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Conserved domains on  [gi|1034625941|ref|XP_016883589|]
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chromodomain-helicase-DNA-binding protein 6 isoform X6 [Homo sapiens]

Protein Classification

DEXHc_CHD6 and SF2_C_SNF domain-containing protein( domain architecture ID 13312860)

protein containing domains CD1_tandem_CHD5-9_like, CD2_tandem_CHD5-9_like, DEXHc_CHD6, and SF2_C_SNF

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
439-660 4.73e-157

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: 484.55  E-value: 4.73e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 518
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  519 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALE 598
Cdd:cd18058     81 GSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034625941  599 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 660
Cdd:cd18058    161 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
438-963 3.32e-153

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: 505.49  E-value: 3.32e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  438 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LRGIHGPFLIIAPLSTITNWEREFRTWTEM-NAI 515
Cdd:PLN03142   169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHeYRGITGPHMVVAPKSTLGNWMNEIRRFCPVlRAV 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  516 VYHGSQISRQMIQQYEMVyrdaqgnplSGvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLM 595
Cdd:PLN03142   249 KFHGNPEERAHQREELLV---------AG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLF 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  596 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF---GDLKTEEQVKKLQSILKPMMLRRLKDDVEKNLAPK 672
Cdd:PLN03142   318 STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPK 397
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  673 QETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNmpnLINTMMELRKCCNHPYLINGAEekiledfrkthsPDAPDFQ 752
Cdd:PLN03142   398 KETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAE------------PGPPYTT 462
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  753 LQAMIQAAGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDRFV 832
Cdd:PLN03142   463 GEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFV 542
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  833 FLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQD 912
Cdd:PLN03142   543 FLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ 622
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034625941  913 inrkggtNGVQQLSKMEVEDLLRKGAYGALMDEEDEGSKFCEEDIDQILQR 963
Cdd:PLN03142   623 -------GRLAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAK 666
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
350-408 1.14e-35

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


:

Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 130.10  E-value: 1.14e-35
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034625941  350 PDYVEVDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAKVKEFESLQ 408
Cdd:cd18663      1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
266-331 6.11e-27

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: 105.50  E-value: 6.11e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034625941  266 EDDANIIEKILASKTVQ-EVHPGEPPFDLELFYVKYRNFSYLHCKWATMEELEK-DPRIAQKIKRFRN 331
Cdd:cd18668      1 EEDTMIIEKILASRKKKkEKEEGAEEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFKQ 68
BRK super family cl02688
BRK domain; The function of this domain is unknown. It is often found associated with ...
2380-2415 3.99e-05

BRK domain; The function of this domain is unknown. It is often found associated with helicases and transcription factors.


The actual alignment was detected with superfamily member smart00592:

Pssm-ID: 470653  Cd Length: 45  Bit Score: 43.11  E-value: 3.99e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1034625941  2380 SGEERVPAIPKEPGLRG----FLPENKFNHTLAEPILRDT 2415
Cdd:smart00592    1 DGEERVPVINRETGKKLtgddAPKAKDLERWLEENPEYEV 40
PHA03247 super family cl33720
large tegument protein UL36; Provisional
2297-2671 1.99e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 1.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941 2297 PGQATLSTTHPEGPGPATSAPEPATAASSQAEKSIPSKSLLDWLRQQADYS-------LEVPGFGANFSDKPKQRRPRCK 2369
Cdd:PHA03247  2609 RGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGrvsrprrARRLGRAAQASSPPQRPRRRAA 2688
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941 2370 EPGkldVSSLSGEERVPAIPKEPGLRgflpenkfnhtlAEPILRDTGPRRRGRRPRSELLKAPSIVADSPSGMGPLfmng 2449
Cdd:PHA03247  2689 RPT---VGSLTSLADPPPPPPTPEPA------------PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA---- 2749
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941 2450 LIAGMDLVGLQNMRNMPGIPLTglvgfPAGFATMPTGEEVKSTLSMLPMMLPGMAAVPQMFGVGGLLSPPMATTCTSTAP 2529
Cdd:PHA03247  2750 TPGGPARPARPPTTAGPPAPAP-----PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941 2530 ASLSSTTKSGTAVTEKTAEDKPSSHDVKTDTLAedkPGpGPFSDQSEPAITTSSPVAfnPFLIPGVSpgLIYPSMFLSPg 2609
Cdd:PHA03247  2825 AGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA---PG-GDVRRRPPSRSPAAKPAA--PARPPVRR--LARPAVSRST- 2895
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034625941 2610 MGMALPAMQQARHSEivglesqkrkkkktkgdnPNSHPEPAPSCEREPSGDENCAEPSAPLP 2671
Cdd:PHA03247  2896 ESFALPPDQPERPPQ------------------PQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
82-351 7.89e-03

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 41.60  E-value: 7.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941   82 QEGAAKGSKDrepkPKRKREPKEPKEPRKAKEPKKAKEHKEPKQKDGAKKARKPREASGTKEAKEKRSctDSAARTKSRK 161
Cdd:PTZ00449   533 EHEDSKESDE----PKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPEEPKK--PKRPRSAQRP 606
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  162 ASKEQGPTPVEKKKKGKRKSETTVESLELDQGLTNPSlrSPE--ESTESTDSQKRRSGRQV------KRRKYNEDLDFKV 233
Cdd:PTZ00449   607 TRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPS--SPErpEGPKIIKSPKPPKSPKPpfdpkfKEKFYDDYLDAAA 684
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  234 VDDDGETIAVLGAGRTSALSaSTLAWQAEEPPEDDANIIEKILASKTVQEVHPGEP----PFDLELFYVKYRNFSYLHCK 309
Cdd:PTZ00449   685 KSKETKTTVVLDESFESILK-ETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPdaeqPDDIEFFTPPEEERTFFHET 763
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1034625941  310 WAT------MEELEKDPRIAQKIKrfrnkqaqmkhiftEPDEDLFNPD 351
Cdd:PTZ00449   764 PADtplpdiLAEEFKEEDIHAETG--------------EPDEAMKRPD 797
 
Name Accession Description Interval E-value
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
439-660 4.73e-157

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: 484.55  E-value: 4.73e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 518
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  519 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALE 598
Cdd:cd18058     81 GSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034625941  599 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 660
Cdd:cd18058    161 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
438-963 3.32e-153

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 505.49  E-value: 3.32e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  438 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LRGIHGPFLIIAPLSTITNWEREFRTWTEM-NAI 515
Cdd:PLN03142   169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHeYRGITGPHMVVAPKSTLGNWMNEIRRFCPVlRAV 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  516 VYHGSQISRQMIQQYEMVyrdaqgnplSGvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLM 595
Cdd:PLN03142   249 KFHGNPEERAHQREELLV---------AG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLF 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  596 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF---GDLKTEEQVKKLQSILKPMMLRRLKDDVEKNLAPK 672
Cdd:PLN03142   318 STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPK 397
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  673 QETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNmpnLINTMMELRKCCNHPYLINGAEekiledfrkthsPDAPDFQ 752
Cdd:PLN03142   398 KETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAE------------PGPPYTT 462
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  753 LQAMIQAAGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDRFV 832
Cdd:PLN03142   463 GEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFV 542
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  833 FLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQD 912
Cdd:PLN03142   543 FLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ 622
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034625941  913 inrkggtNGVQQLSKMEVEDLLRKGAYGALMDEEDEGSKFCEEDIDQILQR 963
Cdd:PLN03142   623 -------GRLAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAK 666
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
438-911 4.43e-129

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 423.48  E-value: 4.43e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  438 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 516
Cdd:COG0553    241 TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFApGLRVLV 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  517 YHGSQisrqmiqqyemvYRDAQGNPLSgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMA 596
Cdd:COG0553    321 LDGTR------------ERAKGANPFE---DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  597 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKT---EEQVKKLQSILKPMMLRRLKDDVEKNLAPKQ 673
Cdd:COG0553    386 ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEkgdEEALERLRRLLRPFLLRRTKEDVLKDLPEKT 465
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  674 ETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNMPNLINTMMELRKCCNHPYLingaeekILEDFRKTHSPDapdfql 753
Cdd:COG0553    466 EETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLILAALTRLRQICSHPAL-------LLEEGAELSGRS------ 532
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  754 qamiqaaGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFcKPDSDRFVF 833
Cdd:COG0553    533 -------AKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRF-QEGPEAPVF 604
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034625941  834 LLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQ 911
Cdd:COG0553    605 LISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
442-729 5.90e-86

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 283.42  E-value: 5.90e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  442 YQLEGMNWLLFNWYNRK-NCILADEMGLGKTIQSITFLSeiFLRGIH----GPFLIIAPLSTITNWEREFRTWT---EMN 513
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLL--YLKHVDknwgGPTLIVVPLSLLHNWMNEFERWVsppALR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  514 AIVYHGSQISRQMIQQYEMVYRDaqgnplsgvfkFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLK 593
Cdd:pfam00176   79 VVVLHGNKRPQERWKNDPNFLAD-----------FDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  594 LMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----DLKTEEQVKKLQSILKPMMLRRLKDDVEKNL 669
Cdd:pfam00176  148 SLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpieRGGGKKGVSRLHKLLKPFLLRRTKKDVEKSL 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034625941  670 APKQETIIEVELTNIQKKYY-RAILEKNFSFLTKG-ANQHNMPNLINTMMELRKCCNHPYLI 729
Cdd:pfam00176  228 PPKVEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGeGGREIKASLLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
761-886 2.17e-57

