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Conserved domains on  [gi|19114386|ref|NP_593474|]
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transcription factor TFIIH complex ERCC-3 subunit Ptr8 [Schizosaccharomyces pombe]

Protein Classification

rad25 family protein( domain architecture ID 11489419)

rad25 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
rad25 TIGR00603
DNA repair helicase rad25; All proteins in this family for which functions are known are ...
75-797 0e+00

DNA repair helicase rad25; All proteins in this family for which functions are known are DNA-DNA helicases used for the initiation of nucleotide excision repair and transacription as part of the TFIIH complex.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


:

Pssm-ID: 273168 [Multi-domain]  Cd Length: 732  Bit Score: 1322.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386    75 DFSNLLGLKLDHTARPLWINPiDGRIILEAFSPLAEQAIDFLVTISEPVSRPAFIHEYRITAYSLYAAVSVGLKTEDIIA 154
Cdd:TIGR00603   1 DYSKQLELKPDHGSRPLWVAP-DGHIFLESFSPLYKQAQDFLVAIAEPVCRPEHIHEYKLTAYSLYAAVSVGLETEDIIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   155 VLDRLSKTPIPPSIVDFIRACTVSYGKVKLVLKKNRYFIESGDASVLRLLLRDPVIGPLRIDYSTQSSKQKSSKPSNEDN 234
Cdd:TIGR00603  80 VLGRLSKTPIPKGIIEFIRLCTQSYGKVKLVLKHNRYFVESPHPEVLQRLLKDPVIAPCRIDPTEEESLQTPTYGSKEDF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   235 VEDKKDITNDSSKETAEKSSSDELFSAVVG----LQEEEDDED---AVHLFEIKHSSVETIKKRCAEIDYPLLEEYDFRN 307
Cdd:TIGR00603 160 IINKPGFTGGASAGQLEANQGESAVPKDIAdfyeLEEEEEDEDeetATHSFEIDQEQVEEVKKRCIELDYPLLEEYDFRN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   308 DNINPDLPIDLKPSTQIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKTLVGITAACTIKKSVIVLCTSSVSVMQWRQQFL 387
Cdd:TIGR00603 240 DTVNPDLNIDLKPTTQIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKSLVGVTAACTVKKSCLVLCTSAVSVEQWKQQFK 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   388 QWSNIKPDHIAVFTADHKERFHSEAGVVVSTYSMVANTRNRSYDSQKMMDFLTGREWGFILLDEVHVVPAAMFRRVVTTI 467
Cdd:TIGR00603 320 MWSTIDDSQICRFTSDAKERFHGEAGVVVSTYSMVAHTGKRSYESEKVMEWLTNREWGLILLDEVHVVPAAMFRRVLTIV 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   468 AAHTKLGLTATLVREDDKIDDLNFLIGPKMYEANWMDLAQKGHIAKVQCAEVWCAMTTEFYNEYLRENSRKRMLLYIMNP 547
Cdd:TIGR00603 400 QAHCKLGLTATLVREDDKITDLNFLIGPKLYEANWMELQKKGFIANVQCAEVWCPMTPEFYREYLRENSRKRMLLYVMNP 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   548 KKFQACQFLIDYHEKRGDKIIVFSDNVYALRAYAIKLGKYFIYGGTPQQERMRILENFQYNELVNTIFLSKVGDTSIDLP 627
Cdd:TIGR00603 480 NKFRACQFLIRFHEQRGDKIIVFSDNVFALKEYAIKLGKPFIYGPTSQQERMQILQNFQHNPKVNTIFLSKVGDTSIDLP 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   628 EATCLIQISSHYGSRRQEAQRLGRILRAKRRND-EGFNAFFYSLVSKDTQEMYYSSKRQAFLIDQGYAFKVITNLKGMEN 706
Cdd:TIGR00603 560 EANVLIQISSHYGSRRQEAQRLGRILRAKKGSDaEEYNAFFYSLVSKDTQEMYYSTKRQRFLVDQGYSFKVITHLPGMDN 639
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   707 LPNLAYASKAERLELLQEVLLQNEEAADLDDGED-----TSFGSRSLSRAPAKAKRSSGSLSTLAGADNMAYVEYNKSAN 781
Cdd:TIGR00603 640 ESNLAYSSKEEQLELLQKVLLAGDLDAELEVLEGefgsrALGASRSMSSASGKAVRRGGSLSSLSGGDDMAYMEYRKPAI 719
                         730
                  ....*....|....*.
gi 19114386   782 kqlKKDSKEHHALFRK 797
Cdd:TIGR00603 720 ---KKSKKEVHPLFKK 732
 
Name Accession Description Interval E-value
rad25 TIGR00603
DNA repair helicase rad25; All proteins in this family for which functions are known are ...
75-797 0e+00

