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Conserved domains on  [gi|768018477|ref|XP_011527382|]
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chromodomain-helicase-DNA-binding protein 6 isoform X3 [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; ...
459-680 5.40e-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: 484.16  E-value: 5.40e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 538
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  539 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALE 618
Cdd:cd18058    81 GSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768018477  619 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 680
Cdd:cd18058   161 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
458-983 1.52e-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: 506.65  E-value: 1.52e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  458 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LRGIHGPFLIIAPLSTITNWEREFRTWTEM-NAI 535
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHeYRGITGPHMVVAPKSTLGNWMNEIRRFCPVlRAV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  536 VYHGSQISRQMIQQYEMVyrdaqgnplSGvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLM 615
Cdd:PLN03142  249 KFHGNPEERAHQREELLV---------AG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLF 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  616 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF---GDLKTEEQVKKLQSILKPMMLRRLKDDVEKNLAPK 692
Cdd:PLN03142  318 STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPK 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  693 QETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNmpnLINTMMELRKCCNHPYLINGAEekiledfrkthsPDAPDFQ 772
Cdd:PLN03142  398 KETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAE------------PGPPYTT 462
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  773 LQAMIQAAGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDRFV 852
Cdd:PLN03142  463 GEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFV 542
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  853 FLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQD 932
Cdd:PLN03142  543 FLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ 622
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768018477  933 inrkggtNGVQQLSKMEVEDLLRKGAYGALMDEEDEGSKFCEEDIDQILQR 983
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, ...
370-428 1.01e-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: 130.49  E-value: 1.01e-35
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 768018477  370 PDYVEVDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAKVKEFESLQ 428
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, ...
286-351 5.53e-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: 105.88  E-value: 5.53e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768018477  286 EDDANIIEKILASKTVQ-EVHPGEPPFDLELFYVKYRNFSYLHCKWATMEELEK-DPRIAQKIKRFRN 351
Cdd:cd18668     1 EEDTMIIEKILASRKKKkEKEEGAEEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFKQ 68
BRK super family cl02688
BRK domain; The function of this domain is unknown. It is often found associated with ...
2400-2435 3.94e-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: 3.94e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 768018477   2400 SGEERVPAIPKEPGLRG----FLPENKFNHTLAEPILRDT 2435
Cdd:smart00592    1 DGEERVPVINRETGKKLtgddAPKAKDLERWLEENPEYEV 40
PHA03247 super family cl33720
large tegument protein UL36; Provisional
2317-2691 1.74e-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: 44.16  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477 2317 PGQATLSTTHPEGPGPATSAPEPATAASSQAEKSIPSKSLLDWLRQQADYS-------LEVPGFGANFSDKPKQRRPRCK 2389
Cdd:PHA03247 2609 RGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGrvsrprrARRLGRAAQASSPPQRPRRRAA 2688
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477 2390 EPGkldVSSLSGEERVPAIPKEPGLRgflpenkfnhtlAEPILRDTGPRRRGRRPRSELLKAPSIVADSPSGMGPLfmng 2469
Cdd:PHA03247 2689 RPT---VGSLTSLADPPPPPPTPEPA------------PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA---- 2749
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477 2470 LIAGMDLVGLQNMRNMPGIPLTglvgfPAGFATMPTGEEVKSTLSMLPMMLPGMAAVPQMFGVGGLLSPPMATTCTSTAP 2549
Cdd:PHA03247 2750 TPGGPARPARPPTTAGPPAPAP-----PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477 2550 ASLSSTTKSGTAVTEKTAEDKPSSHDVKTDTLAedkPGpGPFSDQSEPAITTSSPVAfnPFLIPGVSpgLIYPSMFLSPg 2629
Cdd:PHA03247 2825 AGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA---PG-GDVRRRPPSRSPAAKPAA--PARPPVRR--LARPAVSRST- 2895
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768018477 2630 MGMALPAMQQARHSEivglesqkrkkkktkgdnPNSHPEPAPSCEREPSGDENCAEPSAPLP 2691
Cdd:PHA03247 2896 ESFALPPDQPERPPQ------------------PQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
102-371 7.49e-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: 41.98  E-value: 7.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  102 QEGAAKGSKDrepkPKRKREPKEPKEPRKAKEPKKAKEHKEPKQKDGAKKARKPREASGTKEAKEKRSctDSAARTKSRK 181
Cdd:PTZ00449  533 EHEDSKESDE----PKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPEEPKK--PKRPRSAQRP 606
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  182 ASKEQGPTPVEKKKKGKRKSETTVESLELDQGLTNPSlrSPE--ESTESTDSQKRRSGRQV------KRRKYNEDLDFKV 253
Cdd:PTZ00449  607 TRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPS--SPErpEGPKIIKSPKPPKSPKPpfdpkfKEKFYDDYLDAAA 684
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  254 VDDDGETIAVLGAGRTSALSaSTLAWQAEEPPEDDANIIEKILASKTVQEVHPGEP----PFDLELFYVKYRNFSYLHCK 329
Cdd:PTZ00449  685 KSKETKTTVVLDESFESILK-ETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPdaeqPDDIEFFTPPEEERTFFHET 763
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 768018477  330 WAT------MEELEKDPRIAQKIKrfrnkqaqmkhiftEPDEDLFNPD 371
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; ...
459-680 5.40e-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: 484.16  E-value: 5.40e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 538
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  539 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALE 618
Cdd:cd18058    81 GSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768018477  619 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 680
Cdd:cd18058   161 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
458-983 1.52e-153

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 506.65  E-value: 1.52e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  458 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LRGIHGPFLIIAPLSTITNWEREFRTWTEM-NAI 535
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHeYRGITGPHMVVAPKSTLGNWMNEIRRFCPVlRAV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  536 VYHGSQISRQMIQQYEMVyrdaqgnplSGvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLM 615
Cdd:PLN03142  249 KFHGNPEERAHQREELLV---------AG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLF 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  616 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF---GDLKTEEQVKKLQSILKPMMLRRLKDDVEKNLAPK 692
Cdd:PLN03142  318 STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPK 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  693 QETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNmpnLINTMMELRKCCNHPYLINGAEekiledfrkthsPDAPDFQ 772
Cdd:PLN03142  398 KETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAE------------PGPPYTT 462
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  773 LQAMIQAAGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDRFV 852
Cdd:PLN03142  463 GEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFV 542
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  853 FLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQD 932
Cdd:PLN03142  543 FLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ 622
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768018477  933 inrkggtNGVQQLSKMEVEDLLRKGAYGALMDEEDEGSKFCEEDIDQILQR 983
Cdd:PLN03142  623 -------GRLAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAK 666
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
458-931 3.56e-129

