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Conserved domains on  [gi|19421557|gb|AAK56405|]
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chromodomain helicase DNA binding protein 5 [Homo sapiens]

Protein Classification

chromo domain-containing DEAD/DEAH box helicase( domain architecture ID 13312860)

chromo (chromatin organization modifier) domain-containing DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; similar to chromodomain helicase DNA-binding (CHD) family of ATP-dependent chromatin remodelers

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 6.50e-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: 6.50e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 538
Cdd:cd18058    1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  539 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALE 618
Cdd:cd18058   81 GSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALE 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19421557  619 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 680
Cdd:cd18058  161 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
458-983 5.66e-153

Probable chromatin-remodeling complex ATPase chain; Provisional


The actual alignment was detected with superfamily member PLN03142:

Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 505.10  E-value: 5.66e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   458 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LRGIHGPFLIIAPLSTITNWEREFRTWTEM-NAI 535
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHeYRGITGPHMVVAPKSTLGNWMNEIRRFCPVlRAV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   536 VYHGSQISRQMIQQYEMVyrdaqgnplSGvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLM 615
Cdd:PLN03142  249 KFHGNPEERAHQREELLV---------AG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLF 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   616 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF---GDLKTEEQVKKLQSILKPMMLRRLKDDVEKNLAPK 692
Cdd:PLN03142  318 STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPK 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   693 QETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNmpnLINTMMELRKCCNHPYLINGAEekiledfrkthsPDAPDFQ 772
Cdd:PLN03142  398 KETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAE------------PGPPYTT 462
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   773 LQAMIQAAGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDRFV 852
Cdd:PLN03142  463 GEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFV 542
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   853 FLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQD 932
Cdd:PLN03142  543 FLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ 622
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 19421557   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 1.14e-35

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


:

Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 130.10  E-value: 1.14e-35
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 19421557  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 8.65e-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: 105.11  E-value: 8.65e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19421557  286 EDDANIIEKILASKTVQ-EVHPGEPPFDLELFYVKYRNFSYLHCKWATMEELEK-DPRIAQKIKRFRN 351
Cdd:cd18668    1 EEDTMIIEKILASRKKKkEKEEGAEEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFKQ 68
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
102-371 1.81e-06

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: 53.93  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   102 QEGAAKGSKDrepkPKRKREPKEPKEPRKAEEPKKAKEHKEPKQKDGAKKARKPREASGTKEAKEKRSctDSAARTKSRK 181
Cdd:PTZ00449  533 EHEDSKESDE----PKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPEEPKK--PKRPRSAQRP 606
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   182 ASKEQGPTPVEKKKKGKRKSETTVESLELDQGLTNPSlrSPE--ESTESTDSQKRRSGRQV------KRRKYNEDLDFKV 253
Cdd:PTZ00449  607 TRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPS--SPErpEGPKIIKSPKPPKSPKPpfdpkfKEKFYDDYLDAAA 684
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   254 VDDDGETIAVLGAGRTSALSaSTLAWQAEEPPEDDANIIEKILASKTVQEVHPGEP----PFDLELFYVKYRNFSYLHCK 329
Cdd:PTZ00449  685 KSKETKTTVVLDESFESILK-ETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPdaeqPDDIEFFTPPEEERTFFHET 763
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 19421557   330 WAT------MEELEKDPRIAQKIKrfrnkqaqmkhiftEPDEDLFNPD 371
Cdd:PTZ00449  764 PADtplpdiLAEEFKEEDIHAETG--------------EPDEAMKRPD 797
BRK super family cl02688
BRK domain; The function of this domain is unknown. It is often found associated with ...
2400-2435 4.14e-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: 4.14e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 19421557    2400 SGEERVPAIPKEPGLRG----FLPENKFNHTLAEPILRDT 2435
Cdd:smart00592    1 DGEERVPVINRETGKKLtgddAPKAKDLERWLEENPEYEV 40
PHA03247 super family cl33720
large tegument protein UL36; Provisional
2317-2691 2.03e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  2317 PGQATLSTTHPEGPGPATSAPEPATAASSQAEKSIPSKSLLDWLRQQADYS-------LEVPGFGANFSDKPKQRRPRCK 2389
Cdd:PHA03247 2609 RGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGrvsrprrARRLGRAAQASSPPQRPRRRAA 2688
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  2390 EPGkldVSSLSGEERVPAIPKEPGLRgflpenkfnhtlAEPILRDTGPRRRGRRPRSELLKAPSIVADSPSGMGPLfmng 2469
Cdd:PHA03247 2689 RPT---VGSLTSLADPPPPPPTPEPA------------PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA---- 2749
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  2470 LIAGMDLVGLQNMRNMPGIPLTglvgfPAGFATMPTGEEVKSTLSMLPMMLPGMAAVPQMFGVGGLLSPPMATTCTSTAP 2549
Cdd:PHA03247 2750 TPGGPARPARPPTTAGPPAPAP-----PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  2550 ASLSSTTKSGTAVTEKTAEDKPSSHDVKTDTLAedkPGpGPFSDQSEPAITTSSPVAfnPFLIPGVSpgLIYPSMFLSPg 2629
Cdd:PHA03247 2825 AGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA---PG-GDVRRRPPSRSPAAKPAA--PARPPVRR--LARPAVSRST- 2895
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19421557  2630 MGMALPAMQQARHSEivglesqkrkkkktkggnPNSHPEPAPSCEREPSGDENCAEPSAPLP 2691
Cdd:PHA03247 2896 ESFALPPDQPERPPQ------------------PQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939
 
Name Accession Description Interval E-value
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
459-680 6.50e-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: 6.50e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 538
Cdd:cd18058    1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  539 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALE 618
Cdd:cd18058   81 GSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALE 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19421557  619 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 680
Cdd:cd18058  161 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
458-983 5.66e-153

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 505.10  E-value: 5.66e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   458 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LRGIHGPFLIIAPLSTITNWEREFRTWTEM-NAI 535
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHeYRGITGPHMVVAPKSTLGNWMNEIRRFCPVlRAV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   536 VYHGSQISRQMIQQYEMVyrdaqgnplSGvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLM 615
Cdd:PLN03142  249 KFHGNPEERAHQREELLV---------AG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLF 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   616 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF---GDLKTEEQVKKLQSILKPMMLRRLKDDVEKNLAPK 692
Cdd:PLN03142  318 STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPK 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   693 QETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNmpnLINTMMELRKCCNHPYLINGAEekiledfrkthsPDAPDFQ 772
Cdd:PLN03142  398 KETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAE------------PGPPYTT 462
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   773 LQAMIQAAGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDRFV 852
Cdd:PLN03142  463 GEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFV 542
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   853 FLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQD 932
Cdd:PLN03142  543 FLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ 622
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 19421557   933 inrkggtNGVQQLSKMEVEDLLRKGAYGALMDEEDEGSKFCEEDIDQILQR 983
Cdd:PLN03142  623 -------GRLAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAK 666
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
458-931 3.63e-129

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 423.48  E-value: 3.63e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  458 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 536
Cdd:COG0553  241 TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFApGLRVLV 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  537 YHGSQisrqmiqqyemvYRDAQGNPLSgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMA 616
Cdd:COG0553  321 LDGTR------------ERAKGANPFE---DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  617 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKT---EEQVKKLQSILKPMMLRRLKDDVEKNLAPKQ 693
Cdd:COG0553  386 ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEkgdEEALERLRRLLRPFLLRRTKEDVLKDLPEKT 465
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  694 ETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNMPNLINTMMELRKCCNHPYLingaeekILEDFRKTHSPDapdfql 773
Cdd:COG0553  466 EETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLILAALTRLRQICSHPAL-------LLEEGAELSGRS------ 532
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  774 qamiqaaGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFcKPDSDRFVF 853
Cdd:COG0553  533 -------AKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRF-QEGPEAPVF 604
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19421557  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 19421557    462 YQLEGMNWLLFNWYNRK-NCILADEMGLGKTIQSITFLSeiFLRGIH----GPFLIIAPLSTITNWEREFRTWT---EMN 533
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLL--YLKHVDknwgGPTLIVVPLSLLHNWMNEFERWVsppALR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557    534 AIVYHGSQISRQMIQQYEMVYRDaqgnplsgvfkFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLK 613
Cdd:pfam00176   79 VVVLHGNKRPQERWKNDPNFLAD-----------FDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557    614 LMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----DLKTEEQVKKLQSILKPMMLRRLKDDVEKNL 689
Cdd:pfam00176  148 SLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpieRGGGKKGVSRLHKLLKPFLLRRTKKDVEKSL 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19421557    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 19421557  781 GKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFcKPDSDRFVFLLCTRAG 860
Cdd:cd18793   11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRF-NEDPDIRVFLLSTKAG 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 19421557  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 1.14e-35

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


Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 130.10  E-value: 1.14e-35
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 19421557  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 19421557     452 EYKNSNQLREYQLEGMNWLLFNWynrKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTIT-NWEREFRTWT 530
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAeQWAEELKKLG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557     531 EMNAI----VYHGSQISRQMIQQYEmvyrdaqgnplsgvFKFHVVITTFEMILADCPE--LKKIHWSCVIIDEAHRLKN- 603
Cdd:smart00487   79 PSLGLkvvgLYGGDSKREQLRKLES--------------GKTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDg 144
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|..
gi 19421557     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 8.65e-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: 105.11  E-value: 8.65e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19421557  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 19421557    781 GKLVLIDKLLPKliAGGHKVLIFSQMVRCLDilEDYLIQRR-YTYERIDGRVRGNLRQAAIDRFCKPDSDrfvFLLCTRA 859
Cdd:pfam00271    1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 19421557    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 6.85e-23