DNA repair helicase rad25; All proteins in this family for which functions are known are DNA-DNA helicases used for the initiation of nucleotide excision repair and transacription as part of the TFIIH complex.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273168 [Multi-domain]  Cd Length: 732  Bit Score: 1322.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386    75 DFSNLLGLKLDHTARPLWINPiDGRIILEAFSPLAEQAIDFLVTISEPVSRPAFIHEYRITAYSLYAAVSVGLKTEDIIA 154
Cdd:TIGR00603   1 DYSKQLELKPDHGSRPLWVAP-DGHIFLESFSPLYKQAQDFLVAIAEPVCRPEHIHEYKLTAYSLYAAVSVGLETEDIIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   155 VLDRLSKTPIPPSIVDFIRACTVSYGKVKLVLKKNRYFIESGDASVLRLLLRDPVIGPLRIDYSTQSSKQKSSKPSNEDN 234
Cdd:TIGR00603  80 VLGRLSKTPIPKGIIEFIRLCTQSYGKVKLVLKHNRYFVESPHPEVLQRLLKDPVIAPCRIDPTEEESLQTPTYGSKEDF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   235 VEDKKDITNDSSKETAEKSSSDELFSAVVG----LQEEEDDED---AVHLFEIKHSSVETIKKRCAEIDYPLLEEYDFRN 307
Cdd:TIGR00603 160 IINKPGFTGGASAGQLEANQGESAVPKDIAdfyeLEEEEEDEDeetATHSFEIDQEQVEEVKKRCIELDYPLLEEYDFRN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   308 DNINPDLPIDLKPSTQIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKTLVGITAACTIKKSVIVLCTSSVSVMQWRQQFL 387
Cdd:TIGR00603 240 DTVNPDLNIDLKPTTQIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKSLVGVTAACTVKKSCLVLCTSAVSVEQWKQQFK 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   388 QWSNIKPDHIAVFTADHKERFHSEAGVVVSTYSMVANTRNRSYDSQKMMDFLTGREWGFILLDEVHVVPAAMFRRVVTTI 467
Cdd:TIGR00603 320 MWSTIDDSQICRFTSDAKERFHGEAGVVVSTYSMVAHTGKRSYESEKVMEWLTNREWGLILLDEVHVVPAAMFRRVLTIV 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   468 AAHTKLGLTATLVREDDKIDDLNFLIGPKMYEANWMDLAQKGHIAKVQCAEVWCAMTTEFYNEYLRENSRKRMLLYIMNP 547
Cdd:TIGR00603 400 QAHCKLGLTATLVREDDKITDLNFLIGPKLYEANWMELQKKGFIANVQCAEVWCPMTPEFYREYLRENSRKRMLLYVMNP 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   548 KKFQACQFLIDYHEKRGDKIIVFSDNVYALRAYAIKLGKYFIYGGTPQQERMRILENFQYNELVNTIFLSKVGDTSIDLP 627
Cdd:TIGR00603 480 NKFRACQFLIRFHEQRGDKIIVFSDNVFALKEYAIKLGKPFIYGPTSQQERMQILQNFQHNPKVNTIFLSKVGDTSIDLP 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   628 EATCLIQISSHYGSRRQEAQRLGRILRAKRRND-EGFNAFFYSLVSKDTQEMYYSSKRQAFLIDQGYAFKVITNLKGMEN 706
Cdd:TIGR00603 560 EANVLIQISSHYGSRRQEAQRLGRILRAKKGSDaEEYNAFFYSLVSKDTQEMYYSTKRQRFLVDQGYSFKVITHLPGMDN 639
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   707 LPNLAYASKAERLELLQEVLLQNEEAADLDDGED-----TSFGSRSLSRAPAKAKRSSGSLSTLAGADNMAYVEYNKSAN 781
Cdd:TIGR00603 640 ESNLAYSSKEEQLELLQKVLLAGDLDAELEVLEGefgsrALGASRSMSSASGKAVRRGGSLSSLSGGDDMAYMEYRKPAI 719
                         730
                  ....*....|....*.
gi 19114386   782 kqlKKDSKEHHALFRK 797
Cdd:TIGR00603 720 ---KKSKKEVHPLFKK 732
ERCC3_RAD25_C pfam16203
ERCC3/RAD25/XPB C-terminal helicase; This is the C-terminal helicase domain of ERCC3, RAD25 ...
505-747 3.20e-174

ERCC3/RAD25/XPB C-terminal helicase; This is the C-terminal helicase domain of ERCC3, RAD25 and XPB helicases.


Pssm-ID: 406585  Cd Length: 248  Bit Score: 500.98  E-value: 3.20e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   505 LAQKGHIAKVQCAEVWCAMTTEFYNEYLRENSRKRMLLYIMNPKKFQACQFLIDYHEKRGDKIIVFSDNVYALRAYAIKL 584
Cdd:pfam16203   1 LQEKGHIANVQCAEVWCPMTAEFYREYLRSKSRKKRLLYVMNPNKFRACQFLIRYHERRGDKIIVFSDNVFALKEYAKKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   585 GKYFIYGGTPQQERMRILENFQYNELVNTIFLSKVGDTSIDLPEATCLIQISSHYGSRRQEAQRLGRILRAKRR-NDEGF 663
Cdd:pfam16203  81 NKPYIYGGTSQAERMRILQNFKHNPNVNTIFLSKVGDTSIDLPEANVLIQISSHFGSRRQEAQRLGRILRAKRRsNDEGF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   664 NAFFYSLVSKDTQEMYYSSKRQAFLIDQGYAFKVITNLKGMENLPNLAYASKAERLELLQEVLLQNEEAADLDDGEDTSF 743
Cdd:pfam16203 161 NAFFYSLVSKDTQEMYYSTKRQQFLVDQGYAFKVITNLAGMEDEENLAYSTKEEQLELLQKVLAANDTDAEEEVIADDLG 240

                  ....
gi 19114386   744 GSRS 747
Cdd:pfam16203 241 KDRK 244
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
316-485 1.23e-113

DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 341.97  E-value: 1.23e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 316 IDLKPSTQIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKTLVGITAACTIKKSVIVLCTSSVSVMQWRQQFLQWSNIKPD 395
Cdd:cd18029   1 IDLKPSTQLRPYQEKALSKMFGNGRARSGVIVLPCGAGKTLVGITAACTIKKSTLVLCTSAVSVEQWRRQFLDWTTIDDE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 396 HIAVFTADHKERFHsEAGVVVSTYSMVANTRNRSYDSQKMMDFLTGREWGFILLDEVHVVPAAMFRRVVTTIAAHTKLGL 475
Cdd:cd18029  81 QIGRFTSDKKEIFP-EAGVTVSTYSMLANTRKRSPESEKFMEFITEREWGLIILDEVHVVPAPMFRRVLTLQKAHCKLGL 159
                       170
                ....*....|
gi 19114386 476 TATLVREDDK 485
Cdd:cd18029 160 TATLVREDDK 169
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
323-740 3.05e-55