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 423.87  E-value: 3.56e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  458 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 536
Cdd:COG0553   241 TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFApGLRVLV 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  537 YHGSQisrqmiqqyemvYRDAQGNPLSgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMA 616
Cdd:COG0553   321 LDGTR------------ERAKGANPFE---DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  617 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKT---EEQVKKLQSILKPMMLRRLKDDVEKNLAPKQ 693
Cdd:COG0553   386 ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEkgdEEALERLRRLLRPFLLRRTKEDVLKDLPEKT 465
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  694 ETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNMPNLINTMMELRKCCNHPYLingaeekILEDFRKTHSPDapdfql 773
Cdd:COG0553   466 EETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLILAALTRLRQICSHPAL-------LLEEGAELSGRS------ 532
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  774 qamiqaaGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFcKPDSDRFVF 853
Cdd:COG0553   533 -------AKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRF-QEGPEAPVF 604
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768018477  854 LLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQ 931
Cdd:COG0553   605 LISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
462-749 5.95e-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: 5.95e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477   462 YQLEGMNWLLFNWYNRK-NCILADEMGLGKTIQSITFLSeiFLRGIH----GPFLIIAPLSTITNWEREFRTWT---EMN 533
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLL--YLKHVDknwgGPTLIVVPLSLLHNWMNEFERWVsppALR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477   534 AIVYHGSQISRQMIQQYEMVYRDaqgnplsgvfkFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLK 613
Cdd:pfam00176   79 VVVLHGNKRPQERWKNDPNFLAD-----------FDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477   614 LMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----DLKTEEQVKKLQSILKPMMLRRLKDDVEKNL 689
Cdd:pfam00176  148 SLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpieRGGGKKGVSRLHKLLKPFLLRRTKKDVEKSL 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768018477   690 APKQETIIEVELTNIQKKYY-RAILEKNFSFLTKG-ANQHNMPNLINTMMELRKCCNHPYLI 749
Cdd:pfam00176  228 PPKVEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGeGGREIKASLLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
781-906 2.19e-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: 2.19e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  781 GKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFcKPDSDRFVFLLCTRAG 860
Cdd:cd18793    11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRF-NEDPDIRVFLLSTKAG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 768018477  861 GLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI 906
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, ...
370-428 1.01e-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: 130.49  E-value: 1.01e-35
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 768018477  370 PDYVEVDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAKVKEFESLQ 428
Cdd:cd18663     1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
DEXDc smart00487
DEAD-like helicases superfamily;
452-650 1.08e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 124.14  E-value: 1.08e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477    452 EYKNSNQLREYQLEGMNWLLFNWynrKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTIT-NWEREFRTWT 530
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAeQWAEELKKLG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477    531 EMNAI----VYHGSQISRQMIQQYEmvyrdaqgnplsgvFKFHVVITTFEMILADCPE--LKKIHWSCVIIDEAHRLKN- 603
Cdd:smart00487   79 PSLGLkvvgLYGGDSKREQLRKLES--------------GKTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDg 144
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|..
gi 768018477    604 -RNCKLLEGLKLMALE-HKVLLTGTP---LQNSVEELFSLLNFLEPSQFPSE 650
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, ...
286-351 5.53e-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: 105.88  E-value: 5.53e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768018477  286 EDDANIIEKILASKTVQ-EVHPGEPPFDLELFYVKYRNFSYLHCKWATMEELEK-DPRIAQKIKRFRN 351
Cdd:cd18668     1 EEDTMIIEKILASRKKKkEKEEGAEEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFKQ 68
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
781-895 9.10e-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: 9.10e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477   781 GKLVLIDKLLPKliAGGHKVLIFSQMVRCLDilEDYLIQRR-YTYERIDGRVRGNLRQAAIDRFCKPDSDrfvFLLCTRA 859
Cdd:pfam00271    1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 768018477   860 GGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIG 895
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 ...
481-929 5.00e-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: 107.85  E-value: 5.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  481 ILADEMGLGKTIQS---ITFLSEIFLRGIhgpfLIIAPLSTITNWEREFRTWTEMNAIVyhgsqISRQMIQQ-YEMVYRD 556
Cdd:NF038318   51 ILADEVGLGKTIEAglvLKYVLESGAKKI----LIILPANLRKQWEIELEEKFDLESLI-----LDSLTVEKdAKKWNKR 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  557 AQGNPlsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKN--RNCKLLEGL-KLMALEHKVLLTGTPLQNSVE 633
Cdd:NF038318  122 LTDNK-----KVRIVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRNvhKGGKRAKNLyELTKGIPKILLTATPLQNSLL 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  634 ELFSLLNFLEPSQFPSETAFL------EEFGDLKTEeqvkklqsiLKPMMLRRLKDDVEKNLAPKQETII---------E 698
Cdd:NF038318  197 DLYGLVSFIDPRIFGSEKVFSkryikdEDYSDLKRE---------LSPVLYRTLRKDVADYMQFKKRKCItvdfelspdE 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  699 VELTN-----IQKKYYRAILEKNFSFLT----KGANQHNMPnLINTMMELRKCCNHPY---LINGAEEKI------LEDF 760
Cdd:NF038318  268 IELYVrvnnfLKRDILYSIPTSNRTLIIlvirKLLASSSFA-LAETFEVLKKRLEKLKegtRSANAQEGFdlfwsfVEDE 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  761 RKTHSPDAPDFQL----QAMIQAAGKLV--LIDKL-----------LPKLIAGG----------HKVLIFSQMVRCLDIL 813
Cdd:NF038318  347 IDESGFEEKQDELytrqKEFIQHEIDEVdaIIDVAkriktnakvtaLKTALEIAfeyqreegiaQKVVVFTESKRTQKYI 426
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  814 EDYLIQRRYTYERI---DG--------------RVR--GN--------LRQAAIDRFckpdSDRFVFLLCTRAGGLGINL 866
Cdd:NF038318  427 AEELRKSGYEGEDIllfNGdfddamtkeiyrawQVKnyGKanygrsveYKHAIVDYF----KNNAKILIVTDAGSEGLNL 502
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768018477  867 TAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI-TRNSYEREMFDKASLKLGLDKAV 929
Cdd:NF038318  503 QFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYEILSEKFELFEGV 566
HELICc smart00490
helicase superfamily c-terminal domain;
811-895 5.25e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 89.19  E-value: 5.25e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477    811 DILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDrfvFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQAR 890
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 768018477    891 CHRIG 895
Cdd:smart00490   78 AGRAG 82
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
374-426 6.66e-10

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 56.82  E-value: 6.66e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 768018477   374 EVDRIleVAHTKDAETGEEvthYLVKWCSLPYEESTWELEEDVD--PAKVKEFES 426
Cdd:pfam00385    2 EVERI--LDHRKDKGGKEE---YLVKWKGYPYDENTWEPEENLSkcPELIEEFKD 51
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
291-352 3.84e-06

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 46.03  E-value: 3.84e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768018477   291 IIEKILASKTVQEvhpgeppfDLELFYVKYRNFSYLHCKWATMEELEKDPRIaqkIKRFRNK 352
Cdd:pfam00385    2 EVERILDHRKDKG--------GKEEYLVKWKGYPYDENTWEPEENLSKCPEL---IEEFKDR 52
CHROMO smart00298
Chromatin organization modifier domain;
374-425 2.46e-05

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 43.74  E-value: 2.46e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 768018477    374 EVDRILevAHTKDAETGEEvthYLVKWCSLPYEESTWELEEDV--DPAKVKEFE 425
Cdd:smart00298    3 EVEKIL--DHRWKKKGELE---YLVKWKGYSYSEDTWEPEENLlnCSKKLDNYK 51
BRK smart00592
domain in transcription and CHROMO domain helicases;
2400-2435 3.94e-05

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 43.11  E-value: 3.94e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 768018477   2400 SGEERVPAIPKEPGLRG----FLPENKFNHTLAEPILRDT 2435
Cdd:smart00592    1 DGEERVPVINRETGKKLtgddAPKAKDLERWLEENPEYEV 40
PHA03247 PHA03247
large tegument protein UL36; Provisional
2317-2691 1.74e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477 2317 PGQATLSTTHPEGPGPATSAPEPATAASSQAEKSIPSKSLLDWLRQQADYS-------LEVPGFGANFSDKPKQRRPRCK 2389
Cdd:PHA03247 2609 RGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGrvsrprrARRLGRAAQASSPPQRPRRRAA 2688
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477 2390 EPGkldVSSLSGEERVPAIPKEPGLRgflpenkfnhtlAEPILRDTGPRRRGRRPRSELLKAPSIVADSPSGMGPLfmng 2469
Cdd:PHA03247 2689 RPT---VGSLTSLADPPPPPPTPEPA------------PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA---- 2749
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477 2470 LIAGMDLVGLQNMRNMPGIPLTglvgfPAGFATMPTGEEVKSTLSMLPMMLPGMAAVPQMFGVGGLLSPPMATTCTSTAP 2549
Cdd:PHA03247 2750 TPGGPARPARPPTTAGPPAPAP-----PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477 2550 ASLSSTTKSGTAVTEKTAEDKPSSHDVKTDTLAedkPGpGPFSDQSEPAITTSSPVAfnPFLIPGVSpgLIYPSMFLSPg 2629
Cdd:PHA03247 2825 AGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA---PG-GDVRRRPPSRSPAAKPAA--PARPPVRR--LARPAVSRST- 2895
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768018477 2630 MGMALPAMQQARHSEivglesqkrkkkktkgdnPNSHPEPAPSCEREPSGDENCAEPSAPLP 2691
Cdd:PHA03247 2896 ESFALPPDQPERPPQ------------------PQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939
CHROMO smart00298
Chromatin organization modifier domain;
292-354 2.43e-03