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


Pssm-ID: 468472 [Multi-domain]  Cd Length: 868  Bit Score: 107.46  E-value: 6.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   481 ILADEMGLGKTIQS---ITFLSEIFLRGIhgpfLIIAPLSTITNWEREFRTWTEMNAIVyhgsqISRQMIQQ-YEMVYRD 556
Cdd:NF038318   51 ILADEVGLGKTIEAglvLKYVLESGAKKI----LIILPANLRKQWEIELEEKFDLESLI-----LDSLTVEKdAKKWNKR 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   557 AQGNPlsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKN--RNCKLLEGL-KLMALEHKVLLTGTPLQNSVE 633
Cdd:NF038318  122 LTDNK-----KVRIVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRNvhKGGKRAKNLyELTKGIPKILLTATPLQNSLL 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   634 ELFSLLNFLEPSQFPSETAFL------EEFGDLKTEeqvkklqsiLKPMMLRRLKDDVEKNLAPKQETII---------E 698
Cdd:NF038318  197 DLYGLVSFIDPRIFGSEKVFSkryikdEDYSDLKRE---------LSPVLYRTLRKDVADYMQFKKRKCItvdfelspdE 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   699 VELTN-----IQKKYYRAILEKNFSFLT----KGANQHNMPnLINTMMELRKCCNHPY---LINGAEEKI------LEDF 760
Cdd:NF038318  268 IELYVrvnnfLKRDILYSIPTSNRTLIIlvirKLLASSSFA-LAETFEVLKKRLEKLKegtRSANAQEGFdlfwsfVEDE 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   761 RKTHSPDAPDFQL----QAMIQAAGKLV--LIDKL-----------LPKLIAGG----------HKVLIFSQMVRCLDIL 813
Cdd:NF038318  347 IDESGFEEKQDELytrqKEFIQHEIDEVdaIIDVAkriktnakvtaLKTALEIAfeyqreegiaQKVVVFTESKRTQKYI 426
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   814 EDYLIQRRYTYERI---DG--------------RVR--GN--------LRQAAIDRFckpdSDRFVFLLCTRAGGLGINL 866
Cdd:NF038318  427 AEELRKSGYEGEDIllfNGdfddamtkeiyrawQVKnyGKanygrsveYKHAIVDYF----KNNAKILIVTDAGSEGLNL 502
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19421557   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 19421557     811 DILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDrfvFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQAR 890
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 19421557     891 CHRIG 895
Cdd:smart00490   78 AGRAG 82
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
374-426 8.26e-10

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 56.43  E-value: 8.26e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 19421557    374 EVDRIleVAHTKDAETGEEvthYLVKWCSLPYEESTWELEEDVD--PAKVKEFES 426
Cdd:pfam00385    2 EVERI--LDHRKDKGGKEE---YLVKWKGYPYDENTWEPEENLSkcPELIEEFKD 51
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
102-371 1.81e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 53.93  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   102 QEGAAKGSKDrepkPKRKREPKEPKEPRKAEEPKKAKEHKEPKQKDGAKKARKPREASGTKEAKEKRSctDSAARTKSRK 181
Cdd:PTZ00449  533 EHEDSKESDE----PKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPEEPKK--PKRPRSAQRP 606
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   182 ASKEQGPTPVEKKKKGKRKSETTVESLELDQGLTNPSlrSPE--ESTESTDSQKRRSGRQV------KRRKYNEDLDFKV 253
Cdd:PTZ00449  607 TRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPS--SPErpEGPKIIKSPKPPKSPKPpfdpkfKEKFYDDYLDAAA 684
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   254 VDDDGETIAVLGAGRTSALSaSTLAWQAEEPPEDDANIIEKILASKTVQEVHPGEP----PFDLELFYVKYRNFSYLHCK 329
Cdd:PTZ00449  685 KSKETKTTVVLDESFESILK-ETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPdaeqPDDIEFFTPPEEERTFFHET 763
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 19421557   330 WAT------MEELEKDPRIAQKIKrfrnkqaqmkhiftEPDEDLFNPD 371
Cdd:PTZ00449  764 PADtplpdiLAEEFKEEDIHAETG--------------EPDEAMKRPD 797
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
291-352 4.41e-06

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 46.03  E-value: 4.41e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19421557    291 IIEKILASKTVQEvhpgeppfDLELFYVKYRNFSYLHCKWATMEELEKDPRIaqkIKRFRNK 352
Cdd:pfam00385    2 EVERILDHRKDKG--------GKEEYLVKWKGYPYDENTWEPEENLSKCPEL---IEEFKDR 52
CHROMO smart00298
Chromatin organization modifier domain;
374-425 2.80e-05

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 43.74  E-value: 2.80e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 19421557     374 EVDRILevAHTKDAETGEEvthYLVKWCSLPYEESTWELEEDV--DPAKVKEFE 425
Cdd:smart00298    3 EVEKIL--DHRWKKKGELE---YLVKWKGYSYSEDTWEPEENLlnCSKKLDNYK 51
BRK smart00592
domain in transcription and CHROMO domain helicases;
2400-2435 4.14e-05

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 43.11  E-value: 4.14e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 19421557    2400 SGEERVPAIPKEPGLRG----FLPENKFNHTLAEPILRDT 2435
Cdd:smart00592    1 DGEERVPVINRETGKKLtgddAPKAKDLERWLEENPEYEV 40
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
103-186 8.57e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 47.53  E-value: 8.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557    103 EGAAKGSKDREPKPKRKREPKEPKEP-RKAEEPKKAKEHKEPKQKDGAKKARKPREASGTKEAKEKRSCTDSAARTKSRK 181
Cdd:TIGR02794  123 EAKAKQAAEAKAKAEAEAERKAKEEAaKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAK 202

                   ....*
gi 19421557    182 ASKEQ 186
Cdd:TIGR02794  203 AKAAA 207
PHA03247 PHA03247
large tegument protein UL36; Provisional
2317-2691 2.03e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  2317 PGQATLSTTHPEGPGPATSAPEPATAASSQAEKSIPSKSLLDWLRQQADYS-------LEVPGFGANFSDKPKQRRPRCK 2389
Cdd:PHA03247 2609 RGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGrvsrprrARRLGRAAQASSPPQRPRRRAA 2688
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  2390 EPGkldVSSLSGEERVPAIPKEPGLRgflpenkfnhtlAEPILRDTGPRRRGRRPRSELLKAPSIVADSPSGMGPLfmng 2469
Cdd:PHA03247 2689 RPT---VGSLTSLADPPPPPPTPEPA------------PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA---- 2749
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  2470 LIAGMDLVGLQNMRNMPGIPLTglvgfPAGFATMPTGEEVKSTLSMLPMMLPGMAAVPQMFGVGGLLSPPMATTCTSTAP 2549
Cdd:PHA03247 2750 TPGGPARPARPPTTAGPPAPAP-----PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  2550 ASLSSTTKSGTAVTEKTAEDKPSSHDVKTDTLAedkPGpGPFSDQSEPAITTSSPVAfnPFLIPGVSpgLIYPSMFLSPg 2629
Cdd:PHA03247 2825 AGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA---PG-GDVRRRPPSRSPAAKPAA--PARPPVRR--LARPAVSRST- 2895
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19421557  2630 MGMALPAMQQARHSEivglesqkrkkkktkggnPNSHPEPAPSCEREPSGDENCAEPSAPLP 2691
Cdd:PHA03247 2896 ESFALPPDQPERPPQ------------------PQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
115-289 2.44e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 43.10  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  115 KPKRKREPKEPKEPRKAEEPKKAKEHKEPKQKDGAKKARKPREASGTKEAKEKRSCTDSAARTKSRKASKEQGPTPVEKK 194
Cdd:COG3064   88 EAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAA 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  195 KKGKRKSETTVESLELDQGLTNPSLRSPEESTESTDSQKRRSGRQVKRRKYNEDLDFKVVDDDGETIAVLGAGRTSALSA 274
Cdd:COG3064  168 AAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGG 247
                        170
                 ....*....|....*
gi 19421557  275 STLAWQAEEPPEDDA 289
Cdd:COG3064  248 AEEAADLAAVGVLGA 262
CHROMO smart00298
Chromatin organization modifier domain;
292-354 2.66e-03

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 37.96  E-value: 2.66e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19421557     292 IEKILASKTVQEvhpGEppfdlELFYVKYRNFSYLHCKWATMEELEKDPRiaqKIKRFRNKQA 354
Cdd:smart00298    4 VEKILDHRWKKK---GE-----LEYLVKWKGYSYSEDTWEPEENLLNCSK---KLDNYKKKER 55
RNA_polI_A34 pfam08208
DNA-directed RNA polymerase I subunit RPA34.5; This is a family of proteins conserved from ...
109-185 3.86e-03

DNA-directed RNA polymerase I subunit RPA34.5; This is a family of proteins conserved from yeasts to human. Subunit A34.5 of RNA polymerase I is a non-essential subunit which is thought to help Pol I overcome topological constraints imposed on ribosomal DNA during the process of transcription.


