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Conserved domains on  [gi|1246743034|ref|NP_001342861|]
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CHD family chromatin remodeller Hrp3 [Schizosaccharomyces pombe]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
339-895 1.06e-155

Probable chromatin-remodeling complex ATPase chain; Provisional


The actual alignment was detected with superfamily member PLN03142:

Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 497.40  E-value: 1.06e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  339 EREESALSPSRGTnygnsrpkyrKLEQQPSYITGgELRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLA 418
Cdd:PLN03142   145 KEEEDGLGGSGGT----------RLLVQPSCIKG-KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLH 213
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  419 HSLRQHGPFLVVVPLSTVPAWQETLALWASDMNCISYLGNTTSRQVIRDyEFYVDGtqkiKFNLLLTTYEYVLKDRSVLS 498
Cdd:PLN03142   214 EYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQRE-ELLVAG----KFDVCVTSFEMAIKEKTALK 288
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  499 NIKWQYMAIDEAHRLKNSESSLYEALSQFKNSNRLLITGTPLQNNIRELAALVDFLMPGKF---EIREEINLEAPDEEQE 575
Cdd:PLN03142   289 RFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFssaETFDEWFQISGENDQQ 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  576 AYIRSLQEHLQPYILRRLKKDVEKSLPSKSERILRVELSDLQMYWYKNILTRNYRVLTQSISSGSqisLLNIVVELKKAS 655
Cdd:PLN03142   369 EVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCC 445
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  656 NHPYLFDGVEEswmqkinsqGRRDEVLKGLIMNSGKMVLLDKLLSRLRRDGHRVLIFSQMVRMLDILGDYLSLRGYPHQR 735
Cdd:PLN03142   446 NHPYLFQGAEP---------GPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCR 516
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  736 LDGTVPAAVRRTSIDHFNAPNSPDFVFLLSTRAGGLGINLMTADTVIIFDSDWNPQADLQAMARAHRIGQKNHVMVYRLL 815
Cdd:PLN03142   517 IDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFC 596
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  816 SKDTIEEDVLERARRKMILEYAIISLGVTDKQKNSKNDkfsaeELSAILKFGASNMFKAENNQkkLEDMNLDEILEHAED 895
Cdd:PLN03142   597 TEYTIEEKVIERAYKKLALDALVIQQGRLAEQKTVNKD-----ELLQMVRYGAEMVFSSKDST--ITDEDIDRIIAKGEE 669
CD1_tandem_CHD1_yeast_like cd18665
repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
189-250 2.07e-29

repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein 1, and similar proteins; Repeat 1 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: 349312  Cd Length: 65  Bit Score: 111.71  E-value: 2.07e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246743034  189 DTRAIDVVLDHRLIEGHDGS---TPSEDYEFLIKWVNFSHLHCTWEPYNNISMIRGSKKVDNHIK 250
Cdd:cd18665      1 DEHGIDIVLDHRLKEGLEEGeldDPKENYEFLIKWTDESHLHNTWETYESLKQVRGLKKVDNYIK 65
DUF4208 pfam13907
Domain of unknown function (DUF4208); This domain is found at the C-terminus of ...
1300-1384 8.29e-28

Domain of unknown function (DUF4208); This domain is found at the C-terminus of chromodomain-helicase-DNA-binding proteins. The exact function of the domain is undetermined.


:

Pssm-ID: 464035  Cd Length: 93  Bit Score: 108.11  E-value: 8.29e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034 1300 ARCKELMYPVRKHMKRLRKDSSGLGRAELVKLLTECLTTIGKHIEKTVNDTPSEEKATVRKNLWMFACYFWPKeEVKYTS 1379
Cdd:pfam13907    9 EECKELMRPVKKSLKRLKKGTKGLSRKERAKILKKELLKIGDFIDSLLEETKKEKKEKLRKHLWSFVSKFWPN-KVSGKK 87

                   ....*
gi 1246743034 1380 LISMY 1384
Cdd:pfam13907   88 LKEMY 92
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
286-339 8.09e-20

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: 84.16  E-value: 8.09e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1246743034  286 EYKQVDRIVAKHLNSDGSVEYLVKWKQLLYDFCTWEASSIIEPIAATEIQAFQE 339
Cdd:cd18659      1 EYTIVERIIAHREDDEGVTEYLVKWKGLPYDECTWESEEDISDIFQEAIDEYKK 54
Cdh1_DBD_1 super family cl39557
Chromodomain helicase DNA-binding domain 1; This domain can be found in chromodomain helicase ...
997-1081 4.50e-06

Chromodomain helicase DNA-binding domain 1; This domain can be found in chromodomain helicase DNA-binding protein 1 (Chd1) present in Saccharomyces cerevisiae. Cdh1 proteins have been associated with the efficient assembly and spacing of nucleosomes. The domain consists of four helices, alpha helix 1-4, and can be divided into regions SANT, HL1 and the beta-linker. The HL1 region comprises of some 40 residues specific to budding yeast that are unlikely to form such a prominent feature or perform a conserved function in other species. The domain itself forms part of the DNA-binding domain. Basic residues on the alpha-1 helix are thought to be important for DNA interaction.


The actual alignment was detected with superfamily member pfam18196:

Pssm-ID: 408024 [Multi-domain]  Cd Length: 120  Bit Score: 47.09  E-value: 4.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  997 EKEIRLLYRAMIRYGSLEHRYNDIVKYADLTTQDAHVIKKIAADLVTASRKAV-----------SAAEKD---------- 1055
Cdd:pfam18196    3 EREIRALYKAILRYGDLSNMFEELIADGSLPQKSIERYEELYRELIEQAKRVVkeeeekrneelEALEADamaykaalkg 82
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1246743034 1056 -----LSNDQSN-------NKSSRKALLITFKGVKNIN 1081
Cdd:pfam18196   83 ggvtaDDQPKDTpitklaaKRREKKAILFEFYGVKNLN 120
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
339-895 1.06e-155

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 497.40  E-value: 1.06e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  339 EREESALSPSRGTnygnsrpkyrKLEQQPSYITGgELRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLA 418
Cdd:PLN03142   145 KEEEDGLGGSGGT----------RLLVQPSCIKG-KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLH 213
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  419 HSLRQHGPFLVVVPLSTVPAWQETLALWASDMNCISYLGNTTSRQVIRDyEFYVDGtqkiKFNLLLTTYEYVLKDRSVLS 498
Cdd:PLN03142   214 EYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQRE-ELLVAG----KFDVCVTSFEMAIKEKTALK 288
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  499 NIKWQYMAIDEAHRLKNSESSLYEALSQFKNSNRLLITGTPLQNNIRELAALVDFLMPGKF---EIREEINLEAPDEEQE 575
Cdd:PLN03142   289 RFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFssaETFDEWFQISGENDQQ 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  576 AYIRSLQEHLQPYILRRLKKDVEKSLPSKSERILRVELSDLQMYWYKNILTRNYRVLTQSISSGSqisLLNIVVELKKAS 655
Cdd:PLN03142   369 EVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCC 445
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  656 NHPYLFDGVEEswmqkinsqGRRDEVLKGLIMNSGKMVLLDKLLSRLRRDGHRVLIFSQMVRMLDILGDYLSLRGYPHQR 735
Cdd:PLN03142   446 NHPYLFQGAEP---------GPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCR 516
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  736 LDGTVPAAVRRTSIDHFNAPNSPDFVFLLSTRAGGLGINLMTADTVIIFDSDWNPQADLQAMARAHRIGQKNHVMVYRLL 815
Cdd:PLN03142   517 IDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFC 596
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  816 SKDTIEEDVLERARRKMILEYAIISLGVTDKQKNSKNDkfsaeELSAILKFGASNMFKAENNQkkLEDMNLDEILEHAED 895
Cdd:PLN03142   597 TEYTIEEKVIERAYKKLALDALVIQQGRLAEQKTVNKD-----ELLQMVRYGAEMVFSSKDST--ITDEDIDRIIAKGEE 669
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
374-592 4.69e-147

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: 444.88  E-value: 4.69e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  374 ELRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLSTVPAWQETLALWASDMNCI 453
Cdd:cd17993      1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  454 SYLGNTTSRQVIRDYEFYVDGTQKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFKNSNRL 533
Cdd:cd17993     81 VYLGDIKSRDTIREYEFYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1246743034  534 LITGTPLQNNIRELAALVDFLMPGKFEIREEINLEaPDEEQEAYIRSLQEHLQPYILRR 592
Cdd:cd17993    161 LITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEE-HDEEQEKGIADLHKELEPFILRR 218
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
251-834 4.58e-125

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 404.22  E-value: 4.58e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  251 QVILLDREIREDPTTTREDIEAMDIEKERKRENYEEYKQVDRIVAKHLNSDGSVEYLVKWKQLLYDFCTWEASSIIEPIA 330
Cdd:COG0553    130 LLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLL 209
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  331 ATEIQAFQEREESALSPSRgtnygnsrpkyRKLEQQPSYItGGELRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQT 410
Cdd:COG0553    210 ELELLAEAAVDAFRLRRLR-----------EALESLPAGL-KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQA 277
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  411 VAFLSYLAHSlRQHGPFLVVVPLSTVPAWQETLALWASDMNCISYLGNTTSRQVIRDYEfyvdgtqkiKFNLLLTTYEYV 490
Cdd:COG0553    278 LALLLELKER-GLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRERAKGANPFE---------DADLVITSYGLL 347
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  491 LKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFKNSNRLLITGTPLQNNIRELAALVDFLMPG------KFEIREE 564
Cdd:COG0553    348 RRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGllgslkAFRERFA 427
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  565 INLEAPDEEQEAYIRSLqehLQPYILRRLKKDVEKSLPSKSERILRVELSDLQMYWYKNILTRNYRVLTQSISSGSQISL 644
Cdd:COG0553    428 RPIEKGDEEALERLRRL---LRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLI 504
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  645 LNIVVELKKASNHPYLFDGVEESwmqkinsqgrrdevlkgLIMNSGKMVLLDKLLSRLRRDGHRVLIFSQMVRMLDILGD 724
Cdd:COG0553    505 LAALTRLRQICSHPALLLEEGAE-----------------LSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEE 567
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  725 YLSLRGYPHQRLDGTVPAAVRRTSIDHFNAPNSPDfVFLLSTRAGGLGINLMTADTVIIFDSDWNPQADLQAMARAHRIG 804
Cdd:COG0553    568 RLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAP-VFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIG 646
                          570       580       590
                   ....*....|....*....|....*....|
gi 1246743034  805 QKNHVMVYRLLSKDTIEEDVLERARRKMIL 834
Cdd:COG0553    647 QTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
379-661 1.16e-85