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 38.35  E-value: 2.43e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768018477    292 IEKILASKTVQEvhpGEppfdlELFYVKYRNFSYLHCKWATMEELEKDPRiaqKIKRFRNKQA 354
Cdd:smart00298    4 VEKILDHRWKKK---GE-----LEYLVKWKGYSYSEDTWEPEENLLNCSK---KLDNYKKKER 55
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
102-371 7.49e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 41.98  E-value: 7.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  102 QEGAAKGSKDrepkPKRKREPKEPKEPRKAKEPKKAKEHKEPKQKDGAKKARKPREASGTKEAKEKRSctDSAARTKSRK 181
Cdd:PTZ00449  533 EHEDSKESDE----PKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPEEPKK--PKRPRSAQRP 606
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  182 ASKEQGPTPVEKKKKGKRKSETTVESLELDQGLTNPSlrSPE--ESTESTDSQKRRSGRQV------KRRKYNEDLDFKV 253
Cdd:PTZ00449  607 TRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPS--SPErpEGPKIIKSPKPPKSPKPpfdpkfKEKFYDDYLDAAA 684
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  254 VDDDGETIAVLGAGRTSALSaSTLAWQAEEPPEDDANIIEKILASKTVQEVHPGEP----PFDLELFYVKYRNFSYLHCK 329
Cdd:PTZ00449  685 KSKETKTTVVLDESFESILK-ETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPdaeqPDDIEFFTPPEEERTFFHET 763
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 768018477  330 WAT------MEELEKDPRIAQKIKrfrnkqaqmkhiftEPDEDLFNPD 371
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; ...
459-680 5.40e-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: 484.16  E-value: 5.40e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 538
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  539 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALE 618
Cdd:cd18058    81 GSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768018477  619 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 680
Cdd:cd18058   161 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
458-983 1.52e-153

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 506.65  E-value: 1.52e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  458 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LRGIHGPFLIIAPLSTITNWEREFRTWTEM-NAI 535
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHeYRGITGPHMVVAPKSTLGNWMNEIRRFCPVlRAV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  536 VYHGSQISRQMIQQYEMVyrdaqgnplSGvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLM 615
Cdd:PLN03142  249 KFHGNPEERAHQREELLV---------AG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLF 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  616 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF---GDLKTEEQVKKLQSILKPMMLRRLKDDVEKNLAPK 692
Cdd:PLN03142  318 STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPK 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  693 QETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNmpnLINTMMELRKCCNHPYLINGAEekiledfrkthsPDAPDFQ 772
Cdd:PLN03142  398 KETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAE------------PGPPYTT 462
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  773 LQAMIQAAGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDRFV 852
Cdd:PLN03142  463 GEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFV 542
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  853 FLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQD 932
Cdd:PLN03142  543 FLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ 622
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768018477  933 inrkggtNGVQQLSKMEVEDLLRKGAYGALMDEEDEGSKFCEEDIDQILQR 983
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; ...
459-680 1.20e-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: 1.20e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLR-GIHGPFLIIAPLSTITNWEREFRTWTEMNAIVY 537
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVeGIRGPFLVIAPLSTIPNWQREFETWTDMNVVVY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  538 HGSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMAL 617
Cdd:cd17995    81 HGSGESRQIIQQYEMYFKDAQGRKKKGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768018477  618 EHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 680
Cdd:cd17995   161 EHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEQVEKLQALLKPYMLRR 223
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
458-931 3.56e-129

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 423.87  E-value: 3.56e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  458 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 536
Cdd:COG0553   241 TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFApGLRVLV 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  537 YHGSQisrqmiqqyemvYRDAQGNPLSgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMA 616
Cdd:COG0553   321 LDGTR------------ERAKGANPFE---DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  617 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKT---EEQVKKLQSILKPMMLRRLKDDVEKNLAPKQ 693
Cdd:COG0553   386 ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEkgdEEALERLRRLLRPFLLRRTKEDVLKDLPEKT 465
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  694 ETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNMPNLINTMMELRKCCNHPYLingaeekILEDFRKTHSPDapdfql 773
Cdd:COG0553   466 EETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLILAALTRLRQICSHPAL-------LLEEGAELSGRS------ 532
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  774 qamiqaaGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFcKPDSDRFVF 853
Cdd:COG0553   533 -------AKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRF-QEGPEAPVF 604
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768018477  854 LLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQ 931
Cdd:COG0553   605 LISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRALAESVLG 682
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
459-680 1.11e-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: 1.11e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 538
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  539 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALE 618
Cdd:cd18060    81 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768018477  619 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 680
Cdd:cd18060   161 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
459-680 1.81e-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: 1.81e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 538
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  539 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALE 618
Cdd:cd18059    81 GSQASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768018477  619 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 680
Cdd:cd18059   161 HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
459-680 2.74e-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: 2.74e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 538
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDLNVVVYH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  539 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALE 618
Cdd:cd18061    81 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768018477  619 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 680
Cdd:cd18061   161 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
462-749 5.95e-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: 5.95e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477   462 YQLEGMNWLLFNWYNRK-NCILADEMGLGKTIQSITFLSeiFLRGIH----GPFLIIAPLSTITNWEREFRTWT---EMN 533
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLL--YLKHVDknwgGPTLIVVPLSLLHNWMNEFERWVsppALR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477   534 AIVYHGSQISRQMIQQYEMVYRDaqgnplsgvfkFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLK 613
Cdd:pfam00176   79 VVVLHGNKRPQERWKNDPNFLAD-----------FDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477   614 LMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----DLKTEEQVKKLQSILKPMMLRRLKDDVEKNL 689
Cdd:pfam00176  148 SLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpieRGGGKKGVSRLHKLLKPFLLRRTKKDVEKSL 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768018477   690 APKQETIIEVELTNIQKKYY-RAILEKNFSFLTKG-ANQHNMPNLINTMMELRKCCNHPYLI 749
Cdd:pfam00176  228 PPKVEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGeGGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
458-680 3.12e-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: 3.12e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  458 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAI 535
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFhSQQQYGPFLVVVPLSTMPAWQREFAKWApDMNVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  536 VYHGSQISRQMIQQYEMvYRDaQGNPLsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLM 615
Cdd:cd17993    81 VYLGDIKSRDTIREYEF-YFS-QTKKL----KFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEF 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768018477  616 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFlEEFGDLKTEEQVKKLQSILKPMMLRR 680
Cdd:cd17993   155 KTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEF-EEEHDEEQEKGIADLHKELEPFILRR 218
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
459-644 6.43e-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: 6.43e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSE-IFLRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 536
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYlLKEGKERGPVLVVCPLSVLENWEREFEKWTpDLRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  537 YHGSQISRQMIQQYEMVYrdaqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMA 616
Cdd:cd17919    81 YHGSQRERAQIRAKEKLD------------KFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR 148
                         170       180
                  ....*....|....*....|....*...
gi 768018477  617 LEHKVLLTGTPLQNSVEELFSLLNFLEP 644
Cdd:cd17919   149 AKRRLLLTGTPLQNNLEELWALLDFLDP 176
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
458-682 5.75e-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: 5.75e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  458 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 536
Cdd:cd18009     3 VMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTpSVPVLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  537 YHGSQISRQMIQqyemvyRDAQGNPLSGVfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMA 616
Cdd:cd18009    83 YHGTKEERERLR------KKIMKREGTLQ-DFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  617 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG-----------DLKTEEQ----VKKLQSILKPMMLRRL 681
Cdd:cd18009   156 SDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDfsslsdnaadiSNLSEEReqniVHMLHAILKPFLLRRL 235

                  .
gi 768018477  682 K 682
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; ...
459-680 4.00e-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: 4.00e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRG-IHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 536
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWApDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  537 YHGSqisrqmiqqyemvyrdaqgnplsgvfkfHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMA 616
Cdd:cd17994    81 YVGD----------------------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYK 132
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768018477  617 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 680
Cdd:cd17994   133 IGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQIKKLHDLLGPHMLRR 196
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
456-682 8.08e-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: 8.08e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  456 SNQLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSeiFL---RGIHGPFLIIAPLSTITNWEREFRTWT-E 531
Cdd:cd17997     1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLG--YLkhyKNINGPHLIIVPKSTLDNWMREFKRWCpS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  532 MNAIVYHGSQISRQMIQQYEMVYRdaqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEG 611
Cdd:cd17997    79 LRVVVLIGDKEERADIIRDVLLPG-----------KFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQI 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768018477  612 LKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF----GDLKTEEQVKKLQSILKPMMLRRLK 682
Cdd:cd17997   148 VRLFNSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFnvnnCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
459-680 2.38e-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: 233.75  E-value: 2.38e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRG-IHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 536
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhTKGPFLVSAPLSTIINWEREFQMWApDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  537 YHGSQISRQMIQQYEMVYRDAQGNPLSGVFK--------FHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKL 608
Cdd:cd18055    81 YTGDKDSRAIIRENEFSFDDNAVKGGKKAFKmkreaqvkFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768018477  609 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 680
Cdd:cd18055   161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
458-682 1.29e-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: 1.29e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  458 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSI---TFLSEIflRGIHGPFLIIAPLSTITNWEREFRTWT-EMN 533
Cdd:cd17996     3 TLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTIsliTYLMEK--KKNNGPYLVIVPLSTLSNWVSEFEKWApSVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  534 AIVYHGSQISRQMIQQYEMVYrdaqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLK 613
Cdd:cd17996    81 KIVYKGTPDVRKKLQSQIRAG------------KFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLN 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  614 LMAL-EHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG------------DLKTEEQV---KKLQSILKPMM 677
Cdd:cd17996   149 TYYHaRYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNtpfantgeqvkiELNEEETLliiRRLHKVLRPFL 228