Pssm-ID: 462395  Cd Length: 205  Bit Score: 41.21  E-value: 3.86e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19421557    109 SKDREPKPKRKREPKEPKEPRKAEEPKKAKE--HKEPKQKDGAKKARKPREASGTKEAKEKRSctdsaarTKSRKASKE 185
Cdd:pfam08208  134 SEESEGEEEKRKVPAAKKKSKKKKKKKAETEeeEEVPKKKKKKKKKKKEKKEPEKKEKKEKKS-------KKSKKEKKK 205
 
Name Accession Description Interval E-value
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
459-680 6.50e-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: 6.50e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 538
Cdd:cd18058    1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  539 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALE 618
Cdd:cd18058   81 GSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALE 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19421557  619 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 680
Cdd:cd18058  161 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
458-983 5.66e-153

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 505.10  E-value: 5.66e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   458 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LRGIHGPFLIIAPLSTITNWEREFRTWTEM-NAI 535
Cdd:PLN03142  169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHeYRGITGPHMVVAPKSTLGNWMNEIRRFCPVlRAV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   536 VYHGSQISRQMIQQYEMVyrdaqgnplSGvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLM 615
Cdd:PLN03142  249 KFHGNPEERAHQREELLV---------AG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLF 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   616 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF---GDLKTEEQVKKLQSILKPMMLRRLKDDVEKNLAPK 692
Cdd:PLN03142  318 STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPK 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   693 QETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNmpnLINTMMELRKCCNHPYLINGAEekiledfrkthsPDAPDFQ 772
Cdd:PLN03142  398 KETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAE------------PGPPYTT 462
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   773 LQAMIQAAGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDRFV 852
Cdd:PLN03142  463 GEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFV 542
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   853 FLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQD 932
Cdd:PLN03142  543 FLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ 622
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 19421557   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 1.18e-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: 1.18e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLR-GIHGPFLIIAPLSTITNWEREFRTWTEMNAIVY 537
Cdd:cd17995    1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVeGIRGPFLVIAPLSTIPNWQREFETWTDMNVVVY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  538 HGSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMAL 617
Cdd:cd17995   81 HGSGESRQIIQQYEMYFKDAQGRKKKGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19421557  618 EHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKTEEQVKKLQSILKPMMLRR 680
Cdd:cd17995  161 EHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEQVEKLQALLKPYMLRR 223
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
458-931 3.63e-129

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 423.48  E-value: 3.63e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  458 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 536
Cdd:COG0553  241 TLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFApGLRVLV 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  537 YHGSQisrqmiqqyemvYRDAQGNPLSgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMA 616
Cdd:COG0553  321 LDGTR------------ERAKGANPFE---DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALK 385
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  617 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLKT---EEQVKKLQSILKPMMLRRLKDDVEKNLAPKQ 693
Cdd:COG0553  386 ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEkgdEEALERLRRLLRPFLLRRTKEDVLKDLPEKT 465
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  694 ETIIEVELTNIQKKYYRAILEKNFSFLTKGANQHNMPNLINTMMELRKCCNHPYLingaeekILEDFRKTHSPDapdfql 773
Cdd:COG0553  466 EETLYVELTPEQRALYEAVLEYLRRELEGAEGIRRRGLILAALTRLRQICSHPAL-------LLEEGAELSGRS------ 532
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  774 qamiqaaGKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFcKPDSDRFVF 853
Cdd:COG0553  533 -------AKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRF-QEGPEAPVF 604
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19421557  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 1.44e-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: 402.89  E-value: 1.44e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 538
Cdd:cd18060    1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  539 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALE 618
Cdd:cd18060   81 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19421557  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 19421557  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 538
Cdd:cd18059    1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVYH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  539 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALE 618
Cdd:cd18059   81 GSQASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLE 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19421557  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 2.94e-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: 2.94e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 538
Cdd:cd18061    1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDLNVVVYH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  539 GSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALE 618
Cdd:cd18061   81 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19421557  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 19421557    462 YQLEGMNWLLFNWYNRK-NCILADEMGLGKTIQSITFLSeiFLRGIH----GPFLIIAPLSTITNWEREFRTWT---EMN 533
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLL--YLKHVDknwgGPTLIVVPLSLLHNWMNEFERWVsppALR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557    534 AIVYHGSQISRQMIQQYEMVYRDaqgnplsgvfkFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLK 613
Cdd:pfam00176   79 VVVLHGNKRPQERWKNDPNFLAD-----------FDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557    614 LMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----DLKTEEQVKKLQSILKPMMLRRLKDDVEKNL 689
Cdd:pfam00176  148 SLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpieRGGGKKGVSRLHKLLKPFLLRRTKKDVEKSL 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19421557    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 19421557  458 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAI 535
Cdd:cd17993    1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFhSQQQYGPFLVVVPLSTMPAWQREFAKWApDMNVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  536 VYHGSQISRQMIQQYEMvYRDaQGNPLsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLM 615
Cdd:cd17993   81 VYLGDIKSRDTIREYEF-YFS-QTKKL----KFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEF 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19421557  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 19421557  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSE-IFLRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 536
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYlLKEGKERGPVLVVCPLSVLENWEREFEKWTpDLRVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  537 YHGSQISRQMIQQYEMVYrdaqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMA 616
Cdd:cd17919   81 YHGSQRERAQIRAKEKLD------------KFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR 148
                        170       180
                 ....*....|....*....|....*...
gi 19421557  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 19421557  458 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 536
Cdd:cd18009    3 VMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTpSVPVLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  537 YHGSQISRQMIQqyemvyRDAQGNPLSGVfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMA 616
Cdd:cd18009   83 YHGTKEERERLR------KKIMKREGTLQ-DFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  617 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG-----------DLKTEEQ----VKKLQSILKPMMLRRL 681
Cdd:cd18009  156 SDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDfsslsdnaadiSNLSEEReqniVHMLHAILKPFLLRRL 235

                 .
gi 19421557  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 3.50e-72

DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD3, CHD4, and CHD5 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350752 [Multi-domain]  Cd Length: 196  Bit Score: 240.03  E-value: 3.50e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRG-IHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 536
Cdd:cd17994    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWApDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  537 YHGSqisrqmiqqyemvyrdaqgnplsgvfkfHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMA 616
Cdd:cd17994   81 YVGD----------------------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYK 132
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19421557  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 19421557  456 SNQLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSeiFL---RGIHGPFLIIAPLSTITNWEREFRTWT-E 531
Cdd:cd17997    1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLG--YLkhyKNINGPHLIIVPKSTLDNWMREFKRWCpS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  532 MNAIVYHGSQISRQMIQQYEMVYRdaqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEG 611
Cdd:cd17997   79 LRVVVLIGDKEERADIIRDVLLPG-----------KFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQI 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19421557  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 2.68e-69

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


Pssm-ID: 350813 [Multi-domain]  Cd Length: 232  Bit Score: 233.36  E-value: 2.68e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRG-IHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 536
Cdd:cd18055    1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhTKGPFLVSAPLSTIINWEREFQMWApDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  537 YHGSQISRQMIQQYEMVYRDAQGNPLSGVFK--------FHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKL 608
Cdd:cd18055   81 YTGDKDSRAIIRENEFSFDDNAVKGGKKAFKmkreaqvkFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19421557  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 19421557  458 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSI---TFLSEIflRGIHGPFLIIAPLSTITNWEREFRTWT-EMN 533
Cdd:cd17996    3 TLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTIsliTYLMEK--KKNNGPYLVIVPLSTLSNWVSEFEKWApSVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  534 AIVYHGSQISRQMIQQYEMVYrdaqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLK 613
Cdd:cd17996   81 KIVYKGTPDVRKKLQSQIRAG------------KFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLN 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  614 LMAL-EHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG------------DLKTEEQV---KKLQSILKPMM 677
Cdd:cd17996  149 TYYHaRYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNtpfantgeqvkiELNEEETLliiRRLHKVLRPFL 228

