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Conserved domains on  [gi|1370993229|emb|SPJ10783|]
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DNA repair helicase RAD25, putative [Plasmodium sp. DRC-Itaito]

Protein Classification

Ercc3/Rad25/XPB family helicase( domain architecture ID 1004556)

Ercc3/Rad25/XPB family helicase (also known as RepB/Ssl2/haywire) is a core subunit of the eukaryotic basal transcription factor complex TFIIH and is involved in nucleotide excision repair (NER) of DNA and in RNA transcription by RNA polymerase II

CATH:  3.40.50.300
EC:  3.6.4.12
Gene Ontology:  GO:0003677|GO:0003678|GO:0005524
PubMed:  8202161
SCOP:  4000282

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
rad25 super family cl36703
DNA repair helicase rad25; All proteins in this family for which functions are known are ...
94-884 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]


The actual alignment was detected with superfamily member TIGR00603:

Pssm-ID: 273168 [Multi-domain]  Cd Length: 732  Bit Score: 759.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229  94 DYSKDMKLKKNHMNKPLWICSDGFIYLEMFNSCSKQASDFLITIAEPICRPELIHEFQLTIFSLYAAISVGITLDELLIN 173
Cdd:TIGR00603   1 DYSKQLELKPDHGSRPLWVAPDGHIFLESFSPLYKQAQDFLVAIAEPVCRPEHIHEYKLTAYSLYAAVSVGLETEDIIEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 174 LDKFSKNVLPNELICNITKSAESFGKVKLVLRENKYYIEATNKSELDYLLNNDTIQNARIYSTDNnndknmislynlnnr 253
Cdd:TIGR00603  81 LGRLSKTPIPKGIIEFIRLCTQSYGKVKLVLKHNRYFVESPHPEVLQRLLKDPVIAPCRIDPTEE--------------- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 254 lldsrhrdnnkndnknnnnDNNNIEKTTSNL-LSEQQKGKDCYVTYEAPVLDTTQLGFKISESEKQLMMEEkknanlnaN 332
Cdd:TIGR00603 146 -------------------ESLQTPTYGSKEdFIINKPGFTGGASAGQLEANQGESAVPKDIADFYELEEE--------E 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 333 ENSTNSAEVYSFEVNCDKIEEVKQEALQtMQRPLLMEYDFRRDKKNPNLICSLKSHVQIRYYQEKALRKMFSNGRSRSGI 412
Cdd:TIGR00603 199 EDEDEETATHSFEIDQEQVEEVKKRCIE-LDYPLLEEYDFRNDTVNPDLNIDLKPTTQIRPYQEKSLSKMFGNGRARSGI 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 413 IVLPCGVGKTLTGITAASTIKKSALFLTTSAVAVEQWKKQFEDFTNIHPRHIRILTSDYKLDlwPINEAGVLISTYTMLS 492
Cdd:TIGR00603 278 IVLPCGAGKSLVGVTAACTVKKSCLVLCTSAVSVEQWKQQFKMWSTIDDSQICRFTSDAKER--FHGEAGVVVSTYSMVA 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 493 YSGKRSEQSLRIVNDIRRREWGLLVFDEVQFAPAPSFRRINDIVKSHCKLGLTATLVREDLLIRDLHWIIGPKLYEANWV 572
Cdd:TIGR00603 356 HTGKRSYESEKVMEWLTNREWGLILLDEVHVVPAAMFRRVLTIVQAHCKLGLTATLVREDDKITDLNFLIGPKLYEANWM 435
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 573 ELQNKGFLAKALCKEIWCSMPCSFYKYYLKSNSFIKRRLYTCNPRKLMMCEYLIKYHEQNNDKIIVFSDNIFALLHIAKT 652
Cdd:TIGR00603 436 ELQKKGFIANVQCAEVWCPMTPEFYREYLRENSRKRMLLYVMNPNKFRACQFLIRFHEQRGDKIIVFSDNVFALKEYAIK 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 653 LNKPFIYGKLSPIERIAIINKFKHDSSINTILLSKVGDNAIDIPIANVVIQISFNFASRRQEAQRLGRIIRPKNKANEKK 732
Cdd:TIGR00603 516 LGKPFIYGPTSQQERMQILQNFQHNPKVNTIFLSKVGDTSIDLPEANVLIQISSHYGSRRQEAQRLGRILRAKKGSDAEE 595
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 733 NindpDSFFYSLVSKDTIEMCYSDKRQRFLINQGYAYNVLSDNIVDFNKLNLVYKNKKIQENLLKCILASTDDGNmdedd 812
Cdd:TIGR00603 596 Y----NAFFYSLVSKDTQEMYYSTKRQRFLVDQGYSFKVITHLPGMDNESNLAYSSKEEQLELLQKVLLAGDLDA----- 666
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370993229 813 dlfEDQSFKKDNTKVNKTNSNILLNKKedslKKIDNNTGGLLKLSSNMDVTFADKKKIPTKKFADK-HILFRK 884
Cdd:TIGR00603 667 ---ELEVLEGEFGSRALGASRSMSSAS----GKAVRRGGSLSSLSGGDDMAYMEYRKPAIKKSKKEvHPLFKK 732
 