                  ....*
gi 768018477  678 LRRLK 682
Cdd:cd17996   229 LRRLK 233
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
459-680 7.56e-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: 7.56e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRG-IHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 536
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWApDMYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  537 YHGSQISRQMIQQYEMVYRD--------AQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKL 608
Cdd:cd18056    81 YVGDKDSRAIIRENEFSFEDnairggkkASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768018477  609 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 680
Cdd:cd18056   161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQIKKLHDMLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
459-680 1.69e-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: 1.69e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRG-IHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 536
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWApDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  537 YHGSQISRQMIQQYEMVYRDAQGNPLSGVF--------KFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKL 608
Cdd:cd18057    81 YTGDKESRSVIRENEFSFEDNAIRSGKKVFrmkkeaqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768018477  609 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 680
Cdd:cd18057   161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
458-680 3.26e-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: 3.26e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  458 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAI 535
Cdd:cd18054    20 ELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFhQHQLYGPFLLVVPLSTLTSWQREFEIWApEINVV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  536 VYHGSQISRQMIQQYEMVYrdaqgnPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLM 615
Cdd:cd18054   100 VYIGDLMSRNTIREYEWIH------SQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDF 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768018477  616 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKtEEQVKKLQSILKPMMLRR 680
Cdd:cd18054   174 KSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGR-ENGYQSLHKVLEPFLLRR 237
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
457-682 3.98e-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: 3.98e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  457 NQLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAI 535
Cdd:cd18012     3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFApELKVL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  536 VYHGSQISRQMIQQYEmvyrdaqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLM 615
Cdd:cd18012    83 VIHGTKRKREKLRALE---------------DYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKAL 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768018477  616 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----DLKTEEQVKKLQSILKPMMLRRLK 682
Cdd:cd18012   148 KADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAkpieKDGDEEALEELKKLISPFILRRLK 218
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
459-680 1.07e-58

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: 1.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEI-FLRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 536
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLaGRLKLLGPFLVLCPLSVLDNWKEELNRFApDLSVIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  537 YHGSQISRQMIQQyemvyrDAQGNPlsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMA 616
Cdd:cd18006    81 YMGDKEKRLDLQQ------DIKSTN-----RFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFS 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768018477  617 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETA--FLEEFGDLKTE-EQVKKLQSILKPMMLRR 680
Cdd:cd18006   150 VDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKLddFIKAYSETDDEsETVEELHLLLQPFLLRR 216
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
781-906 2.19e-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: 2.19e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  781 GKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFcKPDSDRFVFLLCTRAG 860
Cdd:cd18793    11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRF-NEDPDIRVFLLSTKAG 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 768018477  861 GLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI 906
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 ...
459-680 1.64e-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: 1.64e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFL-RGIHGPFLIIAPLSTITNWEREFRTWTE-MNAIV 536
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACeKGNWGPHLIVVPTSVMLNWEMEFKRWCPgFKILT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  537 YHGSQISRQMIQQYEMvyrdaqgNPLSgvfkFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMA 616
Cdd:cd18003    81 YYGSAKERKLKRQGWM-------KPNS----FHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFN 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768018477  617 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKT----------EEQVKKLQSILKPMMLRR 680
Cdd:cd18003   150 TQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLTamsegsqeenEELVRRLHKVLRPFLLRR 223
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
458-680 2.91e-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: 2.91e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  458 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLR-GIHGPFLIIAPLSTITNWEREFRTWT-EMNAI 535
Cdd:cd18053    20 ELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEhQLYGPFLLVVPLSTLTSWQREIQTWApQMNAV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  536 VYHGSQISRQMIQQYEMVYrdaqgnPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLM 615
Cdd:cd18053   100 VYLGDINSRNMIRTHEWMH------PQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDF 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768018477  616 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKtEEQVKKLQSILKPMMLRR 680
Cdd:cd18053   174 KSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGR-EYGYASLHKELEPFLLRR 237
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
459-680 1.86e-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: 1.86e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLfNWYNRK-NCILADEMGLGKTIQSITFLSEIFLR-GIHGPFLIIAPLSTITNWEREF-RTWTEMNAI 535
Cdd:cd18002     1 LKEYQLKGLNWLA-NLYEQGiNGILADEMGLGKTVQSIAVLAHLAEEhNIWGPFLVIAPASTLHNWQQEIsRFVPQFKVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  536 VYHGSQISRQMIQQY----EMVYRDAqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEG 611
Cdd:cd18002    80 PYWGNPKDRKVLRKFwdrkNLYTRDA---------PFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKT 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768018477  612 LKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG-DLKT---------EEQVKKLQSILKPMMLRR 680
Cdd:cd18002   151 LLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSkDIEShaenktglnEHQLKRLHMILKPFMLRR 229
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
459-647 4.97e-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: 4.97e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIVY 537
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCpSLKVEPY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  538 HGSQISRqmiqqyemvyRDAQGNPLSGVFKFHVVITTFEMILADCPE---LKKIHWSCVIIDEAHRLKNRNCKLLEGLKL 614
Cdd:cd17998    81 YGSQEER----------KHLRYDILKGLEDFDVIVTTYNLATSNPDDrsfFKRLKLNYVVYDEGHMLKNMTSERYRHLMT 150
                         170       180       190
                  ....*....|....*....|....*....|...
gi 768018477  615 MALEHKVLLTGTPLQNSVEELFSLLNFLEPSQF 647
Cdd:cd17998   151 INANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
459-680 1.58e-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: 1.58e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLlFNWY-NRKNCILADEMGLGKTIQSITFLSEI----------------FLRGIH-----GPFLIIAPL 516
Cdd:cd18005     1 LRDYQREGVEFM-YDLYkNGRGGILGDDMGLGKTVQVIAFLAAVlgktgtrrdrennrprFKKKPPassakKPVLIVAPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  517 STITNWEREFRTWTEMNAIVYHGSQISRQMIQQYEmvyrdaQGnplsgvfKFHVVITTFEMILADCPELKKIHWSCVIID 596
Cdd:cd18005    80 SVLYNWKDELDTWGHFEVGVYHGSRKDDELEGRLK------AG-------RLEVVVTTYDTLRRCIDSLNSINWSAVIAD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  597 EAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGD---------------LK 661
Cdd:cd18005   147 EAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEpikrgqrhtatarelRL 226
                         250
                  ....*....|....*....
gi 768018477  662 TEEQVKKLQSILKPMMLRR 680
Cdd:cd18005   227 GRKRKQELAVKLSKFFLRR 245
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
445-682 1.28e-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: 177.54  E-value: 1.28e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  445 QKLEKSREYKNSNQLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LRGIHGPFLIIAPLSTITNWE 523
Cdd:cd18062    10 EKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMeHKRINGPFLIIVPLSTLSNWV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  524 REFRTWT-EMNAIVYHGSQISRQMIQqyemvyrdaqgnPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLK 602
Cdd:cd18062    90 YEFDKWApSVVKVSYKGSPAARRAFV------------PQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  603 NRNCKLLEGLKLMALE-HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----------DLKTEEQ---VKK 668
Cdd:cd18062   158 NHHCKLTQVLNTHYVApRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRR 237
                         250
                  ....*....|....
gi 768018477  669 LQSILKPMMLRRLK 682
Cdd:cd18062   238 LHKVLRPFLLRRLK 251
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
446-693 8.93e-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: 8.93e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  446 KLEKSREYKNSNQLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEI-FLRGIHGPFLIIAPLSTITNWER 524
Cdd:cd18064     3 RFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMkHYRNIPGPHMVLVPKSTLHNWMA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  525 EFRTWT-EMNAIVYHGSQisrqmiQQYEMVYRDAQgnpLSGvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKN 603
Cdd:cd18064    83 EFKRWVpTLRAVCLIGDK------DQRAAFVRDVL---LPG--EWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  604 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGD---LKTEEQVKKLQSILKPMMLRR 680
Cdd:cd18064   152 EKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTnncLGDQKLVERLHMVLRPFLLRR 231
                         250
                  ....*....|...
gi 768018477  681 LKDDVEKNLAPKQ 693
Cdd:cd18064   232 IKADVEKSLPPKK 244
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
445-682 1.25e-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: 171.78  E-value: 1.25e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  445 QKLEKSREYKNSNQLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LRGIHGPFLIIAPLSTITNWE 523
Cdd:cd18063    10 ERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMeHKRLNGPYLIIVPLSTLSNWT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  524 REFRTWT-EMNAIVYHGS-QISRQMIQQYEmvyrdaqgnplSGvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRL 601
Cdd:cd18063    90 YEFDKWApSVVKISYKGTpAMRRSLVPQLR-----------SG--KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRM 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  602 KNRNCKLLEGLKLMALE-HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----------DLKTEEQ---VK 667
Cdd:cd18063   157 KNHHCKLTQVLNTHYVApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgervDLNEEETiliIR 236
                         250
                  ....*....|....*
gi 768018477  668 KLQSILKPMMLRRLK 682
Cdd:cd18063   237 RLHKVLRPFLLRRLK 251
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
446-682 9.48e-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: 9.48e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  446 KLEKSREYKNSNQLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEI-FLRGIHGPFLIIAPLSTITNWER 524
Cdd:cd18065     3 RFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLkHYRNIPGPHMVLVPKSTLHNWMN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  525 EFRTWT-EMNAIVYHGSQISRQMIQQYEMvyrdaqgnpLSGvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKN 603
Cdd:cd18065    83 EFKRWVpSLRAVCLIGDKDARAAFIRDVM---------MPG--EWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  604 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGD---LKTEEQVKKLQSILKPMMLRR 680
Cdd:cd18065   152 EKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 231