                 ....*
gi 19421557  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 7.94e-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: 7.94e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRG-IHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 536
Cdd:cd18056    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWApDMYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  537 YHGSQISRQMIQQYEMVYRD--------AQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKL 608
Cdd:cd18056   81 YVGDKDSRAIIRENEFSFEDnairggkkASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19421557  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 1.75e-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: 1.75e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRG-IHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 536
Cdd:cd18057    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWApDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  537 YHGSQISRQMIQQYEMVYRDAQGNPLSGVF--------KFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKL 608
Cdd:cd18057   81 YTGDKESRSVIRENEFSFEDNAIRSGKKVFrmkkeaqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19421557  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 19421557  458 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAI 535
Cdd:cd18054   20 ELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFhQHQLYGPFLLVVPLSTLTSWQREFEIWApEINVV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  536 VYHGSQISRQMIQQYEMVYrdaqgnPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLM 615
Cdd:cd18054  100 VYIGDLMSRNTIREYEWIH------SQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDF 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19421557  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 19421557  457 NQLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAI 535
Cdd:cd18012    3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFApELKVL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  536 VYHGSQISRQMIQQYEmvyrdaqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLM 615
Cdd:cd18012   83 VIHGTKRKREKLRALE---------------DYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKAL 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19421557  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 19421557  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEI-FLRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIV 536
Cdd:cd18006    1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLaGRLKLLGPFLVLCPLSVLDNWKEELNRFApDLSVIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  537 YHGSQISRQMIQQyemvyrDAQGNPlsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMA 616
Cdd:cd18006   81 YMGDKEKRLDLQQ------DIKSTN-----RFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFS 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19421557  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 19421557  781 GKLVLIDKLLPKLIAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFcKPDSDRFVFLLCTRAG 860
Cdd:cd18793   11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRF-NEDPDIRVFLLSTKAG 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 19421557  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 19421557  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFL-RGIHGPFLIIAPLSTITNWEREFRTWTE-MNAIV 536
Cdd:cd18003    1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACeKGNWGPHLIVVPTSVMLNWEMEFKRWCPgFKILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  537 YHGSQISRQMIQQYEMvyrdaqgNPLSgvfkFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMA 616
Cdd:cd18003   81 YYGSAKERKLKRQGWM-------KPNS----FHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFN 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19421557  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 3.08e-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: 196.04  E-value: 3.08e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  458 QLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLR-GIHGPFLIIAPLSTITNWEREFRTWT-EMNAI 535
Cdd:cd18053   20 ELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEhQLYGPFLLVVPLSTLTSWQREIQTWApQMNAV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  536 VYHGSQISRQMIQQYEMVYrdaqgnPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEGLKLM 615
Cdd:cd18053  100 VYLGDINSRNMIRTHEWMH------PQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDF 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19421557  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 2.03e-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: 2.03e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  459 LREYQLEGMNWLLfNWYNRK-NCILADEMGLGKTIQSITFLSEIFLR-GIHGPFLIIAPLSTITNWEREF-RTWTEMNAI 535
Cdd:cd18002    1 LKEYQLKGLNWLA-NLYEQGiNGILADEMGLGKTVQSIAVLAHLAEEhNIWGPFLVIAPASTLHNWQQEIsRFVPQFKVL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  536 VYHGSQISRQMIQQY----EMVYRDAqgnplsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLLEG 611
Cdd:cd18002   80 PYWGNPKDRKVLRKFwdrkNLYTRDA---------PFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKT 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19421557  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 19421557  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWT-EMNAIVY 537
Cdd:cd17998    1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCpSLKVEPY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  538 HGSQISRqmiqqyemvyRDAQGNPLSGVFKFHVVITTFEMILADCPE---LKKIHWSCVIIDEAHRLKNRNCKLLEGLKL 614
Cdd:cd17998   81 YGSQEER----------KHLRYDILKGLEDFDVIVTTYNLATSNPDDrsfFKRLKLNYVVYDEGHMLKNMTSERYRHLMT 150
                        170       180       190
                 ....*....|....*....|....*....|...
gi 19421557  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 19421557  459 LREYQLEGMNWLlFNWY-NRKNCILADEMGLGKTIQSITFLSEI----------------FLRGIH-----GPFLIIAPL 516
Cdd:cd18005    1 LRDYQREGVEFM-YDLYkNGRGGILGDDMGLGKTVQVIAFLAAVlgktgtrrdrennrprFKKKPPassakKPVLIVAPL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  517 STITNWEREFRTWTEMNAIVYHGSQISRQMIQQYEmvyrdaQGnplsgvfKFHVVITTFEMILADCPELKKIHWSCVIID 596
Cdd:cd18005   80 SVLYNWKDELDTWGHFEVGVYHGSRKDDELEGRLK------AG-------RLEVVVTTYDTLRRCIDSLNSINWSAVIAD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  597 EAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGD---------------LK 661
Cdd:cd18005  147 EAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEpikrgqrhtatarelRL 226
                        250
                 ....*....|....*....
gi 19421557  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 1.33e-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: 1.33e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  445 QKLEKSREYKNSNQLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LRGIHGPFLIIAPLSTITNWE 523
Cdd:cd18062   10 EKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMeHKRINGPFLIIVPLSTLSNWV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  524 REFRTWT-EMNAIVYHGSQISRQMIQqyemvyrdaqgnPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLK 602
Cdd:cd18062   90 YEFDKWApSVVKVSYKGSPAARRAFV------------PQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  603 NRNCKLLEGLKLMALE-HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----------DLKTEEQ---VKK 668
Cdd:cd18062  158 NHHCKLTQVLNTHYVApRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRR 237
                        250
                 ....*....|....
gi 19421557  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 9.19e-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: 9.19e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  446 KLEKSREYKNSNQLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEI-FLRGIHGPFLIIAPLSTITNWER 524
Cdd:cd18064    3 RFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMkHYRNIPGPHMVLVPKSTLHNWMA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  525 EFRTWT-EMNAIVYHGSQisrqmiQQYEMVYRDAQgnpLSGvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKN 603
Cdd:cd18064   83 EFKRWVpTLRAVCLIGDK------DQRAAFVRDVL---LPG--EWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKN 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  604 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGD---LKTEEQVKKLQSILKPMMLRR 680
Cdd:cd18064  152 EKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTnncLGDQKLVERLHMVLRPFLLRR 231
                        250
                 ....*....|...
gi 19421557  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 1.38e-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: 1.38e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  445 QKLEKSREYKNSNQLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LRGIHGPFLIIAPLSTITNWE 523
Cdd:cd18063   10 ERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMeHKRLNGPYLIIVPLSTLSNWT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  524 REFRTWT-EMNAIVYHGS-QISRQMIQQYEmvyrdaqgnplSGvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRL 601
Cdd:cd18063   90 YEFDKWApSVVKISYKGTpAMRRSLVPQLR-----------SG--KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  602 KNRNCKLLEGLKLMALE-HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG----------DLKTEEQ---VK 667
Cdd:cd18063  157 KNHHCKLTQVLNTHYVApRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgervDLNEEETiliIR 236
                        250
                 ....*....|....*
gi 19421557  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 19421557  446 KLEKSREYKNSNQLREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEI-FLRGIHGPFLIIAPLSTITNWER 524
Cdd:cd18065    3 RFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLkHYRNIPGPHMVLVPKSTLHNWMN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  525 EFRTWT-EMNAIVYHGSQISRQMIQQYEMvyrdaqgnpLSGvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKN 603
Cdd:cd18065   83 EFKRWVpSLRAVCLIGDKDARAAFIRDVM---------MPG--EWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKN 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  604 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGD---LKTEEQVKKLQSILKPMMLRR 680
Cdd:cd18065  152 EKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRR 231

                 ..
gi 19421557  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 19421557  459 LREYQLEGMNWLLFnwynrKNCILADEMGLGKTIQSI--------TFLSEIFLRGIHGPF----------LIIAPLSTIT 520
Cdd:cd18008    1 LLPYQKQGLAWMLP-----RGGILADEMGLGKTIQALalilatrpQDPKIPEELEENSSDpkklylskttLIVVPLSLLS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  521 NWEREFRTWTE---MNAIVYHGSQisrqmiqqyemvyrdaQGNPLSGVFKFHVVITTFEMILADCPE------------- 584
Cdd:cd18008   76 QWKDEIEKHTKpgsLKVYVYHGSK----------------RIKSIEELSDYDIVITTYGTLASEFPKnkkgggrdskeke 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  585 ---LKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFGDLK 661
Cdd:cd18008  140 aspLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPF 219
                        250       260
                 ....*....|....*....|..
gi 19421557  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 19421557  459 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTE-MNAIVY 537
Cdd:cd18001    1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPgLRVKVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  538 HGSQisrqmiqqyemvyRDAQGNPLSGVFK-FHVVITTFEMILADCPEL-----KKIHWSCVIIDEAHRLKNRNCKLLEG 611
Cdd:cd18001   81 HGTS-------------KKERERNLERIQRgGGVLLTTYGMVLSNTEQLsaddhDEFKWDYVILDEGHKIKNSKTKSAKS 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  612 LKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQ-FPSETAFLEEFGDLKTEEQVKK---------------LQSILKP 675
Cdd:cd18001  148 LREIPAKNRIILTGTPIQNNLKELWALFDFACNGSlLGTRKTFKMEFENPITRGRDKDatqgekalgsevaenLRQIIKP 227

                 ....*
gi 19421557  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 1.69e-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: 1.69e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  459 LREYQLEGMNWLL-----FNWYNRKNCILADEMGLGKTIQSITFLSeIFLRgiHGPF--------LIIAPLSTITNWERE 525
Cdd:cd18004    1 LRPHQREGVQFLYdcltgRRGYGGGGAILADEMGLGKTLQAIALVW-TLLK--QGPYgkptakkaLIVCPSSLVGNWKAE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  526 FRTWTemnaivyhGSQISRQMIQQYEMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHwSC--VIIDEAHRLKN 603
Cdd:cd18004   78 FDKWL--------GLRRIKVVTADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKKI-SIdlLICDEGHRLKN 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  604 RNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAF-------------------LEEFGDLKTEE 664
Cdd:cd18004  149 SESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFrkvfeepilrsrdpdaseeDKELGAERSQE 228
                        250
                 ....*....|....*.
gi 19421557  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 19421557  459 LREYQLEGMNWLLF-NWYNRKNcILADEMGLGKTIQSITFL-SEIFLR-----GIHGPFLIIAPLSTITNWEREFRTWTE 531
Cdd:cd17999    1 LRPYQQEGINWLAFlNKYNLHG-ILCDDMGLGKTLQTLCILaSDHHKRansfnSENLPSLVVCPPTLVGHWVAEIKKYFP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  532 ---MNAIVYHGSQISRQMIQQyemvyrdaQGNplsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKL 608
Cdd:cd17999   80 nafLKPLAYVGPPQERRRLRE--------QGE------KHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  609 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEFG-------DLK-----TEEQVKKLQSILK-- 674
Cdd:cd17999  146 SKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLkpilasrDSKasakeQEAGALALEALHKqv 225

                 ....*..
gi 19421557  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 1.14e-35