Name Accession Description Interval E-value
rad25 TIGR00603
DNA repair helicase rad25; All proteins in this family for which functions are known are ...
94-884 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: 759.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229  94 DYSKDMKLKKNHMNKPLWICSDGFIYLEMFNSCSKQASDFLITIAEPICRPELIHEFQLTIFSLYAAISVGITLDELLIN 173
Cdd:TIGR00603   1 DYSKQLELKPDHGSRPLWVAPDGHIFLESFSPLYKQAQDFLVAIAEPVCRPEHIHEYKLTAYSLYAAVSVGLETEDIIEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 174 LDKFSKNVLPNELICNITKSAESFGKVKLVLRENKYYIEATNKSELDYLLNNDTIQNARIYSTDNnndknmislynlnnr 253
Cdd:TIGR00603  81 LGRLSKTPIPKGIIEFIRLCTQSYGKVKLVLKHNRYFVESPHPEVLQRLLKDPVIAPCRIDPTEE--------------- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 254 lldsrhrdnnkndnknnnnDNNNIEKTTSNL-LSEQQKGKDCYVTYEAPVLDTTQLGFKISESEKQLMMEEkknanlnaN 332
Cdd:TIGR00603 146 -------------------ESLQTPTYGSKEdFIINKPGFTGGASAGQLEANQGESAVPKDIADFYELEEE--------E 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 333 ENSTNSAEVYSFEVNCDKIEEVKQEALQtMQRPLLMEYDFRRDKKNPNLICSLKSHVQIRYYQEKALRKMFSNGRSRSGI 412
Cdd:TIGR00603 199 EDEDEETATHSFEIDQEQVEEVKKRCIE-LDYPLLEEYDFRNDTVNPDLNIDLKPTTQIRPYQEKSLSKMFGNGRARSGI 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 413 IVLPCGVGKTLTGITAASTIKKSALFLTTSAVAVEQWKKQFEDFTNIHPRHIRILTSDYKLDlwPINEAGVLISTYTMLS 492
Cdd:TIGR00603 278 IVLPCGAGKSLVGVTAACTVKKSCLVLCTSAVSVEQWKQQFKMWSTIDDSQICRFTSDAKER--FHGEAGVVVSTYSMVA 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 493 YSGKRSEQSLRIVNDIRRREWGLLVFDEVQFAPAPSFRRINDIVKSHCKLGLTATLVREDLLIRDLHWIIGPKLYEANWV 572
Cdd:TIGR00603 356 HTGKRSYESEKVMEWLTNREWGLILLDEVHVVPAAMFRRVLTIVQAHCKLGLTATLVREDDKITDLNFLIGPKLYEANWM 435
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 573 ELQNKGFLAKALCKEIWCSMPCSFYKYYLKSNSFIKRRLYTCNPRKLMMCEYLIKYHEQNNDKIIVFSDNIFALLHIAKT 652
Cdd:TIGR00603 436 ELQKKGFIANVQCAEVWCPMTPEFYREYLRENSRKRMLLYVMNPNKFRACQFLIRFHEQRGDKIIVFSDNVFALKEYAIK 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 653 LNKPFIYGKLSPIERIAIINKFKHDSSINTILLSKVGDNAIDIPIANVVIQISFNFASRRQEAQRLGRIIRPKNKANEKK 732
Cdd:TIGR00603 516 LGKPFIYGPTSQQERMQILQNFQHNPKVNTIFLSKVGDTSIDLPEANVLIQISSHYGSRRQEAQRLGRILRAKKGSDAEE 595
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 733 NindpDSFFYSLVSKDTIEMCYSDKRQRFLINQGYAYNVLSDNIVDFNKLNLVYKNKKIQENLLKCILASTDDGNmdedd 812
Cdd:TIGR00603 596 Y----NAFFYSLVSKDTQEMYYSTKRQRFLVDQGYSFKVITHLPGMDNESNLAYSSKEEQLELLQKVLLAGDLDA----- 666
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370993229 813 dlfEDQSFKKDNTKVNKTNSNILLNKKedslKKIDNNTGGLLKLSSNMDVTFADKKKIPTKKFADK-HILFRK 884
Cdd:TIGR00603 667 ---ELEVLEGEFGSRALGASRSMSSAS----GKAVRRGGSLSSLSGGDDMAYMEYRKPAIKKSKKEvHPLFKK 732
ERCC3_RAD25_C pfam16203
ERCC3/RAD25/XPB C-terminal helicase; This is the C-terminal helicase domain of ERCC3, RAD25 ...
574-803 1.70e-119

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: 362.69  E-value: 1.70e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 574 LQNKGFLAKALCKEIWCSMPCSFYKYYLKSNSFIKRRLYTCNPRKLMMCEYLIKYHEQNNDKIIVFSDNIFALLHIAKTL 653
Cdd:pfam16203   1 LQEKGHIANVQCAEVWCPMTAEFYREYLRSKSRKKRLLYVMNPNKFRACQFLIRYHERRGDKIIVFSDNVFALKEYAKKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 654 NKPFIYGKLSPIERIAIINKFKHDSSINTILLSKVGDNAIDIPIANVVIQISFNFASRRQEAQRLGRIIRPKNKANEkkn 733
Cdd:pfam16203  81 NKPYIYGGTSQAERMRILQNFKHNPNVNTIFLSKVGDTSIDLPEANVLIQISSHFGSRRQEAQRLGRILRAKRRSND--- 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 734 iNDPDSFFYSLVSKDTIEMCYSDKRQRFLINQGYAYNVLSDNIVDFNKLNLVYKNKKIQENLLKCILAST 803
Cdd:pfam16203 158 -EGFNAFFYSLVSKDTQEMYYSTKRQQFLVDQGYAFKVITNLAGMEDEENLAYSTKEEQLELLQKVLAAN 226
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
384-552 3.98e-87

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: 274.56  E-value: 3.98e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 384 SLKSHVQIRYYQEKALRKMFSNGRSRSGIIVLPCGVGKTLTGITAASTIKKSALFLTTSAVAVEQWKKQFEDFTNIHPRH 463
Cdd:cd18029     2 DLKPSTQLRPYQEKALSKMFGNGRARSGVIVLPCGAGKTLVGITAACTIKKSTLVLCTSAVSVEQWRRQFLDWTTIDDEQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 464 IRILTSDYKLdlwPINEAGVLISTYTMLSYSGKRSEQSLRIVNDIRRREWGLLVFDEVQFAPAPSFRRINDIVKSHCKLG 543
Cdd:cd18029    82 IGRFTSDKKE---IFPEAGVTVSTYSMLANTRKRSPESEKFMEFITEREWGLIILDEVHVVPAPMFRRVLTLQKAHCKLG 158

