGRKSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSL-SQFT 335
Cdd:cd18062    99 VVKVSYKGSPAARRA------FVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYV 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334187075  336 SKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQ--------------DINKEEQ---ISRLHQMLAPHLLRRLK 397
Cdd:cd18062   173 APRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEqwfnapfamtgekvDLNEEETiliIRRLHKVLRPFLLRRLK 251
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
184-407 1.45e-45

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


Pssm-ID: 350763 [Multi-domain]  Cd Length: 245  Bit Score: 164.47  E-value: 1.45e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFE--------ENLSPH--------------LVVAPLS 241
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGktgtrrdrENNRPRfkkkppassakkpvLIVAPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  242 TIRNWEREFATWApHMNVVMYTGDSEARDVIwehefyfSEGRKSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLK 321
Cdd:cd18005    81 VLYNWKDELDTWG-HFEVGVYHGSRKDDELE-------GRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  322 NQKSKLYSSLSQFTSKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQDiNKEEQISRLHQMLAPHLLRRL---KK 398
Cdd:cd18005   153 NPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKK-HFSEPIKRGQRHTATARELRLgrkRK 231

                  ....*....
gi 334187075  399 DVLKDKVPP 407
Cdd:cd18005   232 QELAVKLSK 240
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
184-373 1.20e-43

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


Pssm-ID: 350762 [Multi-domain]  Cd Length: 240  Bit Score: 158.99  E-value: 1.20e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFL-----RYSWSKKTNVILADEMGLGKTIQSIAFLASLFE--ENLSPH----LVVAPLSTIRNWEREFAT 252
Cdd:cd18004     1 LRPHQREGVQFLydcltGRRGYGGGGAILADEMGLGKTLQAIALVWTLLKqgPYGKPTakkaLIVCPSSLVGNWKAEFDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  253 WAPHMNVVMYTGDSEARDVIWEHEFYFSEGRkskFDVLLTTYEMVHPGISVLS-PIKWTCMIIDEGHRLKNQKSKLYSSL 331
Cdd:cd18004    81 WLGLRRIKVVTADGNAKDVKASLDFFSSAST---YPVLIISYETLRRHAEKLSkKISIDLLICDEGHRLKNSESKTTKAL 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 334187075  332 SQFTSKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQ 373
Cdd:cd18004   158 NSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFR 199
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
184-360 4.36e-41

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: 149.78  E-value: 4.36e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLASLFEENLS--PHLVVAPLSTIRNWEREFATWAPHMNVVM 261
Cdd:cd18000     1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGlgPSLIVCPATVLKQWVKEFHRWWPPFRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  262 ------YTGDSEARDVIWEHEFYFSEGRKsKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQFT 335
Cdd:cd18000    81 lhssgsGTGSEEKLGSIERKSQLIRKVVG-DGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLR 159
                         170       180
                  ....*....|....*....|....*
gi 334187075  336 SKHIVLLTGTPLQNNLNELFALMHF 360
Cdd:cd18000   160 TPHRLILSGTPIQNNLKELWSLFDF 184
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
184-395 4.45e-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: 145.57  E-value: 4.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYSWSKKTNVILADEMGLGKTIQSIAFLAS-------LFEENLSPHLVVAPLSTIRNWEREFATWAPH 256
Cdd:cd17999     1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASdhhkranSFNSENLPSLVVCPPTLVGHWVAEIKKYFPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  257 --MNVVMYTGDSEARDVIwEHEFyfsegrkSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQF 334
Cdd:cd17999    81 afLKPLAYVGPPQERRRL-REQG-------EKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  335 TSKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQD-----IN---------KEEQ-----ISRLHQMLAPHLLRR 395
Cdd:cd17999   153 KANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRrflkpILasrdskasaKEQEagalaLEALHKQVLPFLLRR 232
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
184-374 3.08e-38

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: 143.20  E-value: 3.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFL-------RYSWSKKTNVILADEMGLGKTIQSIAFLASL---FEENLSPhLVVAPLSTIRNWEREFATW 253
Cdd:cd18007     1 LKPHQVEGVRFLwsnlvgtDVGSDEGGGCILAHTMGLGKTLQVITFLHTYlaaAPRRSRP-LVLCPASTLYNWEDEFKKW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  254 AP------HMNVVM-YTGDSEAR-DVI--WehefyFSEGrkskfDVLLTTYEM----VHPGISVLSP----IKWTCM--- 312
Cdd:cd18007    80 LPpdlrplLVLVSLsASKRADARlRKInkW-----HKEG-----GVLLIGYELfrnlASNATTDPRLkqefIAALLDpgp 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187075  313 ---IIDEGHRLKNQKSKLYSSLSQFTSKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQD 374
Cdd:cd18007   150 dllVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKK 214
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
184-395 3.17e-38