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: 281.11  E-value: 1.16e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  379 QLTGVNWMAYLWHK-NENGILADEMGLGKTVQTVAFLSYLAHSLRQHG-PFLVVVPLSTVPAWQETLALWA--SDMNCIS 454
Cdd:pfam00176    2 QIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVVV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  455 YLGNTTSRQvirdyEFYVDGTQKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFKNSNRLL 534
Cdd:pfam00176   82 LHGNKRPQE-----RWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  535 ITGTPLQNNIRELAALVDFLMPGKF----EIREEINLEAPDEEQEAYIRSLQEHLQPYILRRLKKDVEKSLPSKSERILR 610
Cdd:pfam00176  157 LTGTPLQNNLEELWALLNFLRPGPFgslsTFRNWFDRPIERGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILF 236
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1246743034  611 VELSDLQMYWYKN-ILTRNY-RVLTQSISSGSQISLLNIVVELKKASNHPYLF 661
Cdd:pfam00176  237 CRLSKLQRKLYQTfLLKKDLnAIKTGEGGREIKASLLNILMRLRKICNHPGLI 289
CD1_tandem_CHD1_yeast_like cd18665
repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
189-250 2.07e-29

repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein 1, and similar proteins; Repeat 1 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: 349312  Cd Length: 65  Bit Score: 111.71  E-value: 2.07e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246743034  189 DTRAIDVVLDHRLIEGHDGS---TPSEDYEFLIKWVNFSHLHCTWEPYNNISMIRGSKKVDNHIK 250
Cdd:cd18665      1 DEHGIDIVLDHRLKEGLEEGeldDPKENYEFLIKWTDESHLHNTWETYESLKQVRGLKKVDNYIK 65
DUF4208 pfam13907
Domain of unknown function (DUF4208); This domain is found at the C-terminus of ...
1300-1384 8.29e-28

Domain of unknown function (DUF4208); This domain is found at the C-terminus of chromodomain-helicase-DNA-binding proteins. The exact function of the domain is undetermined.


Pssm-ID: 464035  Cd Length: 93  Bit Score: 108.11  E-value: 8.29e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034 1300 ARCKELMYPVRKHMKRLRKDSSGLGRAELVKLLTECLTTIGKHIEKTVNDTPSEEKATVRKNLWMFACYFWPKeEVKYTS 1379
Cdd:pfam13907    9 EECKELMRPVKKSLKRLKKGTKGLSRKERAKILKKELLKIGDFIDSLLEETKKEKKEKLRKHLWSFVSKFWPN-KVSGKK 87

                   ....*
gi 1246743034 1380 LISMY 1384
Cdd:pfam13907   88 LKEMY 92
DEXDc smart00487
DEAD-like helicases superfamily;
374-558 3.04e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 107.58  E-value: 3.04e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034   374 ELRDFQLTGVNWMaylWHKNENGILADEMGLGKTVQTVAFLSYLAHSlRQHGPFLVVVPL-STVPAWQETLALWASDMN- 451
Cdd:smart00487    8 PLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAALLPALEALKR-GKGGRVLVLVPTrELAEQWAEELKKLGPSLGl 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034   452 -CISYLGNTTSRQVIRDYEfyvdgtqKIKFNLLLTTYEYVLKD--RSVLSNIKWQYMAIDEAHRLKNS--ESSLYEALSQ 526
Cdd:smart00487   84 kVVGLYGGDSKREQLRKLE-------SGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKL 156
                           170       180       190
                    ....*....|....*....|....*....|....*.
gi 1246743034   527 F-KNSNRLLITGTP---LQNNIRELAALVDFLMPGK 558
Cdd:smart00487  157 LpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGF 192
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
286-339 8.09e-20

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: 84.16  E-value: 8.09e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1246743034  286 EYKQVDRIVAKHLNSDGSVEYLVKWKQLLYDFCTWEASSIIEPIAATEIQAFQE 339
Cdd:cd18659      1 EYTIVERIIAHREDDEGVTEYLVKWKGLPYDECTWESEEDISDIFQEAIDEYKK 54
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
288-340 2.86e-11

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 59.90  E-value: 2.86e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1246743034  288 KQVDRIVAKHLNSDGSVEYLVKWKQLLYDFCTWEASSIIEPIAAtEIQAFQER 340
Cdd:pfam00385    1 YEVERILDHRKDKGGKEEYLVKWKGYPYDENTWEPEENLSKCPE-LIEEFKDR 52
CHROMO smart00298
Chromatin organization modifier domain;
286-342 5.62e-10

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 56.07  E-value: 5.62e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1246743034   286 EYKqVDRIVAKHLNSDGSVEYLVKWKQLLYDFCTWEASSIIEPiAATEIQAFQEREE 342
Cdd:smart00298    1 EYE-VEKILDHRWKKKGELEYLVKWKGYSYSEDTWEPEENLLN-CSKKLDNYKKKER 55
CHROMO smart00298
Chromatin organization modifier domain;
192-250 8.36e-08

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 49.90  E-value: 8.36e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1246743034   192 AIDVVLDHRLIEGhdgstpsEDYEFLIKWVNFSHLHCTWEPYNNISmiRGSKKVDNHIK 250
Cdd:smart00298    3 EVEKILDHRWKKK-------GELEYLVKWKGYSYSEDTWEPEENLL--NCSKKLDNYKK 52
Cdh1_DBD_1 pfam18196
Chromodomain helicase DNA-binding domain 1; This domain can be found in chromodomain helicase ...
997-1081 4.50e-06

Chromodomain helicase DNA-binding domain 1; This domain can be found in chromodomain helicase DNA-binding protein 1 (Chd1) present in Saccharomyces cerevisiae. Cdh1 proteins have been associated with the efficient assembly and spacing of nucleosomes. The domain consists of four helices, alpha helix 1-4, and can be divided into regions SANT, HL1 and the beta-linker. The HL1 region comprises of some 40 residues specific to budding yeast that are unlikely to form such a prominent feature or perform a conserved function in other species. The domain itself forms part of the DNA-binding domain. Basic residues on the alpha-1 helix are thought to be important for DNA interaction.


Pssm-ID: 408024 [Multi-domain]  Cd Length: 120  Bit Score: 47.09  E-value: 4.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  997 EKEIRLLYRAMIRYGSLEHRYNDIVKYADLTTQDAHVIKKIAADLVTASRKAV-----------SAAEKD---------- 1055
Cdd:pfam18196    3 EREIRALYKAILRYGDLSNMFEELIADGSLPQKSIERYEELYRELIEQAKRVVkeeeekrneelEALEADamaykaalkg 82
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1246743034 1056 -----LSNDQSN-------NKSSRKALLITFKGVKNIN 1081
Cdd:pfam18196   83 ggvtaDDQPKDTpitklaaKRREKKAILFEFYGVKNLN 120
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
191-237 1.69e-04

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 40.64  E-value: 1.69e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1246743034  191 RAIDVVLDHRLIEGHDGstpsedyEFLIKWVNFSHLHCTWEPYNNIS 237
Cdd:pfam00385    1 YEVERILDHRKDKGGKE-------EYLVKWKGYPYDENTWEPEENLS 40
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
339-895 1.06e-155

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 497.40  E-value: 1.06e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  339 EREESALSPSRGTnygnsrpkyrKLEQQPSYITGgELRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLA 418
Cdd:PLN03142   145 KEEEDGLGGSGGT----------RLLVQPSCIKG-KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLH 213
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  419 HSLRQHGPFLVVVPLSTVPAWQETLALWASDMNCISYLGNTTSRQVIRDyEFYVDGtqkiKFNLLLTTYEYVLKDRSVLS 498
Cdd:PLN03142   214 EYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQRE-ELLVAG----KFDVCVTSFEMAIKEKTALK 288
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  499 NIKWQYMAIDEAHRLKNSESSLYEALSQFKNSNRLLITGTPLQNNIRELAALVDFLMPGKF---EIREEINLEAPDEEQE 575
Cdd:PLN03142   289 RFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFssaETFDEWFQISGENDQQ 368
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  576 AYIRSLQEHLQPYILRRLKKDVEKSLPSKSERILRVELSDLQMYWYKNILTRNYRVLTQSISSGSqisLLNIVVELKKAS 655
Cdd:PLN03142   369 EVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCC 445
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  656 NHPYLFDGVEEswmqkinsqGRRDEVLKGLIMNSGKMVLLDKLLSRLRRDGHRVLIFSQMVRMLDILGDYLSLRGYPHQR 735
Cdd:PLN03142   446 NHPYLFQGAEP---------GPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCR 516
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  736 LDGTVPAAVRRTSIDHFNAPNSPDFVFLLSTRAGGLGINLMTADTVIIFDSDWNPQADLQAMARAHRIGQKNHVMVYRLL 815
Cdd:PLN03142   517 IDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFC 596
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  816 SKDTIEEDVLERARRKMILEYAIISLGVTDKQKNSKNDkfsaeELSAILKFGASNMFKAENNQkkLEDMNLDEILEHAED 895
Cdd:PLN03142   597 TEYTIEEKVIERAYKKLALDALVIQQGRLAEQKTVNKD-----ELLQMVRYGAEMVFSSKDST--ITDEDIDRIIAKGEE 669
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
374-592 4.69e-147