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 200.25  E-value: 3.05e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 323 QIRPYQEKSLSKMFGNGRA--RSGIIVLPCGAGKTLVGITAACTI--KKSVIVLCTSSVSVMQWRQQFLQWsnikpDHIA 398
Cdd:COG1061  80 ELRPYQQEALEALLAALERggGRGLVVAPTGTGKTVLALALAAELlrGKRVLVLVPRRELLEQWAEELRRF-----LGDP 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 399 VFTADHKERfhsEAGVVVSTYSMVANtrnrsydsqKMMDFLTGREWGFILLDEVHVVPAAMFRRVVTTIAAHTKLGLTAT 478
Cdd:COG1061 155 LAGGGKKDS---DAPITVATYQSLAR---------RAHLDELGDRFGLVIIDEAHHAGAPSYRRILEAFPAAYRLGLTAT 222
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 479 LVREDDKIDDLNFLIGPKmYEANWMDLAQKGHIAKVQCAEVWCAMTTEFyNEYLRENSRKRMLLYIMNPKKFQACQFLID 558
Cdd:COG1061 223 PFRSDGREILLFLFDGIV-YEYSLKEAIEDGYLAPPEYYGIRVDLTDER-AEYDALSERLREALAADAERKDKILRELLR 300
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 559 YHeKRGDKIIVFSDNVYALRAYAIKLGK-----YFIYGGTPQQERMRILENFQYNELvNTIFLSKVGDTSIDLPEATCLI 633
Cdd:COG1061 301 EH-PDDRKTLVFCSSVDHAEALAELLNEagiraAVVTGDTPKKEREEILEAFRDGEL-RILVTVDVLNEGVDVPRLDVAI 378
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 634 QISSHyGSRRQEAQRLGRILRAKRRNDEgfnAFFYSLVSKDTQEMYYSSKRQAFLIDQGYAFKVITNLKGMENLPNLAYA 713
Cdd:COG1061 379 LLRPT-GSPREFIQRLGRGLRPAPGKED---ALVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPA 454
                       410       420
                ....*....|....*....|....*..
gi 19114386 714 SKAERLELLQEVLLQNEEAADLDDGED 740
Cdd:COG1061 455 LEVKGELEEELLEELELLEDALLLVLA 481
DEXDc smart00487
DEAD-like helicases superfamily;
316-491 8.97e-20

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 88.32  E-value: 8.97e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386    316 IDLKPSTQIRPYQEKSLSKMFGNGRarSGIIVLPCGAGKTLVGITAA-----CTIKKSVIVLCTSSVSVMQWRQQFLQWS 390
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLR--DVILAAPTGSGKTLAALLPAlealkRGKGGRVLVLVPTRELAEQWAEELKKLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386    391 NIKPDHIAVFT------ADHKERFHSEAGVVVSTYSMVANtrnrsydsQKMMDFLTGREWGFILLDEVHVVPAAMFRRVV 464
Cdd:smart00487  79 PSLGLKVVGLYggdskrEQLRKLESGKTDILVTTPGRLLD--------LLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150
                          170       180       190
                   ....*....|....*....|....*....|..
gi 19114386    465 TTIAAHTK-----LGLTATLVREDDKIDDLNF 491
Cdd:smart00487 151 EKLLKLLPknvqlLLLSATPPEEIENLLELFL 182
PRK13766 PRK13766
Hef nuclease; Provisional
318-455 9.10e-03

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 39.47  E-value: 9.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386  318 LKPST-QIRPYQEKslskMFGNGRARSGIIVLPCGAGKTLVGI-TAACTIKKS---VIVLCTSSVSVMQWRQQFLQWSNI 392
Cdd:PRK13766   9 IKPNTiEARLYQQL----LAATALKKNTLVVLPTGLGKTAIALlVIAERLHKKggkVLILAPTKPLVEQHAEFFRKFLNI 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19114386  393 KPDHIAVFT-----ADHKERFhSEAGVVVSTYSMVANtrnrsydsqkmmDFLTGRewgfILLDEV-HVV 455
Cdd:PRK13766  85 PEEKIVVFTgevspEKRAELW-EKAKVIVATPQVIEN------------DLIAGR----ISLEDVsLLI 136
 
Name Accession Description Interval E-value
rad25 TIGR00603
DNA repair helicase rad25; All proteins in this family for which functions are known are ...
75-797 0e+00

DNA repair helicase rad25; All proteins in this family for which functions are known are DNA-DNA helicases used for the initiation of nucleotide excision repair and transacription as part of the TFIIH complex.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273168 [Multi-domain]  Cd Length: 732  Bit Score: 1322.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386    75 DFSNLLGLKLDHTARPLWINPiDGRIILEAFSPLAEQAIDFLVTISEPVSRPAFIHEYRITAYSLYAAVSVGLKTEDIIA 154
Cdd:TIGR00603   1 DYSKQLELKPDHGSRPLWVAP-DGHIFLESFSPLYKQAQDFLVAIAEPVCRPEHIHEYKLTAYSLYAAVSVGLETEDIIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   155 VLDRLSKTPIPPSIVDFIRACTVSYGKVKLVLKKNRYFIESGDASVLRLLLRDPVIGPLRIDYSTQSSKQKSSKPSNEDN 234
Cdd:TIGR00603  80 VLGRLSKTPIPKGIIEFIRLCTQSYGKVKLVLKHNRYFVESPHPEVLQRLLKDPVIAPCRIDPTEEESLQTPTYGSKEDF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   235 VEDKKDITNDSSKETAEKSSSDELFSAVVG----LQEEEDDED---AVHLFEIKHSSVETIKKRCAEIDYPLLEEYDFRN 307
Cdd:TIGR00603 160 IINKPGFTGGASAGQLEANQGESAVPKDIAdfyeLEEEEEDEDeetATHSFEIDQEQVEEVKKRCIELDYPLLEEYDFRN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   308 DNINPDLPIDLKPSTQIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKTLVGITAACTIKKSVIVLCTSSVSVMQWRQQFL 387
Cdd:TIGR00603 240 DTVNPDLNIDLKPTTQIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKSLVGVTAACTVKKSCLVLCTSAVSVEQWKQQFK 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   388 QWSNIKPDHIAVFTADHKERFHSEAGVVVSTYSMVANTRNRSYDSQKMMDFLTGREWGFILLDEVHVVPAAMFRRVVTTI 467
Cdd:TIGR00603 320 MWSTIDDSQICRFTSDAKERFHGEAGVVVSTYSMVAHTGKRSYESEKVMEWLTNREWGLILLDEVHVVPAAMFRRVLTIV 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   468 AAHTKLGLTATLVREDDKIDDLNFLIGPKMYEANWMDLAQKGHIAKVQCAEVWCAMTTEFYNEYLRENSRKRMLLYIMNP 547
Cdd:TIGR00603 400 QAHCKLGLTATLVREDDKITDLNFLIGPKLYEANWMELQKKGFIANVQCAEVWCPMTPEFYREYLRENSRKRMLLYVMNP 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   548 KKFQACQFLIDYHEKRGDKIIVFSDNVYALRAYAIKLGKYFIYGGTPQQERMRILENFQYNELVNTIFLSKVGDTSIDLP 627
Cdd:TIGR00603 480 NKFRACQFLIRFHEQRGDKIIVFSDNVFALKEYAIKLGKPFIYGPTSQQERMQILQNFQHNPKVNTIFLSKVGDTSIDLP 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   628 EATCLIQISSHYGSRRQEAQRLGRILRAKRRND-EGFNAFFYSLVSKDTQEMYYSSKRQAFLIDQGYAFKVITNLKGMEN 706
Cdd:TIGR00603 560 EANVLIQISSHYGSRRQEAQRLGRILRAKKGSDaEEYNAFFYSLVSKDTQEMYYSTKRQRFLVDQGYSFKVITHLPGMDN 639
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   707 LPNLAYASKAERLELLQEVLLQNEEAADLDDGED-----TSFGSRSLSRAPAKAKRSSGSLSTLAGADNMAYVEYNKSAN 781
Cdd:TIGR00603 640 ESNLAYSSKEEQLELLQKVLLAGDLDAELEVLEGefgsrALGASRSMSSASGKAVRRGGSLSSLSGGDDMAYMEYRKPAI 719
                         730
                  ....*....|....*.
gi 19114386   782 kqlKKDSKEHHALFRK 797
Cdd:TIGR00603 720 ---KKSKKEVHPLFKK 732
ERCC3_RAD25_C pfam16203
ERCC3/RAD25/XPB C-terminal helicase; This is the C-terminal helicase domain of ERCC3, RAD25 ...
505-747 3.20e-174

