TFB5_YEAST
ID TFB5_YEAST Reviewed; 72 AA.
AC Q3E7C1; D6VS66;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=General transcription and DNA repair factor IIH subunit TFB5;
DE Short=TFIIH subunit TFB5;
DE AltName: Full=RNA polymerase II transcription factor B subunit 5;
GN Name=TFB5; OrderedLocusNames=YDR079C-A;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP PROTEIN SEQUENCE OF 6-17, AND IDENTIFICATION IN THE TFIIH CORE COMPLEX.
RX PubMed=15220919; DOI=10.1038/ng1385;
RA Ranish J.A., Hahn S., Lu Y., Yi E.C., Li X.-J., Eng J., Aebersold R.;
RT "Identification of TFB5, a new component of general transcription and DNA
RT repair factor IIH.";
RL Nat. Genet. 36:707-713(2004).
RN [4]
RP FUNCTION OF TFIIH IN RNA POLYMERASE II TRANSCRIPTION.
RX PubMed=7961739; DOI=10.1016/s0021-9258(18)46892-5;
RA Svejstrup J.Q., Feaver W.J., LaPointe J., Kornberg R.D.;
RT "RNA polymerase transcription factor IIH holoenzyme from yeast.";
RL J. Biol. Chem. 269:28044-28048(1994).
RN [5]
RP FUNCTION OF THE TFIIH CORE COMPLEX IN DNA REPAIR.
RX PubMed=8631896; DOI=10.1074/jbc.271.18.10821;
RA Sung P., Guzder S.N., Prakash L., Prakash S.;
RT "Reconstitution of TFIIH and requirement of its DNA helicase subunits, Rad3
RT and Rad25, in the incision step of nucleotide excision repair.";
RL J. Biol. Chem. 271:10821-10826(1996).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-72, AND INTERACTION WITH TFB2.
RX PubMed=19172752; DOI=10.1038/nsmb.1478;
RA Kainov D.E., Vitorino M., Cavarelli J., Poterszman A., Egly J.M.;
RT "Structural basis for group A trichothiodystrophy.";
RL Nat. Struct. Mol. Biol. 15:980-984(2008).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (6.00 ANGSTROMS) OF 2-64.
RX PubMed=26483468; DOI=10.1073/pnas.1518255112;
RA Murakami K., Tsai K.L., Kalisman N., Bushnell D.A., Asturias F.J.,
RA Kornberg R.D.;
RT "Structure of an RNA polymerase II preinitiation complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13543-13548(2015).
RN [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (15.30 ANGSTROMS).
RX PubMed=27610567; DOI=10.1016/j.cell.2016.08.050;
RA Robinson P.J., Trnka M.J., Bushnell D.A., Davis R.E., Mattei P.J.,
RA Burlingame A.L., Kornberg R.D.;
RT "Structure of a complete mediator-RNA polymerase II pre-initiation
RT complex.";
RL Cell 166:1411-1422(2016).
CC -!- FUNCTION: Component of the general transcription and DNA repair factor
CC IIH (TFIIH) core complex, which is involved in general and
CC transcription-coupled nucleotide excision repair (NER) of damaged DNA
CC and, when complexed to TFIIK, in RNA transcription by RNA polymerase
CC II. In NER, TFIIH acts by opening DNA around the lesion to allow the
CC excision of the damaged oligonucleotide and its replacement by a new
CC DNA fragment. In transcription, TFIIH has an essential role in
CC transcription initiation. When the pre-initiation complex (PIC) has
CC been established, TFIIH is required for promoter opening and promoter
CC escape. Phosphorylation of the C-terminal tail (CTD) of the largest
CC subunit of RNA polymerase II by the kinase module TFIIK controls the
CC initiation of transcription. TFB5 is required for stable recruitment of
CC TFIIH to a promoter, but not for stability of TFIIH subunits.
CC {ECO:0000269|PubMed:7961739, ECO:0000269|PubMed:8631896}.
CC -!- SUBUNIT: Component of the 7-subunit TFIIH core complex composed of
CC XPB/SSL2, XPD/RAD3, SSL1, TFB1, TFB2, TFB4 and TFB5, which is active in
CC NER. The core complex associates with the 3-subunit CTD-kinase module
CC TFIIK composed of CCL1, KIN28 and TFB3 to form the 10-subunit
CC holoenzyme (holo-TFIIH) active in transcription (PubMed:15220919).
CC Interacts with TFB2 (PubMed:19172752). {ECO:0000269|PubMed:15220919,
CC ECO:0000269|PubMed:19172752}.
CC -!- INTERACTION:
CC Q3E7C1; Q02939: TFB2; NbExp=6; IntAct=EBI-2095127, EBI-2345544;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- SIMILARITY: Belongs to the TFB5 family. {ECO:0000305}.
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DR EMBL; Z74376; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006938; DAA11926.1; -; Genomic_DNA.
