RAD15_SCHPO
ID RAD15_SCHPO Reviewed; 772 AA.
AC P26659;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=General transcription and DNA repair factor IIH helicase subunit XPD;
DE Short=TFIIH subunit XPD;
DE EC=3.6.4.12;
DE AltName: Full=DNA repair helicase RAD3 homolog {ECO:0000305|PubMed:1534406};
DE Short=Protein rhp3 {ECO:0000303|PubMed:1534406};
DE AltName: Full=DNA repair helicase rad15 {ECO:0000303|PubMed:1319571};
DE AltName: Full=RNA polymerase II transcription factor B subunit rad15;
DE Short=TFB subunit rad15;
GN Name=rad15 {ECO:0000303|PubMed:1319571};
GN Synonyms=rad5 {ECO:0000303|PubMed:8960127},
GN rhp3 {ECO:0000303|PubMed:1534406};
GN ORFNames=SPAC1D4.12 {ECO:0000312|PomBase:SPAC1D4.12};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=1534406; DOI=10.1093/nar/20.9.2327;
RA Reynolds P.R., Biggar S., Prakash L., Prakash S.;
RT "The Schizosaccharomyces pombe rhp3+ gene required for DNA repair and cell
RT viability is functionally interchangeable with the RAD3 gene of
RT Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 20:2327-2334(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1319571; DOI=10.1093/nar/20.11.2673;
RA Murray J.M., Doe C., Schenk P., Carr A.M., Lehmann A.R., Watts F.Z.;
RT "Cloning and characterisation of the S. pombe rad15 gene, a homologue to
RT the S. cerevisiae RAD3 and human ERCC2 genes.";
RL Nucleic Acids Res. 20:2673-2678(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP FUNCTION.
RX PubMed=8960127;
RA Fortunato E.A., Osman F., Subramani S.;
RT "Analysis of spontaneous and double-strand break-induced recombination in
RT rad mutants of S. pombe.";
RL Mutat. Res. 364:14-60(1996).
RN [5]
RP SUBUNIT.
RX PubMed=14534314; DOI=10.1074/jbc.m306750200;
RA Spaehr H., Khorosjutina O., Baraznenok V., Linder T., Samuelsen C.O.,
RA Hermand D., Maekelae T.P., Holmberg S., Gustafsson C.M.;
RT "Mediator influences Schizosaccharomyces pombe RNA polymerase II-dependent
RT transcription in vitro.";
RL J. Biol. Chem. 278:51301-51306(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: ATP-dependent 5'-3' 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 TFIIK, 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 ATP-dependent helicase
CC activity of XPD/rad15 is required for DNA opening. In transcription,
CC TFIIH has an essential role in transcription initiation. When the pre-
CC initiation complex (PIC) has been established, TFIIH 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 TFIIK controls the initiation of transcription. XPD/rad15 acts
CC by forming a bridge between TFIIK and the core-TFIIH complex. Involved
CC in the maintenance of the fidelity of DNA replication.
CC {ECO:0000269|PubMed:1534406, ECO:0000269|PubMed:8960127}.
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 Evidence={ECO:0000250|UniProtKB:P06839};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P06839};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P06839};
CC -!- SUBUNIT: Component of the 7-subunit TFIIH core complex composed of
CC XPB/ptr8, XPD/rad15, ssl1, tfb1, tfb2, tfb4 and tfb5, which is active
CC in NER. The core complex associates with the 3-subunit CTD-kinase
CC module TFIIK composed of mcs2/cyclin H, mcs6/cdk7 and pmh1/tfb3 to form
CC the 10-subunit holoenzyme (holo-TFIIH) active in transcription.
CC {ECO:0000269|PubMed:14534314}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily.
CC {ECO:0000305}.
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DR EMBL; X64583; CAA45870.1; -; Genomic_DNA.
DR EMBL; X60499; CAA43022.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA93221.1; -; Genomic_DNA.
DR PIR; S22660; S22660.
DR RefSeq; NP_593025.1; NM_001018424.2.
DR AlphaFoldDB; P26659; -.
DR SMR; P26659; -.
DR IntAct; P26659; 1.
DR STRING; 4896.SPAC1D4.12.1; -.
DR MaxQB; P26659; -.
DR PaxDb; P26659; -.
DR EnsemblFungi; SPAC1D4.12.1; SPAC1D4.12.1:pep; SPAC1D4.12.