                  ....*....
gi 1370993229 544 LTATLVRED 552
Cdd:cd18029   159 LTATLVRED 167
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
390-726 3.59e-56

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 203.72  E-value: 3.59e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 390 QIRYYQEKALRKMFS--NGRSRSGIIVLPCGVGKTLTGITAASTI--KKSALFLTTSAVAVEQWKKQFEDFTNIHPRHIR 465
Cdd:COG1061    80 ELRPYQQEALEALLAalERGGGRGLVVAPTGTGKTVLALALAAELlrGKRVLVLVPRRELLEQWAEELRRFLGDPLAGGG 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 466 ILTSDYKldlwpineagVLISTYtmlsysgkrseQSLRIVNDIRR--REWGLLVFDEVQFAPAPSFRRINDIVKSHCKLG 543
Cdd:COG1061   160 KKDSDAP----------ITVATY-----------QSLARRAHLDElgDRFGLVIIDEAHHAGAPSYRRILEAFPAAYRLG 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 544 LTATLVREDLLIRDLHWIIGpKLYEANWVELQNKGFLAKALCKEIWCSMPcSFYKYYLKSNSFIKRRLYTCNPRKLMMCE 623
Cdd:COG1061   219 LTATPFRSDGREILLFLFDG-IVYEYSLKEAIEDGYLAPPEYYGIRVDLT-DERAEYDALSERLREALAADAERKDKILR 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 624 YLIKYHEqNNDKIIVFSDNIFALLHIAKTLNK-----PFIYGKLSPIERIAIINKFKhDSSINTILLSKVGDNAIDIPIA 698
Cdd:COG1061   297 ELLREHP-DDRKTLVFCSSVDHAEALAELLNEagiraAVVTGDTPKKEREEILEAFR-DGELRILVTVDVLNEGVDVPRL 374
                         330       340
                  ....*....|....*....|....*...
gi 1370993229 699 NVVIQISfNFASRRQEAQRLGRIIRPKN 726
Cdd:COG1061   375 DVAILLR-PTGSPREFIQRLGRGLRPAP 401
HELICc smart00490
helicase superfamily c-terminal domain;
649-725 4.38e-10

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 56.84  E-value: 4.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229  649 IAKTLNKP-----FIYGKLSPIERIAIINKFKHDsSINTILLSKVGDNAIDIPIANVVIQISFNFaSRRQEAQRLGRIIR 723
Cdd:smart00490   3 LAELLKELgikvaRLHGGLSQEEREEILDKFNNG-KIKVLVATDVAERGLDLPGVDLVIIYDLPW-SPASYIQRIGRAGR 80

                   ..
gi 1370993229  724 PK 725
Cdd:smart00490  81 AG 82
PRK13766 PRK13766
Hef nuclease; Provisional
362-546 5.35e-04

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 43.71  E-value: 5.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 362 MQRPLLmeydfrrdkkNPNLIcslkshvQIRYYQE----KALRKmfsngrsrSGIIVLPCGVGKTLTGI-TAASTIKKS- 435
Cdd:PRK13766    4 IEHPLI----------KPNTI-------EARLYQQllaaTALKK--------NTLVVLPTGLGKTAIALlVIAERLHKKg 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 436 --ALFLTTSAVAVEQWKKQFEDFTNIHPRHIRILTSDYKLD----LWpiNEAGVLISTytmlsysgkrsEQSlrIVNDI- 508
Cdd:PRK13766   59 gkVLILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTGEVSPEkraeLW--EKAKVIVAT-----------PQV--IENDLi 123
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1370993229 509 -RR---REWGLLVFDEVQFAP---APSF--RRINDIVKSHCKLGLTA 546
Cdd:PRK13766  124 aGRislEDVSLLIFDEAHRAVgnyAYVYiaERYHEDAKNPLVLGLTA 170
 