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: 444.88  E-value: 4.69e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  374 ELRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLSTVPAWQETLALWASDMNCI 453
Cdd:cd17993      1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  454 SYLGNTTSRQVIRDYEFYVDGTQKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFKNSNRL 533
Cdd:cd17993     81 VYLGDIKSRDTIREYEFYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1246743034  534 LITGTPLQNNIRELAALVDFLMPGKFEIREEINLEaPDEEQEAYIRSLQEHLQPYILRR 592
Cdd:cd17993    161 LITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEE-HDEEQEKGIADLHKELEPFILRR 218
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
251-834 4.58e-125

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 404.22  E-value: 4.58e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  251 QVILLDREIREDPTTTREDIEAMDIEKERKRENYEEYKQVDRIVAKHLNSDGSVEYLVKWKQLLYDFCTWEASSIIEPIA 330
Cdd:COG0553    130 LLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLL 209
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  331 ATEIQAFQEREESALSPSRgtnygnsrpkyRKLEQQPSYItGGELRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQT 410
Cdd:COG0553    210 ELELLAEAAVDAFRLRRLR-----------EALESLPAGL-KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQA 277
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  411 VAFLSYLAHSlRQHGPFLVVVPLSTVPAWQETLALWASDMNCISYLGNTTSRQVIRDYEfyvdgtqkiKFNLLLTTYEYV 490
Cdd:COG0553    278 LALLLELKER-GLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRERAKGANPFE---------DADLVITSYGLL 347
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  491 LKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFKNSNRLLITGTPLQNNIRELAALVDFLMPG------KFEIREE 564
Cdd:COG0553    348 RRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGllgslkAFRERFA 427
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  565 INLEAPDEEQEAYIRSLqehLQPYILRRLKKDVEKSLPSKSERILRVELSDLQMYWYKNILTRNYRVLTQSISSGSQISL 644
Cdd:COG0553    428 RPIEKGDEEALERLRRL---LRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLI 504
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  645 LNIVVELKKASNHPYLFDGVEESwmqkinsqgrrdevlkgLIMNSGKMVLLDKLLSRLRRDGHRVLIFSQMVRMLDILGD 724
Cdd:COG0553    505 LAALTRLRQICSHPALLLEEGAE-----------------LSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEE 567
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  725 YLSLRGYPHQRLDGTVPAAVRRTSIDHFNAPNSPDfVFLLSTRAGGLGINLMTADTVIIFDSDWNPQADLQAMARAHRIG 804
Cdd:COG0553    568 RLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAP-VFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIG 646
                          570       580       590
                   ....*....|....*....|....*....|
gi 1246743034  805 QKNHVMVYRLLSKDTIEEDVLERARRKMIL 834
Cdd:COG0553    647 QTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
357-592 3.40e-92

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: 297.69  E-value: 3.40e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  357 RPKYRKLEQQPSYITGG--ELRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLS 434
Cdd:cd18054      1 RPRFVALKKQPSYIGGEnlELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  435 TVPAWQETLALWASDMNCISYLGNTTSRQVIRDYEFYVDGTQKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLK 514
Cdd:cd18054     81 TLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLK 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246743034  515 NSESSLYEALSQFKNSNRLLITGTPLQNNIRELAALVDFLMPGKFEIREEINLEAPDEEQEAYiRSLQEHLQPYILRR 592
Cdd:cd18054    161 NDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENGY-QSLHKVLEPFLLRR 237
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
379-661 1.16e-85

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: 281.11  E-value: 1.16e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  379 QLTGVNWMAYLWHK-NENGILADEMGLGKTVQTVAFLSYLAHSLRQHG-PFLVVVPLSTVPAWQETLALWA--SDMNCIS 454
Cdd:pfam00176    2 QIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVVV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  455 YLGNTTSRQvirdyEFYVDGTQKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFKNSNRLL 534
Cdd:pfam00176   82 LHGNKRPQE-----RWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  535 ITGTPLQNNIRELAALVDFLMPGKF----EIREEINLEAPDEEQEAYIRSLQEHLQPYILRRLKKDVEKSLPSKSERILR 610
Cdd:pfam00176  157 LTGTPLQNNLEELWALLNFLRPGPFgslsTFRNWFDRPIERGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILF 236
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1246743034  611 VELSDLQMYWYKN-ILTRNY-RVLTQSISSGSQISLLNIVVELKKASNHPYLF 661
Cdd:pfam00176  237 CRLSKLQRKLYQTfLLKKDLnAIKTGEGGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
375-592 5.39e-85

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: 276.82  E-value: 5.39e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLSTVPAWQETLALWaSDMNCIS 454
Cdd:cd17995      1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETW-TDMNVVV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  455 YLGNTTSRQVIRDYEFY--VDGTQKI----KFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFK 528
Cdd:cd17995     80 YHGSGESRQIIQQYEMYfkDAQGRKKkgvyKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246743034  529 NSNRLLITGTPLQNNIRELAALVDFLMPGKFEIREEINLEAPDEEQEAYIRSLQEHLQPYILRR 592
Cdd:cd17995    160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEQVEKLQALLKPYMLRR 223
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
358-592 9.37e-77

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: 253.82  E-value: 9.37e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  358 PKYRKLEQQPSYITGGE---LRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLS 434
Cdd:cd18053      1 PRFVALKKQPSYIGGHEgleLRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  435 TVPAWQETLALWASDMNCISYLGNTTSRQVIRDYEFYVDGTQKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLK 514
Cdd:cd18053     81 TLTSWQREIQTWAPQMNAVVYLGDINSRNMIRTHEWMHPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLK 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246743034  515 NSESSLYEALSQFKNSNRLLITGTPLQNNIRELAALVDFLMPGKFEIREEINLEAPDEEQEAYIrSLQEHLQPYILRR 592
Cdd:cd18053    161 NDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYGYA-SLHKELEPFLLRR 237
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
372-594 2.46e-76

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: 252.67  E-value: 2.46e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  372 GGELRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLSTVPAWQETLALWASDMN 451
Cdd:cd17996      1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  452 CISYLGNTTSRQVIRDYEfyvdgtQKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFKNS- 530
Cdd:cd17996     81 KIVYKGTPDVRKKLQSQI------RAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHAr 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246743034  531 NRLLITGTPLQNNIRELAALVDFLMPGKFEIR---------------EEINLEAPDEEQEAYIRSLQEHLQPYILRRLK 594
Cdd:cd17996    155 YRLLLTGTPLQNNLPELWALLNFLLPKIFKSCktfeqwfntpfantgEQVKIELNEEETLLIIRRLHKVLRPFLLRRLK 233
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
375-556 5.98e-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: 246.32  E-value: 5.98e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLSTVPAWQETLALWASDMNCIS 454
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  455 YLGNTTSRQVIRDYEfyvdgtQKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFKNSNRLL 534
Cdd:cd17919     81 YHGSQRERAQIRAKE------KLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLL 154
                          170       180
                   ....*....|....*....|..
gi 1246743034  535 ITGTPLQNNIRELAALVDFLMP 556
Cdd:cd17919    155 LTGTPLQNNLEELWALLDFLDP 176
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
372-594 4.74e-70

DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 and 5 (SMARCA1 and SMARCA5) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350755 [Multi-domain]  Cd Length: 222  Bit Score: 234.14  E-value: 4.74e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  372 GGELRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLSTVPAWQETLALWASDMN 451
Cdd:cd17997      1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  452 CISYLGNTTSR-QVIRDYefYVDGtqkiKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFKNS 530
Cdd:cd17997     81 VVVLIGDKEERaDIIRDV--LLPG----KFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSR 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246743034  531 NRLLITGTPLQNNIRELAALVDFLMPGKFEIREE----INLEAPDEEQEAYIRSLQEHLQPYILRRLK 594
Cdd:cd17997    155 NRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDfdewFNVNNCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
372-594 3.76e-65

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: 220.72  E-value: 3.76e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  372 GGELRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSlRQHGPFLVVVPLSTVPAWQETLALWASDMN 451
Cdd:cd18009      1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRER-GVWGPFLVIAPLSTLPNWVNEFARFTPSVP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  452 CISYLGNTTSRQVIRDyEFYVDGTQKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFKNSN 531
Cdd:cd18009     80 VLLYHGTKEERERLRK-KIMKREGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDN 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  532 RLLITGTPLQNNIRELAALVDFLMPGKF----------------EIREEINLEApdEEQEAYI-RSLQEHLQPYILRRLK 594
Cdd:cd18009    159 RLLLTGTPLQNNLSELWSLLNFLLPDVFddlssfeswfdfsslsDNAADISNLS--EEREQNIvHMLHAILKPFLLRRLK 236
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
375-592 8.87e-63

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: 213.37  E-value: 8.87e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLSTVPAWQETLALWASDMNCIS 454
Cdd:cd18003      1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  455 YLGNTTSRQVIRdyefyVDGTQKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFKNSNRLL 534
Cdd:cd18003     81 YYGSAKERKLKR-----QGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLL 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246743034  535 ITGTPLQNNIRELAALVDFLMPGKFEIREEIN------LEAPDEEQEAY----IRSLQEHLQPYILRR 592
Cdd:cd18003    156 LTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKewfsnpLTAMSEGSQEEneelVRRLHKVLRPFLLRR 223
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
375-592 5.81e-61

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: 208.06  E-value: 5.81e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNWMAyLWHKNENG-ILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLSTVPAWQETLALWASDMNCI 453
Cdd:cd18006      1 LRPYQLEGVNWLL-QCRAEQHGcILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  454 SYLGNTTSRQVIRDyefyvDGTQKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFKNSNRL 533
Cdd:cd18006     80 TYMGDKEKRLDLQQ-----DIKSTNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRL 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246743034  534 LITGTPLQNNIRELAALVDFLMPGKF---EIREEINLEAPDEEQEAYIRSLQEHLQPYILRR 592
Cdd:cd18006    155 LLTGTPIQNSLQELYALLSFIEPNVFpkdKLDDFIKAYSETDDESETVEELHLLLQPFLLRR 216
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
689-815 1.80e-59