                  ..
gi 768018477  681 LK 682
Cdd:cd18065   232 IK 233
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
459-680 1.32e-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: 1.32e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLFnwynrKNCILADEMGLGKTIQSI--------TFLSEIFLRGIHGPF----------LIIAPLSTIT 520
Cdd:cd18008     1 LLPYQKQGLAWMLP-----RGGILADEMGLGKTIQALalilatrpQDPKIPEELEENSSDpkklylskttLIVVPLSLLS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  521 NWEREFRTWTE---MNAIVYHGSQisrqmiqqyemvyrdaQGNPLSGVFKFHVVITTFEMILADCPE------------- 584
Cdd:cd18008    76 QWKDEIEKHTKpgsLKVYVYHGSK----------------RIKSIEELSDYDIVITTYGTLASEFPKnkkgggrdskeke 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  585 ---LKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLK 661
Cdd:cd18008   140 aspLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPF 219
                         250       260
                  ....*....|....*....|..
gi 768018477  662 TE---EQVKKLQSILKPMMLRR 680
Cdd:cd18008   220 SKndrKALERLQALLKPILLRR 241
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
459-680 4.86e-41

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


Pssm-ID: 350759 [Multi-domain]  Cd Length: 232  Bit Score: 152.14  E-value: 4.86e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTE-MNAIVY 537
Cdd:cd18001     1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPgLRVKVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  538 HGSQisrqmiqqyemvyRDAQGNPLSGVFK-FHVVITTFEMILADCPEL-----KKIHWSCVIIDEAHRLKNRNCKLLEG 611
Cdd:cd18001    81 HGTS-------------KKERERNLERIQRgGGVLLTTYGMVLSNTEQLsaddhDEFKWDYVILDEGHKIKNSKTKSAKS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  612 LKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQ-FPSETAFLEEFGDLKTEEQVKK---------------LQSILKP 675
Cdd:cd18001   148 LREIPAKNRIILTGTPIQNNLKELWALFDFACNGSlLGTRKTFKMEFENPITRGRDKDatqgekalgsevaenLRQIIKP 227

                  ....*
gi 768018477  676 MMLRR 680
Cdd:cd18001   228 YFLRR 232
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
459-680 1.74e-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: 1.74e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLL-----FNWYNRKNCILADEMGLGKTIQSITFLSeIFLRgiHGPF--------LIIAPLSTITNWERE 525
Cdd:cd18004     1 LRPHQREGVQFLYdcltgRRGYGGGGAILADEMGLGKTLQAIALVW-TLLK--QGPYgkptakkaLIVCPSSLVGNWKAE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  526 FRTWTemnaivyhGSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHwSC--VIIDEAHRLKN 603
Cdd:cd18004    78 FDKWL--------GLRRIKVVTADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKKI-SIdlLICDEGHRLKN 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  604 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAF-------------------LEEFGDLKTEE 664
Cdd:cd18004   149 SESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFrkvfeepilrsrdpdaseeDKELGAERSQE 228
                         250
                  ....*....|....*.
gi 768018477  665 qvkkLQSILKPMMLRR 680
Cdd:cd18004   229 ----LSELTSRFILRR 240
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
459-680 4.68e-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: 4.68e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLF-NWYNRKNcILADEMGLGKTIQSITFL-SEIFLR-----GIHGPFLIIAPLSTITNWEREFRTWTE 531
Cdd:cd17999     1 LRPYQQEGINWLAFlNKYNLHG-ILCDDMGLGKTLQTLCILaSDHHKRansfnSENLPSLVVCPPTLVGHWVAEIKKYFP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  532 ---MNAIVYHGSQISRQMIQQyemvyrdaQGNplsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKL 608
Cdd:cd17999    80 nafLKPLAYVGPPQERRRLRE--------QGE------KHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  609 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG-------DLK-----TEEQVKKLQSILK-- 674
Cdd:cd17999   146 SKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLkpilasrDSKasakeQEAGALALEALHKqv 225

                  ....*..
gi 768018477  675 -PMMLRR 680
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, ...
370-428 1.01e-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: 130.49  E-value: 1.01e-35
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 768018477  370 PDYVEVDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAKVKEFESLQ 428
Cdd:cd18663     1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
459-644 3.51e-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: 3.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLfnWYNRKNC--ILADEMGLGKTIQSITflseiFLRGIH------GPFLIIAPLSTITNWEREFRTW- 529
Cdd:cd18000     1 LFKYQQTGVQWLW--ELHCQRVggILGDEMGLGKTIQIIA-----FLAALHhsklglGPSLIVCPATVLKQWVKEFHRWw 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  530 TEMNAIVYHGSQISRQMIQQYEMVYRDAQGNPlSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLL 609
Cdd:cd18000    74 PPFRVVVLHSSGSGTGSEEKLGSIERKSQLIR-KVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEIT 152
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 768018477  610 EGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEP 644
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 ...
459-657 8.08e-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: 8.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGmnwLLFNWYN----------RKNCILADEMGLGKTIQSITFLsEIFLRgiHGP----FLIIAPLSTITNWER 524
Cdd:cd18007     1 LKPHQVEG---VRFLWSNlvgtdvgsdeGGGCILAHTMGLGKTLQVITFL-HTYLA--AAPrrsrPLVLCPASTLYNWED 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  525 EFRTWTEMNAIVYHGsqisrqmiqqyeMVYRDAQGNP---LSGVFKFH----VVITTFEM--ILADCPELKK------IH 589
Cdd:cd18007    75 EFKKWLPPDLRPLLV------------LVSLSASKRAdarLRKINKWHkeggVLLIGYELfrNLASNATTDPrlkqefIA 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768018477  590 WSC------VIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF 657
Cdd:cd18007   143 ALLdpgpdlLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
DEXDc smart00487
DEAD-like helicases superfamily;
452-650 1.08e-31

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 124.14  E-value: 1.08e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477    452 EYKNSNQLREYQLEGMNWLLFNWynrKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTIT-NWEREFRTWT 530
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAeQWAEELKKLG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477    531 EMNAI----VYHGSQISRQMIQQYEmvyrdaqgnplsgvFKFHVVITTFEMILADCPE--LKKIHWSCVIIDEAHRLKN- 603
Cdd:smart00487   79 PSLGLkvvgLYGGDSKREQLRKLES--------------GKTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDg 144
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|..
gi 768018477    604 -RNCKLLEGLKLMALE-HKVLLTGTP---LQNSVEELFSLLNFLEPSQFPSE 650
Cdd:smart00487  145 gFGDQLEKLLKLLPKNvQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLE 196
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
459-653 9.26e-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: 9.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGmnwLLFNWY--------NRKNCILADEMGLGKTIQSITFLSEIFLRGIHGP------FLIIAPLSTITNWER 524
Cdd:cd18066     1 LRPHQREG---IEFLYEcvmgmrvnERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGkpvikrALIVTPGSLVKNWKK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  525 EFRTWtemnaivyhgsqISRQMIQQYeMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNR 604
Cdd:cd18066    78 EFQKW------------LGSERIKVF-TVDQDHKVEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNT 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 768018477  605 NCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAF 653
Cdd:cd18066   145 SIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTY 193
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
459-680 3.17e-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: 3.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLfnwynRKN--CILADEMGLGKTIQSITFLSeiFLRGiHGPFLIIAPLSTITNWEREFRTW----TEM 532
Cdd:cd18010     1 LLPFQREGVCFAL-----RRGgrVLIADEMGLGKTVQAIAIAA--YYRE-EWPLLIVCPSSLRLTWADEIERWlpslPPD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  533 NAIVYHGSQISRQMiqqyemvyRDAQgnplsgvfkfhVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRN---CKLL 609
Cdd:cd18010    73 DIQVIVKSKDGLRD--------GDAK-----------VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKakrTKAA 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  610 EGLkLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEE---------FGDLKTEEQVKKLQSIL-KPMMLR 679
Cdd:cd18010   134 LPL-LKRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRycaakqggfGWDYSGSSNLEELHLLLlATIMIR 212