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: 143.20  E-value: 3.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYSWSkktnvILADEMGLGKTIQSIAFLAS-----------LFEENLSPH--------LVVAPLSTIR 244
Cdd:cd18008     1 LLPYQKQGLAWMLPRGG-----ILADEMGLGKTIQALALILAtrpqdpkipeeLEENSSDPKklylskttLIVVPLSLLS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  245 NWEREFA--TWAPHMNVVMYTGDSEARDVIWehefyfsegrKSKFDVLLTTYEMV----------------HPGISVLSP 306
Cdd:cd18008    76 QWKDEIEkhTKPGSLKVYVYHGSKRIKSIEE----------LSDYDIVITTYGTLasefpknkkgggrdskEKEASPLHR 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  307 IKWTCMIIDEGHRLKNQKSKLYSSLSQFTSKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKF-QDI------NKEE 379
Cdd:cd18008   146 IRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFnSDIskpfskNDRK 225
                         250
                  ....*....|....*.
gi 334187075  380 QISRLHQMLAPHLLRR 395
Cdd:cd18008   226 ALERLQALLKPILLRR 241
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
184-378 2.61e-31

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: 123.03  E-value: 2.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYS-----WSKKTNVILADEMGLGKTIQSIAFLASLFEEN-------LSPHLVVAPLSTIRNWEREFA 251
Cdd:cd18066     1 LRPHQREGIEFLYECvmgmrVNERFGAILADEMGLGKTLQCISLIWTLLRQGpyggkpvIKRALIVTPGSLVKNWKKEFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  252 TWAPHMNVVMYTGDSEARdviwEHEFYFSegrkSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSL 331
Cdd:cd18066    81 KWLGSERIKVFTVDQDHK----VEEFIAS----PLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTAL 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 334187075  332 SQFTSKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQDINKE 378
Cdd:cd18066   153 TSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEE 199
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
184-372 5.55e-30

DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a like 1, also known as HARP) is recruited to stalled replication forks to promote repair and helps restart replication. It plays a role in DNA repair, telomere maintenance and replication fork stability in response to DNA replication stress. Mutations cause Schimke Immunoosseous Dysplasia. SMARCAL1 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350768 [Multi-domain]  Cd Length: 213  Bit Score: 118.46  E-value: 5.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNF-LRyswsKKTNVILADEMGLGKTIQSIAFLASLFEEnlSPHLVVAPLSTIRNWEREFATWAPHM----- 257
Cdd:cd18010     1 LLPFQREGVCFaLR----RGGRVLIADEMGLGKTVQAIAIAAYYREE--WPLLIVCPSSLRLTWADEIERWLPSLppddi 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  258 NVVMytgdsEARDVIwehefyfsegRKSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQFT-- 335
Cdd:cd18010    75 QVIV-----KSKDGL----------RDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLLkr 139
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 334187075  336 SKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKF 372
Cdd:cd18010   140 AKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDF 176
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
184-373 1.30e-29

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: 118.34  E-value: 1.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYSWSKKTN-----VILADEMGLGKTIQSIAFLASLFEEnlSPH--------LVVAPLSTIRNWEREF 250
Cdd:cd18067     1 LRPHQREGVKFLYRCVTGRRIrgshgCIMADEMGLGKTLQCITLMWTLLRQ--SPQckpeidkaIVVSPSSLVKNWANEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  251 ATW-APHMNVVMYTGDSEARDVIWEHEFYFSEGRKSKFDVLLTTYEMVHPGISVLSPIKWTCMIIDEGHRLKNQKSKLYS 329
Cdd:cd18067    79 GKWlGGRLQPLAIDGGSKKEIDRKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQ 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 334187075  330 SLSQFTSKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQ 373
Cdd:cd18067   159 ALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFK 202
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
206-395 2.45e-28