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


Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 130.10  E-value: 1.14e-35
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 19421557  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 19421557  459 LREYQLEGMNWLLfnWYNRKNC--ILADEMGLGKTIQSITflseiFLRGIH------GPFLIIAPLSTITNWEREFRTW- 529
Cdd:cd18000    1 LFKYQQTGVQWLW--ELHCQRVggILGDEMGLGKTIQIIA-----FLAALHhsklglGPSLIVCPATVLKQWVKEFHRWw 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  530 TEMNAIVYHGSQISRQMIQQYEMVYRDAQGNPlSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKLL 609
Cdd:cd18000   74 PPFRVVVLHSSGSGTGSEEKLGSIERKSQLIR-KVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEIT 152
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 19421557  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 19421557  459 LREYQLEGmnwLLFNWYN----------RKNCILADEMGLGKTIQSITFLsEIFLRgiHGP----FLIIAPLSTITNWER 524
Cdd:cd18007    1 LKPHQVEG---VRFLWSNlvgtdvgsdeGGGCILAHTMGLGKTLQVITFL-HTYLA--AAPrrsrPLVLCPASTLYNWED 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  525 EFRTWTEMNAIVYHGsqisrqmiqqyeMVYRDAQGNP---LSGVFKFH----VVITTFEM--ILADCPELKK------IH 589
Cdd:cd18007   75 EFKKWLPPDLRPLLV------------LVSLSASKRAdarLRKINKWHkeggVLLIGYELfrNLASNATTDPrlkqefIA 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19421557  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 19421557     452 EYKNSNQLREYQLEGMNWLLFNWynrKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTIT-NWEREFRTWT 530
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAeQWAEELKKLG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557     531 EMNAI----VYHGSQISRQMIQQYEmvyrdaqgnplsgvFKFHVVITTFEMILADCPE--LKKIHWSCVIIDEAHRLKN- 603
Cdd:smart00487   79 PSLGLkvvgLYGGDSKREQLRKLES--------------GKTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDg 144
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|..
gi 19421557     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 9.17e-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: 9.17e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  459 LREYQLEGmnwLLFNWY--------NRKNCILADEMGLGKTIQSITFLSEIFLRGIHGP------FLIIAPLSTITNWER 524
Cdd:cd18066    1 LRPHQREG---IEFLYEcvmgmrvnERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGkpvikrALIVTPGSLVKNWKK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  525 EFRTWtemnaivyhgsqISRQMIQQYeMVYRDAQGNPLSGVFKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNR 604
Cdd:cd18066   78 EFQKW------------LGSERIKVF-TVDQDHKVEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNT 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 19421557  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 19421557  459 LREYQLEGMNWLLfnwynRKN--CILADEMGLGKTIQSITFLSeiFLRGiHGPFLIIAPLSTITNWEREFRTW----TEM 532
Cdd:cd18010    1 LLPFQREGVCFAL-----RRGgrVLIADEMGLGKTVQAIAIAA--YYRE-EWPLLIVCPSSLRLTWADEIERWlpslPPD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  533 NAIVYHGSQISRQMiqqyemvyRDAQgnplsgvfkfhVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRN---CKLL 609
Cdd:cd18010   73 DIQVIVKSKDGLRD--------GDAK-----------VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKakrTKAA 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  610 EGLkLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEE---------FGDLKTEEQVKKLQSIL-KPMMLR 679
Cdd:cd18010  134 LPL-LKRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRycaakqggfGWDYSGSSNLEELHLLLlATIMIR 212

                 .
gi 19421557  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 8.65e-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: 105.11  E-value: 8.65e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19421557  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 19421557  477 RKNCILADEMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITNWEREFRTWTEMNAIVyhgsqISRQMIQQYEmvyRD 556
Cdd:cd18011   17 PVRLLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDELQDKFGLPFLI-----LDRETAAQLR---RL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  557 AQGNPLSgvfkFHVVITTFEMI-----LADcpELKKIHWSCVIIDEAHRLKNRNCKLLEGL-KLMAL-----EHKVLLTG 625
Cdd:cd18011   89 IGNPFEE----FPIVIVSLDLLkrseeRRG--LLLSEEWDLVVVDEAHKLRNSGGGKETKRyKLGRLlakraRHVLLLTA 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 19421557  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 19421557    781 GKLVLIDKLLPKliAGGHKVLIFSQMVRCLDilEDYLIQRR-YTYERIDGRVRGNLRQAAIDRFCKPDSDrfvFLLCTRA 859
Cdd:pfam00271    1 EKLEALLELLKK--ERGGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 19421557    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 1.78e-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: 1.78e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  481 ILADEMGLGKTIQSITFLseiflrgIHGPFLIIAPLSTITNWEREFRTWTE---MNAIVYHGSQisrqmiqqyemvyRDA 557
Cdd:cd18071   52 ILADDMGLGKTLTTISLI-------LANFTLIVCPLSVLSNWETQFEEHVKpgqLKVYTYHGGE-------------RNR 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  558 QGNPLSgvfKFHVVITTFEMI------LADCPeLKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNS 631
Cdd:cd18071  112 DPKLLS---KYDIVLTTYNTLasdfgaKGDSP-LHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNS 187
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19421557  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 2.64e-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: 2.64e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  459 LREYQLEGMNWLLFNWYNRKN-----CILADEMGLGKTIQSITFLSEIFLRGIHGPFLI-----IAPLSTITNWEREFRT 528
Cdd:cd18067    1 LRPHQREGVKFLYRCVTGRRIrgshgCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaivVSPSSLVKNWANELGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  529 WTEMNAIVYHGSQISRQMIQQYEMVYRDAQGNPLSGvfkfHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKNRNCKL 608
Cdd:cd18067   81 WLGGRLQPLAIDGGSKKEIDRKLVQWASQQGRRVST----PVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  609 LEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETAFLEEF---------GD------LKTEEQVKKLQSIL 673
Cdd:cd18067  157 YQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFelpilkgrdADasekerQLGEEKLQELISIV 236

                 ....*..
gi 19421557  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 6.85e-23

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


Pssm-ID: 468472 [Multi-domain]  Cd Length: 868  Bit Score: 107.46  E-value: 6.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   481 ILADEMGLGKTIQS---ITFLSEIFLRGIhgpfLIIAPLSTITNWEREFRTWTEMNAIVyhgsqISRQMIQQ-YEMVYRD 556
Cdd:NF038318   51 ILADEVGLGKTIEAglvLKYVLESGAKKI----LIILPANLRKQWEIELEEKFDLESLI-----LDSLTVEKdAKKWNKR 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   557 AQGNPlsgvfKFHVVITTFEMILADCPELKKIHWSCVIIDEAHRLKN--RNCKLLEGL-KLMALEHKVLLTGTPLQNSVE 633
Cdd:NF038318  122 LTDNK-----KVRIVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRNvhKGGKRAKNLyELTKGIPKILLTATPLQNSLL 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   634 ELFSLLNFLEPSQFPSETAFL------EEFGDLKTEeqvkklqsiLKPMMLRRLKDDVEKNLAPKQETII---------E 698
Cdd:NF038318  197 DLYGLVSFIDPRIFGSEKVFSkryikdEDYSDLKRE---------LSPVLYRTLRKDVADYMQFKKRKCItvdfelspdE 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   699 VELTN-----IQKKYYRAILEKNFSFLT----KGANQHNMPnLINTMMELRKCCNHPY---LINGAEEKI------LEDF 760
Cdd:NF038318  268 IELYVrvnnfLKRDILYSIPTSNRTLIIlvirKLLASSSFA-LAETFEVLKKRLEKLKegtRSANAQEGFdlfwsfVEDE 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   761 RKTHSPDAPDFQL----QAMIQAAGKLV--LIDKL-----------LPKLIAGG----------HKVLIFSQMVRCLDIL 813
Cdd:NF038318  347 IDESGFEEKQDELytrqKEFIQHEIDEVdaIIDVAkriktnakvtaLKTALEIAfeyqreegiaQKVVVFTESKRTQKYI 426
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   814 EDYLIQRRYTYERI---DG--------------RVR--GN--------LRQAAIDRFckpdSDRFVFLLCTRAGGLGINL 866
Cdd:NF038318  427 AEELRKSGYEGEDIllfNGdfddamtkeiyrawQVKnyGKanygrsveYKHAIVDYF----KNNAKILIVTDAGSEGLNL 502
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19421557   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 19421557     811 DILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFCKPDSDrfvFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQAR 890
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 19421557     891 CHRIG 895
Cdd:smart00490   78 AGRAG 82
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
459-680 5.78e-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: 94.47  E-value: 5.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  459 LREYQLEGMNWLLfnWYNRKNC---ILADEMGLGKTIQSITF------------------LSEIFLRGIHGPF-----LI 512
Cdd:cd18072    1 LLLHQKQALAWLL--WRERQKPrggILADDMGLGKTLTMIALilaqkntqnrkeeekekaLTEWESKKDSTLVpsagtLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  513 IAPLSTITNWEREFRTWTEMNAI---VYHGSQisrqmiqqyemvyRDAQGNPLSgvfKFHVVITTFEMILADCPELKK-- 587
Cdd:cd18072   79 VCPASLVHQWKNEVESRVASNKLrvcLYHGPN-------------RERIGEVLR---DYDIVITTYSLVAKEIPTYKEes 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  588 -------IHWSCVIIDEAHRLKNRNCKLLEGL-KLMALEHKVLlTGTPLQNSVEELFSLLNFLEPSQFpSETAFLEEFGD 659
Cdd:cd18072  143 rssplfrIAWARIILDEAHNIKNPKVQASIAVcKLRAHARWAL-TGTPIQNNLLDMYSLLKFLRCSPF-DDLKVWKKQVD 220
                        250       260
                 ....*....|....*....|.
gi 19421557  660 LKTEEQVKKLQSILKPMMLRR 680
Cdd:cd18072  221 NKSRKGGERLNILTKSLLLRR 241
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
480-657 6.95e-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: 6.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  480 CILADEMGLGKTIQSITFLSEIFLRGIHGPF---LIIAPLSTITNWEREFRTWTEMNA---------------------I 535
Cdd:cd18068   31 CILAHCMGLGKTLQVVTFLHTVLLCEKLENFsrvLVVCPLNTVLNWLNEFEKWQEGLKdeekievnelatykrpqersyK 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  536 VYHGSQISRQMIQQYEMvYRD-AQGNPLSGVFKFHvviTTFEMILAD-CPELkkihwscVIIDEAHRLKNRNCKLLEGLK 613
Cdd:cd18068  111 LQRWQEEGGVMIIGYDM-YRIlAQERNVKSREKLK---EIFNKALVDpGPDF-------VVCDEGHILKNEASAVSKAMN 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 19421557  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 19421557  480 CILADEMGLGKTIQSITFLsEIFLRGIHGP-FLIIAPLSTITNWEREFRTWteMNAIVYHGSQISRQM---IQQYEMVYR 555
Cdd:cd18069   31 CILAHSMGLGKTLQVISFL-DVLLRHTGAKtVLAIVPVNTLQNWLSEFNKW--LPPPEALPNVRPRPFkvfILNDEHKTT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  556 DAQGNPLSG-VFKFHVVITTFEMI-LADCPELkkihwscVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVE 633
Cdd:cd18069  108 AARAKVIEDwVKDGGVLLMGYEMFrLRPGPDV-------VICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLI 180
                        170       180
                 ....*....|....*....|....
gi 19421557  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 1.40e-17