Name Accession Description Interval E-value
rad25 TIGR00603
DNA repair helicase rad25; All proteins in this family for which functions are known are ...
94-884 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: 759.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229  94 DYSKDMKLKKNHMNKPLWICSDGFIYLEMFNSCSKQASDFLITIAEPICRPELIHEFQLTIFSLYAAISVGITLDELLIN 173
Cdd:TIGR00603   1 DYSKQLELKPDHGSRPLWVAPDGHIFLESFSPLYKQAQDFLVAIAEPVCRPEHIHEYKLTAYSLYAAVSVGLETEDIIEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 174 LDKFSKNVLPNELICNITKSAESFGKVKLVLRENKYYIEATNKSELDYLLNNDTIQNARIYSTDNnndknmislynlnnr 253
Cdd:TIGR00603  81 LGRLSKTPIPKGIIEFIRLCTQSYGKVKLVLKHNRYFVESPHPEVLQRLLKDPVIAPCRIDPTEE--------------- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 254 lldsrhrdnnkndnknnnnDNNNIEKTTSNL-LSEQQKGKDCYVTYEAPVLDTTQLGFKISESEKQLMMEEkknanlnaN 332
Cdd:TIGR00603 146 -------------------ESLQTPTYGSKEdFIINKPGFTGGASAGQLEANQGESAVPKDIADFYELEEE--------E 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 333 ENSTNSAEVYSFEVNCDKIEEVKQEALQtMQRPLLMEYDFRRDKKNPNLICSLKSHVQIRYYQEKALRKMFSNGRSRSGI 412
Cdd:TIGR00603 199 EDEDEETATHSFEIDQEQVEEVKKRCIE-LDYPLLEEYDFRNDTVNPDLNIDLKPTTQIRPYQEKSLSKMFGNGRARSGI 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 413 IVLPCGVGKTLTGITAASTIKKSALFLTTSAVAVEQWKKQFEDFTNIHPRHIRILTSDYKLDlwPINEAGVLISTYTMLS 492
Cdd:TIGR00603 278 IVLPCGAGKSLVGVTAACTVKKSCLVLCTSAVSVEQWKQQFKMWSTIDDSQICRFTSDAKER--FHGEAGVVVSTYSMVA 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 493 YSGKRSEQSLRIVNDIRRREWGLLVFDEVQFAPAPSFRRINDIVKSHCKLGLTATLVREDLLIRDLHWIIGPKLYEANWV 572
Cdd:TIGR00603 356 HTGKRSYESEKVMEWLTNREWGLILLDEVHVVPAAMFRRVLTIVQAHCKLGLTATLVREDDKITDLNFLIGPKLYEANWM 435
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 573 ELQNKGFLAKALCKEIWCSMPCSFYKYYLKSNSFIKRRLYTCNPRKLMMCEYLIKYHEQNNDKIIVFSDNIFALLHIAKT 652
Cdd:TIGR00603 436 ELQKKGFIANVQCAEVWCPMTPEFYREYLRENSRKRMLLYVMNPNKFRACQFLIRFHEQRGDKIIVFSDNVFALKEYAIK 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 653 LNKPFIYGKLSPIERIAIINKFKHDSSINTILLSKVGDNAIDIPIANVVIQISFNFASRRQEAQRLGRIIRPKNKANEKK 732
Cdd:TIGR00603 516 LGKPFIYGPTSQQERMQILQNFQHNPKVNTIFLSKVGDTSIDLPEANVLIQISSHYGSRRQEAQRLGRILRAKKGSDAEE 595
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 733 NindpDSFFYSLVSKDTIEMCYSDKRQRFLINQGYAYNVLSDNIVDFNKLNLVYKNKKIQENLLKCILASTDDGNmdedd 812
Cdd:TIGR00603 596 Y----NAFFYSLVSKDTQEMYYSTKRQRFLVDQGYSFKVITHLPGMDNESNLAYSSKEEQLELLQKVLLAGDLDA----- 666
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370993229 813 dlfEDQSFKKDNTKVNKTNSNILLNKKedslKKIDNNTGGLLKLSSNMDVTFADKKKIPTKKFADK-HILFRK 884
Cdd:TIGR00603 667 ---ELEVLEGEFGSRALGASRSMSSAS----GKAVRRGGSLSSLSGGDDMAYMEYRKPAIKKSKKEvHPLFKK 732
ERCC3_RAD25_C pfam16203
ERCC3/RAD25/XPB C-terminal helicase; This is the C-terminal helicase domain of ERCC3, RAD25 ...
574-803 1.70e-119

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: 362.69  E-value: 1.70e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 574 LQNKGFLAKALCKEIWCSMPCSFYKYYLKSNSFIKRRLYTCNPRKLMMCEYLIKYHEQNNDKIIVFSDNIFALLHIAKTL 653
Cdd:pfam16203   1 LQEKGHIANVQCAEVWCPMTAEFYREYLRSKSRKKRLLYVMNPNKFRACQFLIRYHERRGDKIIVFSDNVFALKEYAKKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 654 NKPFIYGKLSPIERIAIINKFKHDSSINTILLSKVGDNAIDIPIANVVIQISFNFASRRQEAQRLGRIIRPKNKANEkkn 733
Cdd:pfam16203  81 NKPYIYGGTSQAERMRILQNFKHNPNVNTIFLSKVGDTSIDLPEANVLIQISSHFGSRRQEAQRLGRILRAKRRSND--- 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 734 iNDPDSFFYSLVSKDTIEMCYSDKRQRFLINQGYAYNVLSDNIVDFNKLNLVYKNKKIQENLLKCILAST 803
Cdd:pfam16203 158 -EGFNAFFYSLVSKDTQEMYYSTKRQQFLVDQGYAFKVITNLAGMEDEENLAYSTKEEQLELLQKVLAAN 226
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
384-552 3.98e-87

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: 274.56  E-value: 3.98e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 384 SLKSHVQIRYYQEKALRKMFSNGRSRSGIIVLPCGVGKTLTGITAASTIKKSALFLTTSAVAVEQWKKQFEDFTNIHPRH 463
Cdd:cd18029     2 DLKPSTQLRPYQEKALSKMFGNGRARSGVIVLPCGAGKTLVGITAACTIKKSTLVLCTSAVSVEQWRRQFLDWTTIDDEQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 464 IRILTSDYKLdlwPINEAGVLISTYTMLSYSGKRSEQSLRIVNDIRRREWGLLVFDEVQFAPAPSFRRINDIVKSHCKLG 543
Cdd:cd18029    82 IGRFTSDKKE---IFPEAGVTVSTYSMLANTRKRSPESEKFMEFITEREWGLIILDEVHVVPAPMFRRVLTLQKAHCKLG 158

                  ....*....
gi 1370993229 544 LTATLVRED 552
Cdd:cd18029   159 LTATLVRED 167
SF2_C_XPB cd18789
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ...
585-745 2.64e-66

