ERCC3_DROME
ID ERCC3_DROME Reviewed; 798 AA.
AC Q02870; Q1LZ27; Q2PJB4; Q960M8; Q9VTA2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=General transcription and DNA repair factor IIH helicase subunit XPB;
DE Short=TFIIH subunit XPB;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent DNA helicase hay;
DE AltName: Full=DNA excision repair protein haywire;
DE AltName: Full=ERCC-3 homolog protein;
DE AltName: Full=ERCC3Dm;
GN Name=hay; Synonyms=ERCC3; ORFNames=CG8019;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1454518; DOI=10.1093/nar/20.21.5541;
RA Koken M.H., Vreeken C., Bol S.A., Cheng N.C., Jaspers-Dekker I.,
RA Hoeijmakers J.H., Eeken J.C., Weeda G., Pastink A.;
RT "Cloning and characterization of the Drosophila homolog of the Xeroderma
RT pigmentosum complementation-group B correcting gene, ERCC3.";
RL Nucleic Acids Res. 20:5541-5548(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=1458540; DOI=10.1016/0092-8674(92)90389-t;
RA Mounkes L.C., Jones R.S., Liang B.-C., Gelbart W.M., Fuller M.T.;
RT "A Drosophila model for Xeroderma pigmentosum and Cockayne's syndrome:
RT haywire encodes the fly homolog of ERCC3, a human excision repair gene.";
RL Cell 71:925-937(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent 3'-5' DNA helicase, component of the general
CC transcription and DNA repair factor IIH (TFIIH) core complex, which is
CC involved in general and transcription-coupled nucleotide excision
CC repair (NER) of damaged DNA and, when complexed to CAK, in RNA
CC transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA
CC around the lesion to allow the excision of the damaged oligonucleotide
CC and its replacement by a new DNA fragment. The ATPase activity of
CC haywire/XPB/ERCC3, but not its helicase activity, is required for DNA
CC opening. In transcription, TFIIH has an essential role in transcription
CC initiation. When the pre-initiation complex (PIC) has been established,
CC TFIIH is required for promoter opening and promoter escape. The ATP-
CC dependent helicase activity of haywire/XPB/ERCC3 is required for
CC promoter opening and promoter escape. Phosphorylation of the C-terminal
CC tail (CTD) of the largest subunit of RNA polymerase II by the kinase
CC module CAK controls the initiation of transcription.
CC {ECO:0000250|UniProtKB:P19447}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Component of the 7-subunit TFIIH core complex composed of
CC haywire/XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2, GTF2H3, GTF2H4 and
CC GTF2H5, which is active in NER. The core complex associates with the 3-
CC subunit CDK-activating kinase (CAK) module composed of CCNH/cyclin H,
CC CDK7 and MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH) active in
CC transcription. Interacts with PUF60. Interacts with ATF7IP. Interacts
CC with Epstein-Barr virus EBNA2. {ECO:0000250|UniProtKB:P19447}.
CC -!- INTERACTION:
CC Q02870; O96757: stumps; NbExp=4; IntAct=EBI-74952, EBI-74922;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC {ECO:0000305}.
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DR EMBL; S50517; AAA12421.1; -; mRNA.
DR EMBL; X68309; CAA48386.1; -; mRNA.
DR EMBL; L02965; AAA74931.1; -; mRNA.
DR EMBL; AE014296; AAF50150.1; -; Genomic_DNA.
DR EMBL; AY051975; AAK93399.1; -; mRNA.
DR EMBL; BT025199; ABF17890.1; -; mRNA.
DR PIR; A44223; A44223.
DR RefSeq; NP_001137931.1; NM_001144459.2.
DR RefSeq; NP_524020.2; NM_079296.4.
DR AlphaFoldDB; Q02870; -.
DR SMR; Q02870; -.
DR BioGRID; 64581; 11.
DR IntAct; Q02870; 1.
DR STRING; 7227.FBpp0075982; -.
DR PaxDb; Q02870; -.
DR PRIDE; Q02870; -.
DR DNASU; 39202; -.
DR EnsemblMetazoa; FBtr0076253; FBpp0075982; FBgn0001179.
DR EnsemblMetazoa; FBtr0114599; FBpp0113091; FBgn0001179.
DR GeneID; 39202; -.
DR KEGG; dme:Dmel_CG8019; -.
DR UCSC; CG8019-RA; d. melanogaster.
DR CTD; 39202; -.
DR FlyBase; FBgn0001179; hay.
DR VEuPathDB; VectorBase:FBgn0001179; -.
DR eggNOG; KOG1123; Eukaryota.
DR GeneTree; ENSGT00390000002204; -.
DR HOGENOM; CLU_008213_0_0_1; -.
DR InParanoid; Q02870; -.
DR OMA; PTHIHEY; -.
DR OrthoDB; 100698at2759; -.
DR PhylomeDB; Q02870; -.
DR Reactome; R-DME-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-DME-113418; Formation of the Early Elongation Complex.