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


Pssm-ID: 349306 [Multi-domain]  Cd Length: 54  Bit Score: 78.39  E-value: 1.40e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 19421557  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 19421557  459 LREYQLEGMNWLLfnwYNRKNCILADeMGLGKTIQSITFLSEIFLRGIHGPFLIIAPLSTITN-WEREFRTWTEMNAIVY 537
Cdd:cd18013    1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARStWPDEVEKWNHLRNLTV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  538 H---GSQisRQMIqqyemvyRDAQGNPlsgvfkfHVVITTFEMiLADCPELKKIHW--SCVIIDEAHRLKNRNCKllEGL 612
Cdd:cd18013   77 SvavGTE--RQRS-------KAANTPA-------DLYVINREN-LKWLVNKSGDPWpfDMVVIDELSSFKSPRSK--RFK 137
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 19421557  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 4.44e-14

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


Pssm-ID: 349307 [Multi-domain]  Cd Length: 70  Bit Score: 69.31  E-value: 4.44e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19421557  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 3.85e-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: 3.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  401 CSLPYEESTWELEEDVDPAKVKEFESLQVLPEIKHVERPASDSWQKLEKS------REYKNSNQLREYQLEGMN-WLLFN 473
Cdd:COG1061   17 SLLLLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEaleagdEASGTSFELRPYQQEALEaLLAAL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  474 WYNRKNCILADEMGLGKTIQSITFLSEIFLRGihgPFLIIAPLSTITN-WEREFRTWTemNAIVYHGSQISRQmiqqyem 552
Cdd:COG1061   97 ERGGGRGLVVAPTGTGKTVLALALAAELLRGK---RVLVLVPRRELLEqWAEELRRFL--GDPLAGGGKKDSD------- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  553 vyrdaqgnplsgvfkFHVVITTFEmILADCPELKKI--HWSCVIIDEAHRLKNRncKLLEGLKLMALEHKVLLTGTPlqn 630
Cdd:COG1061  165 ---------------APITVATYQ-SLARRAHLDELgdRFGLVIIDEAHHAGAP--SYRRILEAFPAAYRLGLTATP--- 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  631 sveelfsllnflepsqfpsetafleEFGDLKTEEqVKKLQSILKPMMLRRLKDDveKNLAPKQETIIEVELTNIQKKY-- 708
Cdd:COG1061  224 -------------------------FRSDGREIL-LFLFDGIVYEYSLKEAIED--GYLAPPEYYGIRVDLTDERAEYda 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  709 YRAILEKNfsfltkganqhnmpnlintmmelrkccnhpyLINGAEEK--ILEDFRKTHspdapdfqlqamiqaagklvli 786
Cdd:COG1061  276 LSERLREA-------------------------------LAADAERKdkILRELLREH---------------------- 302
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  787 dkllpkliAGGHKVLIFSQMVRCLDILEDYLIQRRYTYERIDGRVRGNLRQAAIDRFckpDSDRFVFLLCTRAGGLGINL 866
Cdd:COG1061  303 --------PDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAF---RDGELRILVTVDVLNEGVDV 371
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  867 TAADTCIIFDSDWNPQNDLQAQARCHRIGQSK-AVKVYRLITRNSYEREMFDKASLKLGLDKAVLQDINRKGGTNgVQQL 945
Cdd:COG1061  372 PRLDVAILLRPTGSPREFIQRLGRGLRPAPGKeDALVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELA-LLIA 450
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  946 SKMEVEDLLRKGAYGALMDEEDEGSKFCEEDIDQILQRRTHTITIQSEGKGSTFAKASFVASGNRTDISLDDPNFWQKWA 1025
Cdd:COG1061  451 VKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLLLLL 530
                        650       660
                 ....*....|....*....|....
gi 19421557 1026 KIAKLDTEAKNEKESLVIDRPRVR 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 19421557  459 LREYQLEGMNWLLfnwyNRKNcILADEMGLGKTIQSI----------------TFLSEIFLRGIH----------GPFLI 512
Cdd:cd18070    1 LLPYQRRAVNWML----VPGG-ILADEMGLGKTVEVLalillhprpdndldaaDDDSDEMVCCPDclvaetpvssKATLI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  513 IAPLSTITNWEREFRTWTEMNAIVYHgsqisrqmiqqYEMVYRD--AQGNPLSGVFKFHVVITTFEmILAD--------- 581
Cdd:cd18070   76 VCPSAILAQWLDEINRHVPSSLKVLT-----------YQGVKKDgaLASPAPEILAEYDIVVTTYD-VLRTelhyaeanr 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  582 ---------------CPeLKKIHWSCVIIDEAHRLKNRNCKLLEGLKLMALEHKVLLTGTPLQNSVEELFSLLNFLEPSQ 646
Cdd:cd18070  144 snrrrrrqkryeappSP-LVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEP 222

                 .
gi 19421557  647 F 647
Cdd:cd18070  223 F 223
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
374-426 8.26e-10

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 56.43  E-value: 8.26e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 19421557    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 5.72e-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: 5.72e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 19421557  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 19421557  478 KNCILADEMGLGKTIQ-SITFLSEIFLRGihGPFLIIAPLSTITN-WEREFRTWTEMNA--IVYHGsqiSRQMIQQYEMV 553
Cdd:cd00046    2 ENVLITAPTGSGKTLAaLLAALLLLLKKG--KKVLVLVPTKALALqTAERLRELFGPGIrvAVLVG---GSSAEEREKNK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  554 YRDAqgnplsgvfkfHVVITTFEMILADCPELKKIH---WSCVIIDEAHRL----KNRNCKLLEGLKLMALEHK-VLLTG 625
Cdd:cd00046   77 LGDA-----------DIIIATPDMLLNLLLREDRLFlkdLKLIIVDEAHALlidsRGALILDLAVRKAGLKNAQvILLSA 145

                 .
gi 19421557  626 T 626
Cdd:cd00046  146 T 146
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
102-371 1.81e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 53.93  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   102 QEGAAKGSKDrepkPKRKREPKEPKEPRKAEEPKKAKEHKEPKQKDGAKKARKPREASGTKEAKEKRSctDSAARTKSRK 181
Cdd:PTZ00449  533 EHEDSKESDE----PKEGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDPKHPKDPEEPKK--PKRPRSAQRP 606
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   182 ASKEQGPTPVEKKKKGKRKSETTVESLELDQGLTNPSlrSPE--ESTESTDSQKRRSGRQV------KRRKYNEDLDFKV 253
Cdd:PTZ00449  607 TRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQRPS--SPErpEGPKIIKSPKPPKSPKPpfdpkfKEKFYDDYLDAAA 684
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   254 VDDDGETIAVLGAGRTSALSaSTLAWQAEEPPEDDANIIEKILASKTVQEVHPGEP----PFDLELFYVKYRNFSYLHCK 329
Cdd:PTZ00449  685 KSKETKTTVVLDESFESILK-ETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPdaeqPDDIEFFTPPEEERTFFHET 763
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 19421557   330 WAT------MEELEKDPRIAQKIKrfrnkqaqmkhiftEPDEDLFNPD 371
Cdd:PTZ00449  764 PADtplpdiLAEEFKEEDIHAETG--------------EPDEAMKRPD 797
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
374-426 2.09e-06

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


Pssm-ID: 349274 [Multi-domain]  Cd Length: 50  Bit Score: 46.70  E-value: 2.09e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 19421557  374 EVDRILevahtkDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAK--VKEFES 426
Cdd:cd00024    2 EVEKIL------DHRVRKGKLEYLVKWKGYPPEENTWEPEENLTNAPelIKEYEK 50
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
291-352 4.41e-06