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 195.39  E-value: 2.17e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  761 GKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFcKPDSDRFVFLLCTRAG 840
Cdd:cd18793     11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRF-NEDPDIRVFLLSTKAG 89
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1034625941  841 GLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI 886
Cdd:cd18793     90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
350-408 1.14e-35

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


Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 130.10  E-value: 1.14e-35
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034625941  350 PDYVEVDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAKVKEFESLQ 408
Cdd:cd18663      1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
DEXDc smart00487
DEAD-like helicases superfamily;
432-630 1.07e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 124.14  E-value: 1.07e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941   432 EYKNSNQLREYQLEGMNWLLFNWynrKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTIT-NWEREFRTWT 510
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAeQWAEELKKLG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941   511 EMNAI----VYHGSQISRQMIQQYEmvyrdaqgnplsgvFKFHVVITTFEMILADCPE--LKKIHWSCVIIDEAHRLKN- 583
Cdd:smart00487   79 PSLGLkvvgLYGGDSKREQLRKLES--------------GKTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDg 144
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1034625941   584 -RNCKLLEGLKLMALE-HKVLLTGTP---LQNSVEELFSLLNFLEPSQFPSE 630
Cdd:smart00487  145 gFGDQLEKLLKLLPKNvQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLE 196
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
266-331 6.11e-27

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: 105.50  E-value: 6.11e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034625941  266 EDDANIIEKILASKTVQ-EVHPGEPPFDLELFYVKYRNFSYLHCKWATMEELEK-DPRIAQKIKRFRN 331
Cdd:cd18668      1 EEDTMIIEKILASRKKKkEKEEGAEEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFKQ 68
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
761-875 9.04e-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: 103.83  E-value: 9.04e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  761 GKLVLIDKLLPKliAGGHKVLIFSQMVRCLDilEDYLIQRR-YTYERIDGRVRGNLRQAAIDRFCKPDSDrfvFLLCTRA 839
Cdd:pfam00271    1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1034625941  840 GGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIG 875
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
461-909 5.78e-23

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


Pssm-ID: 468472 [Multi-domain]  Cd Length: 868  Bit Score: 107.46  E-value: 5.78e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  461 ILADEMGLGKTIQS---ITFLSEIFLRGIhgpfLIIAPLSTITNWEREFRTWTEMNAIVyhgsqISRQMIQQ-YEMVYRD 536
Cdd:NF038318    51 ILADEVGLGKTIEAglvLKYVLESGAKKI----LIILPANLRKQWEIELEEKFDLESLI-----LDSLTVEKdAKKWNKR 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  537 AQGNPlsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKN--RNCKLLEGL-KLMALEHKVLLTGTPLQNSVE 613
Cdd:NF038318   122 LTDNK-----KVRIVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRNvhKGGKRAKNLyELTKGIPKILLTATPLQNSLL 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  614 ELFSLLNFLEPSQFPSETAFL------EEFGDLKTEeqvkklqsiLKPMMLRRLKDDVEKNLAPKQETII---------E 678
Cdd:NF038318   197 DLYGLVSFIDPRIFGSEKVFSkryikdEDYSDLKRE---------LSPVLYRTLRKDVADYMQFKKRKCItvdfelspdE 267
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  679 VELTN-----IQKKYYRAILEKNFSFLT----KGANQHNMPnLINTMMELRKCCNHPY---LINGAEEKI------LEDF 740
Cdd:NF038318   268 IELYVrvnnfLKRDILYSIPTSNRTLIIlvirKLLASSSFA-LAETFEVLKKRLEKLKegtRSANAQEGFdlfwsfVEDE 346
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  741 RKTHSPDAPDFQL----QAMIQAAGKLV--LIDKL-----------LPKLIAGG----------HKVLIFSQMVRCLDIL 793
Cdd:NF038318   347 IDESGFEEKQDELytrqKEFIQHEIDEVdaIIDVAkriktnakvtaLKTALEIAfeyqreegiaQKVVVFTESKRTQKYI 426
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  794 EDYLIQRRYTYERI---DG--------------RVR--GN--------LRQAAIDRFckpdSDRFVFLLCTRAGGLGINL 846
Cdd:NF038318   427 AEELRKSGYEGEDIllfNGdfddamtkeiyrawQVKnyGKanygrsveYKHAIVDYF----KNNAKILIVTDAGSEGLNL 502
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034625941  847 TAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI-TRNSYEREMFDKASLKLGLDKAV 909
Cdd:NF038318   503 QFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYEILSEKFELFEGV 566
HELICc smart00490
helicase superfamily c-terminal domain;
791-875 5.21e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 89.19  E-value: 5.21e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941   791 DILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDrfvFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQAR 870
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 1034625941   871 CHRIG 875
Cdd:smart00490   78 AGRAG 82
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
354-406 7.15e-10

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 56.43  E-value: 7.15e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034625941  354 EVDRIleVAHTKDAETGEEvthYLVKWCSLPYEESTWELEEDVD--PAKVKEFES 406
Cdd:pfam00385    2 EVERI--LDHRKDKGGKEE---YLVKWKGYPYDENTWEPEENLSkcPELIEEFKD 51
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
271-332 3.93e-06

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 46.03  E-value: 3.93e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034625941  271 IIEKILASKTVQEvhpgeppfDLELFYVKYRNFSYLHCKWATMEELEKDPRIaqkIKRFRNK 332
Cdd:pfam00385    2 EVERILDHRKDKG--------GKEEYLVKWKGYPYDENTWEPEENLSKCPEL---IEEFKDR 52
CHROMO smart00298
Chromatin organization modifier domain;
354-405 2.59e-05

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 43.74  E-value: 2.59e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1034625941   354 EVDRILevAHTKDAETGEEvthYLVKWCSLPYEESTWELEEDV--DPAKVKEFE 405
Cdd:smart00298    3 EVEKIL--DHRWKKKGELE---YLVKWKGYSYSEDTWEPEENLlnCSKKLDNYK 51
BRK smart00592
domain in transcription and CHROMO domain helicases;
2380-2415 3.99e-05

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 43.11  E-value: 3.99e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1034625941  2380 SGEERVPAIPKEPGLRG----FLPENKFNHTLAEPILRDT 2415
Cdd:smart00592    1 DGEERVPVINRETGKKLtgddAPKAKDLERWLEENPEYEV 40
PHA03247 PHA03247
large tegument protein UL36; Provisional
2297-2671 1.99e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 1.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941 2297 PGQATLSTTHPEGPGPATSAPEPATAASSQAEKSIPSKSLLDWLRQQADYS-------LEVPGFGANFSDKPKQRRPRCK 2369
Cdd:PHA03247  2609 RGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGrvsrprrARRLGRAAQASSPPQRPRRRAA 2688
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941 2370 EPGkldVSSLSGEERVPAIPKEPGLRgflpenkfnhtlAEPILRDTGPRRRGRRPRSELLKAPSIVADSPSGMGPLfmng 2449
Cdd:PHA03247  2689 RPT---VGSLTSLADPPPPPPTPEPA------------PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA---- 2749
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941 2450 LIAGMDLVGLQNMRNMPGIPLTglvgfPAGFATMPTGEEVKSTLSMLPMMLPGMAAVPQMFGVGGLLSPPMATTCTSTAP 2529
Cdd:PHA03247  2750 TPGGPARPARPPTTAGPPAPAP-----PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941 2530 ASLSSTTKSGTAVTEKTAEDKPSSHDVKTDTLAedkPGpGPFSDQSEPAITTSSPVAfnPFLIPGVSpgLIYPSMFLSPg 2609
Cdd:PHA03247  2825 AGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA---PG-GDVRRRPPSRSPAAKPAA--PARPPVRR--LARPAVSRST- 2895
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034625941 2610 MGMALPAMQQARHSEivglesqkrkkkktkgdnPNSHPEPAPSCEREPSGDENCAEPSAPLP 2671
Cdd:PHA03247  2896 ESFALPPDQPERPPQ------------------PQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939
CHROMO smart00298
Chromatin organization modifier domain;
272-334 2.54e-03

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 38.35  E-value: 2.54e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034625941   272 IEKILASKTVQEvhpGEppfdlELFYVKYRNFSYLHCKWATMEELEKDPRiaqKIKRFRNKQA 334
Cdd:smart00298    4 VEKILDHRWKKK---GE-----LEYLVKWKGYSYSEDTWEPEENLLNCSK---KLDNYKKKER 55
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
82-351 7.89e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 41.60  E-value: 7.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941   82 QEGAAKGSKDrepkPKRKREPKEPKEPRKAKEPKKAKEHKEPKQKDGAKKARKPREASGTKEAKEKRSctDSAARTKSRK 161
Cdd:PTZ00449   533 EHEDSKESDE----PKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPEEPKK--PKRPRSAQRP 606
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  162 ASKEQGPTPVEKKKKGKRKSETTVESLELDQGLTNPSlrSPE--ESTESTDSQKRRSGRQV------KRRKYNEDLDFKV 233
Cdd:PTZ00449   607 TRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPS--SPErpEGPKIIKSPKPPKSPKPpfdpkfKEKFYDDYLDAAA 684
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  234 VDDDGETIAVLGAGRTSALSaSTLAWQAEEPPEDDANIIEKILASKTVQEVHPGEP----PFDLELFYVKYRNFSYLHCK 309
Cdd:PTZ00449   685 KSKETKTTVVLDESFESILK-ETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPdaeqPDDIEFFTPPEEERTFFHET 763
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1034625941  310 WAT------MEELEKDPRIAQKIKrfrnkqaqmkhiftEPDEDLFNPD 351
Cdd:PTZ00449   764 PADtplpdiLAEEFKEEDIHAETG--------------EPDEAMKRPD 797
 