ERCC3/RAD25/XPB C-terminal helicase; This is the C-terminal helicase domain of ERCC3, RAD25 and XPB helicases.


Pssm-ID: 406585  Cd Length: 248  Bit Score: 500.98  E-value: 3.20e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   505 LAQKGHIAKVQCAEVWCAMTTEFYNEYLRENSRKRMLLYIMNPKKFQACQFLIDYHEKRGDKIIVFSDNVYALRAYAIKL 584
Cdd:pfam16203   1 LQEKGHIANVQCAEVWCPMTAEFYREYLRSKSRKKRLLYVMNPNKFRACQFLIRYHERRGDKIIVFSDNVFALKEYAKKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   585 GKYFIYGGTPQQERMRILENFQYNELVNTIFLSKVGDTSIDLPEATCLIQISSHYGSRRQEAQRLGRILRAKRR-NDEGF 663
Cdd:pfam16203  81 NKPYIYGGTSQAERMRILQNFKHNPNVNTIFLSKVGDTSIDLPEANVLIQISSHFGSRRQEAQRLGRILRAKRRsNDEGF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   664 NAFFYSLVSKDTQEMYYSSKRQAFLIDQGYAFKVITNLKGMENLPNLAYASKAERLELLQEVLLQNEEAADLDDGEDTSF 743
Cdd:pfam16203 161 NAFFYSLVSKDTQEMYYSTKRQQFLVDQGYAFKVITNLAGMEDEENLAYSTKEEQLELLQKVLAANDTDAEEEVIADDLG 240

                  ....
gi 19114386   744 GSRS 747
Cdd:pfam16203 241 KDRK 244
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
316-485 1.23e-113

DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 341.97  E-value: 1.23e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 316 IDLKPSTQIRPYQEKSLSKMFGNGRARSGIIVLPCGAGKTLVGITAACTIKKSVIVLCTSSVSVMQWRQQFLQWSNIKPD 395
Cdd:cd18029   1 IDLKPSTQLRPYQEKALSKMFGNGRARSGVIVLPCGAGKTLVGITAACTIKKSTLVLCTSAVSVEQWRRQFLDWTTIDDE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 396 HIAVFTADHKERFHsEAGVVVSTYSMVANTRNRSYDSQKMMDFLTGREWGFILLDEVHVVPAAMFRRVVTTIAAHTKLGL 475
Cdd:cd18029  81 QIGRFTSDKKEIFP-EAGVTVSTYSMLANTRKRSPESEKFMEFITEREWGLIILDEVHVVPAPMFRRVLTLQKAHCKLGL 159
                       170
                ....*....|
gi 19114386 476 TATLVREDDK 485
Cdd:cd18029 160 TATLVREDDK 169
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
516-671 9.57e-89

C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase 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: 350176 [Multi-domain]  Cd Length: 153  Bit Score: 276.44  E-value: 9.57e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 516 CAEVWCAMTTEFYNEYLR-ENSRKRMLLYIMNPKKFQACQFLIDYHEKrGDKIIVFSDNVYALRAYAIKLGKYFIYGGTP 594
Cdd:cd18789   1 CAEIRCPMTPEFYREYLGlGAHRKRRLLAAMNPNKLRALEELLKRHEQ-GDKIIVFTDNVEALYRYAKRLLKPFITGETP 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19114386 595 QQERMRILENFQYNElVNTIFLSKVGDTSIDLPEATCLIQISSHYGSRRQEAQRLGRILRAKRRNdeGFNAFFYSLV 671
Cdd:cd18789  80 QSEREEILQNFREGE-YNTLVVSKVGDEGIDLPEANVAIQISGHGGSRRQEAQRLGRILRPKKGG--GKNAFFYSLV 153
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
323-740 3.05e-55

