XPB_TRYB2
ID XPB_TRYB2 Reviewed; 938 AA.
AC Q580W5; D6XE64;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=TFIIH basal transcription factor complex helicase XPB subunit;
DE EC=3.6.4.12;
GN Name=XPB {ECO:0000303|PubMed:17259543}; ORFNames=Tb927.3.5100;
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 IDENTIFICATION IN TFIIH COMPLEX.
RX PubMed=17259543; DOI=10.1128/ec.00411-06;
RA Lee J.H., Nguyen T.N., Schimanski B., Guenzl A.;
RT "Spliced leader RNA gene transcription in Trypanosoma brucei requires
RT transcription factor TFIIH.";
RL Eukaryot. Cell 6:641-649(2007).
CC -!- FUNCTION: ATP-dependent 3'-5' DNA helicase, component of the general
CC transcription factor IIH (TFIIH) core complex, involved in spliced
CC leader RNA (SL RNA) gene transcription by RNA polymerase II
CC (PubMed:17259543). 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 is required for promoter opening and
CC promoter escape (By similarity). {ECO:0000250|UniProtKB:Q00578,
CC ECO:0000305|PubMed:17259543}.
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 XPB,
CC XPD, SSL1, TFB1, TFB2, TFB4 and TFB5. {ECO:0000250|UniProtKB:Q00578,
CC ECO:0000305|PubMed:17259543}.
CC -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC {ECO:0000305}.
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DR EMBL; AC093543; AAX81019.1; -; Genomic_DNA.
DR EMBL; CP000066; AAZ10541.1; -; Genomic_DNA.
DR RefSeq; XP_844100.1; XM_839007.1.
DR AlphaFoldDB; Q580W5; -.
DR SMR; Q580W5; -.
DR STRING; 5691.AAZ10541; -.
DR PaxDb; Q580W5; -.
DR GeneID; 3656453; -.
DR KEGG; tbr:Tb927.3.5100; -.
DR VEuPathDB; TriTrypDB:Tb927.3.5100; -.
DR eggNOG; KOG1123; Eukaryota.
DR InParanoid; Q580W5; -.
DR OMA; IRADCYY; -.
DR Proteomes; UP000008524; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR GO; GO:0005654; C:nucleoplasm; IDA:GeneDB.
DR GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:GeneDB.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; IBA:GO_Central.
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:InterPro.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA: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 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 Pfam; PF16203; ERCC3_RAD25_C; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
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; Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..938
FT /note="TFIIH basal transcription factor complex helicase
FT XPB subunit"
FT /id="PRO_0000442798"
FT DOMAIN 394..562
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 627..781
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 515..518
FT /note="DEVH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 407..414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 938 AA; 105211 MW; FB66A3C193DFCE37 CRC64;
MILGPGGRIF INHGHPAYPH LMDFLTACCE PVCRTLYVSE YTISPSSLSA ATAEGTYSME
MVRNVIRYFR LDEQQQIPVD VERYAALERR VRDSVQDTSL DLPMEVGEAK VSANGDVKAE
EGCEEATDEL SPLAGQVKKE ETKEVAAEPR RRFLSLSKRI SAKSEPLVTR AVVNTGALQP
LPADLEQMLR EEENSSRVRI VLQPCLRPVK RRAVGGDKQH SDEQQCQRAE ETKLAYFLTS
PDRNHMEHLV SRLQDFLVPV LLHGTRRWVV SDVDRGVEER STAESGRAKT LRRLFEAPSS
ASGRSVASKS LTNEGANGDG LGGGVGRRCT RIVYKSQVMD GKMRNVRERL YKELSVRADL
FYDYVQDHSL HVCDLELSEN VRLRPYQVAS LERFRSGNKA HQGVIVLPCG AGKTLTGIGA
AATVKKRTIV MCINVMSVLQ WQREFIRWTN LSEDQVTVCI ADKKQMPGDV FITTYSMLIA
RRSNVPEMEQ SADAKLTAKI LASVGEQPWG LLLLDEVHTA LAHNFQEVLN KVKYKCVIGL
SATLLREDDK IGDLRHLVGP KLYEANWLDL TRAGFLARVE CAEIQCPLPK AFLTEYLESQ
SDGDPFARRG TTRMAHSVVC LNPYKLWCTQ ALLEFHRNRS PPDKVIIFCD QIDGIQYYAQ
HLHVPFMDGK TSDMERENLL QYFQHSDNIN AIILSRVGDV ALDIPCASVV IQISGLGASR
RQEAQRLGRI LRPKPASLDN VCSYFYTLVS QDTHEISQSY ERQSWLRDQG FSYRVLQSDM
VLQHFLRTGG KLCCVGPPRW WYECAGPSCD SAVAAKGTYW IPFSQEAALR MQSRFVAGVR
GCDLTATVLR DTPRPPELKN MGVEEKWTVC FSDSCAPETF GTVQLVEGNP LLVRRICCGP
LAVEHDCLHG GEECLQYAVQ QMKVMVAKNS KNRIPLTT