Name Accession Description Interval E-value
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
439-660 4.73e-157

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: 484.55  E-value: 4.73e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 518
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  519 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALE 598
Cdd:cd18058     81 GSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034625941  599 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 660
Cdd:cd18058    161 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
438-963 3.32e-153

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 505.49  E-value: 3.32e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  438 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LRGIHGPFLIIAPLSTITNWEREFRTWTEM-NAI 515
Cdd:PLN03142   169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHeYRGITGPHMVVAPKSTLGNWMNEIRRFCPVlRAV 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  516 VYHGSQISRQMIQQYEMVyrdaqgnplSGvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLM 595
Cdd:PLN03142   249 KFHGNPEERAHQREELLV---------AG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLF 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  596 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF---GDLKTEEQVKKLQSILKPMMLRRLKDDVEKNLAPK 672
Cdd:PLN03142   318 STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPK 397
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  673 QETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNmpnLINTMMELRKCCNHPYLINGAEekiledfrkthsPDAPDFQ 752
Cdd:PLN03142   398 KETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAE------------PGPPYTT 462
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  753 LQAMIQAAGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDRFV 832
Cdd:PLN03142   463 GEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFV 542
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  833 FLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQD 912
Cdd:PLN03142   543 FLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ 622
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034625941  913 inrkggtNGVQQLSKMEVEDLLRKGAYGALMDEEDEGSKFCEEDIDQILQR 963
Cdd:PLN03142   623 -------GRLAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAK 666
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
439-660 1.14e-147

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: 457.48  E-value: 1.14e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLR-GIHGPFLIIAPLSTITNWEREFRTWTEMNAIVY 517
Cdd:cd17995      1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVeGIRGPFLVIAPLSTIPNWQREFETWTDMNVVVY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  518 HGSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMAL 597
Cdd:cd17995     81 HGSGESRQIIQQYEMYFKDAQGRKKKGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTL 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034625941  598 EHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 660
Cdd:cd17995    161 EHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEQVEKLQALLKPYMLRR 223
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
438-911 4.43e-129

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 423.48  E-value: 4.43e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  438 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 516
Cdd:COG0553    241 TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFApGLRVLV 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  517 YHGSQisrqmiqqyemvYRDAQGNPLSgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMA 596
Cdd:COG0553    321 LDGTR------------ERAKGANPFE---DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  597 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKT---EEQVKKLQSILKPMMLRRLKDDVEKNLAPKQ 673
Cdd:COG0553    386 ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEkgdEEALERLRRLLRPFLLRRTKEDVLKDLPEKT 465
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  674 ETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNMPNLINTMMELRKCCNHPYLingaeekILEDFRKTHSPDapdfql 753
Cdd:COG0553    466 EETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLILAALTRLRQICSHPAL-------LLEEGAELSGRS------ 532
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  754 qamiqaaGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFcKPDSDRFVF 833
Cdd:COG0553    533 -------AKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRF-QEGPEAPVF 604
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034625941  834 LLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQ 911
Cdd:COG0553    605 LISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
439-660 1.10e-128

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: 403.28  E-value: 1.10e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 518
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  519 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALE 598
Cdd:cd18060     81 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034625941  599 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 660
Cdd:cd18060    161 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
439-660 1.80e-128

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: 402.49  E-value: 1.80e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 518
Cdd:cd18059      1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  519 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALE 598
Cdd:cd18059     81 GSQASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034625941  599 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 660
Cdd:cd18059    161 HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
439-660 2.72e-125

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: 393.60  E-value: 2.72e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 518
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDLNVVVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  519 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALE 598
Cdd:cd18061     81 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034625941  599 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 660
Cdd:cd18061    161 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
442-729 5.90e-86

SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.


Pssm-ID: 425504 [Multi-domain]  Cd Length: 289  Bit Score: 283.42  E-value: 5.90e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  442 YQLEGMNWLLFNWYNRK-NCILADEMGLGKTIQSITFLSeiFLRGIH----GPFLIIAPLSTITNWEREFRTWT---EMN 513
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLL--YLKHVDknwgGPTLIVVPLSLLHNWMNEFERWVsppALR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  514 AIVYHGSQISRQMIQQYEMVYRDaqgnplsgvfkFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLK 593
Cdd:pfam00176   79 VVVLHGNKRPQERWKNDPNFLAD-----------FDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  594 LMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----DLKTEEQVKKLQSILKPMMLRRLKDDVEKNL 669
Cdd:pfam00176  148 SLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpieRGGGKKGVSRLHKLLKPFLLRRTKKDVEKSL 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034625941  670 APKQETIIEVELTNIQKKYY-RAILEKNFSFLTKG-ANQHNMPNLINTMMELRKCCNHPYLI 729
Cdd:pfam00176  228 PPKVEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGeGGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
438-660 3.09e-82

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: 270.00  E-value: 3.09e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  438 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAI 515
Cdd:cd17993      1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFhSQQQYGPFLVVVPLSTMPAWQREFAKWApDMNVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  516 VYHGSQISRQMIQQYEMvYRDaQGNPLsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLM 595
Cdd:cd17993     81 VYLGDIKSRDTIREYEF-YFS-QTKKL----KFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEF 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034625941  596 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFlEEFGDLKTEEQVKKLQSILKPMMLRR 660
Cdd:cd17993    155 KTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEF-EEEHDEEQEKGIADLHKELEPFILRR 218
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
439-624 6.38e-78

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: 255.95  E-value: 6.38e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSE-IFLRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 516
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYlLKEGKERGPVLVVCPLSVLENWEREFEKWTpDLRVVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  517 YHGSQISRQMIQQYEMVYrdaqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMA 596
Cdd:cd17919     81 YHGSQRERAQIRAKEKLD------------KFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR 148
                          170       180
                   ....*....|....*....|....*...
gi 1034625941  597 LEHKVLLTGTPLQNSVEELFSLLNFLEP 624
Cdd:cd17919    149 AKRRLLLTGTPLQNNLEELWALLDFLDP 176
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
438-662 5.70e-74

DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or SMARCA6) is a major epigenetic regulator crucial for normal heterochromatin structure and function. HELLS is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350767 [Multi-domain]  Cd Length: 236  Bit Score: 246.91  E-value: 5.70e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  438 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 516
Cdd:cd18009      3 VMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTpSVPVLL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  517 YHGSQISRQMIQqyemvyRDAQGNPLSGVfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMA 596
Cdd:cd18009     83 YHGTKEERERLR------KKIMKREGTLQ-DFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFN 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  597 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG-----------DLKTEEQ----VKKLQSILKPMMLRRL 661
Cdd:cd18009    156 SDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDfsslsdnaadiSNLSEEReqniVHMLHAILKPFLLRRL 235

                   .
gi 1034625941  662 K 662
Cdd:cd18009    236 K 236
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
439-660 3.71e-72

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: 240.03  E-value: 3.71e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRG-IHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 516
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWApDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  517 YHGSqisrqmiqqyemvyrdaqgnplsgvfkfHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMA 596
Cdd:cd17994     81 YVGD----------------------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYK 132
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034625941  597 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 660
Cdd:cd17994    133 IGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQIKKLHDLLGPHMLRR 196
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
436-662 7.64e-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: 234.52  E-value: 7.64e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  436 SNQLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSeiFL---RGIHGPFLIIAPLSTITNWEREFRTWT-E 511
Cdd:cd17997      1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLG--YLkhyKNINGPHLIIVPKSTLDNWMREFKRWCpS 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  512 MNAIVYHGSQISRQMIQQYEMVYRdaqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEG 591
Cdd:cd17997     79 LRVVVLIGDKEERADIIRDVLLPG-----------KFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQI 147
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034625941  592 LKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF----GDLKTEEQVKKLQSILKPMMLRRLK 662
Cdd:cd17997    148 VRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFnvnnCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
439-660 2.61e-69

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. CHD3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350813 [Multi-domain]  Cd Length: 232  Bit Score: 233.36  E-value: 2.61e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRG-IHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 516
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhTKGPFLVSAPLSTIINWEREFQMWApDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  517 YHGSQISRQMIQQYEMVYRDAQGNPLSGVFK--------FHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKL 588
Cdd:cd18055     81 YTGDKDSRAIIRENEFSFDDNAVKGGKKAFKmkreaqvkFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034625941  589 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 660
Cdd:cd18055    161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
438-662 1.28e-68

DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, members 2 and 4 (SMARCA2 and SMARCA4) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350754 [Multi-domain]  Cd Length: 233  Bit Score: 231.49  E-value: 1.28e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  438 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSI---TFLSEIflRGIHGPFLIIAPLSTITNWEREFRTWT-EMN 513
Cdd:cd17996      3 TLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTIsliTYLMEK--KKNNGPYLVIVPLSTLSNWVSEFEKWApSVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  514 AIVYHGSQISRQMIQQYEMVYrdaqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLK 593
Cdd:cd17996     81 KIVYKGTPDVRKKLQSQIRAG------------KFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLN 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  594 LMAL-EHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG------------DLKTEEQV---KKLQSILKPMM 657
Cdd:cd17996    149 TYYHaRYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNtpfantgeqvkiELNEEETLliiRRLHKVLRPFL 228

                   ....*
gi 1034625941  658 LRRLK 662
Cdd:cd17996    229 LRRLK 233
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
439-660 7.50e-67