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 46.03  E-value: 4.41e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19421557    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 19421557  459 LREYQLEGM-NWLLFNWYNRKNCILAdeMGLGKTIqsiTFLSEIFLRGIHgPFLIIAP-LSTITNWEREFRTWTemnaiv 536
Cdd:cd17926    1 LRPYQEEALeAWLAHKNNRRGILVLP--TGSGKTL---TALALIAYLKEL-RTLIVVPtDALLDQWKERFEDFL------ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  537 yHGSQISRQmiqqyemvyrdaQGNPLSGVFKFHVVITTFEMILADCPELKKI--HWSCVIIDEAHRLknrNCKLLEGLKL 614
Cdd:cd17926   69 -GDSSIGLI------------GGGKKKDFDDANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAHHL---PAKTFSEILK 132
                        170
                 ....*....|....
gi 19421557  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 7.61e-06

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


Pssm-ID: 349311  Cd Length: 59  Bit Score: 45.34  E-value: 7.61e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19421557  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 2.46e-05

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


Pssm-ID: 349308  Cd Length: 58  Bit Score: 43.83  E-value: 2.46e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 19421557  372 YVEVDRIleVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVD---PAKVKEFES 426
Cdd:cd18661    2 YQIVERI--IAHSPQKSAASGYPDYLCKWQGLPYSECTWEDGALISkkfQACIDEYHS 57
CHROMO smart00298
Chromatin organization modifier domain;
374-425 2.80e-05

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 43.74  E-value: 2.80e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 19421557     374 EVDRILevAHTKDAETGEEvthYLVKWCSLPYEESTWELEEDV--DPAKVKEFE 425
Cdd:smart00298    3 EVEKIL--DHRWKKKGELE---YLVKWKGYSYSEDTWEPEENLlnCSKKLDNYK 51
BRK smart00592
domain in transcription and CHROMO domain helicases;
2400-2435 4.14e-05

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 43.11  E-value: 4.14e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 19421557    2400 SGEERVPAIPKEPGLRG----FLPENKFNHTLAEPILRDT 2435
Cdd:smart00592    1 DGEERVPVINRETGKKLtgddAPKAKDLERWLEENPEYEV 40
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
103-186 8.57e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 47.53  E-value: 8.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557    103 EGAAKGSKDREPKPKRKREPKEPKEP-RKAEEPKKAKEHKEPKQKDGAKKARKPREASGTKEAKEKRSCTDSAARTKSRK 181
Cdd:TIGR02794  123 EAKAKQAAEAKAKAEAEAERKAKEEAaKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAK 202

                   ....*
gi 19421557    182 ASKEQ 186
Cdd:TIGR02794  203 AKAAA 207
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
374-418 1.07e-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: 1.07e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 19421557  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 19421557    460 REYQLEGMNWLLfnwyNRKNCILADEMGLGKT-IQSITFLSEIFLRGIHGPFLIIAPLSTITN-WEREFRTWTEMNAI-- 535
Cdd:pfam00270    1 TPIQAEAIPAIL----EGRDVLVQAPTGSGKTlAFLLPALEALDKLDNGPQALVLAPTRELAEqIYEELKKLGKGLGLkv 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557    536 --VYHGSQISRQMiqqyemvyrdaqgNPLSGVfkfHVVITTFEMILADCPE---LKKIhwSCVIIDEAHRL--KNRNCKL 608
Cdd:pfam00270   77 asLLGGDSRKEQL-------------EKLKGP---DILVGTPGRLLDLLQErklLKNL--KLLVLDEAHRLldMGFGPDL 138
                          170       180
                   ....*....|....*....|....*...
gi 19421557    609 LEGLKLMALEHK-VLLTGTPLQNsVEEL 635
Cdd:pfam00270  139 EEILRRLPKKRQiLLLSATLPRN-LEDL 165
PTZ00121 PTZ00121
MAEBL; Provisional
101-249 3.80e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 3.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   101 DQEGAAKGSKDREPKPKRKREPKEPKEPRKAEEPKKAKEHKEpKQKDGAKKARKPREA-SGTKEAKEKRSCTDSAARTKS 179
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK-KADEAKKKAEEAKKAeEAKKKAEEAKKADEAKKKAEE 1481
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   180 RKASKEQGPTPVEKKKKGKRKSETTVESLELDQGLTNPSLRSPEESTESTDSQKRRSGRQVKRRKYNEDL 249
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
PTZ00121 PTZ00121
MAEBL; Provisional
105-283 4.38e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 4.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   105 AAKGSKDREPKPKRKREPKEPKEPRKAEEP-KKAKEHK---EPKQKDGAKKARKPREASGTKEAKEKRSCTDSAARTKSR 180
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAkKKADEAKkaeEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK 1558
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   181 KASK----EQGPTPVEKKKKGKRKSEtTVESLELDQGLTNPSLRSPEESTESTDSQK----RRSGRQVKR----RKYNED 248
Cdd:PTZ00121 1559 KAEEkkkaEEAKKAEEDKNMALRKAE-EAKKAEEARIEEVMKLYEEEKKMKAEEAKKaeeaKIKAEELKKaeeeKKKVEQ 1637
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 19421557   249 LDFKVVDDDGETIAVLGAGRTSALSASTLAWQAEE 283
Cdd:PTZ00121 1638 LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672
PTZ00121 PTZ00121
MAEBL; Provisional
106-186 5.78e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 5.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   106 AKGSKDREPKPKRKREPKEPKEPRKAEEPKKAKEHKEPKQKDGAKKARKPREASGTKEAKEKRSCTDSAARTKSRKASKE 185
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371

                  .
gi 19421557   186 Q 186
Cdd:PTZ00121 1372 K 1372
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 19421557  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 8.88e-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: 8.88e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19421557  277 LAWQAEEPPEDDAnIIEKILASKTVQEVHPGEPPFDLELFyVKYRNFSYLHCKWATMEELE 337
Cdd:cd18667    9 LTWRWAEPPYPEP-LPEKPDEDPYPPPPRKLQPRPEREFF-VKWHGMSYWHCEWVSELQLE 67
PTZ00121 PTZ00121
MAEBL; Provisional
103-248 1.02e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   103 EGAAKGSKDREPKPKRK-REPKEPKEPRKAEEPKKAKEHKEPKQKDGAKKARK--------PREASGTKEAKEKRSCTDS 173
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKaDEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKaeedknmaLRKAEEAKKAEEARIEEVM 1598
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19421557   174 AARTKSRKASKEQgptpVEKKKKGKRKSETTVESLELDQGLTNPSLRSPEESTESTDSQKRRSGRQVK----RRKYNED 248
Cdd:PTZ00121 1599 KLYEEEKKMKAEE----AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKaaeeAKKAEED 1673
CD_POL_like cd18974
chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the ...
380-420 1.38e-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: 1.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 19421557  380 EVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAK 420
Cdd:cd18974    2 EVEEIVDEKMIDDELHYLVKWKGWPAEYNQWEPEDDMENAP 42
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
101-186 1.43e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.68  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557    101 DQEGAAKgsKDREPKPKRKREPKEPKEPRKAEEPKKaKEHKEPKQKdgAKKARKPREASGTKEAKEKRSCTDSAARTKSR 180
Cdd:TIGR02794   58 QKKPAAK--KEQERQKKLEQQAEEAEKQRAAEQARQ-KELEQRAAA--EKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEA 132

                   ....*.
gi 19421557    181 KASKEQ 186
Cdd:TIGR02794  133 KAKAEA 138
CD_MarY1_POL_like cd18975
chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes ...
396-424 1.47e-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: 1.47e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 19421557  396 YLVKWCSLPYEESTWELEEDVDPAK-VKEF 424
Cdd:cd18975   18 YLIQWKGYPLEEASWELEDNIKNPRlIEEF 47
chromodomain cd18965
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
394-416 1.66e-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: 1.66e-03
                         10        20
                 ....*....|....*....|...
gi 19421557  394 THYLVKWCSLPYEESTWELEEDV 416
Cdd:cd18965   16 LEYLVKWHGLPESENTWEREKDI 38
chromodomain cd18968
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
374-424 2.02e-03