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 200.25  E-value: 3.05e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 323 QIRPYQEKSLSKMFGNGRA--RSGIIVLPCGAGKTLVGITAACTI--KKSVIVLCTSSVSVMQWRQQFLQWsnikpDHIA 398
Cdd:COG1061  80 ELRPYQQEALEALLAALERggGRGLVVAPTGTGKTVLALALAAELlrGKRVLVLVPRRELLEQWAEELRRF-----LGDP 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 399 VFTADHKERfhsEAGVVVSTYSMVANtrnrsydsqKMMDFLTGREWGFILLDEVHVVPAAMFRRVVTTIAAHTKLGLTAT 478
Cdd:COG1061 155 LAGGGKKDS---DAPITVATYQSLAR---------RAHLDELGDRFGLVIIDEAHHAGAPSYRRILEAFPAAYRLGLTAT 222
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 479 LVREDDKIDDLNFLIGPKmYEANWMDLAQKGHIAKVQCAEVWCAMTTEFyNEYLRENSRKRMLLYIMNPKKFQACQFLID 558
Cdd:COG1061 223 PFRSDGREILLFLFDGIV-YEYSLKEAIEDGYLAPPEYYGIRVDLTDER-AEYDALSERLREALAADAERKDKILRELLR 300
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 559 YHeKRGDKIIVFSDNVYALRAYAIKLGK-----YFIYGGTPQQERMRILENFQYNELvNTIFLSKVGDTSIDLPEATCLI 633
Cdd:COG1061 301 EH-PDDRKTLVFCSSVDHAEALAELLNEagiraAVVTGDTPKKEREEILEAFRDGEL-RILVTVDVLNEGVDVPRLDVAI 378
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 634 QISSHyGSRRQEAQRLGRILRAKRRNDEgfnAFFYSLVSKDTQEMYYSSKRQAFLIDQGYAFKVITNLKGMENLPNLAYA 713
Cdd:COG1061 379 LLRPT-GSPREFIQRLGRGLRPAPGKED---ALVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPA 454
                       410       420
                ....*....|....*....|....*..
gi 19114386 714 SKAERLELLQEVLLQNEEAADLDDGED 740
Cdd:COG1061 455 LEVKGELEEELLEELELLEDALLLVLA 481
Helicase_C_3 pfam13625
Helicase conserved C-terminal domain; This domain family is found in a wide variety of ...
91-215 4.74e-45

Helicase conserved C-terminal domain; This domain family is found in a wide variety of helicases and helicase-related proteins.


Pssm-ID: 463939 [Multi-domain]  Cd Length: 121  Bit Score: 157.66  E-value: 4.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386    91 LWINPiDGRIILEAfsPLAEQAIDFLVTISEPVSRpAFIHEYRITAYSLYAAVSVGLKTEDIIAVLDRLSKTPIPPSIVD 170
Cdd:pfam13625   1 LIVQA-DLTILLPG--PLAPEARDFLAAFAELESR-GHAHTYRLTPLSLRRALDAGLTAEDILDFLERHSKYPVPQALEY 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 19114386   171 FIRACTVSYGKVKLVLkKNRYFIESGDASVLRLLLRDPVIGPLRI 215
Cdd:pfam13625  77 LIRDVARRHGRLRLGL-GASSYLRSDDPAVLAELLADPRIAPLGL 120
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
325-479 1.54e-28

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: 111.63  E-value: 1.54e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 325 RPYQEKSLSKMFGNGRARSGIIVLPCGAGKTLVGITAACTIKK-SVIVLCTSSVSVMQWRQQFLQWSNIKPDHIavFTAD 403
Cdd:cd17926   2 RPYQEEALEAWLAHKNNRRGILVLPTGSGKTLTALALIAYLKElRTLIVVPTDALLDQWKERFEDFLGDSSIGL--IGGG 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114386 404 HKERFhSEAGVVVSTYSMVANTRNRSYDSQKmmdfltgrEWGFILLDEVHVVPAAMFRRVVTTIAAHTKLGLTATL 479
Cdd:cd17926  80 KKKDF-DDANVVVATYQSLSNLAEEEKDLFD--------QFGLLIVDEAHHLPAKTFSEILKELNAKYRLGLTATP 146
DEXDc smart00487
DEAD-like helicases superfamily;
316-491 8.97e-20

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 88.32  E-value: 8.97e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386    316 IDLKPSTQIRPYQEKSLSKMFGNGRarSGIIVLPCGAGKTLVGITAA-----CTIKKSVIVLCTSSVSVMQWRQQFLQWS 390
Cdd:smart00487   1 IEKFGFEPLRPYQKEAIEALLSGLR--DVILAAPTGSGKTLAALLPAlealkRGKGGRVLVLVPTRELAEQWAEELKKLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386    391 NIKPDHIAVFT------ADHKERFHSEAGVVVSTYSMVANtrnrsydsQKMMDFLTGREWGFILLDEVHVVPAAMFRRVV 464
Cdd:smart00487  79 PSLGLKVVGLYggdskrEQLRKLESGKTDILVTTPGRLLD--------LLENDKLSLSNVDLVILDEAHRLLDGGFGDQL 150
                          170       180       190
                   ....*....|....*....|....*....|..
gi 19114386    465 TTIAAHTK-----LGLTATLVREDDKIDDLNF 491
Cdd:smart00487 151 EKLLKLLPknvqlLLLSATPPEEIENLLELFL 182
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
312-687 2.31e-17