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: 226.49  E-value: 7.50e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRG-IHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 516
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWApDMYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  517 YHGSQISRQMIQQYEMVYRD--------AQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKL 588
Cdd:cd18056     81 YVGDKDSRAIIRENEFSFEDnairggkkASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034625941  589 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 660
Cdd:cd18056    161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQIKKLHDMLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
439-660 1.77e-66

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350815 [Multi-domain]  Cd Length: 232  Bit Score: 225.33  E-value: 1.77e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRG-IHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 516
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWApDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  517 YHGSQISRQMIQQYEMVYRDAQGNPLSGVF--------KFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKL 588
Cdd:cd18057     81 YTGDKESRSVIRENEFSFEDNAIRSGKKVFrmkkeaqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034625941  589 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 660
Cdd:cd18057    161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
438-660 3.23e-66

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: 224.88  E-value: 3.23e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  438 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAI 515
Cdd:cd18054     20 ELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFhQHQLYGPFLLVVPLSTLTSWQREFEIWApEINVV 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  516 VYHGSQISRQMIQQYEMVYrdaqgnPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLM 595
Cdd:cd18054    100 VYIGDLMSRNTIREYEWIH------SQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDF 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034625941  596 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKtEEQVKKLQSILKPMMLRR 660
Cdd:cd18054    174 KSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGR-ENGYQSLHKVLEPFLLRR 237
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
437-662 3.95e-59

DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350770 [Multi-domain]  Cd Length: 218  Bit Score: 203.57  E-value: 3.95e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  437 NQLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAI 515
Cdd:cd18012      3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFApELKVL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  516 VYHGSQISRQMIQQYEmvyrdaqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLM 595
Cdd:cd18012     83 VIHGTKRKREKLRALE---------------DYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKAL 147
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034625941  596 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----DLKTEEQVKKLQSILKPMMLRRLK 662
Cdd:cd18012    148 KADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAkpieKDGDEEALEELKKLISPFILRRLK 218
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
439-660 9.97e-59

DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, also known as ALC1) is involved in DNA repair by regulating chromatin relaxation following DNA damage. CHD1L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350764 [Multi-domain]  Cd Length: 216  Bit Score: 202.28  E-value: 9.97e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEI-FLRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 516
Cdd:cd18006      1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLaGRLKLLGPFLVLCPLSVLDNWKEELNRFApDLSVIT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  517 YHGSQISRQMIQQyemvyrDAQGNPlsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMA 596
Cdd:cd18006     81 YMGDKEKRLDLQQ------DIKSTN-----RFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFS 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034625941  597 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETA--FLEEFGDLKTE-EQVKKLQSILKPMMLRR 660
Cdd:cd18006    150 VDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKLddFIKAYSETDDEsETVEELHLLLQPFLLRR 216
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
761-886 2.17e-57

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 195.39  E-value: 2.17e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  761 GKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFcKPDSDRFVFLLCTRAG 840
Cdd:cd18793     11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRF-NEDPDIRVFLLSTKAG 89
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1034625941  841 GLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI 886
Cdd:cd18793     90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
439-660 1.63e-56

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: 196.42  E-value: 1.63e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFL-RGIHGPFLIIAPLSTITNWEREFRTWTE-MNAIV 516
Cdd:cd18003      1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACeKGNWGPHLIVVPTSVMLNWEMEFKRWCPgFKILT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  517 YHGSQISRQMIQQYEMvyrdaqgNPLSgvfkFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMA 596
Cdd:cd18003     81 YYGSAKERKLKRQGWM-------KPNS----FHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFN 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034625941  597 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKT----------EEQVKKLQSILKPMMLRR 660
Cdd:cd18003    150 TQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLTamsegsqeenEELVRRLHKVLRPFLLRR 223
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
438-660 2.88e-56

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350811 [Multi-domain]  Cd Length: 237  Bit Score: 196.42  E-value: 2.88e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  438 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLR-GIHGPFLIIAPLSTITNWEREFRTWT-EMNAI 515
Cdd:cd18053     20 ELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEhQLYGPFLLVVPLSTLTSWQREIQTWApQMNAV 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  516 VYHGSQISRQMIQQYEMVYrdaqgnPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLM 595
Cdd:cd18053    100 VYLGDINSRNMIRTHEWMH------PQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDF 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034625941  596 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKtEEQVKKLQSILKPMMLRR 660
Cdd:cd18053    174 KSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGR-EYGYASLHKELEPFLLRR 237
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
439-660 1.79e-52

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: 185.02  E-value: 1.79e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLfNWYNRK-NCILADEMGLGKTIQSITFLSEIFLR-GIHGPFLIIAPLSTITNWEREF-RTWTEMNAI 515
Cdd:cd18002      1 LKEYQLKGLNWLA-NLYEQGiNGILADEMGLGKTVQSIAVLAHLAEEhNIWGPFLVIAPASTLHNWQQEIsRFVPQFKVL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  516 VYHGSQISRQMIQQY----EMVYRDAqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEG 591
Cdd:cd18002     80 PYWGNPKDRKVLRKFwdrkNLYTRDA---------PFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKT 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034625941  592 LKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG-DLKT---------EEQVKKLQSILKPMMLRR 660
Cdd:cd18002    151 LLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSkDIEShaenktglnEHQLKRLHMILKPFMLRR 229
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
439-627 4.94e-52

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: 182.20  E-value: 4.94e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIVY 517
Cdd:cd17998      1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCpSLKVEPY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  518 HGSQISRqmiqqyemvyRDAQGNPLSGVFKFHVVITTFEMILADCPE---LKKIHWSCVIIDEAHRLKNRNCKLLEGLKL 594
Cdd:cd17998     81 YGSQEER----------KHLRYDILKGLEDFDVIVTTYNLATSNPDDrsfFKRLKLNYVVYDEGHMLKNMTSERYRHLMT 150
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1034625941  595 MALEHKVLLTGTPLQNSVEELFSLLNFLEPSQF 627
Cdd:cd17998    151 INANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
439-660 1.56e-51

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: 182.96  E-value: 1.56e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLlFNWY-NRKNCILADEMGLGKTIQSITFLSEI----------------FLRGIH-----GPFLIIAPL 496
Cdd:cd18005      1 LRDYQREGVEFM-YDLYkNGRGGILGDDMGLGKTVQVIAFLAAVlgktgtrrdrennrprFKKKPPassakKPVLIVAPL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  497 STITNWEREFRTWTEMNAIVYHGSQISRQMIQQYEmvyrdaQGnplsgvfKFHVVITTFEMILADCPELKKIHWSCVIID 576
Cdd:cd18005     80 SVLYNWKDELDTWGHFEVGVYHGSRKDDELEGRLK------AG-------RLEVVVTTYDTLRRCIDSLNSINWSAVIAD 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  577 EAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGD---------------LK 641
Cdd:cd18005    147 EAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEpikrgqrhtatarelRL 226
                          250
                   ....*....|....*....
gi 1034625941  642 TEEQVKKLQSILKPMMLRR 660
Cdd:cd18005    227 GRKRKQELAVKLSKFFLRR 245
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
425-662 1.14e-49

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


Pssm-ID: 350820 [Multi-domain]  Cd Length: 251  Bit Score: 177.93  E-value: 1.14e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  425 QKLEKSREYKNSNQLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LRGIHGPFLIIAPLSTITNWE 503
Cdd:cd18062     10 EKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMeHKRINGPFLIIVPLSTLSNWV 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  504 REFRTWT-EMNAIVYHGSQISRQMIQqyemvyrdaqgnPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLK 582
Cdd:cd18062     90 YEFDKWApSVVKVSYKGSPAARRAFV------------PQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMK 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  583 NRNCKLLEGLKLMALE-HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----------DLKTEEQ---VKK 648
Cdd:cd18062    158 NHHCKLTQVLNTHYVApRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRR 237
                          250
                   ....*....|....
gi 1034625941  649 LQSILKPMMLRRLK 662
Cdd:cd18062    238 LHKVLRPFLLRRLK 251
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
426-673 8.86e-49

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


Pssm-ID: 350822 [Multi-domain]  Cd Length: 244  Bit Score: 174.85  E-value: 8.86e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  426 KLEKSREYKNSNQLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEI-FLRGIHGPFLIIAPLSTITNWER 504
Cdd:cd18064      3 RFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMkHYRNIPGPHMVLVPKSTLHNWMA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  505 EFRTWT-EMNAIVYHGSQisrqmiQQYEMVYRDAQgnpLSGvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKN 583
Cdd:cd18064     83 EFKRWVpTLRAVCLIGDK------DQRAAFVRDVL---LPG--EWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  584 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGD---LKTEEQVKKLQSILKPMMLRR 660
Cdd:cd18064    152 EKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTnncLGDQKLVERLHMVLRPFLLRR 231
                          250
                   ....*....|...
gi 1034625941  661 LKDDVEKNLAPKQ 673
Cdd:cd18064    232 IKADVEKSLPPKK 244
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
425-662 1.03e-47

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


Pssm-ID: 350821 [Multi-domain]  Cd Length: 251  Bit Score: 172.17  E-value: 1.03e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  425 QKLEKSREYKNSNQLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LRGIHGPFLIIAPLSTITNWE 503
Cdd:cd18063     10 ERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMeHKRLNGPYLIIVPLSTLSNWT 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  504 REFRTWT-EMNAIVYHGS-QISRQMIQQYEmvyrdaqgnplSGvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRL 581
Cdd:cd18063     90 YEFDKWApSVVKISYKGTpAMRRSLVPQLR-----------SG--KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRM 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  582 KNRNCKLLEGLKLMALE-HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----------DLKTEEQ---VK 647
Cdd:cd18063    157 KNHHCKLTQVLNTHYVApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgervDLNEEETiliIR 236
                          250
                   ....*....|....*
gi 1034625941  648 KLQSILKPMMLRRLK 662
Cdd:cd18063    237 RLHKVLRPFLLRRLK 251
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
426-662 9.50e-46

