ERCC3_DICDI
ID ERCC3_DICDI Reviewed; 800 AA.
AC O00835; Q54XI4;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 152.
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=DNA excision repair cross-complementing protein-3 homolog;
DE AltName: Full=DNA repair helicase repB;
DE AltName: Full=DNA repair protein B;
GN Name=repB; Synonyms=ercc3; ORFNames=DDB_G0278729;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=AX4;
RX PubMed=9171087; DOI=10.1093/nar/25.12.2365;
RA Lee S.-K., Yu S.-L., Garcia M.X.U., Alexander H., Alexander S.;
RT "Differential developmental expression of the rep B and rep D xeroderma
RT pigmentosum related DNA helicase genes from Dictyostelium discoideum.";
RL Nucleic Acids Res. 25:2365-2374(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP MUTAGENESIS OF 755-SER--GLN-800 AND 706-LYS--GLN-800, AND INDUCTION BY UV.
RX PubMed=9765592; DOI=10.1016/s0167-4781(98)00103-1;
RA Lee S.-K., Yu S.-L., Alexander H., Alexander S.;
RT "A mutation in repB, the dictyostelium homolog of the human xeroderma
RT pigmentosum B gene, has increased sensitivity to UV-light but normal
RT morphogenesis.";
RL Biochim. Biophys. Acta 1399:161-172(1998).
RN [4]
RP INDUCTION.
RX PubMed=9649625; DOI=10.1093/nar/26.14.3397;
RA Yu S.-L., Lee S.-K., Alexander H., Alexander S.;
RT "Rapid changes of nucleotide excision repair gene expression following UV-
RT irradiation and cisplatin treatment of Dictyostelium discoideum.";
RL Nucleic Acids Res. 26:3397-3403(1998).
RN [5]
RP INDUCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=11004503; DOI=10.1016/s0167-4781(00)00063-4;
RA Garcia M.X.U., Foote C., van Es S., Devreotes P.N., Alexander S.,
RA Alexander H.;
RT "Differential developmental expression and cell type specificity of
RT Dictyostelium catalases and their response to oxidative stress and UV-
RT light.";
RL Biochim. Biophys. Acta 1492:295-310(2000).
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 XPB/repB, but not its helicase activity, is required for DNA opening.
CC 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 XPB/repB is required for promoter
CC opening and promoter escape. Phosphorylation of the C-terminal tail
CC (CTD) of the largest subunit of RNA polymerase II by the kinase module
CC 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 XPB/repB, XPD/repD, gtf2h1, gtf2h2, gtf2h3, gtf2h4 and gtf2h5, which is
CC active in NER. The core complex associates with the 3-subunit CDK-
CC activating kinase (CAK) module composed of cycH/cyclin H, cdk7 and
CC mnat1 to form the 10-subunit holoenzyme (holo-TFIIH) active in
CC transcription. {ECO:0000250|UniProtKB:P19447}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Constitutively expressed at low levels throughout
CC development. {ECO:0000269|PubMed:11004503, ECO:0000269|PubMed:9171087}.
CC -!- INDUCTION: Up-regulated a dose dependent manner following exposure to
CC both UV LIGHT and cisplatin. Unaffected by exposure to hydrogen
CC peroxide. {ECO:0000269|PubMed:11004503, ECO:0000269|PubMed:9649625,
CC ECO:0000269|PubMed:9765592}.
CC -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U77065; AAB62732.1; -; Genomic_DNA.
DR EMBL; AAFI02000024; EAL67966.1; -; Genomic_DNA.
DR RefSeq; XP_647819.1; XM_642727.1.
DR AlphaFoldDB; O00835; -.
DR SMR; O00835; -.
DR STRING; 44689.DDB0214830; -.
DR PaxDb; O00835; -.
DR PRIDE; O00835; -.
DR EnsemblProtists; EAL67966; EAL67966; DDB_G0278729.
DR GeneID; 8621779; -.
DR KEGG; ddi:DDB_G0278729; -.
DR dictyBase; DDB_G0278729; repB.
DR eggNOG; KOG1123; Eukaryota.
DR HOGENOM; CLU_008213_0_0_1; -.
DR InParanoid; O00835; -.
DR OMA; PTHIHEY; -.
DR PhylomeDB; O00835; -.
DR Reactome; R-DDI-113418; Formation of the Early Elongation Complex.
DR Reactome; R-DDI-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-DDI-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DDI-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-DDI-6782135; Dual incision in TC-NER.
DR Reactome; R-DDI-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-DDI-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-DDI-72086; mRNA Capping.
DR Reactome; R-DDI-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-DDI-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-DDI-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-DDI-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-DDI-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-DDI-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-DDI-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR PRO; PR:O00835; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IBA:GO_Central.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; ISS:dictyBase.
DR GO; GO:0097550; C:transcription preinitiation complex; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
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:0006974; P:cellular response to DNA damage stimulus; IEP:dictyBase.
DR GO; GO:0006289; P:nucleotide-excision repair; ISS:dictyBase.
DR GO; GO:0033683; P:nucleotide-excision repair, DNA incision; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:dictyBase.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0009650; P:UV protection; IMP:dictyBase.
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 2: Evidence at transcript level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..800
FT /note="General transcription and DNA repair factor IIH
FT helicase subunit XPB"
FT /id="PRO_0000376006"
FT DOMAIN 329..491
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 546..704
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 444..447
FT /note="DEVH box"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 342..349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 800 AA; 90257 MW; 0DB636E33067B09A CRC64;
MSSGDSNLKR RRGGNTGQSS KSYNTWTDYE EDLEESGEFN QSIKKTTNTS SATLTSSEEK
GSLLDYSKRC ILKQDNKSRP IWVCPDGHIF LETFSAIYKQ ASDFLVAIAE PVCRPQNIHE
YQLTPYSLYA AVSVGLETND IITVLGRLSK LALPKEVEQF VRQCTQSYGK VKLVLQKNKY
FVESAYPEVL EFLLKDSSIA TARIKPTLEE SVVDPKTGFI INKEVVTGAQ ISGGLQANQS
LDPVLKNDAL SNLLEEEEED TVNNSDQHFH SFEIDPQQVE EVKKRCIQLD YPVLEEYDFR
NDTVNPNLNI DLKPTTMIRP YQEKSLSKMF GNGRARSGII VLPCGAGKSL SGITAACTVK
KSILVLCTSA VSVEQWKYQF KLWSNIEERQ ISKFTSDNKE KISNVAGVTI TTYTMVAFGG
RRSAESLKIM NEITNREWGL VLLDEVHVVP AAMFRKVLTV TKAHCKLGLT ATLLREDEKI
QDLNFLIGPK LYEANWLDLQ KAGFLANVSC SEVWCPMTAE FYKEYLINDS QGKKKLLYTM
NPNKFRACEY LIRFHEQRGD KIIVFSDNVY ALQKYAKGLG RYFIYGPTSG HERMSILSKF
QHDPTVRTIF ISKVGDTSID IPEATVIIQV SSHYGSRRQE AQRLGRILRP KPKSDGLYNA
FFYSLVSKDT QEMYYSTKRQ QFLIDQGYSF KVISELPGID QEVNLKYSSK QDQLDLLAQV
LGEGEDSGKN EILEEDFDDI TRGAKKSKSS APTVSRTTGG STRALSGGND MNYMEYQAPA
IYKSIPTQHA LFKQRAKNKQ