DR GeneID; 2542203; -.
DR KEGG; spo:SPAC1D4.12; -.
DR PomBase; SPAC1D4.12; rad15.
DR VEuPathDB; FungiDB:SPAC1D4.12; -.
DR eggNOG; KOG1131; Eukaryota.
DR HOGENOM; CLU_011312_1_0_1; -.
DR InParanoid; P26659; -.
DR OMA; IREQFFR; -.
DR PhylomeDB; P26659; -.
DR Reactome; R-SPO-113418; Formation of the Early Elongation Complex.
DR Reactome; R-SPO-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-SPO-5696400; Dual Incision in GG-NER.
DR Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SPO-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SPO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SPO-72086; mRNA Capping.
DR Reactome; R-SPO-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-SPO-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-SPO-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-SPO-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-SPO-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-SPO-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-SPO-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR PRO; PR:P26659; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IGI:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000439; C:transcription factor TFIIH core complex; ISO:PomBase.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; ISO:PomBase.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; IC:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0003678; F:DNA helicase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IC:PomBase.
DR GO; GO:0000717; P:nucleotide-excision repair, DNA duplex unwinding; IGI:PomBase.
DR GO; GO:0033683; P:nucleotide-excision repair, DNA incision; IBA:GO_Central.
DR GO; GO:0045951; P:positive regulation of mitotic recombination; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISO:PomBase.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR010614; DEAD_2.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR010643; HBB.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013020; Rad3/Chl1-like.
DR InterPro; IPR001945; RAD3/XPD.
DR PANTHER; PTHR11472; PTHR11472; 1.
DR PANTHER; PTHR11472:SF1; PTHR11472:SF1; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF06777; HBB; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR PRINTS; PR00852; XRODRMPGMNTD.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00604; rad3; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Iron; Iron-sulfur; Metal-binding; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..772
FT /note="General transcription and DNA repair factor IIH
FT helicase subunit XPD"
FT /id="PRO_0000101984"
FT DOMAIN 7..283
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOTIF 233..236
FT /note="DEAH box"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 115
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P06839"
FT BINDING 133
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P06839"
FT BINDING 154
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P06839"
FT BINDING 189
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P06839"
FT CONFLICT 225
FT /note="S -> N (in Ref. 1; CAA45870)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="S -> T (in Ref. 2; CAA43022)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 772 AA; 88149 MW; A21025C298A28F08 CRC64;
MKFYIDDLPI LFPYPRIYPE QYQYMCDLKH SLDAGGIALL EMPSGTGKTI SLLSLIVSYQ
QHYPEHRKLI YCSRTMSEID KALAELKRLM AYRTSQLGYE EPFLGLGLTS RKNLCLHPSV
RREKNGNVVD ARCRSLTAGF VREQRLAGMD VPTCEFHDNL EDLEPHSLIS NGVWTLDDIT
EYGEKTTRCP YFTVRRMLPF CNVIIYSYHY LLDPKIAERV SRELSKDCIV VFDEAHNIDN
VCIESLSIDL TESSLRKASK SILSLEQKVN EVKQSDSKKL QDEYQKLVRG LQDANAANDE
DQFMANPVLP EDVLKEAVPG NIRRAEHFIA FLKRFVEYLK TRMKVLHVIA ETPTSFLQHV
KDITFIDKKP LRFCAERLTS LVRALQISLV EDFHSLQQVV AFATLVATYE RGFILILEPF
ETENATVPNP ILRFSCLDAS IAIKPVFERF RSVIITSGTL SPLDMYPKML QFNTVMQESY
GMSLARNCFL PMVVTRGSDQ VAISSKFEAR NDPSVVRNYG NILVEFSKIT PDGLVAFFPS
YLYLESIVSS WQSMGILDEV WKYKLILVET PDPHETTLAL ETYRAACSNG RGAVLLSVAR
GKVSEGVDFD HHYGRAVIMF GIPYQYTESR VLKARLEFLR DTYQIREADF LTFDAMRHAA
QCLGRVLRGK DDHGIMVLAD KRYGRSDKRT KLPKWIQQYI TEGATNLSTD MSLALAKKFL
RTMAQPFTAS DQEGISWWSL DDLLIHQKKA LKSAAIEQSK HEDEMDIDVV ET