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: 165.96  E-value: 9.50e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  426 KLEKSREYKNSNQLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEI-FLRGIHGPFLIIAPLSTITNWER 504
Cdd:cd18065      3 RFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLkHYRNIPGPHMVLVPKSTLHNWMN 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  505 EFRTWT-EMNAIVYHGSQISRQMIQQYEMvyrdaqgnpLSGvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKN 583
Cdd:cd18065     83 EFKRWVpSLRAVCLIGDKDARAAFIRDVM---------MPG--EWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKN 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  584 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGD---LKTEEQVKKLQSILKPMMLRR 660
Cdd:cd18065    152 EKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 231

                   ..
gi 1034625941  661 LK 662
Cdd:cd18065    232 IK 233
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
439-660 1.31e-42

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: 157.06  E-value: 1.31e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLFnwynrKNCILADEMGLGKTIQSI--------TFLSEIFLRGIHGPF----------LIIAPLSTIT 500
Cdd:cd18008      1 LLPYQKQGLAWMLP-----RGGILADEMGLGKTIQALalilatrpQDPKIPEELEENSSDpkklylskttLIVVPLSLLS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  501 NWEREFRTWTE---MNAIVYHGSQisrqmiqqyemvyrdaQGNPLSGVFKFHVVITTFEMILADCPE------------- 564
Cdd:cd18008     76 QWKDEIEKHTKpgsLKVYVYHGSK----------------RIKSIEELSDYDIVITTYGTLASEFPKnkkgggrdskeke 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  565 ---LKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLK 641
Cdd:cd18008    140 aspLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPF 219
                          250       260
                   ....*....|....*....|..
gi 1034625941  642 TE---EQVKKLQSILKPMMLRR 660
Cdd:cd18008    220 SKndrKALERLQALLKPILLRR 241
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
439-660 4.82e-41

DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint helicase (ERCC6L, also known as RAD26L) is an essential component of the mitotic spindle assembly checkpoint, by acting as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. ERCC6L is proposed to stimulate cancer cell proliferation by promoting cell cycle through a way of RAB31-MAPK-CDK2. ERCC6L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350759 [Multi-domain]  Cd Length: 232  Bit Score: 152.14  E-value: 4.82e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTE-MNAIVY 517
Cdd:cd18001      1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPgLRVKVF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  518 HGSQisrqmiqqyemvyRDAQGNPLSGVFK-FHVVITTFEMILADCPEL-----KKIHWSCVIIDEAHRLKNRNCKLLEG 591
Cdd:cd18001     81 HGTS-------------KKERERNLERIQRgGGVLLTTYGMVLSNTEQLsaddhDEFKWDYVILDEGHKIKNSKTKSAKS 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  592 LKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQ-FPSETAFLEEFGDLKTEEQVKK---------------LQSILKP 655
Cdd:cd18001    148 LREIPAKNRIILTGTPIQNNLKELWALFDFACNGSlLGTRKTFKMEFENPITRGRDKDatqgekalgsevaenLRQIIKP 227

                   ....*
gi 1034625941  656 MMLRR 660
Cdd:cd18001    228 YFLRR 232
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
439-660 1.63e-37

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: 142.42  E-value: 1.63e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLL-----FNWYNRKNCILADEMGLGKTIQSITFLSeIFLRgiHGPF--------LIIAPLSTITNWERE 505
Cdd:cd18004      1 LRPHQREGVQFLYdcltgRRGYGGGGAILADEMGLGKTLQAIALVW-TLLK--QGPYgkptakkaLIVCPSSLVGNWKAE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  506 FRTWTemnaivyhGSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHwSC--VIIDEAHRLKN 583
Cdd:cd18004     78 FDKWL--------GLRRIKVVTADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKKI-SIdlLICDEGHRLKN 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  584 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAF-------------------LEEFGDLKTEE 644
Cdd:cd18004    149 SESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFrkvfeepilrsrdpdaseeDKELGAERSQE 228
                          250
                   ....*....|....*.
gi 1034625941  645 qvkkLQSILKPMMLRR 660
Cdd:cd18004    229 ----LSELTSRFILRR 240
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
439-660 4.64e-37

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: 140.95  E-value: 4.64e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLF-NWYNRKNcILADEMGLGKTIQSITFL-SEIFLR-----GIHGPFLIIAPLSTITNWEREFRTWTE 511
Cdd:cd17999      1 LRPYQQEGINWLAFlNKYNLHG-ILCDDMGLGKTLQTLCILaSDHHKRansfnSENLPSLVVCPPTLVGHWVAEIKKYFP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  512 ---MNAIVYHGSQISRQMIQQyemvyrdaQGNplsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKL 588
Cdd:cd17999     80 nafLKPLAYVGPPQERRRLRE--------QGE------KHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKL 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  589 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG-------DLK-----TEEQVKKLQSILK-- 654
Cdd:cd17999    146 SKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLkpilasrDSKasakeQEAGALALEALHKqv 225

                   ....*..
gi 1034625941  655 -PMMLRR 660
Cdd:cd17999    226 lPFLLRR 232
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
350-408 1.14e-35

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


Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 130.10  E-value: 1.14e-35
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034625941  350 PDYVEVDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAKVKEFESLQ 408
Cdd:cd18663      1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
439-624 3.48e-35

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: 133.99  E-value: 3.48e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLfnWYNRKNC--ILADEMGLGKTIQSITflseiFLRGIH------GPFLIIAPLSTITNWEREFRTW- 509
Cdd:cd18000      1 LFKYQQTGVQWLW--ELHCQRVggILGDEMGLGKTIQIIA-----FLAALHhsklglGPSLIVCPATVLKQWVKEFHRWw 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  510 TEMNAIVYHGSQISRQMIQQYEMVYRDAQGNPlSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLL 589
Cdd:cd18000     74 PPFRVVVLHSSGSGTGSEEKLGSIERKSQLIR-KVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEIT 152
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1034625941  590 EGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEP 624
Cdd:cd18000    153 LACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
439-637 8.02e-32

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: 125.87  E-value: 8.02e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGmnwLLFNWYN----------RKNCILADEMGLGKTIQSITFLsEIFLRgiHGP----FLIIAPLSTITNWER 504
Cdd:cd18007      1 LKPHQVEG---VRFLWSNlvgtdvgsdeGGGCILAHTMGLGKTLQVITFL-HTYLA--AAPrrsrPLVLCPASTLYNWED 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  505 EFRTWTEMNAIVYHGsqisrqmiqqyeMVYRDAQGNP---LSGVFKFH----VVITTFEM--ILADCPELKK------IH 569
Cdd:cd18007     75 EFKKWLPPDLRPLLV------------LVSLSASKRAdarLRKINKWHkeggVLLIGYELfrNLASNATTDPrlkqefIA 142
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034625941  570 WSC------VIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF 637
Cdd:cd18007    143 ALLdpgpdlLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
DEXDc smart00487
DEAD-like helicases superfamily;
432-630 1.07e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 124.14  E-value: 1.07e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941   432 EYKNSNQLREYQLEGMNWLLFNWynrKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTIT-NWEREFRTWT 510
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAeQWAEELKKLG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941   511 EMNAI----VYHGSQISRQMIQQYEmvyrdaqgnplsgvFKFHVVITTFEMILADCPE--LKKIHWSCVIIDEAHRLKN- 583
Cdd:smart00487   79 PSLGLkvvgLYGGDSKREQLRKLES--------------GKTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDg 144
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1034625941   584 -RNCKLLEGLKLMALE-HKVLLTGTP---LQNSVEELFSLLNFLEPSQFPSE 630
Cdd:smart00487  145 gFGDQLEKLLKLLPKNvQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLE 196
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
439-633 9.19e-29

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


Pssm-ID: 350824 [Multi-domain]  Cd Length: 235  Bit Score: 116.87  E-value: 9.19e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGmnwLLFNWY--------NRKNCILADEMGLGKTIQSITFLSEIFLRGIHGP------FLIIAPLSTITNWER 504
Cdd:cd18066      1 LRPHQREG---IEFLYEcvmgmrvnERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGkpvikrALIVTPGSLVKNWKK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  505 EFRTWtemnaivyhgsqISRQMIQQYeMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNR 584
Cdd:cd18066     78 EFQKW------------LGSERIKVF-TVDQDHKVEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNT 144
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1034625941  585 NCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAF 633
Cdd:cd18066    145 SIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTY 193
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
439-660 3.14e-28

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: 114.61  E-value: 3.14e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLfnwynRKN--CILADEMGLGKTIQSITFLSeiFLRGiHGPFLIIAPLSTITNWEREFRTW----TEM 512
Cdd:cd18010      1 LLPFQREGVCFAL-----RRGgrVLIADEMGLGKTVQAIAIAA--YYRE-EWPLLIVCPSSLRLTWADEIERWlpslPPD 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  513 NAIVYHGSQISRQMiqqyemvyRDAQgnplsgvfkfhVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRN---CKLL 589
Cdd:cd18010     73 DIQVIVKSKDGLRD--------GDAK-----------VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKakrTKAA 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  590 EGLkLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEE---------FGDLKTEEQVKKLQSIL-KPMMLR 659
Cdd:cd18010    134 LPL-LKRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRycaakqggfGWDYSGSSNLEELHLLLlATIMIR 212