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: 200.40  E-value: 1.80e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  689 SGKMVLLDKLLSRLRRDGHRVLIFSQMVRMLDILGDYLSLRGYPHQRLDGTVPAAVRRTSIDHFNAPNSpDFVFLLSTRA 768
Cdd:cd18793     10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPD-IRVFLLSTKA 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1246743034  769 GGLGINLMTADTVIIFDSDWNPQADLQAMARAHRIGQKNHVMVYRLL 815
Cdd:cd18793     89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
373-594 9.08e-58

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: 198.94  E-value: 9.08e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  373 GELRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQhGPFLVVVPLSTVPAWQETLALWASDMNC 452
Cdd:cd18012      3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRK-GPSLVVAPTSLIYNWEEEAAKFAPELKV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  453 ISYLGNTTSRQVIRDYEFYvdgtqkikfNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFKNSNR 532
Cdd:cd18012     82 LVIHGTKRKREKLRALEDY---------DLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHR 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246743034  533 LLITGTPLQNNIRELAALVDFLMPG------KFEIREEINLEapDEEQEAYIRSLQEHLQPYILRRLK 594
Cdd:cd18012    153 LALTGTPIENHLGELWSIFDFLNPGllgsykRFKKRFAKPIE--KDGDEEALEELKKLISPFILRRLK 218
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
362-604 1.06e-56

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: 196.81  E-value: 1.06e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  362 KLEQQPSYITGGELRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLSTVPAWQE 441
Cdd:cd18064      3 RFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  442 TLALWASDMNCISYLGNTTSRQVirdyeFYVDGTQKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLY 521
Cdd:cd18064     83 EFKRWVPTLRAVCLIGDKDQRAA-----FVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLS 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  522 EALSQFKNSNRLLITGTPLQNNIRELAALVDFLMPGKFEIREEINLEAPDEE---QEAYIRSLQEHLQPYILRRLKKDVE 598
Cdd:cd18064    158 EIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNclgDQKLVERLHMVLRPFLLRRIKADVE 237

                   ....*.
gi 1246743034  599 KSLPSK 604
Cdd:cd18064    238 KSLPPK 243
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
375-592 1.04e-55

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: 192.96  E-value: 1.04e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLaHSLRQHGPFLVVVPLSTVPAWQETLALWaSDMNCIS 454
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEV-YNVGIHGPFLVIAPLSTITNWEREFNTW-TEMNTIV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  455 YLGNTTSRQVIRDYEFYVDGTQ------KIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFK 528
Cdd:cd18060     79 YHGSLASRQMIQQYEMYCKDSRgrlipgAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246743034  529 NSNRLLITGTPLQNNIRELAALVDFLMPGKFEIREEINLEAPDEEQEAYIRSLQEHLQPYILRR 592
Cdd:cd18060    159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
362-594 1.30e-55

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: 193.31  E-value: 1.30e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  362 KLEQQPSYITGGELRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLSTVPAWQE 441
Cdd:cd18065      3 RFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMN 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  442 TLALWASDMNCISYLGNTTSRQVirdyeFYVDGTQKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLY 521
Cdd:cd18065     83 EFKRWVPSLRAVCLIGDKDARAA-----FIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLS 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246743034  522 EALSQFKNSNRLLITGTPLQNNIRELAALVDFLMPGKFEIREEINLEAPDEE---QEAYIRSLQEHLQPYILRRLK 594
Cdd:cd18065    158 EIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNclgDQKLVERLHAVLKPFLLRRIK 233
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
375-592 1.59e-55

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: 192.72  E-value: 1.59e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLSTVPAWQETLALWASDMNCIS 454
Cdd:cd18002      1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  455 YLGNTTSRQVIRDY----EFYvdgTQKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFKNS 530
Cdd:cd18002     81 YWGNPKDRKVLRKFwdrkNLY---TRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246743034  531 NRLLITGTPLQNNIRELAALVDFLMPGKFEIREEIN----------LEAPDEEQEAYIRSLQEHLQPYILRR 592
Cdd:cd18002    158 NRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNewfskdieshAENKTGLNEHQLKRLHMILKPFMLRR 229
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
362-594 1.64e-55

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: 193.72  E-value: 1.64e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  362 KLEQQPSYITGGELRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLSTVPAWQE 441
Cdd:cd18062     11 KVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWVY 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  442 TLALWASDMNCISYLGNTTSRQVirdyefYVDGTQKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLY 521
Cdd:cd18062     91 EFDKWAPSVVKVSYKGSPAARRA------FVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLT 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  522 EAL-SQFKNSNRLLITGTPLQNNIRELAALVDFLMPGKFE---------------IREEINLEapDEEQEAYIRSLQEHL 585
Cdd:cd18062    165 QVLnTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKscstfeqwfnapfamTGEKVDLN--EEETILIIRRLHKVL 242

                   ....*....
gi 1246743034  586 QPYILRRLK 594
Cdd:cd18062    243 RPFLLRRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
362-594 4.04e-55

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: 192.59  E-value: 4.04e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  362 KLEQQPSYITGGELRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLSTVPAWQE 441
Cdd:cd18063     11 RVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTY 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  442 TLALWASDMNCISYLGNTTSRQVIrdyefyVDGTQKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLY 521
Cdd:cd18063     91 EFDKWAPSVVKISYKGTPAMRRSL------VPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLT 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  522 EAL-SQFKNSNRLLITGTPLQNNIRELAALVDFLMPGKFE---------------IREEINLEapDEEQEAYIRSLQEHL 585
Cdd:cd18063    165 QVLnTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKscstfeqwfnapfamTGERVDLN--EEETILIIRRLHKVL 242

                   ....*....
gi 1246743034  586 QPYILRRLK 594
Cdd:cd18063    243 RPFLLRRLK 251
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
375-592 4.80e-55

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: 190.34  E-value: 4.80e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLSTVPAWQETLALWASDMNCIS 454
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  455 YLGNttsrqvirdyefyvdgtqkikfNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFKNSNRLL 534
Cdd:cd17994     81 YVGD----------------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLL 138
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1246743034  535 ITGTPLQNNIRELAALVDFLMPGKFEIREEINLEAPDEEQEAYIRSLQEHLQPYILRR 592
Cdd:cd17994    139 LTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQIKKLHDLLGPHMLRR 196
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
375-562 4.89e-55

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: 189.90  E-value: 4.89e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRqHGPFLVVVPLSTVPAWQETLALWASDMNCIS 454
Cdd:cd17998      1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGI-PGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  455 YLGNTTSRQVIRDYEFyvdgTQKIKFNLLLTTYEYVL---KDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFKNSN 531
Cdd:cd17998     80 YYGSQEERKHLRYDIL----KGLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANF 155
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1246743034  532 RLLITGTPLQNNIRELAALVDFLMPGKFEIR 562
Cdd:cd17998    156 RLLLTGTPLQNNLLELMSLLNFIMPKPFILR 186
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
375-592 2.16e-54

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: 189.84  E-value: 2.16e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLSTVPAWQETLALWASDMNCIS 454
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  455 YLGNTTSRQVIRDYEFYVDGT--------------QKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSL 520
Cdd:cd18055     81 YTGDKDSRAIIRENEFSFDDNavkggkkafkmkreAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246743034  521 YEALSQFKNSNRLLITGTPLQNNIRELAALVDFLMPGKFEIREEINLEAPDEEQEAYIRSLQEHLQPYILRR 592
Cdd:cd18055    161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
375-592 3.90e-54

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: 188.70  E-value: 3.90e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLsYLAHSLRQHGPFLVVVPLSTVPAWQETLALWaSDMNCIS 454
Cdd:cd18059      1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTW-TELNVVV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  455 YLGNTTSRQVIRDYEFYVDGTQ------KIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFK 528
Cdd:cd18059     79 YHGSQASRRTIQLYEMYFKDPQgrvikgSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246743034  529 NSNRLLITGTPLQNNIRELAALVDFLMPGKFEIREEINLEAPDEEQEAYIRSLQEHLQPYILRR 592
Cdd:cd18059    159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
375-592 5.76e-54

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: 188.33  E-value: 5.76e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLaHSLRQHGPFLVVVPLSTVPAWQETLALWaSDMNCIS 454
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEI-FLMGIRGPFLIIAPLSTITNWEREFRTW-TEMNAIV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  455 YLGNTTSRQVIRDYEFYVDGTQ------KIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFK 528
Cdd:cd18058     79 YHGSQISRQMIQQYEMYYRDEQgnplsgIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246743034  529 NSNRLLITGTPLQNNIRELAALVDFLMPGKFEIREEINLEAPDEEQEAYIRSLQEHLQPYILRR 592
Cdd:cd18058    159 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
375-592 8.61e-54

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: 187.96  E-value: 8.61e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLSTVPAWQETLALWASDMNCIS 454
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  455 YLGNTTSRQVIRDYEFYVDGTQ--------------KIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSL 520
Cdd:cd18057     81 YTGDKESRSVIRENEFSFEDNAirsgkkvfrmkkeaQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246743034  521 YEALSQFKNSNRLLITGTPLQNNIRELAALVDFLMPGKFEIREEINLEAPDEEQEAYIRSLQEHLQPYILRR 592
Cdd:cd18057    161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
375-592 4.98e-53

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: 185.65  E-value: 4.98e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLSTVPAWQETLALWASDMNCIS 454
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  455 YLGNTTSRQVIRDYEFY-----VDGTQK---------IKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSL 520
Cdd:cd18056     81 YVGDKDSRAIIRENEFSfednaIRGGKKasrmkkeasVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246743034  521 YEALSQFKNSNRLLITGTPLQNNIRELAALVDFLMPGKFEIREEINLEAPDEEQEAYIRSLQEHLQPYILRR 592
Cdd:cd18056    161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQIKKLHDMLGPHMLRR 232
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
375-592 2.75e-48