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: 218.27  E-value: 2.64e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 585 CKEIWCSMPCSFYKYYLKSNSFIKRR-LYTCNPRKLMMCEYLIKYHEQNnDKIIVFSDNIFALLHIAKTLNKPFIYGKLS 663
Cdd:cd18789     1 CAEIRCPMTPEFYREYLGLGAHRKRRlLAAMNPNKLRALEELLKRHEQG-DKIIVFTDNVEALYRYAKRLLKPFITGETP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 664 PIERIAIINKFKHdSSINTILLSKVGDNAIDIPIANVVIQISFNFASRRQEAQRLGRIIRPKNKANekKNindpdSFFYS 743
Cdd:cd18789    80 QSEREEILQNFRE-GEYNTLVVSKVGDEGIDLPEANVAIQISGHGGSRRQEAQRLGRILRPKKGGG--KN-----AFFYS 151

                  ..
gi 1370993229 744 LV 745
Cdd:cd18789   152 LV 153
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
390-726 3.59e-56

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 203.72  E-value: 3.59e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 390 QIRYYQEKALRKMFS--NGRSRSGIIVLPCGVGKTLTGITAASTI--KKSALFLTTSAVAVEQWKKQFEDFTNIHPRHIR 465
Cdd:COG1061    80 ELRPYQQEALEALLAalERGGGRGLVVAPTGTGKTVLALALAAELlrGKRVLVLVPRRELLEQWAEELRRFLGDPLAGGG 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 466 ILTSDYKldlwpineagVLISTYtmlsysgkrseQSLRIVNDIRR--REWGLLVFDEVQFAPAPSFRRINDIVKSHCKLG 543
Cdd:COG1061   160 KKDSDAP----------ITVATY-----------QSLARRAHLDElgDRFGLVIIDEAHHAGAPSYRRILEAFPAAYRLG 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 544 LTATLVREDLLIRDLHWIIGpKLYEANWVELQNKGFLAKALCKEIWCSMPcSFYKYYLKSNSFIKRRLYTCNPRKLMMCE 623
Cdd:COG1061   219 LTATPFRSDGREILLFLFDG-IVYEYSLKEAIEDGYLAPPEYYGIRVDLT-DERAEYDALSERLREALAADAERKDKILR 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 624 YLIKYHEqNNDKIIVFSDNIFALLHIAKTLNK-----PFIYGKLSPIERIAIINKFKhDSSINTILLSKVGDNAIDIPIA 698
Cdd:COG1061   297 ELLREHP-DDRKTLVFCSSVDHAEALAELLNEagiraAVVTGDTPKKEREEILEAFR-DGELRILVTVDVLNEGVDVPRL 374
                         330       340
                  ....*....|....*....|....*...
gi 1370993229 699 NVVIQISfNFASRRQEAQRLGRIIRPKN 726
Cdd:COG1061   375 DVAILLR-PTGSPREFIQRLGRGLRPAP 401
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
392-548 1.20e-29

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: 114.71  E-value: 1.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 392 RYYQEKALRKMFSNGRSRSGIIVLPCGVGKTLTGITAASTIKK-SALFLTTSAVAVEQWKKQFEDFTNIHPrhIRILTSD 470
Cdd:cd17926     2 RPYQEEALEAWLAHKNNRRGILVLPTGSGKTLTALALIAYLKElRTLIVVPTDALLDQWKERFEDFLGDSS--IGLIGGG 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370993229 471 YKLDlwpINEAGVLISTYTmlsySGKRSEQSLRIVNDirrrEWGLLVFDEVQFAPAPSFRRINDIVKSHCKLGLTATL 548
Cdd:cd17926    80 KKKD---FDDANVVVATYQ----SLSNLAEEEKDLFD----QFGLLIVDEAHHLPAKTFSEILKELNAKYRLGLTATP 146
Helicase_C_3 pfam13625
Helicase conserved C-terminal domain; This domain family is found in a wide variety of ...
110-233 5.04e-25

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: 100.65  E-value: 5.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 110 LWICSDGFIYLEmfNSCSKQASDFLITIAEPICRpELIHEFQLTIFSLYAAISVGITLDELLINLDKFSKNVLPNELICN 189
Cdd:pfam13625   1 LIVQADLTILLP--GPLAPEARDFLAAFAELESR-GHAHTYRLTPLSLRRALDAGLTAEDILDFLERHSKYPVPQALEYL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1370993229 190 ITKSAESFGKVKLVLrENKYYIEATNKSELDYLLNNDTIQNARI 233
Cdd:pfam13625  78 IRDVARRHGRLRLGL-GASSYLRSDDPAVLAELLADPRIAPLGL 120
ResIII pfam04851
Type III restriction enzyme, res subunit;
390-550 1.17e-18

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 83.88  E-value: 1.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 390 QIRYYQEKALRK---MFSNGRSRsGIIVLPCGVGKTLTGITAA-----STIKKSALFLTTSAVAVEQWKKQFEDFTNIHP 461
Cdd:pfam04851   3 ELRPYQIEAIENlleSIKNGQKR-GLIVMATGSGKTLTAAKLIarlfkKGPIKKVLFLVPRKDLLEQALEEFKKFLPNYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 462 RHIRILTSDYKLDlwPINEAGVLISTYTMLSysGKRSEQSLRIVNDirrrEWGLLVFDEVQFAPAPSFRRINDIVKSHCK 541
Cdd:pfam04851  82 EIGEIISGDKKDE--SVDDNKIVVTTIQSLY--KALELASLELLPD----FFDVIIIDEAHRSGASSYRNILEYFKPAFL 153

                  ....*....
gi 1370993229 542 LGLTATLVR 550
Cdd:pfam04851 154 LGLTATPER 162
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
388-751 1.10e-16

