ERCC3_SCHPO
ID ERCC3_SCHPO Reviewed; 804 AA.
AC O13768; Q9US81;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 158.
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 repair helicase ptr8;
DE AltName: Full=Poly(A)+ RNA transport protein 8;
DE AltName: Full=RNA polymerase II transcription factor B subunit ercc3;
DE Short=TFB subunit ercc3;
GN Name=ptr8 {ECO:0000303|PubMed:17212653}; Synonyms=ercc3;
GN ORFNames=SPAC17A5.06;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 126-313, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=17212653; DOI=10.1111/j.1365-2443.2006.01032.x;
RA Mizuki F., Namiki T., Sato H., Furukawa H., Matsusaka T., Ohshima Y.,
RA Ishibashi R., Andoh T., Tani T.;
RT "Participation of XPB/Ptr8p, a component of TFIIH, in nucleocytoplasmic
RT transport of mRNA in fission yeast.";
RL Genes Cells 12:35-47(2007).
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 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 ATPase activity of
CC XPB/ptr8, 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/ptr8 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 TFIIK controls the initiation of transcription (By similarity). Plays a
CC role in mRNA export (PubMed:17212653). {ECO:0000250|UniProtKB:Q00578,
CC ECO:0000269|PubMed:17212653}.
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/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:10759889}.
CC -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB11506.1; -; Genomic_DNA.
DR EMBL; AB027988; BAA87292.1; -; Genomic_DNA.
DR PIR; T37821; T37821.
DR RefSeq; NP_593474.1; NM_001018907.2.
DR AlphaFoldDB; O13768; -.
DR SMR; O13768; -.
DR BioGRID; 278649; 5.
DR IntAct; O13768; 1.
DR STRING; 4896.SPAC17A5.06.1; -.
DR iPTMnet; O13768; -.
DR MaxQB; O13768; -.
DR PaxDb; O13768; -.
DR PRIDE; O13768; -.
DR EnsemblFungi; SPAC17A5.06.1; SPAC17A5.06.1:pep; SPAC17A5.06.
DR GeneID; 2542174; -.
DR KEGG; spo:SPAC17A5.06; -.
DR PomBase; SPAC17A5.06; ptr8.
DR VEuPathDB; FungiDB:SPAC17A5.06; -.
DR eggNOG; KOG1123; Eukaryota.
DR HOGENOM; CLU_008213_0_0_1; -.
DR InParanoid; O13768; -.
DR OMA; PTHIHEY; -.
DR PhylomeDB; O13768; -.
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:O13768; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; IDA: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: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; ISM:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IC:PomBase.
DR GO; GO:0003678; F:DNA helicase activity; ISM:PomBase.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IC:PomBase.
DR GO; GO:0033683; P:nucleotide-excision repair, DNA incision; IBA:GO_Central.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IMP:PomBase.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; ISS:PomBase.
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..804
FT /note="General transcription and DNA repair factor IIH
FT helicase subunit XPB"
FT /id="PRO_0000101993"
FT DOMAIN 335..497
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 551..705
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 450..453
FT /note="DEVH box"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..33
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 348..355
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 804 AA; 91345 MW; 093AC203A3115614 CRC64;
MSLKRKNNAR EGTPDEDLEE YSDYSDVDNY GEEDDDSYKP APRIRINNNK TKAQTTTNSN
EARQSGISAM FGQNDFSNLL GLKLDHTARP LWINPIDGRI ILEAFSPLAE QAIDFLVTIS
EPVSRPAFIH EYRITAYSLY AAVSVGLKTE DIIAVLDRLS KTPIPPSIVD FIRACTVSYG
KVKLVLKKNR YFIESGDASV LRLLLRDPVI GPLRIDYSTQ SSKQKSSKPS NEDNVEDKKD
ITNDSSKETA EKSSSDELFS AVVGLQEEED DEDAVHLFEI KHSSVETIKK RCAEIDYPLL
EEYDFRNDNI NPDLPIDLKP STQIRPYQEK SLSKMFGNGR ARSGIIVLPC GAGKTLVGIT
AACTIKKSVI VLCTSSVSVM QWRQQFLQWS NIKPDHIAVF TADHKERFHS EAGVVVSTYS
MVANTRNRSY DSQKMMDFLT GREWGFILLD EVHVVPAAMF RRVVTTIAAH TKLGLTATLV
REDDKIDDLN FLIGPKMYEA NWMDLAQKGH IAKVQCAEVW CAMTTEFYNE YLRENSRKRM
LLYIMNPKKF QACQFLIDYH EKRGDKIIVF SDNVYALRAY AIKLGKYFIY GGTPQQERMR
ILENFQYNEL VNTIFLSKVG DTSIDLPEAT CLIQISSHYG SRRQEAQRLG RILRAKRRND
EGFNAFFYSL VSKDTQEMYY SSKRQAFLID QGYAFKVITN LKGMENLPNL AYASKAERLE
LLQEVLLQNE EAADLDDGED TSFGSRSLSR APAKAKRSSG SLSTLAGADN MAYVEYNKSA
NKQLKKDSKE HHALFRKHLY TKRR