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: 171.73  E-value: 2.75e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLsYLAHSLRQHGPFLVVVPLSTVPAWQETLALWaSDMNCIS 454
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWEREFRTW-TDLNVVV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  455 YLGNTTSRQVIRDYEFYVDGTQ------KIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFK 528
Cdd:cd18061     79 YHGSLISRQMIQQYEMYFRDSQgriirgAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246743034  529 NSNRLLITGTPLQNNIRELAALVDFLMPGKFEIREEINLEAPDEEQEAYIRSLQEHLQPYILRR 592
Cdd:cd18061    159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
375-592 3.68e-44

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: 158.64  E-value: 3.68e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHSLRQHGPFLVVVPLSTVPAWQETLALWASDMNcIS 454
Cdd:cd18000      1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFR-VV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  455 YLGNTTSRQVIRDY---EFYVDGTQKIKFN---LLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFK 528
Cdd:cd18000     80 VLHSSGSGTGSEEKlgsIERKSQLIRKVVGdggILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLR 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246743034  529 NSNRLLITGTPLQNNIRELAALVDFLMPgkfeireeinleapdeeqeayirslqehlqPYILRR 592
Cdd:cd18000    160 TPHRLILSGTPIQNNLKELWSLFDFVFP------------------------------PYLLRR 193
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
375-592 5.02e-44

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: 159.82  E-value: 5.02e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLsYLAHSLRQ------HGPFLVVVPLSTVPAWQETLALWAS 448
Cdd:cd17999      1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCIL-ASDHHKRAnsfnseNLPSLVVCPPTLVGHWVAEIKKYFP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  449 D--MNCISYLGNTTSRQVIRDyefyvdgtQKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQ 526
Cdd:cd17999     80 NafLKPLAYVGPPQERRRLRE--------QGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQ 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  527 FKNSNRLLITGTPLQNNIRELAALVDFLMPG------KFE------IREEINLEAPDEEQEAYIRSL-QEHLQ--PYILR 591
Cdd:cd17999    152 LKANHRLILSGTPIQNNVLELWSLFDFLMPGylgtekQFQrrflkpILASRDSKASAKEQEAGALALeALHKQvlPFLLR 231

                   .
gi 1246743034  592 R 592
Cdd:cd17999    232 R 232
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
375-592 1.05e-42

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: 155.99  E-value: 1.05e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYLAHS-LRQHGpfLVVVPLSTVPAWQETLALWASDMNCI 453
Cdd:cd18001      1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSgLIKSV--LVVMPTSLIPHWVKEFAKWTPGLRVK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  454 SYLGntTSRQVIRDYEFYVdgtqKIKFNLLLTTYEYVLKDRSVLSN-----IKWQYMAIDEAHRLKNSESSLYEALSQFK 528
Cdd:cd18001     79 VFHG--TSKKERERNLERI----QRGGGVLLTTYGMVLSNTEQLSAddhdeFKWDYVILDEGHKIKNSKTKSAKSLREIP 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  529 NSNRLLITGTPLQNNIRELAALVDFLMPG-----------KFE---IREEINLEAPDEEQEAYI--RSLQEHLQPYILRR 592
Cdd:cd18001    153 AKNRIILTGTPIQNNLKELWALFDFACNGsllgtrktfkmEFEnpiTRGRDKDATQGEKALGSEvaENLRQIIKPYFLRR 232
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
375-559 7.64e-35

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: 134.04  E-value: 7.64e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNWMAYLWHKNENGILADEMGLGKTVQTVAFLSYL--------------------AHSLRQHGPFLVVVPLS 434
Cdd:cd18005      1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVlgktgtrrdrennrprfkkkPPASSAKKPVLIVAPLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  435 TVPAWQETLALWASdMNCISYLGNTTSRQVIRDYefyvdgtQKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLK 514
Cdd:cd18005     81 VLYNWKDELDTWGH-FEVGVYHGSRKDDELEGRL-------KAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIK 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1246743034  515 NSESSLYEALSQFKNSNRLLITGTPLQNNIRELAALVDFLMPGKF 559
Cdd:cd18005    153 NPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGAL 197
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
375-592 3.56e-32

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: 125.86  E-value: 3.56e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNWM--AYLWHKNENG---ILADEMGLGKTVQTVAFLSYLAHSLRQHGP----FLVVVPLSTVPAWQETLAL 445
Cdd:cd18004      1 LRPHQREGVQFLydCLTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKPtakkALIVCPSSLVGNWKAEFDK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  446 WASDMNCISYLGNTTSRQVIRDYEFYvdGTQKIkFNLLLTTYEYVLKDRSVLSNIKWQYMAI-DEAHRLKNSESSLYEAL 524
Cdd:cd18004     81 WLGLRRIKVVTADGNAKDVKASLDFF--SSAST-YPVLIISYETLRRHAEKLSKKISIDLLIcDEGHRLKNSESKTTKAL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  525 SQFKNSNRLLITGTPLQNNIRELAALVDFLMPG----------KFEIREEINLE--APDEEQE-AYIRS--LQEHLQPYI 589
Cdd:cd18004    158 NSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGilgslasfrkVFEEPILRSRDpdASEEDKElGAERSqeLSELTSRFI 237

                   ...
gi 1246743034  590 LRR 592
Cdd:cd18004    238 LRR 240
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
397-565 4.14e-30

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: 120.09  E-value: 4.14e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  397 ILADEMGLGKTVQTVAFL-SYLAHSLRQHGPfLVVVPLSTVPAWQETLALWASDM-----NCISYLGNTTSRQVIRD-YE 469
Cdd:cd18007     30 ILAHTMGLGKTLQVITFLhTYLAAAPRRSRP-LVLCPASTLYNWEDEFKKWLPPDlrpllVLVSLSASKRADARLRKiNK 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  470 FYVDGtqkikfNLLLTTYEY---VLKDRSVLSNIKWQYMA-----------IDEAHRLKNSESSLYEALSQFKNSNRLLI 535
Cdd:cd18007    109 WHKEG------GVLLIGYELfrnLASNATTDPRLKQEFIAalldpgpdllvLDEGHRLKNEKSQLSKALSKVKTKRRILL 182
                          170       180       190
                   ....*....|....*....|....*....|
gi 1246743034  536 TGTPLQNNIRELAALVDFLMPGKFEIREEI 565
Cdd:cd18007    183 TGTPLQNNLKEYWTMVDFARPKYLGTLKEF 212
CD1_tandem_CHD1_yeast_like cd18665
repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
189-250 2.07e-29

repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein 1, and similar proteins; Repeat 1 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: 349312  Cd Length: 65  Bit Score: 111.71  E-value: 2.07e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246743034  189 DTRAIDVVLDHRLIEGHDGS---TPSEDYEFLIKWVNFSHLHCTWEPYNNISMIRGSKKVDNHIK 250
Cdd:cd18665      1 DEHGIDIVLDHRLKEGLEEGeldDPKENYEFLIKWTDESHLHNTWETYESLKQVRGLKKVDNYIK 65
DUF4208 pfam13907
Domain of unknown function (DUF4208); This domain is found at the C-terminus of ...
1300-1384 8.29e-28

Domain of unknown function (DUF4208); This domain is found at the C-terminus of chromodomain-helicase-DNA-binding proteins. The exact function of the domain is undetermined.


Pssm-ID: 464035  Cd Length: 93  Bit Score: 108.11  E-value: 8.29e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034 1300 ARCKELMYPVRKHMKRLRKDSSGLGRAELVKLLTECLTTIGKHIEKTVNDTPSEEKATVRKNLWMFACYFWPKeEVKYTS 1379
Cdd:pfam13907    9 EECKELMRPVKKSLKRLKKGTKGLSRKERAKILKKELLKIGDFIDSLLEETKKEKKEKLRKHLWSFVSKFWPN-KVSGKK 87

                   ....*
gi 1246743034 1380 LISMY 1384
Cdd:pfam13907   88 LKEMY 92
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
375-592 8.51e-28

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: 113.54  E-value: 8.51e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNWMayLWHkneNGILADEMGLGKTVQTVA-----------------FLSYLAHSLRQHGPFLVVVPLSTVP 437
Cdd:cd18008      1 LLPYQKQGLAWM--LPR---GGILADEMGLGKTIQALAlilatrpqdpkipeeleENSSDPKKLYLSKTTLIVVPLSLLS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  438 AWQETLA--LWASDMNCISYLGnttSRQVIRDYEFYvdgtqkiKFNLLLTTY-----EY-----------VLKDRSVLSN 499
Cdd:cd18008     76 QWKDEIEkhTKPGSLKVYVYHG---SKRIKSIEELS-------DYDIVITTYgtlasEFpknkkgggrdsKEKEASPLHR 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  500 IKWQYMAIDEAHRLKNSESSLYEALSQFKNSNRLLITGTPLQNNIRELAALVDFL------MPGKFeiREEINLEAPDEE 573
Cdd:cd18008    146 IRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLrvepfgDYPWF--NSDISKPFSKND 223
                          250
                   ....*....|....*....
gi 1246743034  574 QEAYIRsLQEHLQPYILRR 592
Cdd:cd18008    224 RKALER-LQALLKPILLRR 241
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
690-804 2.29e-26

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 104.60  E-value: 2.29e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  690 GKMVLLDKLLSRLRrdGHRVLIFSQMVRMLDIlgDYLSLR-GYPHQRLDGTVPAAVRRTSIDHFNAPNSPdfvFLLSTRA 768
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKKTLEA--ELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1246743034  769 GGLGINLMTADTVIIFDSDWNPQADLQAMARAHRIG 804
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXDc smart00487
DEAD-like helicases superfamily;
374-558 3.04e-26