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 86.82  E-value: 2.31e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 312 PDLPIDLKpsTQIRPYQEKSLSKMFGNGRARSGII----VlpcGAGKTLVGITAACTIK-----KSVIVLCTSSVsVMQW 382
Cdd:COG0553 232 ESLPAGLK--ATLRPYQLEGAAWLLFLRRLGLGGLladdM---GLGKTIQALALLLELKerglaRPVLIVAPTSL-VGNW 305
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 383 RQQFLQWSnikPD-HIAVFTAD----HKERFHSEAGVVVSTYSMVAntRNRsydsqkmmDFLTGREWGFILLDEVHVV-- 455
Cdd:COG0553 306 QRELAKFA---PGlRVLVLDGTreraKGANPFEDADLVITSYGLLR--RDI--------ELLAAVDWDLVILDEAQHIkn 372
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 456 PAAMFRRVVTTIAAHTKLGLTAT-----------------------------------LVREDDKIDDLNFLIGPKMyea 500
Cdd:COG0553 373 PATKRAKAVRALKARHRLALTGTpvenrleelwslldflnpgllgslkafrerfarpiEKGDEEALERLRRLLRPFL--- 449
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 501 nwmdLA-QKGHIAK----VQCAEVWCAMTTE---FYNEYL---------RENSRKRML----------------LYIMNP 547
Cdd:COG0553 450 ----LRrTKEDVLKdlpeKTEETLYVELTPEqraLYEAVLeylrrelegAEGIRRRGLilaaltrlrqicshpaLLLEEG 525
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 548 K-------KFQACQFLIDYHEKRGDKIIVFSDNV-------YALRAYAIKLgkYFIYGGTPQQERMRILENFQYNELVNT 613
Cdd:COG0553 526 AelsgrsaKLEALLELLEELLAEGEKVLVFSQFTdtldlleERLEERGIEY--AYLHGGTSAEERDELVDRFQEGPEAPV 603
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 614 IFLS-KVGDTSIDLPEATCLIqissHYG-----SRrqEAQRLGRILR--AKRrndegfNAFFYSLVSKDTQEMY----YS 681
Cdd:COG0553 604 FLISlKAGGEGLNLTAADHVI----HYDlwwnpAV--EEQAIDRAHRigQTR------DVQVYKLVAEGTIEEKilelLE 671

                ....*.
gi 19114386 682 SKRQAF 687
Cdd:COG0553 672 EKRALA 677
ResIII pfam04851
Type III restriction enzyme, res subunit;
323-481 6.56e-17

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 78.87  E-value: 6.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   323 QIRPYQE---KSLSKMFGNGRARsGIIVLPCGAGKTLVGITAACTIKKS-----VIVLCTSSVSVMQWRQQFLQWSNIKP 394
Cdd:pfam04851   3 ELRPYQIeaiENLLESIKNGQKR-GLIVMATGSGKTLTAAKLIARLFKKgpikkVLFLVPRKDLLEQALEEFKKFLPNYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   395 DHIAVFTADHKERFHSEAGVVVSTYSMVANTRNRSYDSqkmmdfLTGREWGFILLDEVHVVPAAMFRRVVTTIAAHTKLG 474
Cdd:pfam04851  82 EIGEIISGDKKDESVDDNKIVVTTIQSLYKALELASLE------LLPDFFDVIIIDEAHRSGASSYRNILEYFKPAFLLG 155

                  ....*..
gi 19114386   475 LTATLVR 481
Cdd:pfam04851 156 LTATPER 162
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
325-478 1.46e-12

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: 66.82  E-value: 1.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 325 RPYQEKSLSKMFGNGRARSGIIVLPC-GAGKTLVGITAACTIKKS------VIVLCTSSVsVMQWRQQFLQWSnikPD-H 396
Cdd:cd17919   2 RPYQLEGLNFLLELYENGPGGILADEmGLGKTLQAIAFLAYLLKEgkergpVLVVCPLSV-LENWEREFEKWT---PDlR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 397 IAVFTADHKERFH-------SEAGVVVSTYSMVantrnrsydsQKMMDFLTGREWGFILLDEVHVV--PAAMFRRVVTTI 467
Cdd:cd17919  78 VVVYHGSQRERAQirakeklDKFDVVLTTYETL----------RRDKASLRKFRWDLVVVDEAHRLknPKSQLSKALKAL 147
                       170
                ....*....|.
gi 19114386 468 AAHTKLGLTAT 478
Cdd:cd17919 148 RAKRRLLLTGT 158
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
548-656 6.02e-12

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: 63.00  E-value: 6.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   548 KKFQACQFLIDyhEKRGDKIIVFSDNVYALRA-YAIKLGKY---FIYGGTPQQERMRILENFQYNE---LVNTiflsKVG 620
Cdd:pfam00271   1 EKLEALLELLK--KERGGKVLIFSQTKKTLEAeLLLEKEGIkvaRLHGDLSQEEREEILEDFRKGKidvLVAT----DVA 74
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 19114386   621 DTSIDLPEATCLIQISSHYgSRRQEAQRLGRILRAK 656
Cdd:pfam00271  75 ERGLDLPDVDLVINYDLPW-NPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
587-656 6.29e-11

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 59.15  E-value: 6.29e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386    587 YFIYGGTPQQERMRILENFQyNELVNTIFLSKVGDTSIDLPEATCLIQISSHYgSRRQEAQRLGRILRAK 656
Cdd:smart00490  15 ARLHGGLSQEEREEILDKFN-NGKIKVLVATDVAERGLDLPGVDLVIIYDLPW-SPASYIQRIGRAGRAG 82
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
325-485 5.47e-10

DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs 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: 350790 [Multi-domain]  Cd Length: 163  Bit Score: 58.73  E-value: 5.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 325 RPYQEKSLSKM---FGNGRaRSGIIVLPCGAGKTLVGITAA-----CTIKKSVIVLCTSSVSVMQWRQQFlqwSNIKPDH 396
Cdd:cd18032   2 RYYQQEAIEALeeaREKGQ-RRALLVMATGTGKTYTAAFLIkrlleANRKKRILFLAHREELLEQAERSF---KEVLPDG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 397 -IAVFTADHKERfhSEAGVVVSTY-SMVANTRNRSYDSqkmmDFltgreWGFILLDEVHVVPAAMFRRVVTTIAAHTKLG 474
Cdd:cd18032  78 sFGNLKGGKKKP--DDARVVFATVqTLNKRKRLEKFPP----DY-----FDLIIIDEAHHAIASSYRKILEYFEPAFLLG 146
                       170
                ....*....|.
gi 19114386 475 LTATLVREDDK 485
Cdd:cd18032 147 LTATPERTDGL 157
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
351-453 2.44e-09