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


Pssm-ID: 350829 [Multi-domain]  Cd Length: 239  Bit Score: 114.87  E-value: 2.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  206 ILADEMGLGKTIQSIAFLASlfeenlSPHLVVAPLSTIRNWEREFA--TWAPHMNVVMYTGDSEARDViwehefyfseGR 283
Cdd:cd18071    52 ILADDMGLGKTLTTISLILA------NFTLIVCPLSVLSNWETQFEehVKPGQLKVYTYHGGERNRDP----------KL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  284 KSKFDVLLTTYEMV-----HPGISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQFTSKHIVLLTGTPLQNNLNELFALM 358
Cdd:cd18071   116 LSKYDIVLTTYNTLasdfgAKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLL 195
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 334187075  359 HFLDADKFGSLEKFQDI-------NKEEQISRLHQMLAPHLLRR 395
Cdd:cd18071   196 SFLHLKPFSNPEYWRRLiqrpltmGDPTGLKRLQVLMKQITLRR 239
DEXDc smart00487
DEAD-like helicases superfamily;
176-359 6.79e-27

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 109.12  E-value: 6.79e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075    176 TPEFLTGTLHTYQLEGLNFLrysWSKKTNVILADEMGLGKTIQ-SIAFLASLFEENLSPHLVVAPL-STIRNWEREFATW 253
Cdd:smart00487    1 IEKFGFEPLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAaLLPALEALKRGKGGRVLVLVPTrELAEQWAEELKKL 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075    254 APHMN---VVMYTGDSEARDviwehefyFSEGRKSKFDVLLTTYEMV--HPGISVLSPIKWTCMIIDEGHRLKNQ--KSK 326
Cdd:smart00487   78 GPSLGlkvVGLYGGDSKREQ--------LRKLESGKTDILVTTPGRLldLLENDKLSLSNVDLVILDEAHRLLDGgfGDQ 149
                           170       180       190
                    ....*....|....*....|....*....|....
gi 334187075    327 LYSSLSQF-TSKHIVLLTGTPLQNNLNELFALMH 359
Cdd:smart00487  150 LEKLLKLLpKNVQLLLLSATPPEEIENLLELFLN 183
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
184-374 2.14e-25

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: 105.67  E-value: 2.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFL---------RYSWSKKTNVILADEMGLGKTIQSIAFLASLFEE-NLSPHLVVAPLSTIRNWEREFATW 253
Cdd:cd18069     1 LKPHQIGGIRFLydniiesleRYKGSSGFGCILAHSMGLGKTLQVISFLDVLLRHtGAKTVLAIVPVNTLQNWLSEFNKW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  254 APH----------------MNVVMYTGDSEArDVI--WEHefyfsegrksKFDVLLTTYEM--VHPGISVLspikwtcmI 313
Cdd:cd18069    81 LPPpealpnvrprpfkvfiLNDEHKTTAARA-KVIedWVK----------DGGVLLMGYEMfrLRPGPDVV--------I 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334187075  314 IDEGHRLKNQKSKLYSSLSQFTSKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQD 374
Cdd:cd18069   142 CDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSN 202
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
483-597 5.43e-25

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: 100.36  E-value: 5.43e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075   483 GKLQLLDKMMvkLKEQGHRVLIYTQFQHTLYllEDYFTFK-NWNYERIDGKISGPERQVRIDRFNAENSNrfcFLLSTRA 561
Cdd:pfam00271    1 EKLEALLELL--KKERGGKVLIFSQTKKTLE--AELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 334187075   562 GGIGINLATADTVIIYDSDWNPHADLQAMARVHRLG 597
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
184-395 2.99e-21

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


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 93.12  E-value: 2.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNF-LRyswSKKTNVILADEMGLGKTIQSIAFLASLFEENLS-PHLVVAPLSTIRNWEREFATWApHMNVVM 261
Cdd:cd18011     1 PLPHQIDAVLRaLR---KPPVRLLLADEVGLGKTIEAGLIIKELLLRGDAkRVLILCPASLVEQWQDELQDKF-GLPFLI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  262 YTGDSEARDViWEHEFYFSEgrkskFDVLLTTYEMVHPGI---SVLSPIKWTCMIIDEGHRLKNQKSKLYSSLSQF---- 334
Cdd:cd18011    77 LDRETAAQLR-RLIGNPFEE-----FPIVIVSLDLLKRSEerrGLLLSEEWDLVVVDEAHKLRNSGGGKETKRYKLgrll 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334187075  335 --TSKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQDINKEEQIsrlhqmLAPHLLRR 395
Cdd:cd18011   151 akRARHVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLRLDGLREV------LAKVLLRR 207
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
206-395 3.46e-21

DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called Forkhead-box E1/FOXE1 ) is a transcription termination factor that couples ATP hydrolysis with the removal of RNA polymerase II from the DNA template. Single nucleotide polymorphism (SNP) within the 5'-UTR of TTF2 is associated with thyroid cancer risk.TTF2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 94.08  E-value: 3.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  206 ILADEMGLGKTIQSIAF-LASLFEENLSPH-----------------------LVVAPLSTIRNWEREFATWAPHMNVVM 261
Cdd:cd18072    24 ILADDMGLGKTLTMIALiLAQKNTQNRKEEekekalteweskkdstlvpsagtLVVCPASLVHQWKNEVESRVASNKLRV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  262 YTGDSEARDVIWEhefYFSEgrkskFDVLLTTYEMV---HP------GISVLSPIKWTCMIIDEGHRLKNQKSKLYSSLS 332
Cdd:cd18072   104 CLYHGPNRERIGE---VLRD-----YDIVITTYSLVakeIPtykeesRSSPLFRIAWARIILDEAHNIKNPKVQASIAVC 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334187075  333 QFTSKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLE---KFQDINKEEQISRLHQMLAPHLLRR 395
Cdd:cd18072   176 KLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKvwkKQVDNKSRKGGERLNILTKSLLLRR 241
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
206-374 4.22e-20

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: 91.10  E-value: 4.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  206 ILADEMGLGKTIQSIAFLASLF----EENLSPHLVVAPLSTIRNWEREFATWAPHMN---------VVMYTGDSEARDVI 272
Cdd:cd18068    32 ILAHCMGLGKTLQVVTFLHTVLlcekLENFSRVLVVCPLNTVLNWLNEFEKWQEGLKdeekievneLATYKRPQERSYKL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  273 WEhefYFSEGrkskfDVLLTTYEM------------------------VHPGISVLspikwtcmIIDEGHRLKNQKSKLY 328
Cdd:cd18068   112 QR---WQEEG-----GVMIIGYDMyrilaqernvksreklkeifnkalVDPGPDFV--------VCDEGHILKNEASAVS 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 334187075  329 SSLSQFTSKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQD 374
Cdd:cd18068   176 KAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRN 221
HELICc smart00490
helicase superfamily c-terminal domain;
515-597 1.26e-19

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 84.19  E-value: 1.26e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075    515 LEDYFTFKNWNYERIDGKISGPERQVRIDRFNaenSNRFCFLLSTRAGGIGINLATADTVIIYDSDWNPHADLQAMARVH 594
Cdd:smart00490    3 LAELLKELGIKVARLHGGLSQEEREEILDKFN---NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAG 79

                    ...
gi 334187075    595 RLG 597
Cdd:smart00490   80 RAG 82
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
99-150 5.64e-18

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: 78.77  E-value: 5.64e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 334187075   99 EWKTVDRIIACREGDDGE-EYLVKYKELSYRNSYWESESDISD-FQNEIQRFKD 150
Cdd:cd18659     1 EYTIVERIIAHREDDEGVtEYLVKWKGLPYDECTWESEEDISDiFQEAIDEYKK 54
DUF1087 pfam06465
CHD subfamily II, DUF1087; This domain is found in chromatin remodelling factors (CHDs) from ...
733-775 6.96e-15

CHD subfamily II, DUF1087; This domain is found in chromatin remodelling factors (CHDs) from subfamily II including CHD3/4/5 from animals and PICKLE. from Arabidopsis. The exact function is, as yet, unknown.