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 107.58  E-value: 3.04e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034   374 ELRDFQLTGVNWMaylWHKNENGILADEMGLGKTVQTVAFLSYLAHSlRQHGPFLVVVPL-STVPAWQETLALWASDMN- 451
Cdd:smart00487    8 PLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAALLPALEALKR-GKGGRVLVLVPTrELAEQWAEELKKLGPSLGl 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034   452 -CISYLGNTTSRQVIRDYEfyvdgtqKIKFNLLLTTYEYVLKD--RSVLSNIKWQYMAIDEAHRLKNS--ESSLYEALSQ 526
Cdd:smart00487   84 kVVGLYGGDSKREQLRKLE-------SGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKL 156
                           170       180       190
                    ....*....|....*....|....*....|....*.
gi 1246743034   527 F-KNSNRLLITGTP---LQNNIRELAALVDFLMPGK 558
Cdd:smart00487  157 LpKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGF 192
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
375-592 6.23e-24

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: 102.16  E-value: 6.23e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNwmaYLWH-------KNENG-ILADEMGLGKTVQTVAFLSYLahsLRQhGP--------FLVVVPLSTVPA 438
Cdd:cd18067      1 LRPHQREGVK---FLYRcvtgrriRGSHGcIMADEMGLGKTLQCITLMWTL---LRQ-SPqckpeidkAIVVSPSSLVKN 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  439 WQETLALW-ASDMNCISYLGNTTSRQVIRDYEFYVDGTQKIKFNLLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSE 517
Cdd:cd18067     74 WANELGKWlGGRLQPLAIDGGSKKEIDRKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSD 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  518 SSLYEALSQFKNSNRLLITGTPLQNNIRELAALVDFLMPGKFEIREEI--NLEAP----------DEEQEAYIRSLQE-- 583
Cdd:cd18067    154 NQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFkkNFELPilkgrdadasEKERQLGEEKLQEli 233
                          250
                   ....*....|
gi 1246743034  584 -HLQPYILRR 592
Cdd:cd18067    234 sIVNRCIIRR 243
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
375-557 2.27e-22

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: 97.61  E-value: 2.27e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVnwmAYLWH----KNENG----ILADEMGLGKTVQTVAflsyLAHSLRQHGPF---------LVVVPLSTVP 437
Cdd:cd18066      1 LRPHQREGI---EFLYEcvmgMRVNErfgaILADEMGLGKTLQCIS----LIWTLLRQGPYggkpvikraLIVTPGSLVK 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  438 AWQETLALWasdmncisyLGnttsRQVIRdyEFYVDGTQKIK-------FNLLLTTYEYVLKDRSVLSNIKWQYMAIDEA 510
Cdd:cd18066     74 NWKKEFQKW---------LG----SERIK--VFTVDQDHKVEefiasplYSVLIISYEMLLRSLDQISKLNFDLVICDEG 138
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1246743034  511 HRLKNSESSLYEALSQFKNSNRLLITGTPLQNNIRELAALVDFLMPG 557
Cdd:cd18066    139 HRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPG 185
HELICc smart00490
helicase superfamily c-terminal domain;
720-804 1.39e-20

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 87.27  E-value: 1.39e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034   720 DILGDYLSLRGYPHQRLDGTVPAAVRRTSIDHFNAPNSpdfVFLLSTRAGGLGINLMTADTVIIFDSDWNPQADLQAMAR 799
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKI---KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 1246743034   800 AHRIG 804
Cdd:smart00490   78 AGRAG 82
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
375-559 4.81e-20

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: 89.96  E-value: 4.81e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNW-MAylwhKNENGILADEMGLGKTVQTVAflsyLAHSLRQHGPFLVVVPLSTVPAWQETLALWASDM--- 450
Cdd:cd18010      1 LLPFQREGVCFaLR----RGGRVLIADEMGLGKTVQAIA----IAAYYREEWPLLIVCPSSLRLTWADEIERWLPSLppd 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  451 --NCIsylgnTTSRQVIRdyefyvDGTQKIkfnlLLTTYEYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQF- 527
Cdd:cd18010     73 diQVI-----VKSKDGLR------DGDAKV----VIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLl 137
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1246743034  528 KNSNR-LLITGTPLQNNIRELAALVDFLMPGKF 559
Cdd:cd18010    138 KRAKRvILLSGTPALSRPIELFTQLDALDPKLF 170
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
286-339 8.09e-20

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: 84.16  E-value: 8.09e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1246743034  286 EYKQVDRIVAKHLNSDGSVEYLVKWKQLLYDFCTWEASSIIEPIAATEIQAFQE 339
Cdd:cd18659      1 EYTIVERIIAHREDDEGVTEYLVKWKGLPYDECTWESEEDISDIFQEAIDEYKK 54
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
396-563 3.11e-19

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: 88.68  E-value: 3.11e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  396 GILADEMGLGKTVQTVAFLsyLAHslrqhgPFLVVVPLSTVPAWQETLA--LWASDMNCISYLGNTTSRQVirdyefyvd 473
Cdd:cd18071     51 GILADDMGLGKTLTTISLI--LAN------FTLIVCPLSVLSNWETQFEehVKPGQLKVYTYHGGERNRDP--------- 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  474 gTQKIKFNLLLTTY-----EYVLKDRSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFKNSNRLLITGTPLQNNIRELA 548
Cdd:cd18071    114 -KLLSKYDIVLTTYntlasDFGAKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLG 192
                          170
                   ....*....|....*
gi 1246743034  549 ALVDFLMPGKFEIRE 563
Cdd:cd18071    193 SLLSFLHLKPFSNPE 207
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
397-564 4.03e-17

DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called RAD54 like 2 or RAD54L2 ) modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. ARIP4 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350827 [Multi-domain]  Cd Length: 227  Bit Score: 82.17  E-value: 4.03e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  397 ILADEMGLGKTVQTVAFLSYLahsLRQHG--PFLVVVPLSTVPAWQETLALWASDMNcisylgnTTSRQVIRDYEFYV-- 472
Cdd:cd18069     32 ILAHSMGLGKTLQVISFLDVL---LRHTGakTVLAIVPVNTLQNWLSEFNKWLPPPE-------ALPNVRPRPFKVFIln 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  473 DGTQKIKFN------------LLLTTYE-YVLKDRSVLsnikwqyMAIDEAHRLKNSESSLYEALSQFKNSNRLLITGTP 539
Cdd:cd18069    102 DEHKTTAARakviedwvkdggVLLMGYEmFRLRPGPDV-------VICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYP 174
                          170       180
                   ....*....|....*....|....*
gi 1246743034  540 LQNNIRELAALVDFLMPGKFEIREE 564
Cdd:cd18069    175 LQNNLIEYWCMVDFVRPDFLGTRQE 199
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
375-579 4.13e-17

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: 81.57  E-value: 4.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNwMAyLWHKNENGILADEMGLGKTVQTVAFLSYLAhsLR-QHGPFLVVVPLSTVPAWQEtlalwasdmnci 453
Cdd:cd18011      1 PLPHQIDAVL-RA-LRKPPVRLLLADEVGLGKTIEAGLIIKELL--LRgDAKRVLILCPASLVEQWQD------------ 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  454 sYLGNTTSRQVIRDYEFYVDGTQKIKFNLLlTTYEYVL----------KDRSVLSNIKWQYMAIDEAHRLKNS----ESS 519
Cdd:cd18011     65 -ELQDKFGLPFLILDRETAAQLRRLIGNPF-EEFPIVIvsldllkrseERRGLLLSEEWDLVVVDEAHKLRNSgggkETK 142
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246743034  520 LYEALSQFKNSNR--LLITGTPLQNNIRELAALVDFLMPGKFE--IREEINLEAPDEEQEAYIR 579
Cdd:cd18011    143 RYKLGRLLAKRARhvLLLTATPHNGKEEDFRALLSLLDPGRFAvlGRFLRLDGLREVLAKVLLR 206
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
396-557 2.36e-16

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: 80.32  E-value: 2.36e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  396 GILADEMGLGKTVQTVAFL-SYLAHS-LRQHGPFLVVVPLSTVPAWQETLALWAS--------DMNCISYLGNTTSRQVI 465
Cdd:cd18068     31 CILAHCMGLGKTLQVVTFLhTVLLCEkLENFSRVLVVCPLNTVLNWLNEFEKWQEglkdeekiEVNELATYKRPQERSYK 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  466 RDYEFYVDGTQKIKFNLL-LTTYEYVLKDRSVLSNIKWQYMA--------IDEAHRLKNSESSLYEALSQFKNSNRLLIT 536
Cdd:cd18068    111 LQRWQEEGGVMIIGYDMYrILAQERNVKSREKLKEIFNKALVdpgpdfvvCDEGHILKNEASAVSKAMNSIRTKRRIVLT 190
                          170       180
                   ....*....|....*....|.
gi 1246743034  537 GTPLQNNIRELAALVDFLMPG 557
Cdd:cd18068    191 GTPLQNNLIEYHCMVNFVKPN 211
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
385-554 1.45e-14

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: 74.82  E-value: 1.45e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  385 WMayLWHKNEN---GILADEMGLGKTVQTVAF----------------------LSYLAHSLRQHGPFLVVVPLSTVPAW 439
Cdd:cd18072     11 WL--LWRERQKprgGILADDMGLGKTLTMIALilaqkntqnrkeeekekaltewESKKDSTLVPSAGTLVVCPASLVHQW 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  440 QETLALWASDMNCISYLGNTTSRQ----VIRDYEfyvdgtqkikfnLLLTTYEYVLKD---------RSVLSNIKWQYMA 506
Cdd:cd18072     89 KNEVESRVASNKLRVCLYHGPNRErigeVLRDYD------------IVITTYSLVAKEiptykeesrSSPLFRIAWARII 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1246743034  507 IDEAHRLKNSESSLYEALSQFKNSNRLLITGTPLQNNIRELAALVDFL 554
Cdd:cd18072    157 LDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFL 204
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
193-250 1.73e-14