                   .
gi 1034625941  660 R 660
Cdd:cd18010    213 R 213
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
266-331 6.11e-27

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: 105.50  E-value: 6.11e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034625941  266 EDDANIIEKILASKTVQ-EVHPGEPPFDLELFYVKYRNFSYLHCKWATMEELEK-DPRIAQKIKRFRN 331
Cdd:cd18668      1 EEDTMIIEKILASRKKKkEKEEGAEEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFKQ 68
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
457-660 2.55e-26

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: 108.92  E-value: 2.55e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  457 RKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVyhgsqISRQMIQQYEmvyRD 536
Cdd:cd18011     17 PVRLLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQDKFGLPFLI-----LDRETAAQLR---RL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  537 AQGNPLSgvfkFHVVITTFEMI-----LADcpELKKIHWSCVIIDEAHRLKNRNCKLLEGL-KLMAL-----EHKVLLTG 605
Cdd:cd18011     89 IGNPFEE----FPIVIVSLDLLkrseeRRG--LLLSEEWDLVVVDEAHKLRNSGGGKETKRyKLGRLlakraRHVLLLTA 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034625941  606 TPLQNSVEELFSLLNFLEPSQFpsetAFLEEFGDLKTEEQVkklqsiLKPMMLRR 660
Cdd:cd18011    163 TPHNGKEEDFRALLSLLDPGRF----AVLGRFLRLDGLREV------LAKVLLRR 207
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
761-875 9.04e-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: 103.83  E-value: 9.04e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  761 GKLVLIDKLLPKliAGGHKVLIFSQMVRCLDilEDYLIQRR-YTYERIDGRVRGNLRQAAIDRFCKPDSDrfvFLLCTRA 839
Cdd:pfam00271    1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1034625941  840 GGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIG 875
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
461-660 1.77e-25

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


Pssm-ID: 350829 [Multi-domain]  Cd Length: 239  Bit Score: 107.55  E-value: 1.77e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  461 ILADEMGLGKTIQSITFLseiflrgIHGPFLIIAPLSTITNWEREFRTWTE---MNAIVYHGSQisrqmiqqyemvyRDA 537
Cdd:cd18071     52 ILADDMGLGKTLTTISLI-------LANFTLIVCPLSVLSNWETQFEEHVKpgqLKVYTYHGGE-------------RNR 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  538 QGNPLSgvfKFHVVITTFEMI------LADCPeLKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNS 611
Cdd:cd18071    112 DPKLLS---KYDIVLTTYNTLasdfgaKGDSP-LHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNS 187
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034625941  612 VEELFSLLNFLEPSQFPSETAFLEEFG---DLKTEEQVKKLQSILKPMMLRR 660
Cdd:cd18071    188 PKDLGSLLSFLHLKPFSNPEYWRRLIQrplTMGDPTGLKRLQVLMKQITLRR 239
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
439-660 2.41e-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: 104.47  E-value: 2.41e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLFNWYNRKN-----CILADEMGLGKTIQSITFLSEIFLRGIHGPFLI-----IAPLSTITNWEREFRT 508
Cdd:cd18067      1 LRPHQREGVKFLYRCVTGRRIrgshgCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaivVSPSSLVKNWANELGK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  509 WTEMNAIVYHGSQISRQMIQQYEMVYRDAQGNPLSGvfkfHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKL 588
Cdd:cd18067     81 WLGGRLQPLAIDGGSKKEIDRKLVQWASQQGRRVST----PVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  589 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF---------GD------LKTEEQVKKLQSIL 653
Cdd:cd18067    157 YQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFelpilkgrdADasekerQLGEEKLQELISIV 236

                   ....*..
gi 1034625941  654 KPMMLRR 660
Cdd:cd18067    237 NRCIIRR 243
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
461-909 5.78e-23

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


Pssm-ID: 468472 [Multi-domain]  Cd Length: 868  Bit Score: 107.46  E-value: 5.78e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  461 ILADEMGLGKTIQS---ITFLSEIFLRGIhgpfLIIAPLSTITNWEREFRTWTEMNAIVyhgsqISRQMIQQ-YEMVYRD 536
Cdd:NF038318    51 ILADEVGLGKTIEAglvLKYVLESGAKKI----LIILPANLRKQWEIELEEKFDLESLI-----LDSLTVEKdAKKWNKR 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  537 AQGNPlsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKN--RNCKLLEGL-KLMALEHKVLLTGTPLQNSVE 613
Cdd:NF038318   122 LTDNK-----KVRIVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRNvhKGGKRAKNLyELTKGIPKILLTATPLQNSLL 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  614 ELFSLLNFLEPSQFPSETAFL------EEFGDLKTEeqvkklqsiLKPMMLRRLKDDVEKNLAPKQETII---------E 678
Cdd:NF038318   197 DLYGLVSFIDPRIFGSEKVFSkryikdEDYSDLKRE---------LSPVLYRTLRKDVADYMQFKKRKCItvdfelspdE 267
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  679 VELTN-----IQKKYYRAILEKNFSFLT----KGANQHNMPnLINTMMELRKCCNHPY---LINGAEEKI------LEDF 740
Cdd:NF038318   268 IELYVrvnnfLKRDILYSIPTSNRTLIIlvirKLLASSSFA-LAETFEVLKKRLEKLKegtRSANAQEGFdlfwsfVEDE 346
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  741 RKTHSPDAPDFQL----QAMIQAAGKLV--LIDKL-----------LPKLIAGG----------HKVLIFSQMVRCLDIL 793
Cdd:NF038318   347 IDESGFEEKQDELytrqKEFIQHEIDEVdaIIDVAkriktnakvtaLKTALEIAfeyqreegiaQKVVVFTESKRTQKYI 426
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  794 EDYLIQRRYTYERI---DG--------------RVR--GN--------LRQAAIDRFckpdSDRFVFLLCTRAGGLGINL 846
Cdd:NF038318   427 AEELRKSGYEGEDIllfNGdfddamtkeiyrawQVKnyGKanygrsveYKHAIVDYF----KNNAKILIVTDAGSEGLNL 502
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034625941  847 TAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI-TRNSYEREMFDKASLKLGLDKAV 909
Cdd:NF038318   503 QFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYEILSEKFELFEGV 566
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
439-660 5.16e-21

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


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 94.85  E-value: 5.16e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLfnWYNRKNC---ILADEMGLGKTIQSITF------------------LSEIFLRGIHGPF-----LI 492
Cdd:cd18072      1 LLLHQKQALAWLL--WRERQKPrggILADDMGLGKTLTMIALilaqkntqnrkeeekekaLTEWESKKDSTLVpsagtLV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  493 IAPLSTITNWEREFRTWTEMNAI---VYHGSQisrqmiqqyemvyRDAQGNPLSgvfKFHVVITTFEMILADCPELKK-- 567
Cdd:cd18072     79 VCPASLVHQWKNEVESRVASNKLrvcLYHGPN-------------RERIGEVLR---DYDIVITTYSLVAKEIPTYKEes 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  568 -------IHWSCVIIDEAHRLKNRNCKLLEGL-KLMALEHKVLlTGTPLQNSVEELFSLLNFLEPSQFpSETAFLEEFGD 639
Cdd:cd18072    143 rssplfrIAWARIILDEAHNIKNPKVQASIAVcKLRAHARWAL-TGTPIQNNLLDMYSLLKFLRCSPF-DDLKVWKKQVD 220
                          250       260
                   ....*....|....*....|.
gi 1034625941  640 LKTEEQVKKLQSILKPMMLRR 660
Cdd:cd18072    221 NKSRKGGERLNILTKSLLLRR 241
HELICc smart00490
helicase superfamily c-terminal domain;
791-875 5.21e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 89.19  E-value: 5.21e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941   791 DILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDrfvFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQAR 870
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 1034625941   871 CHRIG 875
Cdd:smart00490   78 AGRAG 82
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
460-637 6.21e-21

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: 94.57  E-value: 6.21e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  460 CILADEMGLGKTIQSITFLSEIFLRGIHGPF---LIIAPLSTITNWEREFRTWTEMNA---------------------I 515
Cdd:cd18068     31 CILAHCMGLGKTLQVVTFLHTVLLCEKLENFsrvLVVCPLNTVLNWLNEFEKWQEGLKdeekievnelatykrpqersyK 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  516 VYHGSQISRQMIQQYEMvYRD-AQGNPLSGVFKFHvviTTFEMILAD-CPELkkihwscVIIDEAHRLKNRNCKLLEGLK 593
Cdd:cd18068    111 LQRWQEEGGVMIIGYDM-YRIlAQERNVKSREKLK---EIFNKALVDpGPDF-------VVCDEGHILKNEASAVSKAMN 179
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1034625941  594 LMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF 637
Cdd:cd18068    180 SIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
460-637 1.30e-19

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: 90.26  E-value: 1.30e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  460 CILADEMGLGKTIQSITFLsEIFLRGIHGP-FLIIAPLSTITNWEREFRTWteMNAIVYHGSQISRQM---IQQYEMVYR 535
Cdd:cd18069     31 CILAHSMGLGKTLQVISFL-DVLLRHTGAKtVLAIVPVNTLQNWLSEFNKW--LPPPEALPNVRPRPFkvfILNDEHKTT 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  536 DAQGNPLSG-VFKFHVVITTFEMI-LADCPELkkihwscVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVE 613
Cdd:cd18069    108 AARAKVIEDwVKDGGVLLMGYEMFrLRPGPDV-------VICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLI 180
                          170       180
                   ....*....|....*....|....
gi 1034625941  614 ELFSLLNFLEPSQFPSETAFLEEF 637
Cdd:cd18069    181 EYWCMVDFVRPDFLGTRQEFSNMF 204
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
351-406 1.39e-17