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 84.89  E-value: 1.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 388 HVQIRYYQEKALRKMFSNGRSRSGII----VlpcGVGKTLTGITA-----ASTIKKSALFLTTSAVaVEQWKKQFEDFTn 458
Cdd:COG0553   239 KATLRPYQLEGAAWLLFLRRLGLGGLladdM---GLGKTIQALALllelkERGLARPVLIVAPTSL-VGNWQRELAKFA- 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 459 iHPRHIRILTSDYK--LDLWPINEAGVLISTYTMLSysgkrseqslRIVNDIRRREWGLLVFDEVQF---APAPSFRRIN 533
Cdd:COG0553   314 -PGLRVLVLDGTREraKGANPFEDADLVITSYGLLR----------RDIELLAAVDWDLVILDEAQHiknPATKRAKAVR 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 534 DIvKSHCKLGLTAT--------------LVREDLL---------------------IRDLHWIIGP-------------- 564
Cdd:COG0553   383 AL-KARHRLALTGTpvenrleelwslldFLNPGLLgslkafrerfarpiekgdeeaLERLRRLLRPfllrrtkedvlkdl 461
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 565 -----------------KLYEANWVELQNKGFLAKA------------LCKEIwCSMPcsfyKYYLKsnsfiKRRLYTCN 615
Cdd:COG0553   462 pekteetlyveltpeqrALYEAVLEYLRRELEGAEGirrrglilaaltRLRQI-CSHP----ALLLE-----EGAELSGR 531
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 616 PRKLMMCEYLIKYHEQNNDKIIVFSdnIFA--LLHIAKTLNK-----PFIYGKLSPIERIAIINKFKHDSSINTILLS-K 687
Cdd:COG0553   532 SAKLEALLELLEELLAEGEKVLVFS--QFTdtLDLLEERLEErgieyAYLHGGTSAEERDELVDRFQEGPEAPVFLISlK 609
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370993229 688 VGDNAIDIPIANVVIQ--ISFNFAsrrQEAQRLGRIIRPKNkaneKKNIndpdsFFYSLVSKDTIE 751
Cdd:COG0553   610 AGGEGLNLTAADHVIHydLWWNPA---VEEQAIDRAHRIGQ----TRDV-----QVYKLVAEGTIE 663
DEXHc_RE_I_III_res cd18032
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ...
392-552 3.57e-13

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: 67.97  E-value: 3.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 392 RYYQEKALRKM---FSNGRSRSGIiVLPCGVGKTLTGITAA-----STIKKSALFLTTSAVAVEQWKKQFEDFTNIHPRH 463
Cdd:cd18032     2 RYYQQEAIEALeeaREKGQRRALL-VMATGTGKTYTAAFLIkrlleANRKKRILFLAHREELLEQAERSFKEVLPDGSFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 464 IrILTSDYKLDlwpinEAGVLISTYtmlsysgkrseQSLriVNDIRRREWG-----LLVFDEVQFAPAPSFRRINDIVKS 538
Cdd:cd18032    81 N-LKGGKKKPD-----DARVVFATV-----------QTL--NKRKRLEKFPpdyfdLIIIDEAHHAIASSYRKILEYFEP 141
                         170
                  ....*....|....
gi 1370993229 539 HCKLGLTATLVRED 552
Cdd:cd18032   142 AFLLGLTATPERTD 155
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
618-725 3.50e-11

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: 60.69  E-value: 3.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 618 KLMMCEYLIKYHeqNNDKIIVFSDNI----FALLHIAKTLNKPFIYGKLSPIERIAIINKFKhDSSINTILLSKVGDNAI 693
Cdd:pfam00271   2 KLEALLELLKKE--RGGKVLIFSQTKktleAELLLEKEGIKVARLHGDLSQEEREEILEDFR-KGKIDVLVATDVAERGL 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1370993229 694 DIPIANVVIQISFNFaSRRQEAQRLGRIIRPK 725
Cdd:pfam00271  79 DLPDVDLVINYDLPW-NPASYIQRIGRAGRAG 109
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
618-723 3.63e-10

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: 58.64  E-value: 3.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 618 KLMMCEYLIKYHEQNNDKIIVFS---DNIFALLHIAKTLNKPF--IYGKLSPIERIAIINKFKHDSSINTILLS-KVGDN 691
Cdd:cd18793    12 KLEALLELLEELREPGEKVLIFSqftDTLDILEEALRERGIKYlrLDGSTSSKERQKLVDRFNEDPDIRVFLLStKAGGV 91
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1370993229 692 AIDIPIANVVI--QISFNFAsrrQEAQRLGRIIR 723
Cdd:cd18793    92 GLNLTAANRVIlyDPWWNPA---VEEQAIDRAHR 122
HELICc smart00490
helicase superfamily c-terminal domain;
649-725 4.38e-10

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 56.84  E-value: 4.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229  649 IAKTLNKP-----FIYGKLSPIERIAIINKFKHDsSINTILLSKVGDNAIDIPIANVVIQISFNFaSRRQEAQRLGRIIR 723
Cdd:smart00490   3 LAELLKELgikvaRLHGGLSQEEREEILDKFNNG-KIKVLVATDVAERGLDLPGVDLVIIYDLPW-SPASYIQRIGRAGR 80

                   ..
gi 1370993229  724 PK 725
Cdd:smart00490  81 AG 82
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
394-564 3.97e-09

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: 56.81  E-value: 3.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 394 YQEKALRKMFSNGRSRSGIIVLPC-GVGKTLTGITAASTIKKSAL----FLTTS-AVAVEQWKKQFEDFTnihpRHIRIL 467
Cdd:cd17919     4 YQLEGLNFLLELYENGPGGILADEmGLGKTLQAIAFLAYLLKEGKergpVLVVCpLSVLENWEREFEKWT----PDLRVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 468 TSD-------YKLDLWPINEAGVLISTYTMLSysgkRSEQSLRIVndirrrEWGLLVFDEVQFAPAPS---FRRINDIvK 537
Cdd:cd17919    80 VYHgsqreraQIRAKEKLDKFDVVLTTYETLR----RDKASLRKF------RWDLVVVDEAHRLKNPKsqlSKALKAL-R 148
                         170       180
                  ....*....|....*....|....*....
gi 1370993229 538 SHCKLGLTATLVREDL--LIRDLHWIIGP 564
Cdd:cd17919   149 AKRRLLLTGTPLQNNLeeLWALLDFLDPP 177
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
411-547 9.09e-07