                  .
gi 768018477  680 R 680
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, ...
286-351 5.53e-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: 105.88  E-value: 5.53e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768018477  286 EDDANIIEKILASKTVQ-EVHPGEPPFDLELFYVKYRNFSYLHCKWATMEELEK-DPRIAQKIKRFRN 351
Cdd:cd18668     1 EEDTMIIEKILASRKKKkEKEEGAEEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFKQ 68
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
477-680 2.57e-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: 2.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  477 RKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVyhgsqISRQMIQQYEmvyRD 556
Cdd:cd18011    17 PVRLLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQDKFGLPFLI-----LDRETAAQLR---RL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  557 AQGNPLSgvfkFHVVITTFEMI-----LADcpELKKIHWSCVIIDEAHRLKNRNCKLLEGL-KLMAL-----EHKVLLTG 625
Cdd:cd18011    89 IGNPFEE----FPIVIVSLDLLkrseeRRG--LLLSEEWDLVVVDEAHKLRNSGGGKETKRyKLGRLlakraRHVLLLTA 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768018477  626 TPLQNSVEELFSLLNFLEPSQFpsetAFLEEFGDLKTEEQVkklqsiLKPMMLRR 680
Cdd:cd18011   163 TPHNGKEEDFRALLSLLDPGRF----AVLGRFLRLDGLREV------LAKVLLRR 207
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
781-895 9.10e-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: 9.10e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477   781 GKLVLIDKLLPKliAGGHKVLIFSQMVRCLDilEDYLIQRR-YTYERIDGRVRGNLRQAAIDRFCKPDSDrfvFLLCTRA 859
Cdd:pfam00271    1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 768018477   860 GGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIG 895
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
481-680 1.80e-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: 1.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  481 ILADEMGLGKTIQSITFLseiflrgIHGPFLIIAPLSTITNWEREFRTWTE---MNAIVYHGSQisrqmiqqyemvyRDA 557
Cdd:cd18071    52 ILADDMGLGKTLTTISLI-------LANFTLIVCPLSVLSNWETQFEEHVKpgqLKVYTYHGGE-------------RNR 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  558 QGNPLSgvfKFHVVITTFEMI------LADCPeLKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNS 631
Cdd:cd18071   112 DPKLLS---KYDIVLTTYNTLasdfgaKGDSP-LHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNS 187
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 768018477  632 VEELFSLLNFLEPSQFPSETAFLEEFG---DLKTEEQVKKLQSILKPMMLRR 680
Cdd:cd18071   188 PKDLGSLLSFLHLKPFSNPEYWRRLIQrplTMGDPTGLKRLQVLMKQITLRR 239
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
459-680 2.59e-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: 2.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLFNWYNRKN-----CILADEMGLGKTIQSITFLSEIFLRGIHGPFLI-----IAPLSTITNWEREFRT 528
Cdd:cd18067     1 LRPHQREGVKFLYRCVTGRRIrgshgCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaivVSPSSLVKNWANELGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  529 WTEMNAIVYHGSQISRQMIQQYEMVYRDAQGNPLSGvfkfHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKL 608
Cdd:cd18067    81 WLGGRLQPLAIDGGSKKEIDRKLVQWASQQGRRVST----PVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  609 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF---------GD------LKTEEQVKKLQSIL 673
Cdd:cd18067   157 YQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFelpilkgrdADasekerQLGEEKLQELISIV 236

                  ....*..
gi 768018477  674 KPMMLRR 680
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 ...
481-929 5.00e-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: 107.85  E-value: 5.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  481 ILADEMGLGKTIQS---ITFLSEIFLRGIhgpfLIIAPLSTITNWEREFRTWTEMNAIVyhgsqISRQMIQQ-YEMVYRD 556
Cdd:NF038318   51 ILADEVGLGKTIEAglvLKYVLESGAKKI----LIILPANLRKQWEIELEEKFDLESLI-----LDSLTVEKdAKKWNKR 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  557 AQGNPlsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKN--RNCKLLEGL-KLMALEHKVLLTGTPLQNSVE 633
Cdd:NF038318  122 LTDNK-----KVRIVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRNvhKGGKRAKNLyELTKGIPKILLTATPLQNSLL 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  634 ELFSLLNFLEPSQFPSETAFL------EEFGDLKTEeqvkklqsiLKPMMLRRLKDDVEKNLAPKQETII---------E 698
Cdd:NF038318  197 DLYGLVSFIDPRIFGSEKVFSkryikdEDYSDLKRE---------LSPVLYRTLRKDVADYMQFKKRKCItvdfelspdE 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  699 VELTN-----IQKKYYRAILEKNFSFLT----KGANQHNMPnLINTMMELRKCCNHPY---LINGAEEKI------LEDF 760
Cdd:NF038318  268 IELYVrvnnfLKRDILYSIPTSNRTLIIlvirKLLASSSFA-LAETFEVLKKRLEKLKegtRSANAQEGFdlfwsfVEDE 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  761 RKTHSPDAPDFQL----QAMIQAAGKLV--LIDKL-----------LPKLIAGG----------HKVLIFSQMVRCLDIL 813
Cdd:NF038318  347 IDESGFEEKQDELytrqKEFIQHEIDEVdaIIDVAkriktnakvtaLKTALEIAfeyqreegiaQKVVVFTESKRTQKYI 426
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  814 EDYLIQRRYTYERI---DG--------------RVR--GN--------LRQAAIDRFckpdSDRFVFLLCTRAGGLGINL 866
Cdd:NF038318  427 AEELRKSGYEGEDIllfNGdfddamtkeiyrawQVKnyGKanygrsveYKHAIVDYF----KNNAKILIVTDAGSEGLNL 502
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768018477  867 TAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI-TRNSYEREMFDKASLKLGLDKAV 929
Cdd:NF038318  503 QFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYEILSEKFELFEGV 566
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
459-680 5.01e-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: 5.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLfnWYNRKNC---ILADEMGLGKTIQSITF------------------LSEIFLRGIHGPF-----LI 512
Cdd:cd18072     1 LLLHQKQALAWLL--WRERQKPrggILADDMGLGKTLTMIALilaqkntqnrkeeekekaLTEWESKKDSTLVpsagtLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  513 IAPLSTITNWEREFRTWTEMNAI---VYHGSQisrqmiqqyemvyRDAQGNPLSgvfKFHVVITTFEMILADCPELKK-- 587
Cdd:cd18072    79 VCPASLVHQWKNEVESRVASNKLrvcLYHGPN-------------RERIGEVLR---DYDIVITTYSLVAKEIPTYKEes 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  588 -------IHWSCVIIDEAHRLKNRNCKLLEGL-KLMALEHKVLlTGTPLQNSVEELFSLLNFLEPSQFpSETAFLEEFGD 659
Cdd:cd18072   143 rssplfrIAWARIILDEAHNIKNPKVQASIAVcKLRAHARWAL-TGTPIQNNLLDMYSLLKFLRCSPF-DDLKVWKKQVD 220
                         250       260
                  ....*....|....*....|.
gi 768018477  660 LKTEEQVKKLQSILKPMMLRR 680
Cdd:cd18072   221 NKSRKGGERLNILTKSLLLRR 241
HELICc smart00490
helicase superfamily c-terminal domain;
811-895 5.25e-21