Pssm-ID: 461922  Cd Length: 60  Bit Score: 70.14  E-value: 6.96e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 334187075   733 NADRTSHWKDLLKDKYEVQQAEELSALGKRKRNGKQVMYAEDD 775
Cdd:pfam06465   17 ESEDPNYWEKLLKHHYEQQQEEEFNALGKGKRSRKQVVSVEED 59
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
122-576 1.40e-13

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 75.06  E-value: 1.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  122 YKELSYRNSYWESESDISDFQNEIQRFKDINSSSRRDKYVENERNREEFKQFDLTPEFlTGTLHTYQLEGLNFLRYSWSK 201
Cdd:COG1061    20 LLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGT-SFELRPYQQEALEALLAALER 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  202 KTN---VILAdeMGLGKTIQSIAFLASLFEENLSphLVVAPLSTIRN-WEREFATWaphmnvvmytgdseardviwEHEF 277
Cdd:COG1061    99 GGGrglVVAP--TGTGKTVLALALAAELLRGKRV--LVLVPRRELLEqWAEELRRF--------------------LGDP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  278 YFSEGRK-SKFDVLLTTYEMV--HPGISVLSPiKWTCMIIDEGHRLKnqkSKLYS-SLSQFTSKHIVLLTGTPlqnnlne 353
Cdd:COG1061   155 LAGGGKKdSDAPITVATYQSLarRAHLDELGD-RFGLVIIDEAHHAG---APSYRrILEAFPAAYRLGLTATP------- 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  354 lfalmhFLDADKFGSLEKFQDINKEEQISRL--HQMLAPHLLrrlkkdvlkdkvppkkeLILRVDMSSQQKEvykavitn 431
Cdd:COG1061   224 ------FRSDGREILLFLFDGIVYEYSLKEAieDGYLAPPEY-----------------YGIRVDLTDERAE-------- 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  432 nYQVLTKKRDAKISNvlmklrqvcshpyllpdfeprfedaneaftkllEASGKLQLLDKMMVKLKEQgHRVLIYTQFQHT 511
Cdd:COG1061   273 -YDALSERLREALAA---------------------------------DAERKDKILRELLREHPDD-RKTLVFCSSVDH 317
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187075  512 LYLLEDYFTFKNWNYERIDGKISGPERQVRIDRFNAENSNrfcFLLSTRAGGIGINLATADTVII 576
Cdd:COG1061   318 AEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELR---ILVTVDVLNEGVDVPRLDVAIL 379
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
184-362 1.33e-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: 68.15  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRyswSKKTNVILADeMGLGKTIQSIAFLASLFEENLSPH-LVVAPLSTIRN-WEREFATWApHMNVVM 261
Cdd:cd18013     1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRvLVIAPLRVARStWPDEVEKWN-HLRNLT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  262 YTgdseardVIWEHEFYFSEGRKSKFDVLLTTYEMVhPGISVLSPIKWT--CMIIDEGHRLKNQKSKLYSSLSQ--FTSK 337
Cdd:cd18013    76 VS-------VAVGTERQRSKAANTPADLYVINRENL-KWLVNKSGDPWPfdMVVIDELSSFKSPRSKRFKALRKvrPVIK 147
                         170       180
                  ....*....|....*....|....*
gi 334187075  338 HIVLLTGTPLQNNLNELFALMHFLD 362
Cdd:cd18013   148 RLIGLTGTPSPNGLMDLWAQIALLD 172
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
184-366 4.61e-12

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: 67.37  E-value: 4.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYSWSkktnvILADEMGLGKTIQSIAFLAS--------------LFEENLSPH-------------LV 236
Cdd:cd18070     1 LLPYQRRAVNWMLVPGG-----ILADEMGLGKTVEVLALILLhprpdndldaadddSDEMVCCPDclvaetpvsskatLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  237 VAPLSTIRNWEREFATWAP-HMNVVMYTGDSEARDVIWEHEFYFSEgrkskFDVLLTTYEM----VH------------- 298
Cdd:cd18070    76 VCPSAILAQWLDEINRHVPsSLKVLTYQGVKKDGALASPAPEILAE-----YDIVVTTYDVlrteLHyaeanrsnrrrrr 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334187075  299 --PGISVLSP---IKWTCMIIDEGHRLKNQKSKLYSSLSQFTSKHIVLLTGTPLQNNLNELFALMHFLDADKF 366
Cdd:cd18070   151 qkRYEAPPSPlvlVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPF 223
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
101-150 3.98e-11

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 59.13  E-value: 3.98e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 334187075   101 KTVDRIIACREGDDG-EEYLVKYKELSYRNSYWESESDISDFQNEIQRFKD 150
Cdd:pfam00385    1 YEVERILDHRKDKGGkEEYLVKWKGYPYDENTWEPEENLSKCPELIEEFKD 51
CHROMO smart00298
Chromatin organization modifier domain;
99-150 2.74e-10