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 49.32  E-value: 9.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 411 GIIVLPCGVGKTLTG----ITAASTIKKSALFLT-TSAVAvEQWKKQFEDFTNiHPRHIRILTSDY--------KLDLWP 477
Cdd:cd00046     4 VLITAPTGSGKTLAAllaaLLLLLKKGKKVLVLVpTKALA-LQTAERLRELFG-PGIRVAVLVGGSsaeereknKLGDAD 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370993229 478 IneagvLISTYTMLSYSGKRSEQSlrivndiRRREWGLLVFDEVQFAPaPSFRRINDIVKSHCKL--------GLTAT 547
Cdd:cd00046    82 I-----IIATPDMLLNLLLREDRL-------FLKDLKLIIVDEAHALL-IDSRGALILDLAVRKAglknaqviLLSAT 146
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
394-548 5.55e-06

DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 47.64  E-value: 5.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 394 YQEKALRKMFSNGRSRsgIIVLPCGVGKTLTG----ITAASTIKKSALFLTTSAVAVEQ----WKKQFEDFtnihPRHIR 465
Cdd:cd17921     5 IQREALRALYLSGDSV--LVSAPTSSGKTLIAelaiLRALATSGGKAVYIAPTRALVNQkeadLRERFGPL----GKNVG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 466 ILTSDYKLDLWPINEAGVLISTYTML-SYSGKRSEQSLRIVndirrrewGLLVFDEVQFAPAPS--------FRRINDIV 536
Cdd:cd17921    79 LLTGDPSVNKLLLAEADILVATPEKLdLLLRNGGERLIQDV--------RLVVVDEAHLIGDGErgvvlellLSRLLRIN 150
                         170
                  ....*....|...
gi 1370993229 537 KsHCK-LGLTATL 548
Cdd:cd17921   151 K-NARfVGLSATL 162
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
418-547 1.48e-05

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: 46.90  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 418 GVGKTltgITAASTIK--------KSALFLTTSAVaVEQWKKQFEDFTNIHprhIRILTSDYKLDLW-----PINEAGVL 484
Cdd:cd18011    27 GLGKT---IEAGLIIKelllrgdaKRVLILCPASL-VEQWQDELQDKFGLP---FLILDRETAAQLRrlignPFEEFPIV 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370993229 485 ISTYTMLSYSGKRSEQSLRivndirrREWGLLVFDEV-QFAPAP------SFRRINDIVK-SHCKLGLTAT 547
Cdd:cd18011   100 IVSLDLLKRSEERRGLLLS-------EEWDLVVVDEAhKLRNSGggketkRYKLGRLLAKrARHVLLLTAT 163
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
392-547 3.52e-05

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


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 47.42  E-value: 3.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 392 RYYQEKalrkMFSNGRSRSGIIVLPCGVGKTLTGI-TAASTIKKS---ALFLTTSAVAVEQWKKQFEDFTNIHPRHIRIL 467
Cdd:COG1111     5 RLYQLN----LAASALRKNTLVVLPTGLGKTAVALlVIAERLHKKggkVLFLAPTKPLVEQHAEFFKEALNIPEDEIVVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 468 TSDYKLD----LWpiNEAGVLISTytmlsysgkrsEQSLRivNDIRR-----REWGLLVFDEVQFAP---APSF--RRIN 533
Cdd:COG1111    81 TGEVSPEkrkeLW--EKARIIVAT-----------PQVIE--NDLIAgridlDDVSLLIFDEAHRAVgnyAYVYiaERYH 145
                         170
                  ....*....|....
gi 1370993229 534 DIVKSHCKLGLTAT 547
Cdd:COG1111   146 EDAKDPLILGMTAS 159
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
395-522 5.92e-05

Replicative superfamily II helicase [Replication, recombination and repair];


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 46.81  E-value: 5.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 395 QEKALRKMFSNGRSrsGIIVLPCGVGKTLTGITAA-STIKKS--ALFLT-TSAVAVE---QWKKQFEDFtNIHprhIRIL 467
Cdd:COG1204    27 QAEALEAGLLEGKN--LVVSAPTASGKTLIAELAIlKALLNGgkALYIVpLRALASEkyrEFKRDFEEL-GIK---VGVS 100
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 468 TSDYKLDLWPINEAGVLISTYTMLsysgkrseQSLrivndIRRR-EW----GLLVFDEVQ 522
Cdd:COG1204   101 TGDYDSDDEWLGRYDILVATPEKL--------DSL-----LRNGpSWlrdvDLVVVDEAH 147
DEXHc_dicer cd18034
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ...
389-549 3.18e-04

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: 42.64  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 389 VQIRYYQEKALRKmfsnGRSRSGIIVLPCGVGKTL----------TGITAASTIKKSALFLTTSAVAVEQWKKQFEDFTN 458
Cdd:cd18034     1 FTPRSYQLELFEA----ALKRNTIVVLPTGSGKTLiavmlikemgELNRKEKNPKKRAVFLVPTVPLVAQQAEAIRSHTD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 459 IhprHIRILTSDYKLDLWP-------INEAGVLISTYTMLSYSGKRSEQSLRIVNdirrrewgLLVFDEVQFA----Pap 527
Cdd:cd18034    77 L---KVGEYSGEMGVDKWTkerwkeeLEKYDVLVMTAQILLDALRHGFLSLSDIN--------LLIFDECHHAtgdhP-- 143
                         170       180       190
                  ....*....|....*....|....*....|
gi 1370993229 528 sFRRINDIVKsHCK--------LGLTATLV 549
Cdd:cd18034   144 -YARIMKEFY-HLEgrtsrpriLGLTASPV 171
PRK13766 PRK13766
Hef nuclease; Provisional
362-546 5.35e-04