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


Pssm-ID: 349306 [Multi-domain]  Cd Length: 54  Bit Score: 78.39  E-value: 1.39e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034625941  351 DYVEVDRIleVAHTKDAETGEEvthYLVKWCSLPYEESTWELEEDV---DPAKVKEFES 406
Cdd:cd18659      1 EYTIVERI--IAHREDDEGVTE---YLVKWKGLPYDECTWESEEDIsdiFQEAIDEYKK 54
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
439-626 6.12e-16

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: 79.32  E-value: 6.12e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLfnwYNRKNCILADeMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITN-WEREFRTWTEMNAIVY 517
Cdd:cd18013      1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARStWPDEVEKWNHLRNLTV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  518 H---GSQisRQMIqqyemvyRDAQGNPlsgvfkfHVVITTFEMiLADCPELKKIHW--SCVIIDEAHRLKNRNCKllEGL 592
Cdd:cd18013     77 SvavGTE--RQRS-------KAANTPA-------DLYVINREN-LKWLVNKSGDPWpfDMVVIDELSSFKSPRSK--RFK 137
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1034625941  593 KLMALEHKV----LLTGTPLQNSVEELFSLLNFLEPSQ 626
Cdd:cd18013    138 ALRKVRPVIkrliGLTGTPSPNGLMDLWAQIALLDQGE 175
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
268-331 4.00e-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: 4.00e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034625941  268 DANIIEKILASKTVQEVHPG-------EPPFDLELFYVKYRNFSYLHCKWATMEELEKDpRIAQKIKRFRN 331
Cdd:cd18660      1 DEDKIEKILDHRPKGPVEEAsldltdpDEPWDEREFLVKWKGKSYLHCTWVTEETLEQL-RGKKKLKNYIK 70
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
381-1029 3.75e-11

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 68.51  E-value: 3.75e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  381 CSLPYEESTWELEEDVDPAKVKEFESLQVLPEIKHVERPASDSWQKLEKS------REYKNSNQLREYQLEGMN-WLLFN 453
Cdd:COG1061     17 SLLLLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEaleagdEASGTSFELRPYQQEALEaLLAAL 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  454 WYNRKNCILADEMGLGKTIQSITFLSEIFLRGihgPFLIIAPLSTITN-WEREFRTWTemNAIVYHGSQISRQmiqqyem 532
Cdd:COG1061     97 ERGGGRGLVVAPTGTGKTVLALALAAELLRGK---RVLVLVPRRELLEqWAEELRRFL--GDPLAGGGKKDSD------- 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  533 vyrdaqgnplsgvfkFHVVITTFEmILADCPELKKI--HWSCVIIDEAHRLKNRncKLLEGLKLMALEHKVLLTGTPlqn 610
Cdd:COG1061    165 ---------------APITVATYQ-SLARRAHLDELgdRFGLVIIDEAHHAGAP--SYRRILEAFPAAYRLGLTATP--- 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  611 sveelfsllnflepsqfpsetafleEFGDLKTEEqVKKLQSILKPMMLRRLKDDveKNLAPKQETIIEVELTNIQKKY-- 688
Cdd:COG1061    224 -------------------------FRSDGREIL-LFLFDGIVYEYSLKEAIED--GYLAPPEYYGIRVDLTDERAEYda 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  689 YRAILEKNfsfltkganqhnmpnlintmmelrkccnhpyLINGAEEK--ILEDFRKTHspdapdfqlqamiqaagklvli 766
Cdd:COG1061    276 LSERLREA-------------------------------LAADAERKdkILRELLREH---------------------- 302
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  767 dkllpkliAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFckpDSDRFVFLLCTRAGGLGINL 846
Cdd:COG1061    303 --------PDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAF---RDGELRILVTVDVLNEGVDV 371
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  847 TAADTCIIFDSDWNPQNDLQAQARCHRIGQSK-AVKVYRLITRNSYEREMFDKASLKLGLDKAVLQDINRKGGTNgVQQL 925
Cdd:COG1061    372 PRLDVAILLRPTGSPREFIQRLGRGLRPAPGKeDALVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELA-LLIA 450
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  926 SKMEVEDLLRKGAYGALMDEEDEGSKFCEEDIDQILQRRTHTITIQSEGKGSTFAKASFVASGNRTDISLDDPNFWQKWA 1005
Cdd:COG1061    451 VKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLL 530
                          650       660
                   ....*....|....*....|....
gi 1034625941 1006 KIAELDTEAKNEKESLVIDRPRVR 1029
Cdd:COG1061    531 LLLLLLELLELLAALLRLEELAAL 554
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
439-627 4.43e-11

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


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 65.83  E-value: 4.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGMNWLLfnwyNRKNcILADEMGLGKTIQSI----------------TFLSEIFLRGIH----------GPFLI 492
Cdd:cd18070      1 LLPYQRRAVNWML----VPGG-ILADEMGLGKTVEVLalillhprpdndldaaDDDSDEMVCCPDclvaetpvssKATLI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  493 IAPLSTITNWEREFRTWTEMNAIVYHgsqisrqmiqqYEMVYRD--AQGNPLSGVFKFHVVITTFEmILAD--------- 561
Cdd:cd18070     76 VCPSAILAQWLDEINRHVPSSLKVLT-----------YQGVKKDgaLASPAPEILAEYDIVVTTYD-VLRTelhyaeanr 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  562 ---------------CPeLKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQ 626
Cdd:cd18070    144 snrrrrrqkryeappSP-LVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEP 222

                   .
gi 1034625941  627 F 627
Cdd:cd18070    223 F 223
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
354-406 7.15e-10

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 56.43  E-value: 7.15e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034625941  354 EVDRIleVAHTKDAETGEEvthYLVKWCSLPYEESTWELEEDVD--PAKVKEFES 406
Cdd:pfam00385    2 EVERI--LDHRKDKGGKEE---YLVKWKGYPYDENTWEPEENLSkcPELIEEFKD 51
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
350-395 5.62e-09

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: 54.19  E-value: 5.62e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1034625941  350 PDYVEVDRILEvaHTKDAETGeevTHYLVKWCSLPYEESTWELEED 395
Cdd:cd18662      1 PEWLQIHRIIN--HRVDKDGN---TWYLVKWRDLPYDQSTWESEDD 41
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
458-606 7.04e-09

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 56.64  E-value: 7.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  458 KNCILADEMGLGKTIQ-SITFLSEIFLRGihGPFLIIAPLSTITN-WEREFRTWTEMNA--IVYHGsqiSRQMIQQYEMV 533
Cdd:cd00046      2 ENVLITAPTGSGKTLAaLLAALLLLLKKG--KKVLVLVPTKALALqTAERLRELFGPGIrvAVLVG---GSSAEEREKNK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  534 YRDAqgnplsgvfkfHVVITTFEMILADCPELKKIH---WSCVIIDEAHRL----KNRNCKLLEGLKLMALEHK-VLLTG 605
Cdd:cd00046     77 LGDA-----------DIIIATPDMLLNLLLREDRLFlkdLKLIIVDEAHALlidsRGALILDLAVRKAGLKNAQvILLSA 145

                   .
gi 1034625941  606 T 606
Cdd:cd00046    146 T 146
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
354-406 2.01e-06

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


Pssm-ID: 349274 [Multi-domain]  Cd Length: 50  Bit Score: 46.70  E-value: 2.01e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034625941  354 EVDRILevahtkDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAK--VKEFES 406
Cdd:cd00024      2 EVEKIL------DHRVRKGKLEYLVKWKGYPPEENTWEPEENLTNAPelIKEYEK 50
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
271-332 3.93e-06

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 46.03  E-value: 3.93e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034625941  271 IIEKILASKTVQEvhpgeppfDLELFYVKYRNFSYLHCKWATMEELEKDPRIaqkIKRFRNK 332
Cdd:pfam00385    2 EVERILDHRKDKG--------GKEEYLVKWKGYPYDENTWEPEENLSKCPEL---IEEFKDR 52
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
439-607 5.91e-06

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: 48.46  E-value: 5.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  439 LREYQLEGM-NWLLFNWYNRKNCILAdeMGLGKTIqsiTFLSEIFLRGIHgPFLIIAP-LSTITNWEREFRTWTemnaiv 516
Cdd:cd17926      1 LRPYQEEALeAWLAHKNNRRGILVLP--TGSGKTL---TALALIAYLKEL-RTLIVVPtDALLDQWKERFEDFL------ 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  517 yHGSQISRQmiqqyemvyrdaQGNPLSGVFKFHVVITTFEMILADCPELKKI--HWSCVIIDEAHRLknrNCKLLEGLKL 594
Cdd:cd17926     69 -GDSSIGLI------------GGGKKKDFDDANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAHHL---PAKTFSEILK 132
                          170
                   ....*....|....
gi 1034625941  595 MALEHKVL-LTGTP 607
Cdd:cd17926    133 ELNAKYRLgLTATP 146
CD2_tandem_ScCHD1_like cd18664
repeat 2 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
351-406 7.63e-06