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 89.19  E-value: 5.25e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477    811 DILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDrfvFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQAR 890
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 768018477    891 CHRIG 895
Cdd:smart00490   78 AGRAG 82
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
480-657 6.32e-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: 6.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  480 CILADEMGLGKTIQSITFLSEIFLRGIHGPF---LIIAPLSTITNWEREFRTWTEMNA---------------------I 535
Cdd:cd18068    31 CILAHCMGLGKTLQVVTFLHTVLLCEKLENFsrvLVVCPLNTVLNWLNEFEKWQEGLKdeekievnelatykrpqersyK 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  536 VYHGSQISRQMIQQYEMvYRD-AQGNPLSGVFKFHvviTTFEMILAD-CPELkkihwscVIIDEAHRLKNRNCKLLEGLK 613
Cdd:cd18068   111 LQRWQEEGGVMIIGYDM-YRIlAQERNVKSREKLK---EIFNKALVDpGPDF-------VVCDEGHILKNEASAVSKAMN 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 768018477  614 LMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF 657
Cdd:cd18068   180 SIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
480-657 1.31e-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: 1.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  480 CILADEMGLGKTIQSITFLsEIFLRGIHGP-FLIIAPLSTITNWEREFRTWteMNAIVYHGSQISRQM---IQQYEMVYR 555
Cdd:cd18069    31 CILAHSMGLGKTLQVISFL-DVLLRHTGAKtVLAIVPVNTLQNWLSEFNKW--LPPPEALPNVRPRPFkvfILNDEHKTT 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  556 DAQGNPLSG-VFKFHVVITTFEMI-LADCPELkkihwscVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVE 633
Cdd:cd18069   108 AARAKVIEDwVKDGGVLLMGYEMFrLRPGPDV-------VICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLI 180
                         170       180
                  ....*....|....*....|....
gi 768018477  634 ELFSLLNFLEPSQFPSETAFLEEF 657
Cdd:cd18069   181 EYWCMVDFVRPDFLGTRQEFSNMF 204
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
371-426 1.16e-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: 78.77  E-value: 1.16e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 768018477  371 DYVEVDRIleVAHTKDAETGEEvthYLVKWCSLPYEESTWELEEDV---DPAKVKEFES 426
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 ...
459-646 6.17e-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: 6.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLfnwYNRKNCILADeMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITN-WEREFRTWTEMNAIVY 537
Cdd:cd18013     1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARStWPDEVEKWNHLRNLTV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  538 H---GSQisRQMIqqyemvyRDAQGNPlsgvfkfHVVITTFEMiLADCPELKKIHW--SCVIIDEAHRLKNRNCKllEGL 612
Cdd:cd18013    77 SvavGTE--RQRS-------KAANTPA-------DLYVINREN-LKWLVNKSGDPWpfDMVVIDELSSFKSPRSK--RFK 137
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 768018477  613 KLMALEHKV----LLTGTPLQNSVEELFSLLNFLEPSQ 646
Cdd:cd18013   138 ALRKVRPVIkrliGLTGTPSPNGLMDLWAQIALLDQGE 175
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
288-351 3.87e-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: 3.87e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768018477  288 DANIIEKILASKTVQEVHPG-------EPPFDLELFYVKYRNFSYLHCKWATMEELEKDpRIAQKIKRFRN 351
Cdd:cd18660     1 DEDKIEKILDHRPKGPVEEAsldltdpDEPWDEREFLVKWKGKSYLHCTWVTEETLEQL-RGKKKLKNYIK 70
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
401-1049 3.78e-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: 3.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  401 CSLPYEESTWELEEDVDPAKVKEFESLQVLPEIKHVERPASDSWQKLEKS------REYKNSNQLREYQLEGMN-WLLFN 473
Cdd:COG1061    17 SLLLLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEaleagdEASGTSFELRPYQQEALEaLLAAL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  474 WYNRKNCILADEMGLGKTIQSITFLSEIFLRGihgPFLIIAPLSTITN-WEREFRTWTemNAIVYHGSQISRQmiqqyem 552
Cdd:COG1061    97 ERGGGRGLVVAPTGTGKTVLALALAAELLRGK---RVLVLVPRRELLEqWAEELRRFL--GDPLAGGGKKDSD------- 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  553 vyrdaqgnplsgvfkFHVVITTFEmILADCPELKKI--HWSCVIIDEAHRLKNRncKLLEGLKLMALEHKVLLTGTPlqn 630
Cdd:COG1061   165 ---------------APITVATYQ-SLARRAHLDELgdRFGLVIIDEAHHAGAP--SYRRILEAFPAAYRLGLTATP--- 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  631 sveelfsllnflepsqfpsetafleEFGDLKTEEqVKKLQSILKPMMLRRLKDDveKNLAPKQETIIEVELTNIQKKY-- 708
Cdd:COG1061   224 -------------------------FRSDGREIL-LFLFDGIVYEYSLKEAIED--GYLAPPEYYGIRVDLTDERAEYda 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  709 YRAILEKNfsfltkganqhnmpnlintmmelrkccnhpyLINGAEEK--ILEDFRKTHspdapdfqlqamiqaagklvli 786
Cdd:COG1061   276 LSERLREA-------------------------------LAADAERKdkILRELLREH---------------------- 302
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  787 dkllpkliAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFckpDSDRFVFLLCTRAGGLGINL 866
Cdd:COG1061   303 --------PDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAF---RDGELRILVTVDVLNEGVDV 371
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  867 TAADTCIIFDSDWNPQNDLQAQARCHRIGQSK-AVKVYRLITRNSYEREMFDKASLKLGLDKAVLQDINRKGGTNgVQQL 945
Cdd:COG1061   372 PRLDVAILLRPTGSPREFIQRLGRGLRPAPGKeDALVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELA-LLIA 450
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  946 SKMEVEDLLRKGAYGALMDEEDEGSKFCEEDIDQILQRRTHTITIQSEGKGSTFAKASFVASGNRTDISLDDPNFWQKWA 1025
Cdd:COG1061   451 VKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLL 530
                         650       660
                  ....*....|....*....|....
gi 768018477 1026 KIAELDTEAKNEKESLVIDRPRVR 1049
Cdd:COG1061   531 LLLLLLELLELLAALLRLEELAAL 554
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
459-647 4.46e-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: 4.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGMNWLLfnwyNRKNcILADEMGLGKTIQSI----------------TFLSEIFLRGIH----------GPFLI 512
Cdd:cd18070     1 LLPYQRRAVNWML----VPGG-ILADEMGLGKTVEVLalillhprpdndldaaDDDSDEMVCCPDclvaetpvssKATLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  513 IAPLSTITNWEREFRTWTEMNAIVYHgsqisrqmiqqYEMVYRD--AQGNPLSGVFKFHVVITTFEmILAD--------- 581
Cdd:cd18070    76 VCPSAILAQWLDEINRHVPSSLKVLT-----------YQGVKKDgaLASPAPEILAEYDIVVTTYD-VLRTelhyaeanr 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  582 ---------------CPeLKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQ 646
Cdd:cd18070   144 snrrrrrqkryeappSP-LVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEP 222

                  .
gi 768018477  647 F 647
Cdd:cd18070   223 F 223
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
374-426 6.66e-10

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 56.82  E-value: 6.66e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 768018477   374 EVDRIleVAHTKDAETGEEvthYLVKWCSLPYEESTWELEEDVD--PAKVKEFES 426
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 ...
370-415 5.50e-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: 5.50e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 768018477  370 PDYVEVDRILEvaHTKDAETGeevTHYLVKWCSLPYEESTWELEED 415
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 ...
478-626 7.10e-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: 7.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  478 KNCILADEMGLGKTIQ-SITFLSEIFLRGihGPFLIIAPLSTITN-WEREFRTWTEMNA--IVYHGsqiSRQMIQQYEMV 553
Cdd:cd00046     2 ENVLITAPTGSGKTLAaLLAALLLLLKKG--KKVLVLVPTKALALqTAERLRELFGPGIrvAVLVG---GSSAEEREKNK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  554 YRDAqgnplsgvfkfHVVITTFEMILADCPELKKIH---WSCVIIDEAHRL----KNRNCKLLEGLKLMALEHK-VLLTG 625
Cdd:cd00046    77 LGDA-----------DIIIATPDMLLNLLLREDRLFlkdLKLIIVDEAHALlidsRGALILDLAVRKAGLKNAQvILLSA 145

                  .
gi 768018477  626 T 626
Cdd:cd00046   146 T 146
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
374-426 1.97e-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: 1.97e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768018477  374 EVDRILevahtkDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAK--VKEFES 426
Cdd:cd00024     2 EVEKIL------DHRVRKGKLEYLVKWKGYPPEENTWEPEENLTNAPelIKEYEK 50
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
291-352 3.84e-06