Hef nuclease; Provisional


Pssm-ID: 237496 [Multi-domain]  Cd Length: 773  Bit Score: 43.71  E-value: 5.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 362 MQRPLLmeydfrrdkkNPNLIcslkshvQIRYYQE----KALRKmfsngrsrSGIIVLPCGVGKTLTGI-TAASTIKKS- 435
Cdd:PRK13766    4 IEHPLI----------KPNTI-------EARLYQQllaaTALKK--------NTLVVLPTGLGKTAIALlVIAERLHKKg 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 436 --ALFLTTSAVAVEQWKKQFEDFTNIHPRHIRILTSDYKLD----LWpiNEAGVLISTytmlsysgkrsEQSlrIVNDI- 508
Cdd:PRK13766   59 gkVLILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTGEVSPEkraeLW--EKAKVIVAT-----------PQV--IENDLi 123
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1370993229 509 -RR---REWGLLVFDEVQFAP---APSF--RRINDIVKSHCKLGLTA 546
Cdd:PRK13766  124 aGRislEDVSLLIFDEAHRAVgnyAYVYiaERYHEDAKNPLVLGLTA 170
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
394-520 1.93e-03

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: 41.13  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 394 YQEKALRKMFS--NGRSRSGIIVLPCGVGKTLTGITAASTIKKSALFLTTSAVAV------EQWKKQFEDFTNIHPRHIR 465
Cdd:pfam00176   1 YQIEGVNWMLSleNNLGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGGPTLIVvplsllHNWMNEFERWVSPPALRVV 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370993229 466 ILTSDYKLDLWPIN------EAGVLISTYTMLsysgkrseqsLRIVNDIRRREWGLLVFDE 520
Cdd:pfam00176  81 VLHGNKRPQERWKNdpnflaDFDVVITTYETL----------RKHKELLKKVHWHRIVLDE 131
SF2_C_FANCM_Hef cd18801
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ...
608-726 3.81e-03

C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef 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: 350188 [Multi-domain]  Cd Length: 143  Bit Score: 38.49  E-value: 3.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 608 KRRLYTCNPR--KL--MMCEYLIKYHEQNNDKIIVFSDNIFALLHIAKTLNK--PFIYGK-------------LSPIERI 668
Cdd:cd18801     1 KRKVEKIHPKleKLeeIVKEHFKKKQEGSDTRVIIFSEFRDSAEEIVNFLSKirPGIRATrfigqasgksskgMSQKEQK 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370993229 669 AIINKFKhDSSINTILLSKVGDNAIDIPIANVVIQISFNfASRRQEAQRLGRIIRPKN 726
Cdd:cd18801    81 EVIEQFR-KGGYNVLVATSIGEEGLDIGEVDLIICYDAS-PSPIRMIQRMGRTGRKRQ 136
DEXHc_RIG-I cd17927
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ...
389-520 4.03e-03

DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family 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: 350685 [Multi-domain]  Cd Length: 201  Bit Score: 39.34  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 389 VQIRYYQEKALRKMFsngRSRSGIIVLPCGVGKTLTGITAA--------STIKKSALFLTTSAVAVEQWKKQFEDFTNIH 460
Cdd:cd17927     1 FKPRNYQLELAQPAL---KGKNTIICLPTGSGKTFVAVLICehhlkkfpAGRKGKVVFLANKVPLVEQQKEVFRKHFERP 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370993229 461 PRHIRILTSDYKLDLWP---INEAGVLISTYTMLsysgkrsEQSLRIVNDIRRREWGLLVFDE 520
Cdd:cd17927    78 GYKVTGLSGDTSENVSVeqiVESSDVIIVTPQIL-------VNDLKSGTIVSLSDFSLLVFDE 133
DEXHc_Hef cd18035
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ...
389-547 5.69e-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: 38.65  E-value: 5.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 389 VQIRYYQEKAlrkmFSNGRSRSGIIVLPCGVGKTLTGITAASTI----KKSALFLTTSAVAVEQWKKQFEDFTNIhPRHI 464
Cdd:cd18035     1 EERRLYQVLI----AAVALNGNTLIVLPTGLGKTIIAILVAADRltkkGGKVLILAPSRPLVEQHAENLKRVLNI-PDKI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 465 RILTSDYKLD----LWpiNEAGVLISTYTMLsysgkrsEQSLrIVNDIRRREWGLLVFDEVQ-----FAPAPSFRRINDI 535
Cdd:cd18035    76 TSLTGEVKPEeraeRW--DASKIIVATPQVI-------ENDL-LAGRITLDDVSLLIFDEAHhavgnYAYVYIAHRYKRE 145
                         170
                  ....*....|..
gi 1370993229 536 VKSHCKLGLTAT 547
Cdd:cd18035   146 ANNPLILGLTAS 157
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
418-520 6.09e-03

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: 39.11  E-value: 6.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370993229 418 GVGKTLTGITAASTIKKS--ALFLTTSAVaVEQWKKQFEDF-TNIHPRHIRILTS--DYKLDLWPIneagVLISTYTMLS 492
Cdd:cd18010    26 GLGKTVQAIAIAAYYREEwpLLIVCPSSL-RLTWADEIERWlPSLPPDDIQVIVKskDGLRDGDAK----VVIVSYDLLR 100
                          90       100
                  ....*....|....*....|....*...
gi 1370993229 493 ysgkrseqslRIVNDIRRREWGLLVFDE 520
Cdd:cd18010   101 ----------RLEKQLLARKFKVVICDE 118
 
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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