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: 69.31  E-value: 1.73e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1246743034  193 IDVVLDHRLIE--------GHDGSTPSEDYEFLIKWVNFSHLHCTWEPYNNISMIRGSKKVDNHIK 250
Cdd:cd18660      5 IEKILDHRPKGpveeasldLTDPDEPWDEREFLVKWKGKSYLHCTWVTEETLEQLRGKKKLKNYIK 70
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
320-859 1.24e-12

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 72.36  E-value: 1.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  320 WEASSIIEPIAATEIQAFQEREESALSPSRGTNYGNSRPKYRKLEQQPSYITGGELRDFQLTGVN-WMAYLWHKNENGIL 398
Cdd:COG1061     26 LELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFELRPYQQEALEaLLAALERGGGRGLV 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  399 ADEMGLGKTVqtvaFLSYLAHSLRQHGPFLVVVPlstvpawqeTLAL---WASDMncisylgnttsRQVIRDYEFyVDGT 475
Cdd:COG1061    106 VAPTGTGKTV----LALALAAELLRGKRVLVLVP---------RRELleqWAEEL-----------RRFLGDPLA-GGGK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  476 QKIKFNLLLTTYEyVLKDRSVLSNIK--WQYMAIDEAHRLknSESSLYEALSQFKNSNRLLITGTPLQNNIRELaALVDF 553
Cdd:COG1061    161 KDSDAPITVATYQ-SLARRAHLDELGdrFGLVIIDEAHHA--GAPSYRRILEAFPAAYRLGLTATPFRSDGREI-LLFLF 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  554 lmpgkFEIREEINLeapdeeQEAyIRslQEHLQPYILrrlkkdvekslpskseRILRVELSDLQMywykniltrnyrvlt 633
Cdd:COG1061    237 -----DGIVYEYSL------KEA-IE--DGYLAPPEY----------------YGIRVDLTDERA--------------- 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  634 qsissgsqisllnivvelkkasnhpyLFDGVEESWMQKINSQGRRdevlkglimnsgKMVLLDKLLSRlRRDGHRVLIFS 713
Cdd:COG1061    272 --------------------------EYDALSERLREALAADAER------------KDKILRELLRE-HPDDRKTLVFC 312
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  714 QMVRMLDILGDYLSLRGYPHQRLDGTVPAAVRRTSIDHFNApnsPDFVFLLSTRAGGLGINLMTADTVIIFDSDWNPQAD 793
Cdd:COG1061    313 SSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRD---GELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREF 389
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246743034  794 LQAMARAHRIGQ-KNHVMVYRLLSKDT-IEEDVLERARRKMILEYAIISLGVTDKQKNSKNDKFSAEE 859
Cdd:COG1061    390 IQRLGRGLRPAPgKEDALVYDFVGNDVpVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEV 457
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
375-556 2.81e-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: 68.52  E-value: 2.81e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNWMayLWHKnenGILADEMGLGKTVQTVAFLsyLAH---------------------------SLRQHGPF 427
Cdd:cd18070      1 LLPYQRRAVNWM--LVPG---GILADEMGLGKTVEVLALI--LLHprpdndldaadddsdemvccpdclvaeTPVSSKAT 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  428 LVVVPLSTVPAWQETLALWA-SDMNCISYLGNTTSRQVIRDYEFYVdGTQKIkfnlLLTTYEyVLKD------------- 493
Cdd:cd18070     74 LIVCPSAILAQWLDEINRHVpSSLKVLTYQGVKKDGALASPAPEIL-AEYDI----VVTTYD-VLRTelhyaeanrsnrr 147
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246743034  494 ----------RSVLSNIKWQYMAIDEAHRLKNSESSLYEALSQFKNSNRLLITGTPLQNNIRELAALVDFLMP 556
Cdd:cd18070    148 rrrqkryeapPSPLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGV 220
CD2_tandem_ScCHD1_like cd18664
repeat 2 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
286-340 1.29e-11

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: 61.13  E-value: 1.29e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1246743034  286 EYKQVDRIVAKHLNSDGS----VEYLVKWKQLLYDFCTWEASSIIEPIAATEIQAFQER 340
Cdd:cd18664      1 EFHVVERIIASQRASLEDgtsqLQYLVKWRRLNYDECTWEDATLIAKLAPEQVDHFQNR 59
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
288-340 2.86e-11

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 59.90  E-value: 2.86e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1246743034  288 KQVDRIVAKHLNSDGSVEYLVKWKQLLYDFCTWEASSIIEPIAAtEIQAFQER 340
Cdd:pfam00385    1 YEVERILDHRKDKGGKEEYLVKWKGYPYDENTWEPEENLSKCPE-LIEEFKDR 52
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
375-558 3.82e-10

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: 61.21  E-value: 3.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNWMayLWHKnENGILADeMGLGKTVQTVAFLSYLaHSLRQHGPFLVVVPLsTVPA--WQETLALWASDMNC 452
Cdd:cd18013      1 PHPYQKVAINFI--IEHP-YCGLFLD-MGLGKTVTTLTALSDL-QLDDFTRRVLVIAPL-RVARstWPDEVEKWNHLRNL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  453 ISYLGNTTSRQVIR----DYEFYVdgtqkIKFNLllttyeyvLKDRSVLSNIKWQY--MAIDEAHRLKNSESSLYEAL-S 525
Cdd:cd18013     75 TVSVAVGTERQRSKaantPADLYV-----INREN--------LKWLVNKSGDPWPFdmVVIDELSSFKSPRSKRFKALrK 141
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1246743034  526 QFKNSNRLL-ITGTPLQNNIRELAALVDFLMPGK 558
Cdd:cd18013    142 VRPVIKRLIgLTGTPSPNGLMDLWAQIALLDQGE 175
CHROMO smart00298
Chromatin organization modifier domain;
286-342 5.62e-10

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 56.07  E-value: 5.62e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1246743034   286 EYKqVDRIVAKHLNSDGSVEYLVKWKQLLYDFCTWEASSIIEPiAATEIQAFQEREE 342
Cdd:smart00298    1 EYE-VEKILDHRWKKKGELEYLVKWKGYSYSEDTWEPEENLLN-CSKKLDNYKKKER 55
ResIII pfam04851
Type III restriction enzyme, res subunit;
374-539 1.09e-09

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 58.84  E-value: 1.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  374 ELRDFQLTGV-NWMAYLWHKNENGILADEMGLGKTVqTVAFLSYLAHSLRQHGPFLVVVP-LSTVPAWQETLALWASDM- 450
Cdd:pfam04851    3 ELRPYQIEAIeNLLESIKNGQKRGLIVMATGSGKTL-TAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFLPNYv 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  451 -NCISYLGNTTSRQViRDYEFYVDGTQKIkFNLLLTTYEYVLKDRSVlsnikwqYMAIDEAHRLkNSESslYEA-LSQFK 528
Cdd:pfam04851   82 eIGEIISGDKKDESV-DDNKIVVTTIQSL-YKALELASLELLPDFFD-------VIIIDEAHRS-GASS--YRNiLEYFK 149
                          170
                   ....*....|.
gi 1246743034  529 NSNRLLITGTP 539
Cdd:pfam04851  150 PAFLLGLTATP 160
CD1_tandem_CHD1-2_like cd18666
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
189-250 3.08e-08

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


Pssm-ID: 349313  Cd Length: 85  Bit Score: 52.29  E-value: 3.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  189 DTRAIDVVLDHR---------------LIEGHDGS----TPSEDYE--FLIKWVNFSHLHCTWEPYNNISM--IRGSKKV 245
Cdd:cd18666      1 EFETIERVLDHRigrkgatgasttiyaVEADGDPNagfdPEDEETEiqYLIKWKGWSHIHNTWESEESLKDqnVKGMKKL 80

                   ....*
gi 1246743034  246 DNHIK 250
Cdd:cd18666     81 ENYKK 85
CHROMO smart00298
Chromatin organization modifier domain;
192-250 8.36e-08

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 49.90  E-value: 8.36e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1246743034   192 AIDVVLDHRLIEGhdgstpsEDYEFLIKWVNFSHLHCTWEPYNNISmiRGSKKVDNHIK 250
Cdd:smart00298    3 EVEKILDHRWKKK-------GELEYLVKWKGYSYSEDTWEPEENLL--NCSKKLDNYKK 52
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
393-538 1.09e-07

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 52.41  E-value: 1.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  393 NENGILADEMGLGKTvqTVAFLSYLAHSLRQHGPFLVVVPLST-VPAWQETLALWASDMNCISYLGNTTSrqvirDYEFY 471
Cdd:cd00046      1 GENVLITAPTGSGKT--LAALLAALLLLLKKGKKVLVLVPTKAlALQTAERLRELFGPGIRVAVLVGGSS-----AEERE 73
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246743034  472 VDGTQKIKfnLLLTTYEYVLKD-----RSVLSNIKwqYMAIDEAHRLKNSESSLYEALSQ-----FKNSNRLLITGT 538
Cdd:cd00046     74 KNKLGDAD--IIIATPDMLLNLllredRLFLKDLK--LIIVDEAHALLIDSRGALILDLAvrkagLKNAQVILLSAT 146
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
286-322 2.91e-07

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: 48.41  E-value: 2.91e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1246743034  286 EYKQVDRIVAKHLNSDGSVEYLVKWKQLLYDFCTWEA 322
Cdd:cd18662      2 EWLQIHRIINHRVDKDGNTWYLVKWRDLPYDQSTWES 38
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
287-341 2.37e-06

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: 46.13  E-value: 2.37e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  287 YKQVDRI--VAKHLNSDGSVE---YLVKWKQLLYDFCTWEASSIIEPiaaTEIQAFQERE 341
Cdd:cd18663      3 YVEVDRIldVSVSTDPNTGEPvthYLVKWCSLPYEDSTWELEEDVDP---AKIEEFEKLR 59
Cdh1_DBD_1 pfam18196
Chromodomain helicase DNA-binding domain 1; This domain can be found in chromodomain helicase ...
997-1081 4.50e-06

Chromodomain helicase DNA-binding domain 1; This domain can be found in chromodomain helicase DNA-binding protein 1 (Chd1) present in Saccharomyces cerevisiae. Cdh1 proteins have been associated with the efficient assembly and spacing of nucleosomes. The domain consists of four helices, alpha helix 1-4, and can be divided into regions SANT, HL1 and the beta-linker. The HL1 region comprises of some 40 residues specific to budding yeast that are unlikely to form such a prominent feature or perform a conserved function in other species. The domain itself forms part of the DNA-binding domain. Basic residues on the alpha-1 helix are thought to be important for DNA interaction.