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: 57.99  E-value: 2.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 351 GAGKTLVGITAACTIKKS--VIVLCTSSVsVMQWRQQFLQW-SNIKPDHIAVFTADHKERFHSEAGVVVSTYSMVAntrn 427
Cdd:cd18010  26 GLGKTVQAIAIAAYYREEwpLLIVCPSSL-RLTWADEIERWlPSLPPDDIQVIVKSKDGLRDGDAKVVIVSYDLLR---- 100
                        90       100
                ....*....|....*....|....*.
gi 19114386 428 rsydsqKMMDFLTGREWGFILLDEVH 453
Cdd:cd18010 101 ------RLEKQLLARKFKVVICDESH 120
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
344-478 3.15e-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: 56.26  E-value: 3.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 344 GIIVLPCGAGKTLV-GITAAC----TIKKSVIVLCTSSVsVMQWRQQFLQWSNiKPDHIAVFTADH--KERFHSEAG--- 413
Cdd:cd00046   4 VLITAPTGSGKTLAaLLAALLlllkKGKKVLVLVPTKAL-ALQTAERLRELFG-PGIRVAVLVGGSsaEEREKNKLGdad 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114386 414 VVVSTYSMVANTRNRsydsqkmMDFLTGREWGFILLDEVHVVPAAMFRRVVTTIAAHTK-------LGLTAT 478
Cdd:cd00046  82 IIIATPDMLLNLLLR-------EDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAglknaqvILLSAT 146
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
327-478 2.52e-07

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: 53.07  E-value: 2.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   327 YQEKSLSKMFG--NGRARSGIIVLPCGAGKTLVGITAACTIKKS-------VIVLCTSSVsVMQWRQQFLQW-------- 389
Cdd:pfam00176   1 YQIEGVNWMLSleNNLGRGGILADEMGLGKTLQTISLLLYLKHVdknwggpTLIVVPLSL-LHNWMNEFERWvsppalrv 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386   390 ----SNIKPDHIAVftadHKERFHSEAGVVVSTYSMVantrnrsydsQKMMDFLTGREWGFILLDEVHVV--PAAMFRRV 463
Cdd:pfam00176  80 vvlhGNKRPQERWK----NDPNFLADFDVVITTYETL----------RKHKELLKKVHWHRIVLDEGHRLknSKSKLSKA 145
                         170
                  ....*....|....*
gi 19114386   464 VTTIAAHTKLGLTAT 478
Cdd:pfam00176 146 LKSLKTRNRWILTGT 160
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
549-654 3.29e-07

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: 50.17  E-value: 3.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 549 KFQACQFLIDYHEKRGDKIIVFSDNVYALRAYAIKLGKYF-----IYGGTPQQERMRILENFQYNELVNTIFLS-KVGDT 622
Cdd:cd18793  12 KLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGikylrLDGSTSSKERQKLVDRFNEDPDIRVFLLStKAGGV 91
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 19114386 623 SIDLPEATCLIqissHYG-----SRrqEAQRLGRILR 654
Cdd:cd18793  92 GLNLTAANRVI----LYDpwwnpAV--EEQAIDRAHR 122
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
323-478 6.98e-06

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: 47.95  E-value: 6.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 323 QIRPYQE------KSLSKM-FGngrarsGIIVLPCGAGKTLVGITAACTIKKS-----VIVLCTSSVsVMQWRQQFLQWS 390
Cdd:cd18012   4 TLRPYQKegfnwlSFLRHYgLG------GILADDMGLGKTLQTLALLLSRKEEgrkgpSLVVAPTSL-IYNWEEEAAKFA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 391 nikPD-HIAVFT-ADHKERFHSEAG---VVVSTYSMVantrnrsydsQKMMDFLTGREWGFILLDEVHVV--PAAMFRRV 463
Cdd:cd18012  77 ---PElKVLVIHgTKRKREKLRALEdydLVITSYGLL----------RRDIELLKEVKFHYLVLDEAQNIknPQTKTAKA 143
                       170
                ....*....|....*
gi 19114386 464 VTTIAAHTKLGLTAT 478
Cdd:cd18012 144 VKALKADHRLALTGT 158
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
342-478 2.13e-05

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: 46.69  E-value: 2.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 342 RSGIIVLPCGAGKTLVGITAACTiKKSVIVlCTSSVsVMQWRQQFLQwsNIKPDHIAVFTADHKER-----FHSEAGVVV 416
Cdd:cd18071  49 RGGILADDMGLGKTLTTISLILA-NFTLIV-CPLSV-LSNWETQFEE--HVKPGQLKVYTYHGGERnrdpkLLSKYDIVL 123
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19114386 417 STYSMVAntrnrSYDSQKMMDFLTGREWGFILLDEVHVV--PAAMFRRVVTTIAAHTKLGLTAT 478
Cdd:cd18071 124 TTYNTLA-----SDFGAKGDSPLHTINWLRVVLDEGHQIrnPNAQQTKAVLNLSSERRWVLTGT 182
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
322-489 2.25e-05

DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer 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: 350792 [Multi-domain]  Cd Length: 200  Bit Score: 46.11  E-value: 2.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 322 TQIRPYQEKslskMFGNGRARSGIIVLPCGAGKTLVgitAACTIK-------------KSVIVLCTSSVSVMQWRQQFLQ 388
Cdd:cd18034   1 FTPRSYQLE----LFEAALKRNTIVVLPTGSGKTLI---AVMLIKemgelnrkeknpkKRAVFLVPTVPLVAQQAEAIRS 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 389 WSNIKpdhIAVFTAD------HKERFHSE---AGVVVSTYSMVANTRNRSYDSQKMMDFLtgrewgfiLLDEVHVV---- 455
Cdd:cd18034  74 HTDLK---VGEYSGEmgvdkwTKERWKEElekYDVLVMTAQILLDALRHGFLSLSDINLL--------IFDECHHAtgdh 142
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 19114386 456 PAAMFRRVVTTIAAHTK----LGLTATLVREDDKIDDL 489
Cdd:cd18034 143 PYARIMKEFYHLEGRTSrpriLGLTASPVNGKGDPKSV 180
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
324-478 6.56e-05