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


Pssm-ID: 349324  Cd Length: 57  Bit Score: 38.48  E-value: 2.02e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19421557  374 EVDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVDPAK--VKEF 424
Cdd:cd18968    3 EVEVILAARVVKDAESRKKGWKYLVKWAGYPDEENTWEPEESFDGCDdlLERF 55
PHA03247 PHA03247
large tegument protein UL36; Provisional
2317-2691 2.03e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  2317 PGQATLSTTHPEGPGPATSAPEPATAASSQAEKSIPSKSLLDWLRQQADYS-------LEVPGFGANFSDKPKQRRPRCK 2389
Cdd:PHA03247 2609 RGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGrvsrprrARRLGRAAQASSPPQRPRRRAA 2688
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  2390 EPGkldVSSLSGEERVPAIPKEPGLRgflpenkfnhtlAEPILRDTGPRRRGRRPRSELLKAPSIVADSPSGMGPLfmng 2469
Cdd:PHA03247 2689 RPT---VGSLTSLADPPPPPPTPEPA------------PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA---- 2749
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  2470 LIAGMDLVGLQNMRNMPGIPLTglvgfPAGFATMPTGEEVKSTLSMLPMMLPGMAAVPQMFGVGGLLSPPMATTCTSTAP 2549
Cdd:PHA03247 2750 TPGGPARPARPPTTAGPPAPAP-----PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  2550 ASLSSTTKSGTAVTEKTAEDKPSSHDVKTDTLAedkPGpGPFSDQSEPAITTSSPVAfnPFLIPGVSpgLIYPSMFLSPg 2629
Cdd:PHA03247 2825 AGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA---PG-GDVRRRPPSRSPAAKPAA--PARPPVRR--LARPAVSRST- 2895
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19421557  2630 MGMALPAMQQARHSEivglesqkrkkkktkggnPNSHPEPAPSCEREPSGDENCAEPSAPLP 2691
Cdd:PHA03247 2896 ESFALPPDQPERPPQ------------------PQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939
PTZ00121 PTZ00121
MAEBL; Provisional
110-256 2.43e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   110 KDREPKPKRKREPKEPKEPRKAEEPKKAKEHKEPKQKDGAKKARKPREasgtKEAKEKRsctdsaaRTKSRKASKEQGPT 189
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK----KEAEEKK-------KAEELKKAEEENKI 1730
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19421557   190 PVEKKKKGKRKSETTVESLELDQGLTNPSLRSPEESTESTDSQKRRSGRQVKRRKYNEDLDFKVVDD 256
Cdd:PTZ00121 1731 KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
115-289 2.44e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 43.10  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  115 KPKRKREPKEPKEPRKAEEPKKAKEHKEPKQKDGAKKARKPREASGTKEAKEKRSCTDSAARTKSRKASKEQGPTPVEKK 194
Cdd:COG3064   88 EAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAA 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  195 KKGKRKSETTVESLELDQGLTNPSLRSPEESTESTDSQKRRSGRQVKRRKYNEDLDFKVVDDDGETIAVLGAGRTSALSA 274
Cdd:COG3064  168 AAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGG 247
                        170
                 ....*....|....*
gi 19421557  275 STLAWQAEEPPEDDA 289
Cdd:COG3064  248 AEEAADLAAVGVLGA 262
CHROMO smart00298
Chromatin organization modifier domain;
292-354 2.66e-03

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 37.96  E-value: 2.66e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19421557     292 IEKILASKTVQEvhpGEppfdlELFYVKYRNFSYLHCKWATMEELEKDPRiaqKIKRFRNKQA 354
Cdd:smart00298    4 VEKILDHRWKKK---GE-----LEYLVKWKGYSYSEDTWEPEENLLNCSK---KLDNYKKKER 55
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
102-186 3.35e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 42.53  E-value: 3.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557    102 QEGAAKGSKDREPKPKRKREPK---EPKEPRKAEEPK-KAKEHKEPKQKDGAKKARKPREASGTKEAKEKRSCTDSAART 177
Cdd:TIGR02794  159 KAAAEAKKKAEEAKKKAEAEAKakaEAEAKAKAEEAKaKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIF 238

                   ....*....
gi 19421557    178 KSRKASKEQ 186
Cdd:TIGR02794  239 GLASGSNAE 247
PTZ00121 PTZ00121
MAEBL; Provisional
63-267 3.46e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557    63 EEEAATLFPRKMTSHNGMEDSGGGGTGVKKKRKKKEPGDQ-----EGAAKGSKDREPKPKRKR----EPKEPKEPRKAEE 133
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakkaeEAKIKAEELKKAEEEKKKveqlKKKEAEEKKKAEE 1651
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   134 PKKAKEHKEPKQKDGAKKA----RKPREASGTKEAKEKRSCTDSAARTKSRKASKEQGPTPVEKKKKGKRKSETTVESLE 209
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAKKAeedkKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIK 1731
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19421557   210 LDQgltnpSLRSPEESTESTDSQKRRSGRQVKRRKYNEDLDFKVVDDDGETIAVLGAG 267
Cdd:PTZ00121 1732 AEE-----AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
101-185 3.50e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 42.14  E-value: 3.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557    101 DQEGAAKGSKDREPKPKRKREPKEPKEPRKAEEPKKAKEHKEPKQK-DGAKKARKPREASGTKEAKEKRSCTDSAARTKs 179
Cdd:TIGR02794  100 AEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKeEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE- 178

                   ....*.
gi 19421557    180 RKASKE 185
Cdd:TIGR02794  179 AKAKAE 184
RNA_polI_A34 pfam08208
DNA-directed RNA polymerase I subunit RPA34.5; This is a family of proteins conserved from ...
109-185 3.86e-03

DNA-directed RNA polymerase I subunit RPA34.5; This is a family of proteins conserved from yeasts to human. Subunit A34.5 of RNA polymerase I is a non-essential subunit which is thought to help Pol I overcome topological constraints imposed on ribosomal DNA during the process of transcription.


Pssm-ID: 462395  Cd Length: 205  Bit Score: 41.21  E-value: 3.86e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19421557    109 SKDREPKPKRKREPKEPKEPRKAEEPKKAKE--HKEPKQKDGAKKARKPREASGTKEAKEKRSctdsaarTKSRKASKE 185
Cdd:pfam08208  134 SEESEGEEEKRKVPAAKKKSKKKKKKKAETEeeEEVPKKKKKKKKKKKEKKEPEKKEKKEKKS-------KKSKKEKKK 205
PTZ00121 PTZ00121
MAEBL; Provisional
106-185 4.92e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 4.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   106 AKGSKDREPKPKRKREPKEPKEP--RKAEEPKKAKE---HKEPKQKDGAKKARKPREASGTKEAKEKRSCTDSAARTKSR 180
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAakKKAEEAKKAAEaakAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390

                  ....*
gi 19421557   181 KASKE 185
Cdd:PTZ00121 1391 KKADE 1395
PTZ00121 PTZ00121
MAEBL; Provisional
105-249 5.49e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 5.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   105 AAKGSKDREPKPKRKREPKEPKEPRKAEEPKKAKEHKEpKQKDGAKKARKPREA-SGTKEAKEKRSCTDsaARTKSRKAS 183
Cdd:PTZ00121 1420 ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK-KAEEAKKKAEEAKKAdEAKKKAEEAKKADE--AKKKAEEAK 1496
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19421557   184 KEqgptpVEKKKKGKRKSETTVESLELDQGLTNPSLRSPEESTESTDSQKRRSGRQVKRRKYNEDL 249
Cdd:PTZ00121 1497 KK-----ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
PTZ00121 PTZ00121
MAEBL; Provisional
41-185 6.23e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 6.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557    41 DQEEKIEDVASHCLPQKDlytaEEEAAtlfpRKMTSHNGMEDSGGGGTGVKKKRKKKEPGDQEGAAKGSKDREPKPKRKR 120
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKD----AEEAK----KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA 1292
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19421557   121 EpkepkEPRKAEEPKKAKEHK---EPKQK-DGAKK----ARKPREASgTKEAKEKRScTDSAARTKSRKASKE 185
Cdd:PTZ00121 1293 D-----EAKKAEEKKKADEAKkkaEEAKKaDEAKKkaeeAKKKADAA-KKKAEEAKK-AAEAAKAEAEAAADE 1358
PTZ00121 PTZ00121
MAEBL; Provisional
103-247 6.28e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 6.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557   103 EGAAKGSKDREPKPKRKREpkepkEPRKAEEPKKAKEHK---EPKQKDGAKKARKPREASGTKEAKEKRSCTDSAARTKS 179
Cdd:PTZ00121 1143 EEARKAEDAKRVEIARKAE-----DARKAEEARKAEDAKkaeAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEA 1217
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19421557   180 RKASKEQGPTPVEKKKKGKRKSEttvESLELDQGLTNPSLRSPEESTESTDSQKRRSGRQVKRRKYNE 247
Cdd:PTZ00121 1218 RKAEDAKKAEAVKKAEEAKKDAE---EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADE 1282
CD_CMT3_like cd18635
chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier ...
374-424 8.44e-03

chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier (chromo) domain of DNA (cytosine-5)-methyltransferase chromomethylase 3 (CMT3, EC:2.1.1.37), and similar proteins. CMT3 is primarily a CHG (where H is either A, T or C) methyltransferase and is predominantly expressed in actively replicating cells. The protein is involved in preferentially methylating transposon-related sequences, reducing their mobility. Studies suggest that in order to target DNA methylation, CMT3 associates with H3K9me2-containing nucleosomes through binding of its BAH- and chromo-domains to H3K9me2. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349285  Cd Length: 57  Bit Score: 36.91  E-value: 8.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19421557  374 EVDRILEVAHTKDAETGEEVTHYLVKWCSLPYEESTWELEEDVD--PAKVKEF 424
Cdd:cd18635    3 EVEKLVGICYGDPKKTGERGLYFKVRWKGYGPEEDTWEPIEGLSncPEKIKEF 55
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
102-305 9.50e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 41.18  E-value: 9.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  102 QEGAAKGSKDREPKPKRKREPKEPKEPRKAEEPKKAKEHKEPKQKDGAKKARKPREASGTKEAKEKRSCTDSAARTKSRK 181
Cdd:COG3064   94 AAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAAR 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19421557  182 ASKEQGPTPVEKKKKGKRKSETTVESLELDQGLTNPSLRSPEESTESTDSQKRRSGRQVKRRKYNEDLDFKVVDDDGETI 261
Cdd:COG3064  174 AAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAAD 253
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 19421557  262 AVLGAGRTSALSASTLAWQAEEPPEDDANIIEKILASKTVQEVH 305
Cdd:COG3064  254 LAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVL 297
 
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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