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 46.03  E-value: 3.84e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768018477   291 IIEKILASKTVQEvhpgeppfDLELFYVKYRNFSYLHCKWATMEELEKDPRIaqkIKRFRNK 352
Cdd:pfam00385    2 EVERILDHRKDKG--------GKEEYLVKWKGYPYDENTWEPEENLSKCPEL---IEEFKDR 52
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
459-627 5.96e-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: 5.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  459 LREYQLEGM-NWLLFNWYNRKNCILAdeMGLGKTIqsiTFLSEIFLRGIHgPFLIIAP-LSTITNWEREFRTWTemnaiv 536
Cdd:cd17926     1 LRPYQEEALeAWLAHKNNRRGILVLP--TGSGKTL---TALALIAYLKEL-RTLIVVPtDALLDQWKERFEDFL------ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  537 yHGSQISRQmiqqyemvyrdaQGNPLSGVFKFHVVITTFEMILADCPELKKI--HWSCVIIDEAHRLknrNCKLLEGLKL 614
Cdd:cd17926    69 -GDSSIGLI------------GGGKKKDFDDANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAHHL---PAKTFSEILK 132
                         170
                  ....*....|....
gi 768018477  615 MALEHKVL-LTGTP 627
Cdd:cd17926   133 ELNAKYRLgLTATP 146
CD2_tandem_ScCHD1_like cd18664
repeat 2 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
371-426 6.76e-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: 45.73  E-value: 6.76e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768018477  371 DYVEVDRILEvahTKDAETGEEVTH--YLVKWCSLPYEESTWELEEDV---DPAKVKEFES 426
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 ...
372-426 2.34e-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: 44.21  E-value: 2.34e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 768018477  372 YVEVDRIleVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVD---PAKVKEFES 426
Cdd:cd18661     2 YQIVERI--IAHSPQKSAASGYPDYLCKWQGLPYSECTWEDGALISkkfQACIDEYHS 57
CHROMO smart00298
Chromatin organization modifier domain;
374-425 2.46e-05

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 43.74  E-value: 2.46e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 768018477    374 EVDRILevAHTKDAETGEEvthYLVKWCSLPYEESTWELEEDV--DPAKVKEFE 425
Cdd:smart00298    3 EVEKIL--DHRWKKKGELE---YLVKWKGYSYSEDTWEPEENLlnCSKKLDNYK 51
BRK smart00592
domain in transcription and CHROMO domain helicases;
2400-2435 3.94e-05

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 43.11  E-value: 3.94e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 768018477   2400 SGEERVPAIPKEPGLRG----FLPENKFNHTLAEPILRDT 2435
Cdd:smart00592    1 DGEERVPVINRETGKKLtgddAPKAKDLERWLEENPEYEV 40
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
374-418 1.04e-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: 1.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 768018477  374 EVDRILevahtkdAETGEE-VTHYLVKWCSLPYEESTWELEEDVDP 418
Cdd:cd18966     2 EVERIL-------AERRDDgGKRYLVKWEGYPLEEATWEPEENIGD 40
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
460-635 1.15e-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: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477   460 REYQLEGMNWLLfnwyNRKNCILADEMGLGKT-IQSITFLSEIFLRGIHGPFLIIAPLSTITN-WEREFRTWTEMNAI-- 535
Cdd:pfam00270    1 TPIQAEAIPAIL----EGRDVLVQAPTGSGKTlAFLLPALEALDKLDNGPQALVLAPTRELAEqIYEELKKLGKGLGLkv 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477   536 --VYHGSQISRQMiqqyemvyrdaqgNPLSGVfkfHVVITTFEMILADCPE---LKKIhwSCVIIDEAHRL--KNRNCKL 608
Cdd:pfam00270   77 asLLGGDSRKEQL-------------EKLKGP---DILVGTPGRLLDLLQErklLKNL--KLLVLDEAHRLldMGFGPDL 138
                          170       180
                   ....*....|....*....|....*...
gi 768018477   609 LEGLKLMALEHK-VLLTGTPLQNsVEEL 635
Cdd:pfam00270  139 EEILRRLPKKRQiLLLSATLPRN-LEDL 165
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
848-900 7.16e-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: 7.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768018477  848 SDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAV 900
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 ...
277-337 8.21e-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: 8.21e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768018477  277 LAWQAEEPPEDDAnIIEKILASKTVQEVHPGEPPFDLELFyVKYRNFSYLHCKWATMEELE 337
Cdd:cd18667     9 LTWRWAEPPYPEP-LPEKPDEDPYPPPPRKLQPRPEREFF-VKWHGMSYWHCEWVSELQLE 67
CD_POL_like cd18974
chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the ...
380-420 1.24e-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: 1.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 768018477  380 EVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAK 420
Cdd:cd18974     2 EVEEIVDEKMIDDELHYLVKWKGWPAEYNQWEPEDDMENAP 42
CD_MarY1_POL_like cd18975
chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes ...
396-424 1.39e-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: 1.39e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 768018477  396 YLVKWCSLPYEESTWELEEDVDPAK-VKEF 424
Cdd:cd18975    18 YLIQWKGYPLEEASWELEDNIKNPRlIEEF 47
chromodomain cd18965
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
394-416 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 768018477  394 THYLVKWCSLPYEESTWELEEDV 416
Cdd:cd18965    16 LEYLVKWHGLPESENTWEREKDI 38
PHA03247 PHA03247
large tegument protein UL36; Provisional
2317-2691 1.74e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477 2317 PGQATLSTTHPEGPGPATSAPEPATAASSQAEKSIPSKSLLDWLRQQADYS-------LEVPGFGANFSDKPKQRRPRCK 2389
Cdd:PHA03247 2609 RGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGrvsrprrARRLGRAAQASSPPQRPRRRAA 2688
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477 2390 EPGkldVSSLSGEERVPAIPKEPGLRgflpenkfnhtlAEPILRDTGPRRRGRRPRSELLKAPSIVADSPSGMGPLfmng 2469
Cdd:PHA03247 2689 RPT---VGSLTSLADPPPPPPTPEPA------------PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA---- 2749
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477 2470 LIAGMDLVGLQNMRNMPGIPLTglvgfPAGFATMPTGEEVKSTLSMLPMMLPGMAAVPQMFGVGGLLSPPMATTCTSTAP 2549
Cdd:PHA03247 2750 TPGGPARPARPPTTAGPPAPAP-----PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477 2550 ASLSSTTKSGTAVTEKTAEDKPSSHDVKTDTLAedkPGpGPFSDQSEPAITTSSPVAfnPFLIPGVSpgLIYPSMFLSPg 2629
Cdd:PHA03247 2825 AGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA---PG-GDVRRRPPSRSPAAKPAA--PARPPVRR--LARPAVSRST- 2895
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768018477 2630 MGMALPAMQQARHSEivglesqkrkkkktkgdnPNSHPEPAPSCEREPSGDENCAEPSAPLP 2691
Cdd:PHA03247 2896 ESFALPPDQPERPPQ------------------PQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939
chromodomain cd18968
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
374-424 1.90e-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: 1.90e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768018477  374 EVDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAK--VKEF 424
Cdd:cd18968     3 EVEVILAARVVKDAESRKKGWKYLVKWAGYPDEENTWEPEESFDGCDdlLERF 55
CHROMO smart00298
Chromatin organization modifier domain;
292-354 2.43e-03

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 38.35  E-value: 2.43e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768018477    292 IEKILASKTVQEvhpGEppfdlELFYVKYRNFSYLHCKWATMEELEKDPRiaqKIKRFRNKQA 354
Cdd:smart00298    4 VEKILDHRWKKK---GE-----LEYLVKWKGYSYSEDTWEPEENLLNCSK---KLDNYKKKER 55
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
102-371 7.49e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 41.98  E-value: 7.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  102 QEGAAKGSKDrepkPKRKREPKEPKEPRKAKEPKKAKEHKEPKQKDGAKKARKPREASGTKEAKEKRSctDSAARTKSRK 181
Cdd:PTZ00449  533 EHEDSKESDE----PKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPEEPKK--PKRPRSAQRP 606
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  182 ASKEQGPTPVEKKKKGKRKSETTVESLELDQGLTNPSlrSPE--ESTESTDSQKRRSGRQV------KRRKYNEDLDFKV 253
Cdd:PTZ00449  607 TRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPS--SPErpEGPKIIKSPKPPKSPKPpfdpkfKEKFYDDYLDAAA 684
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768018477  254 VDDDGETIAVLGAGRTSALSaSTLAWQAEEPPEDDANIIEKILASKTVQEVHPGEP----PFDLELFYVKYRNFSYLHCK 329
Cdd:PTZ00449  685 KSKETKTTVVLDESFESILK-ETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPdaeqPDDIEFFTPPEEERTFFHET 763
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 768018477  330 WAT------MEELEKDPRIAQKIKrfrnkqaqmkhiftEPDEDLFNPD 371
Cdd:PTZ00449  764 PADtplpdiLAEEFKEEDIHAETG--------------EPDEAMKRPD 797
CD_CMT3_like cd18635
chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier ...
374-424 7.65e-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: 7.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768018477  374 EVDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVD--PAKVKEF 424
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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