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 56.84  E-value: 2.74e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 334187075     99 EWKtVDRIIACREGDDGE-EYLVKYKELSYRNSYWESESDISDFQNEIQRFKD 150
Cdd:smart00298    1 EYE-VEKILDHRWKKKGElEYLVKWKGYSYSEDTWEPEENLLNCSKKLDNYKK 52
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
98-150 2.83e-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: 56.89  E-value: 2.83e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 334187075   98 PEWKTVDRIIACREGDDGE-EYLVKYKELSYRNSYWESE-SDISDFQNEIQRFKD 150
Cdd:cd18662     1 PEWLQIHRIINHRVDKDGNtWYLVKWRDLPYDQSTWESEdDDIPDYEKHIQEYWD 55
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
204-345 1.17e-09

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: 57.80  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  204 NVILADEMGLGKTIQSIAFLASLFEENLSPHLVVAPLSTIRN-WEREFATWA-PHMNVVMYTGDSEArdviwEHEFYFSE 281
Cdd:cd00046     3 NVLITAPTGSGKTLAALLAALLLLLKKGKKVLVLVPTKALALqTAERLRELFgPGIRVAVLVGGSSA-----EEREKNKL 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334187075  282 GRKskfDVLLTTYEMVHPGISVLSPI---KWTCMIIDEGHRLKNQKSKLYSSLSQFTSKH-----IVLLTGT 345
Cdd:cd00046    78 GDA---DIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHALLIDSRGALILDLAVRKAGlknaqVILLSAT 146
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
417-631 2.35e-09

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


Pssm-ID: 402894  Cd Length: 281  Bit Score: 59.65  E-value: 2.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075   417 MSSQQKEVYKAVITNNYQVLTK-----KRDAKISNVLMK------LRQVCSHPYLLPD-FEPR---FEDANEaftKLLEA 481
Cdd:pfam11496   12 MTSYQKELTEQIVSLHYSDILKycetsDSKEDISLIKSMtlclenLSLVATHPYLLVDhYMPKsllLKDEPE---KLAYT 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075   482 SGKLQLLDKMMVKLKEQGHR----VLIYTQFQHTLYLLEDYFTFKNWNYERIDG-KISGPERQVRIDRFNAENSNRFCFL 556
Cdd:pfam11496   89 SGKFLVLNDLVNLLIERDRKepinVAIVARSGKTLDLVEALLLGKGLSYKRYSGeMLYGENKKVSDSGNKKIHSTTCHLL 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075   557 ----LSTRAGGIGINLAtADTVIIYDSDWNP-HADLQAMARVHRLGQtNKVMIYRLIHKGTVEERMMEITKNKMLLEHLV 631
Cdd:pfam11496  169 sstgQLTNDDSLLENYK-FDLIIAFDSSVDTsSPSVEHLRTQNRRKG-NLAPIIRLVVINSIEHVELCFPKPPDSPDYLY 246
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
184-346 1.69e-05

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 45.76  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  184 LHTYQLEGLNFLRYSWSKKTNVIladEM--GLGKTIQSIAFLASLFEENLsphLVVAPLSTIRN-WEREFATWAPHmnvv 260
Cdd:cd17926     1 LRPYQEEALEAWLAHKNNRRGIL---VLptGSGKTLTALALIAYLKELRT---LIVVPTDALLDqWKERFEDFLGD---- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  261 mytgdseardviwEHEFYFSEGRKSKFD---VLLTTYEMVHPGISVLSPIK--WTCMIIDEGHRLknqKSKLYSS-LSQF 334
Cdd:cd17926    71 -------------SSIGLIGGGKKKDFDdanVVVATYQSLSNLAEEEKDLFdqFGLLIVDEAHHL---PAKTFSEiLKEL 134
                         170
                  ....*....|..
gi 334187075  335 TSKHIVLLTGTP 346
Cdd:cd17926   135 NAKYRLGLTATP 146
ResIII pfam04851
Type III restriction enzyme, res subunit;
183-346 4.73e-05