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: 45.34  E-value: 7.63e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034625941  351 DYVEVDRILEvahTKDAETGEEVTH--YLVKWCSLPYEESTWELEEDV---DPAKVKEFES 406
Cdd:cd18664      1 EFHVVERIIA---SQRASLEDGTSQlqYLVKWRRLNYDECTWEDATLIaklAPEQVDHFQN 58
CD2_tandem_CHD1-2_like cd18661
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
352-406 2.39e-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: 2.39e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034625941  352 YVEVDRIleVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVD---PAKVKEFES 406
Cdd:cd18661      2 YQIVERI--IAHSPQKSAASGYPDYLCKWQGLPYSECTWEDGALISkkfQACIDEYHS 57
CHROMO smart00298
Chromatin organization modifier domain;
354-405 2.59e-05

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 43.74  E-value: 2.59e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1034625941   354 EVDRILevAHTKDAETGEEvthYLVKWCSLPYEESTWELEEDV--DPAKVKEFE 405
Cdd:smart00298    3 EVEKIL--DHRWKKKGELE---YLVKWKGYSYSEDTWEPEENLlnCSKKLDNYK 51
BRK smart00592
domain in transcription and CHROMO domain helicases;
2380-2415 3.99e-05

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 43.11  E-value: 3.99e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1034625941  2380 SGEERVPAIPKEPGLRG----FLPENKFNHTLAEPILRDT 2415
Cdd:smart00592    1 DGEERVPVINRETGKKLtgddAPKAKDLERWLEENPEYEV 40
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
354-398 1.12e-04

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


Pssm-ID: 349322  Cd Length: 49  Bit Score: 41.88  E-value: 1.12e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1034625941  354 EVDRILevahtkdAETGEE-VTHYLVKWCSLPYEESTWELEEDVDP 398
Cdd:cd18966      2 EVERIL-------AERRDDgGKRYLVKWEGYPLEEATWEPEENIGD 40
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
440-615 1.14e-04

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 44.93  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  440 REYQLEGMNWLLfnwyNRKNCILADEMGLGKT-IQSITFLSEIFLRGIHGPFLIIAPLSTITN-WEREFRTWTEMNAI-- 515
Cdd:pfam00270    1 TPIQAEAIPAIL----EGRDVLVQAPTGSGKTlAFLLPALEALDKLDNGPQALVLAPTRELAEqIYEELKKLGKGLGLkv 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  516 --VYHGSQISRQMiqqyemvyrdaqgNPLSGVfkfHVVITTFEMILADCPE---LKKIhwSCVIIDEAHRL--KNRNCKL 588
Cdd:pfam00270   77 asLLGGDSRKEQL-------------EKLKGP---DILVGTPGRLLDLLQErklLKNL--KLLVLDEAHRLldMGFGPDL 138
                          170       180
                   ....*....|....*....|....*...
gi 1034625941  589 LEGLKLMALEHK-VLLTGTPLQNsVEEL 615
Cdd:pfam00270  139 EEILRRLPKKRQiLLLSATLPRN-LEDL 165
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
828-880 7.11e-04

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 40.38  E-value: 7.11e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034625941  828 SDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAV 880
Cdd:cd18785     20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGE 72
CD1_tandem_CHD3-4_like cd18667
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
257-317 8.39e-04

repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and 4, 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 CHD3 and CHD4. 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: 349314 [Multi-domain]  Cd Length: 79  Bit Score: 40.40  E-value: 8.39e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034625941  257 LAWQAEEPPEDDAnIIEKILASKTVQEVHPGEPPFDLELFyVKYRNFSYLHCKWATMEELE 317
Cdd:cd18667      9 LTWRWAEPPYPEP-LPEKPDEDPYPPPPRKLQPRPEREFF-VKWHGMSYWHCEWVSELQLE 67
CD_POL_like cd18974
chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the ...
360-400 1.29e-03

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


Pssm-ID: 349330  Cd Length: 50  Bit Score: 39.00  E-value: 1.29e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1034625941  360 EVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAK 400
Cdd:cd18974      2 EVEEIVDEKMIDDELHYLVKWKGWPAEYNQWEPEDDMENAP 42
CD_MarY1_POL_like cd18975
chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes ...
376-404 1.41e-03

chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in the polyprotein from the MarY1 Ty3/Gypsy long terminal repeat (LTR) retroelement from the from the Ectomycorrhizal Basidiomycete Tricholoma matsutake. The pol gene in TY3/gypsy elements generally encodes domains in the following order: prt-reverse transcriptase-RNase H-integrase, in marY1 POL the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349331  Cd Length: 49  Bit Score: 38.68  E-value: 1.41e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034625941  376 YLVKWCSLPYEESTWELEEDVDPAK-VKEF 404
Cdd:cd18975     18 YLIQWKGYPLEEASWELEDNIKNPRlIEEF 47
chromodomain cd18965
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
374-396 1.55e-03

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


Pssm-ID: 349321  Cd Length: 53  Bit Score: 38.61  E-value: 1.55e-03
                           10        20
                   ....*....|....*....|...
gi 1034625941  374 THYLVKWCSLPYEESTWELEEDV 396
Cdd:cd18965     16 LEYLVKWHGLPESENTWEREKDI 38
PHA03247 PHA03247
large tegument protein UL36; Provisional
2297-2671 1.99e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 1.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941 2297 PGQATLSTTHPEGPGPATSAPEPATAASSQAEKSIPSKSLLDWLRQQADYS-------LEVPGFGANFSDKPKQRRPRCK 2369
Cdd:PHA03247  2609 RGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGrvsrprrARRLGRAAQASSPPQRPRRRAA 2688
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941 2370 EPGkldVSSLSGEERVPAIPKEPGLRgflpenkfnhtlAEPILRDTGPRRRGRRPRSELLKAPSIVADSPSGMGPLfmng 2449
Cdd:PHA03247  2689 RPT---VGSLTSLADPPPPPPTPEPA------------PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA---- 2749
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941 2450 LIAGMDLVGLQNMRNMPGIPLTglvgfPAGFATMPTGEEVKSTLSMLPMMLPGMAAVPQMFGVGGLLSPPMATTCTSTAP 2529
Cdd:PHA03247  2750 TPGGPARPARPPTTAGPPAPAP-----PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941 2530 ASLSSTTKSGTAVTEKTAEDKPSSHDVKTDTLAedkPGpGPFSDQSEPAITTSSPVAfnPFLIPGVSpgLIYPSMFLSPg 2609
Cdd:PHA03247  2825 AGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA---PG-GDVRRRPPSRSPAAKPAA--PARPPVRR--LARPAVSRST- 2895
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034625941 2610 MGMALPAMQQARHSEivglesqkrkkkktkgdnPNSHPEPAPSCEREPSGDENCAEPSAPLP 2671
Cdd:PHA03247  2896 ESFALPPDQPERPPQ------------------PQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939
chromodomain cd18968
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
354-404 2.00e-03

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


Pssm-ID: 349324  Cd Length: 57  Bit Score: 38.48  E-value: 2.00e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034625941  354 EVDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAK--VKEF 404
Cdd:cd18968      3 EVEVILAARVVKDAESRKKGWKYLVKWAGYPDEENTWEPEESFDGCDdlLERF 55
CHROMO smart00298
Chromatin organization modifier domain;
272-334 2.54e-03

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 38.35  E-value: 2.54e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034625941   272 IEKILASKTVQEvhpGEppfdlELFYVKYRNFSYLHCKWATMEELEKDPRiaqKIKRFRNKQA 334
Cdd:smart00298    4 VEKILDHRWKKK---GE-----LEYLVKWKGYSYSEDTWEPEENLLNCSK---KLDNYKKKER 55
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
82-351 7.89e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 41.60  E-value: 7.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941   82 QEGAAKGSKDrepkPKRKREPKEPKEPRKAKEPKKAKEHKEPKQKDGAKKARKPREASGTKEAKEKRSctDSAARTKSRK 161
Cdd:PTZ00449   533 EHEDSKESDE----PKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPEEPKK--PKRPRSAQRP 606
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  162 ASKEQGPTPVEKKKKGKRKSETTVESLELDQGLTNPSlrSPE--ESTESTDSQKRRSGRQV------KRRKYNEDLDFKV 233
Cdd:PTZ00449   607 TRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPS--SPErpEGPKIIKSPKPPKSPKPpfdpkfKEKFYDDYLDAAA 684
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034625941  234 VDDDGETIAVLGAGRTSALSaSTLAWQAEEPPEDDANIIEKILASKTVQEVHPGEP----PFDLELFYVKYRNFSYLHCK 309
Cdd:PTZ00449   685 KSKETKTTVVLDESFESILK-ETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPdaeqPDDIEFFTPPEEERTFFHET 763
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1034625941  310 WAT------MEELEKDPRIAQKIKrfrnkqaqmkhiftEPDEDLFNPD 351
Cdd:PTZ00449   764 PADtplpdiLAEEFKEEDIHAETG--------------EPDEAMKRPD 797
CD_CMT3_like cd18635
chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier ...
354-404 8.13e-03

chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier (chromo) domain of DNA (cytosine-5)-methyltransferase chromomethylase 3 (CMT3, EC:2.1.1.37), and similar proteins. CMT3 is primarily a CHG (where H is either A, T or C) methyltransferase and is predominantly expressed in actively replicating cells. The protein is involved in preferentially methylating transposon-related sequences, reducing their mobility. Studies suggest that in order to target DNA methylation, CMT3 associates with H3K9me2-containing nucleosomes through binding of its BAH- and chromo-domains to H3K9me2. 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: 349285  Cd Length: 57  Bit Score: 36.91  E-value: 8.13e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034625941  354 EVDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVD--PAKVKEF 404
Cdd:cd18635      3 EVEKLVGICYGDPKKTGERGLYFKVRWKGYGPEEDTWEPIEGLSncPEKIKEF 55
 
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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