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: 45.03  E-value: 6.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 324 IRPYQEKSLSKM-FGNGRARSGIIVLPCGAGKTL--VGITAACTIKKS---------VIVLCTSSVsVMQWRQ---QFLQ 388
Cdd:cd17999   1 LRPYQQEGINWLaFLNKYNLHGILCDDMGLGKTLqtLCILASDHHKRAnsfnsenlpSLVVCPPTL-VGHWVAeikKYFP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 389 WSNIKPDHIA-VFTADHKER-FHSEAGVVVSTYSMVantRNRSydsqkmmDFLTGREWGFILLDEVHVVPAAMFR--RVV 464
Cdd:cd17999  80 NAFLKPLAYVgPPQERRRLReQGEKHNVIVASYDVL---RNDI-------EVLTKIEWNYCVLDEGHIIKNSKTKlsKAV 149
                       170
                ....*....|....
gi 19114386 465 TTIAAHTKLGLTAT 478
Cdd:cd17999 150 KQLKANHRLILSGT 163
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
325-487 9.46e-05

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 45.88  E-value: 9.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 325 RPYQEKslskMFGNGRARSGIIVLPCGAGKTLVGI-TAACTIKK---SVIVLCTSSVSVMQWRQQFLQWSNIKPDHIAVF 400
Cdd:COG1111   5 RLYQLN----LAASALRKNTLVVLPTGLGKTAVALlVIAERLHKkggKVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 401 T-----ADHKERFhSEAGVVVSTYSMVANtrnrsydsqkmmDFLTGR----EWGFILLDEVHvvpaamfrRVV-----TT 466
Cdd:COG1111  81 TgevspEKRKELW-EKARIIVATPQVIEN------------DLIAGRidldDVSLLIFDEAH--------RAVgnyayVY 139
                       170       180
                ....*....|....*....|....*....
gi 19114386 467 IAAHTK--------LGLTATLVREDDKID 487
Cdd:COG1111 140 IAERYHedakdpliLGMTASPGSDEEKIE 168
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
332-453 1.13e-04

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: 44.28  E-value: 1.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 332 LSKMFGNGRArsGIIVLPCGAGKT------LVGITAACTIKKSVIVLCTSSVSVmqWRQQFLQWS---NIKPDHIAVFTA 402
Cdd:cd18001  12 LWSLHDGGKG--GILADDMGLGKTvqicafLSGMFDSGLIKSVLVVMPTSLIPH--WVKEFAKWTpglRVKVFHGTSKKE 87
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 19114386 403 DHK--ERFHSEAGVVVSTYSMVanTRNRSYDSQkmmDFLTGREWGFILLDEVH 453
Cdd:cd18001  88 RERnlERIQRGGGVLLTTYGMV--LSNTEQLSA---DDHDEFKWDYVILDEGH 135
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
351-478 4.53e-04

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: 42.28  E-value: 4.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 351 GAGKTlvgITAACTIK--------KSVIVLCTSSVsVMQWRQQFLQWSNIKPDHIAVFTADHKERFH----SEAGVVVST 418
Cdd:cd18011  27 GLGKT---IEAGLIIKelllrgdaKRVLILCPASL-VEQWQDELQDKFGLPFLILDRETAAQLRRLIgnpfEEFPIVIVS 102
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19114386 419 YSMVAntRNRSYDSQkmmdfLTGREWGFILLDEVHVVPAAMFR------RVVTTIAAHTK--LGLTAT 478
Cdd:cd18011 103 LDLLK--RSEERRGL-----LLSEEWDLVVVDEAHKLRNSGGGketkryKLGRLLAKRARhvLLLTAT 163
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
344-453 4.69e-04

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: 41.93  E-value: 4.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 344 GIIVLPCGAGKT------LVGITAACTIKKSVIVLCtsSVSVM-QWRQQFLQW--------------SNIKPDHIAVFTA 402
Cdd:cd18000  22 GILGDEMGLGKTiqiiafLAALHHSKLGLGPSLIVC--PATVLkQWVKEFHRWwppfrvvvlhssgsGTGSEEKLGSIER 99
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 19114386 403 DHK--ERFHSEAGVVVSTYSMVantrnrsydsQKMMDFLTGREWGFILLDEVH 453
Cdd:cd18000 100 KSQliRKVVGDGGILITTYEGF----------RKHKDLLLNHNWQYVILDEGH 142
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
345-486 7.93e-03

DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef 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: 350793 [Multi-domain]  Cd Length: 181  Bit Score: 38.26  E-value: 7.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 345 IIVLPCGAGKTLVGITAACTI----KKSVIVLCTSSVSVMQWRQQFLQWSNIkPDHIAVFTA----DHKERFHSEAGVVV 416
Cdd:cd18035  20 LIVLPTGLGKTIIAILVAADRltkkGGKVLILAPSRPLVEQHAENLKRVLNI-PDKITSLTGevkpEERAERWDASKIIV 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386 417 STYSMVANtrnrsydsqkmmDFLTGR----EWGFILLDEVH--------VVPAAMFRRVVTTiaaHTKLGLTATLVREDD 484
Cdd:cd18035  99 ATPQVIEN------------DLLAGRitldDVSLLIFDEAHhavgnyayVYIAHRYKREANN---PLILGLTASPGSDKE 163

                ..
gi 19114386 485 KI 486
Cdd:cd18035 164 KI 165
PRK13766 PRK13766
Hef nuclease; Provisional
318-455 9.10e-03

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 39.47  E-value: 9.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114386  318 LKPST-QIRPYQEKslskMFGNGRARSGIIVLPCGAGKTLVGI-TAACTIKKS---VIVLCTSSVSVMQWRQQFLQWSNI 392
Cdd:PRK13766   9 IKPNTiEARLYQQL----LAATALKKNTLVVLPTGLGKTAIALlVIAERLHKKggkVLILAPTKPLVEQHAEFFRKFLNI 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19114386  393 KPDHIAVFT-----ADHKERFhSEAGVVVSTYSMVANtrnrsydsqkmmDFLTGRewgfILLDEV-HVV 455
Cdd:PRK13766  85 PEEKIVVFTgevspEKRAELW-EKAKVIVATPQVIEN------------DLIAGR----ISLEDVsLLI 136
 
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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