DR Reactome; R-DME-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-DME-5696400; Dual Incision in GG-NER.
DR Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DME-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-DME-6782135; Dual incision in TC-NER.
DR Reactome; R-DME-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-DME-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-DME-72086; mRNA Capping.
DR Reactome; R-DME-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-DME-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-DME-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-DME-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-DME-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-DME-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-DME-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR BioGRID-ORCS; 39202; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39202; -.
DR PRO; PR:Q02870; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0001179; Expressed in eye disc (Drosophila) and 22 other tissues.
DR ExpressionAtlas; Q02870; baseline and differential.
DR Genevisible; Q02870; DM.
DR GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; IDA:FlyBase.
DR GO; GO:0097550; C:transcription preinitiation complex; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; ISS:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; ISS:FlyBase.
DR GO; GO:0006289; P:nucleotide-excision repair; ISS:FlyBase.
DR GO; GO:0033683; P:nucleotide-excision repair, DNA incision; IBA:GO_Central.
DR GO; GO:0001111; P:promoter clearance from RNA polymerase II promoter; ISS:FlyBase.
DR GO; GO:0009411; P:response to UV; IMP:FlyBase.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IGI:FlyBase.
DR GO; GO:0001113; P:transcription open complex formation at RNA polymerase II promoter; ISS:FlyBase.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR032438; ERCC3_RAD25_C.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001161; XPB/Ssl2.
DR InterPro; IPR032830; XPB/Ssl2_N.
DR Pfam; PF16203; ERCC3_RAD25_C; 1.
DR Pfam; PF13625; Helicase_C_3; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00603; rad25; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..798
FT /note="General transcription and DNA repair factor IIH
FT helicase subunit XPB"
FT /id="PRO_0000101990"
FT DOMAIN 343..504
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 558..713
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 6..22
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 457..460
FT /note="DEVH box"
FT COMPBIAS 1..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 360..367
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 15..16
FT /note="DK -> AE (in Ref. 2; AAA74931)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="P -> A (in Ref. 1; AAA12421/CAA48386 and 2;
FT AAA74931)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="A -> AVVAA (in Ref. 1; AAA12421/CAA48386 and 2;
FT AAA74931)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="V -> G (in Ref. 2; AAA74931)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="D -> V (in Ref. 5; AAK93399)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="V -> C (in Ref. 2; AAA74931)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="Missing (in Ref. 2; AAA74931)"
FT /evidence="ECO:0000305"
FT CONFLICT 657
FT /note="G -> V (in Ref. 2; AAA74931)"
FT /evidence="ECO:0000305"
FT CONFLICT 693
FT /note="Q -> H (in Ref. 2; AAA74931)"
FT /evidence="ECO:0000305"
FT CONFLICT 701..702
FT /note="YS -> IC (in Ref. 2; AAA74931)"
FT /evidence="ECO:0000305"
FT CONFLICT 760
FT /note="A -> I (in Ref. 1; AAA12421/CAA48386 and 2;
FT AAA74931)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 798 AA; 90348 MW; DF6798F0B6E2DC22 CRC64;
MGPPKKSRKD RSGGDKFGKK RRAEDEAFTQ LVDDNDSLDA TESEGIPGAA SKNAETNDEQ
INTDEYGAKD YRSQMQLRPD HGNRPLWVAP NGHVFLESFS PVYKHAHDFL IAISEPVCRP
EHIHEYKLTA YSLYAAVSVG LQTHDIVEYL KRLSKTSIPE GILEFIRLCT LSYGKVKLVL
KHNKYFIESP HPEVLQKLLK DPVIQKCRLI RSEGEDFIQG TLDGKAITQF GTKLPPGATD
KPTPDPAAAA GADGTTAVPE DITDFYEKID KEEEDEDEAN LKTVSFEVAQ EKIEVIQKRC
IEIEHPLLAE YDFRNDTNNP DINIDLKPAA VLRPYQEKSL RKMFGNGRAR SGVIVLPCGA
GKSLVGVTAC CTVRKRALVL CNSGVSVEQW KQQFKMWSTA DDSMICRFTS EAKDKPMGCG
ILVTTYSMIT HTQKRSWEAE QTMRWLQEQE WGIMVLDEVH TIPAKMFRRV LTIVQSHCKL
GLTATLLRED DKIADLNFLI GPKLYEANWL ELQKKGYIAR VQCAEVWCPM SPEFYREYLT
TKTSKKMLLY VMNPSKFRSC QFLIKYHEQR GDKTIVFSDN VFALKHYAIK MNKPFIYGPT
SQNERIQILQ NFKFNSKVNT IFVSKVADTS FDLPEANVLI QISSHGGSRR QEAQRLGRIL
RAKKGAIAEE YNAFFYTLVS QDTMEMSYSR KRQRFLVNQG YSYKVITHLK GMDTDSDLMY
GTQEEQGQLL QLVLSASDLD CEDEKLPGEP GYRPSGSGGA VRRVGGLSSM SGGDDAIYYE
HRKKNIGSVH PLFKKFRG
