ID   XPBR_TRYB2              Reviewed;         777 AA.
AC   Q381F9;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=DNA repair helicase XPB-R {ECO:0000303|PubMed:24134817};
DE            EC=3.6.4.12;
GN   Name=XPB-R {ECO:0000303|PubMed:24134817};
GN   ORFNames=Tb11.01.7950, Tb927.11.16270;
OS   Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=185431;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=927/4 GUTat10.1;
RX   PubMed=16020726; DOI=10.1126/science.1112642;
RA   Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA   Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA   Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA   Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA   Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA   Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA   Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA   Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA   Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA   Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA   Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA   Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA   Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA   Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA   Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA   Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA   Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA   Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A.;
RT   "The genome of the African trypanosome Trypanosoma brucei.";
RL   Science 309:416-422(2005).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24134817; DOI=10.1111/mmi.12435;
RA   Badjatia N., Nguyen T.N., Lee J.H., Guenzl A.;
RT   "Trypanosoma brucei harbours a divergent XPB helicase paralogue that is
RT   specialized in nucleotide excision repair and conserved among kinetoplastid
RT   organisms.";
RL   Mol. Microbiol. 90:1293-1308(2013).
CC   -!- FUNCTION: ATP-dependent 3'-5' DNA helicase involved in nucleotide
CC       excision repair (NER) of damaged DNA. XPB-R is a paralog of XBP, but is
CC       not a component of the TFIIH basal transcription factor and is
CC       dispensable for RNA polymerase II transcription.
CC       {ECO:0000269|PubMed:16020726}.
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   -!- DISRUPTION PHENOTYPE: Mutants are much less tolerant than wild-type
CC       cells to UV light- and cisplatin-induced DNA damage.
CC       {ECO:0000269|PubMed:24134817}.
CC   -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CH464491; EAN80572.1; -; Genomic_DNA.
DR   RefSeq; XP_829684.1; XM_824591.1.
DR   AlphaFoldDB; Q381F9; -.
DR   SMR; Q381F9; -.
DR   STRING; 5691.EAN80572; -.
DR   PaxDb; Q381F9; -.
DR   GeneID; 3664517; -.
DR   KEGG; tbr:Tb11.01.7950; -.
DR   VEuPathDB; TriTrypDB:Tb927.11.16270; -.
DR   eggNOG; KOG1123; Eukaryota.
DR   InParanoid; Q381F9; -.
DR   Proteomes; UP000008524; Chromosome 11 Scaffold 1.
DR   GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR   GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISM:GeneDB.
DR   GO; GO:0005675; C:transcription factor TFIIH holo complex; ISA:GeneDB.
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:0003684; F:damaged DNA binding; ISA:GeneDB.
DR   GO; GO:0006281; P:DNA repair; ISA:GeneDB.
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; IBA:GO_Central.
DR   GO; GO:0006351; P:transcription, DNA-templated; ISA:GeneDB.
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; 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; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..777
FT                   /note="DNA repair helicase XPB-R"
FT                   /id="PRO_0000442799"
FT   DOMAIN          212..416
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          484..631
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           369..372
FT                   /note="DEVH box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         225..232
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   777 AA;  85938 MW;  FD0922B05C7FCC27 CRC64;
     MQCLFLEERI KKEGCVVLFA EAFRPSFANI QGFLTTIAEP VSRLSLMHEY RMTYFSLGAA
     ASASISVSEV IQFLDDHVYF FRDKCFASYR ESVCAFAEMY MSRCNLARVV IDESRTLLEC
     KDIVTAKTLL KDRVVRSLCC QPKETVGEDA CPHFLLKSRA AARVVAERCV LLGYPLQQQY
     EYEKDTSIRN VNIALKSQTR PRPYQIAAVD AAASDGALRS GCIVLPCGSG KTLVGIMLLC
     KVKKPTLILC AGGVSVEQWR NQILEFASVC APANNEEGDP SNSTTGEKVR TAAVGAARIS
     CLTGKQKDEI TDETDIVLTT YSMLVTAHKA QARCQVEGFE MNADGRGRNP RRANPKERLF
     QPYGLLIMDE VHMMPADAYK DSLGFINAKG VVGLTATYVR EDSKIRDLFH LVGPKLFDIS
     WERLASSGYL AHVTCIEVLT PLARRFSLEY LERSSELTSP QHGTPLLVML AAANPNKMLC
     VMEIVKRHVA ESSKILVFCD HIMLLKEYSK LLGAPVVCGD TPHRERLMIF SDFQSTSKVN
     VVCLSRVGDV SVNLPSANVV VQVSSHGGSR RQEAQRLGRI LRPKEKASNG KPTDAWFYTV
     ISTDTVEMSY AAHRTAFLVD QGYTCSVTEF NPDGAPEAAV EGVDDTAPGD VVSIRQAKLR
     GTFKKQELKC SVASPTAQGS VNPRSLDYQE KLLCRVVASW ELDYQNATSQ QNEPGVANDT
     ATGLIDKKMK RARDETAEDI KREWNSGAQT TQPRGDFCRL PLQRLVGAND DVVYHES