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 44.97  E-value: 4.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075   183 TLHTYQLEGLNFLRYSWSKK-TNVILADEMGLGKTIQSIAFLASLFEENLSPH-LVVAP-LSTIRNWEREFATWAPHMNV 259
Cdd:pfam04851    3 ELRPYQIEAIENLLESIKNGqKRGLIVMATGSGKTLTAAKLIARLFKKGPIKKvLFLVPrKDLLEQALEEFKKFLPNYVE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075   260 VM--YTGDSEARDViwehefyfsegrkSKFDVLLTTYEMVHPGISV----LSPIKWTCMIIDEGHRLknqkskLYSS--- 330
Cdd:pfam04851   83 IGeiISGDKKDESV-------------DDNKIVVTTIQSLYKALELasleLLPDFFDVIIIDEAHRS------GASSyrn 143
                          170
                   ....*....|....*..
gi 334187075   331 -LSQFTSKHIVLLTGTP 346
Cdd:pfam04851  144 iLEYFKPAFLLGLTATP 160
PRK04914 PRK04914
RNA polymerase-associated protein RapA;
309-380 8.83e-05

RNA polymerase-associated protein RapA;


Pssm-ID: 235319 [Multi-domain]  Cd Length: 956  Bit Score: 46.75  E-value: 8.83e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334187075  309 WTCMIIDEGHRL---KNQKSKLYSSLSQF--TSKHIVLLTGTPLQNNLNELFALMHFLDADKFGSLEKFQdinKEEQ 380
Cdd:PRK04914  273 WDLLVVDEAHHLvwsEEAPSREYQVVEQLaeVIPGVLLLTATPEQLGQESHFARLRLLDPDRFHDYEAFV---EEQQ 346
CD2_tandem_ScCHD1_like cd18664
repeat 2 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
99-139 4.49e-04

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: 39.56  E-value: 4.49e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 334187075   99 EWKTVDRIIACREGDDGE-----EYLVKYKELSYRNSYWESESDIS 139
Cdd:cd18664     1 EFHVVERIIASQRASLEDgtsqlQYLVKWRRLNYDECTWEDATLIA 46
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
550-605 7.67e-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: 39.22  E-value: 7.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 334187075  550 SNRFCFLLSTRAGGIGINLATADTVIIYDSDWNPHADLQAMARVHRLGQTNKVMIY 605
Cdd:cd18785    20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVIL 75
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
101-140 1.36e-03

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: 38.50  E-value: 1.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 334187075  101 KTVDRIIACREGDDGE----------------EYLVKYKELSYRNSYWESESDISD 140
Cdd:cd18660     3 DKIEKILDHRPKGPVEeasldltdpdepwderEFLVKWKGKSYLHCTWVTEETLEQ 58
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
103-149 2.71e-03

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: 37.32  E-value: 2.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334187075  103 VDRIIACREGDDG----------EEYLVKYKELSYRNSYWESESDI----SDFQNEIQRFK 149
Cdd:cd18668     7 IEKILASRKKKKEkeegaeeievEEYLVKYKNFSYLHCEWKTEEELekgdKRIKQKIKRFK 67
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
98-152 3.31e-03

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: 36.88  E-value: 3.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334187075   98 PEWKTVDRII---ACREGDDGEE---YLVKYKELSYRNSYWESESDISdfQNEIQRFKDIN 152
Cdd:cd18663     1 PDYVEVDRILdvsVSTDPNTGEPvthYLVKWCSLPYEDSTWELEEDVD--PAKIEEFEKLR 59
SF2_C_DEAD cd18787
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ...
484-599 6.32e-03

C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, 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: 350174 [Multi-domain]  Cd Length: 131  Bit Score: 38.26  E-value: 6.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187075  484 KLQLLDKMMVKLKEQghRVLIYTQFQHTLYLLEDYFTFKNWNYERIDGKISGPERQVRIDRFNAENSNrfcFLLST---- 559
Cdd:cd18787    14 KLLLLLLLLEKLKPG--KAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR---VLVATdvaa 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 334187075  560 RaggiGINLATADTVIIYDsdwnphadlqaMAR-----VHRLGQT 599
Cdd:cd18787    89 R----GLDIPGVDHVINYD-----------LPRdaedyVHRIGRT 118
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
103-150 7.78e-03

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: 35.53  E-value: 7.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 334187075  103 VDRIIACREGDDGEEYLVKYKELSYRNSYWESESDISDFQNEIQRFKD 150
Cdd:cd00024     3 VEKILDHRVRKGKLEYLVKWKGYPPEENTWEPEENLTNAPELIKEYEK 50
 
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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