Pssm-ID: 408024 [Multi-domain]  Cd Length: 120  Bit Score: 47.09  E-value: 4.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  997 EKEIRLLYRAMIRYGSLEHRYNDIVKYADLTTQDAHVIKKIAADLVTASRKAV-----------SAAEKD---------- 1055
Cdd:pfam18196    3 EREIRALYKAILRYGDLSNMFEELIADGSLPQKSIERYEELYRELIEQAKRVVkeeeekrneelEALEADamaykaalkg 82
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1246743034 1056 -----LSNDQSN-------NKSSRKALLITFKGVKNIN 1081
Cdd:pfam18196   83 ggvtaDDQPKDTpitklaaKRREKKAILFEFYGVKNLN 120
CD2_tandem_CHD1-2_like cd18661
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
286-340 1.35e-05

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


Pssm-ID: 349308  Cd Length: 58  Bit Score: 43.83  E-value: 1.35e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1246743034  286 EYKQVDRIVAkHLNS----DGSVEYLVKWKQLLYDFCTWEASSIIEPIAATEIQAFQER 340
Cdd:cd18661      1 QYQIVERIIA-HSPQksaaSGYPDYLCKWQGLPYSECTWEDGALISKKFQACIDEYHSR 58
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
375-539 1.97e-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: 46.14  E-value: 1.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  375 LRDFQLTGVNwmAYLWHKNEN-GILADEMGLGKTVqTVAFLSYLAHSLRqhgpFLVVVPlstvpawqeTLAL---WASdm 450
Cdd:cd17926      1 LRPYQEEALE--AWLAHKNNRrGILVLPTGSGKTL-TALALIAYLKELR----TLIVVP---------TDALldqWKE-- 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  451 NCISYLGNTTSRQVIRDYEFYVDGtqkikFNLLLTTYEYVLKDRSVLSNIKWQYMAI--DEAHRLknSESSLYEALSQFK 528
Cdd:cd17926     63 RFEDFLGDSSIGLIGGGKKKDFDD-----ANVVVATYQSLSNLAEEEKDLFDQFGLLivDEAHHL--PAKTFSEILKELN 135
                          170
                   ....*....|.
gi 1246743034  529 NSNRLLITGTP 539
Cdd:cd17926    136 AKYRLGLTATP 146
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
187-253 3.69e-05

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: 43.09  E-value: 3.69e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246743034  187 PEDTRAIDVVLDHRL--IEGHDGSTPSEDYEFLIKWVNFSHLHCTWEPYNNIsmirgsKKVDNHIKQVI 253
Cdd:cd18668      1 EEDTMIIEKILASRKkkKEKEEGAEEIEVEEYLVKYKNFSYLHCEWKTEEEL------EKGDKRIKQKI 63
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
691-965 1.04e-04

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 46.65  E-value: 1.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  691 KMVLLDKLLSRLR--RDGHRVLIFSQMVRMLDILGDYLSLRGYPHQRLDGTvpaAVRRTS-----------IDHFNAPns 757
Cdd:COG1111    336 KLSKLREILKEQLgtNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQ---ASKEGDkgltqkeqieiLERFRAG-- 410
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  758 pDFVFLLSTRAGGLGINLMTADTVIIFDSDWNPQADLQAMARAHRIGQKNhvmVYRLLSKDTIEEDVLERARRK---MIL 834
Cdd:COG1111    411 -EFNVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKREGR---VVVLIAKGTRDEAYYWSSRRKekkMKS 486
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  835 EYAIISlGVTDKQKNSKNDKFSAEELSAIlkFGASNMFKAENNQKKLEDMNLDEILEHAEDHDTSNDVGGASMGGEEFLK 914
Cdd:COG1111    487 ILKKLK-KLLDKQEKEKLKESAQATLDEF--ESIKELAEDEINEKDLDEIESSENGAHVDWREPVLLQVIVSTLAESLEL 563
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1246743034  915 QFEVTDykaDVSWDDIIPLTEREKFEEEDRLREEEEALKQEIELSSRRGNR 965
Cdd:COG1111    564 RELGEK---VDDEVNLILEIDRVDVVDDGSVLRVSRLLVEIGELDGKTRVI 611
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
196-237 1.61e-04

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: 40.54  E-value: 1.61e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1246743034  196 VLDHRLIEGHdgstpsedYEFLIKWVNFSHLHCTWEPYNNIS 237
Cdd:cd00024      6 ILDHRVRKGK--------LEYLVKWKGYPPEENTWEPEENLT 39
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
191-237 1.69e-04

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 40.64  E-value: 1.69e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1246743034  191 RAIDVVLDHRLIEGHDGstpsedyEFLIKWVNFSHLHCTWEPYNNIS 237
Cdd:pfam00385    1 YEVERILDHRKDKGGKE-------EYLVKWKGYPYDENTWEPEENLS 40
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
760-812 2.50e-04

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 40.77  E-value: 2.50e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1246743034  760 FVFLLSTRAGGLGINLMTADTVIIFDSDWNPQADLQAMARAHRIGQKNHVMVY 812
Cdd:cd18785     23 LEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVIL 75
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
654-821 6.62e-04

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: 43.47  E-value: 6.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  654 ASNHPYLfdgVEESWMQKinSQGRRDEVLKgLIMNSGKMVLLDKLLS----RLRRDGHRVLIFSQMVRMLD-----ILGD 724
Cdd:pfam11496   60 VATHPYL---LVDHYMPK--SLLLKDEPEK-LAYTSGKFLVLNDLVNllieRDRKEPINVAIVARSGKTLDlvealLLGK 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  725 YLSLRGYPHQRLDGTVpaavRRTSIDHFNAPNSPDFVFLLSTRAGGLGINLMT---ADTVIIFDSDWNPQADLQAMARAH 801
Cdd:pfam11496  134 GLSYKRYSGEMLYGEN----KKVSDSGNKKIHSTTCHLLSSTGQLTNDDSLLEnykFDLIIAFDSSVDTSSPSVEHLRTQ 209
                          170       180
                   ....*....|....*....|
gi 1246743034  802 RIGQKNHVMVYRLLSKDTIE 821
Cdd:pfam11496  210 NRRKGNLAPIIRLVVINSIE 229
CD_HP1alpha_Cbx5 cd18651
chromodomain of heterochromatin protein 1 homolog alpha; CHRomatin Organization Modifier ...
193-236 7.88e-04

chromodomain of heterochromatin protein 1 homolog alpha; CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 homolog alpha (also known as HP1alpha, Cbx5, and Chromobox 5), and related proteins. HP1alpha has diverse functions in heterochromatin formation, gene regulation, and mitotic progression, and forms complex networks of gene, RNA, and protein interactions. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha, HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3).


Pssm-ID: 349298  Cd Length: 50  Bit Score: 38.82  E-value: 7.88e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1246743034  193 IDVVLDHRLIEGHdgstpsedYEFLIKWVNFSHLHCTWEPYNNI 236
Cdd:cd18651      4 VEKVLDRRVVKGQ--------VEYLLKWKGFSEEHNTWEPEKNL 39
CD_Chro-like cd18640
chromodomain of Drosophila melanogaster chromator chromodomain protein, and similar proteins; ...
214-237 1.03e-03

chromodomain of Drosophila melanogaster chromator chromodomain protein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in chromodomain of Drosophila melanogaster chromator (also known as Chriz/Chro) chromodomain protein, and similar proteins. Chromator is a nuclear protein that plays a role in proper spindle dynamics during mitosis. 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: 349290  Cd Length: 52  Bit Score: 38.43  E-value: 1.03e-03
                           10        20
                   ....*....|....*....|....
gi 1246743034  214 YEFLIKWVNFSHLHCTWEPYNNIS 237
Cdd:cd18640     18 WEYLVKWENRSHHENTWEPMANLE 41
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
403-539 1.20e-03

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 41.07  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246743034  403 GLGKTvqTVAFLSYLAH-SLRQHGP-FLVVVPLSTVpAWQ--ETLALWASDMN--CISYLGNTTSRQVIRDYEFYvdgtq 476
Cdd:pfam00270   24 GSGKT--LAFLLPALEAlDKLDNGPqALVLAPTREL-AEQiyEELKKLGKGLGlkVASLLGGDSRKEQLEKLKGP----- 95
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1246743034  477 kikfNLLLTTYE---YVLKDRSVLSNIKwqYMAIDEAHRL--KNSESSLYEALSQFKNSNR-LLITGTP 539
Cdd:pfam00270   96 ----DILVGTPGrllDLLQERKLLKNLK--LLVLDEAHRLldMGFGPDLEEILRRLPKKRQiLLLSATL 158
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
290-339 8.04e-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: 35.92  E-value: 8.04e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1246743034  290 VDRIVAKHLNsDGSVEYLVKWKQLLYDFCTWEASSIIEPiaATE-IQAFQE 339
Cdd:cd00024      3 VEKILDHRVR-KGKLEYLVKWKGYPPEENTWEPEENLTN--APElIKEYEK 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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