DR RefSeq; NP_076886.3; NM_001184469.3.
DR PDB; 3DGP; X-ray; 1.80 A; B=2-72.
DR PDB; 3DOM; X-ray; 2.60 A; B/D=2-72.
DR PDB; 5FMF; EM; 6.00 A; X=2-64.
DR PDB; 5OQJ; EM; 4.70 A; 5=1-72.
DR PDB; 5OQM; EM; 5.80 A; 5=1-72.
DR PDB; 5SVA; EM; 15.30 A; b=1-72.
DR PDB; 6GYM; EM; 6.70 A; 5=1-72.
DR PDB; 7K01; EM; 3.90 A; 5=1-72.
DR PDB; 7K04; EM; 9.25 A; 5=1-72.
DR PDB; 7M2U; EM; 8.20 A; 5=2-67.
DR PDB; 7ML0; EM; 3.00 A; 5=1-72.
DR PDB; 7ML1; EM; 4.00 A; 5=1-72.
DR PDB; 7ML2; EM; 3.40 A; 5=1-72.
DR PDB; 7ML3; EM; 7.60 A; 5=1-72.
DR PDB; 7ML4; EM; 3.10 A; 5=1-72.
DR PDB; 7O4I; EM; 3.20 A; 5=1-72.
DR PDB; 7O4J; EM; 2.90 A; 5=1-72.
DR PDB; 7O4K; EM; 3.60 A; 5=1-72.
DR PDB; 7O4L; EM; 3.40 A; 5=1-72.
DR PDB; 7O72; EM; 3.40 A; 5=1-72.
DR PDB; 7O73; EM; 3.40 A; 5=1-72.
DR PDB; 7O75; EM; 3.20 A; 5=1-72.
DR PDBsum; 3DGP; -.
DR PDBsum; 3DOM; -.
DR PDBsum; 5FMF; -.
DR PDBsum; 5OQJ; -.
DR PDBsum; 5OQM; -.
DR PDBsum; 5SVA; -.
DR PDBsum; 6GYM; -.
DR PDBsum; 7K01; -.
DR PDBsum; 7K04; -.
DR PDBsum; 7M2U; -.
DR PDBsum; 7ML0; -.
DR PDBsum; 7ML1; -.
DR PDBsum; 7ML2; -.
DR PDBsum; 7ML3; -.
DR PDBsum; 7ML4; -.
DR PDBsum; 7O4I; -.
DR PDBsum; 7O4J; -.
DR PDBsum; 7O4K; -.
DR PDBsum; 7O4L; -.
DR PDBsum; 7O72; -.
DR PDBsum; 7O73; -.
DR PDBsum; 7O75; -.
DR AlphaFoldDB; Q3E7C1; -.
DR SMR; Q3E7C1; -.
DR BioGRID; 32135; 214.
DR ComplexPortal; CPX-1659; General transcription factor complex TFIIH.
DR DIP; DIP-48375N; -.
DR IntAct; Q3E7C1; 10.
DR MINT; Q3E7C1; -.
DR STRING; 4932.YDR079C-A; -.
DR iPTMnet; Q3E7C1; -.
DR MaxQB; Q3E7C1; -.
DR PaxDb; Q3E7C1; -.
DR PRIDE; Q3E7C1; -.
DR EnsemblFungi; YDR079C-A_mRNA; YDR079C-A; YDR079C-A.
DR GeneID; 851652; -.
DR KEGG; sce:YDR079C-A; -.
DR SGD; S000007603; TFB5.
DR VEuPathDB; FungiDB:YDR079C-A; -.
DR eggNOG; KOG3451; Eukaryota.
DR HOGENOM; CLU_166246_3_1_1; -.
DR InParanoid; Q3E7C1; -.
DR OMA; KVMQPEE; -.
DR BioCyc; YEAST:G3O-30109-MON; -.
DR Reactome; R-SCE-113418; Formation of the Early Elongation Complex.
DR Reactome; R-SCE-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SCE-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SCE-72086; mRNA Capping.
DR Reactome; R-SCE-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-SCE-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-SCE-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-SCE-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-SCE-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-SCE-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR EvolutionaryTrace; Q3E7C1; -.
DR PRO; PR:Q3E7C1; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q3E7C1; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000439; C:transcription factor TFIIH core complex; IPI:SGD.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; IDA:SGD.
DR GO; GO:0006289; P:nucleotide-excision repair; IDA:ComplexPortal.
DR GO; GO:0006294; P:nucleotide-excision repair, preincision complex assembly; IBA:GO_Central.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IDA:SGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:SGD.
DR Gene3D; 3.30.70.1220; -; 1.
DR InterPro; IPR035935; TFB5-like_sf.
DR InterPro; IPR009400; TFIIH_TTDA/Tfb5.
DR PANTHER; PTHR28580; PTHR28580; 1.
DR Pfam; PF06331; Tfb5; 1.
DR SMART; SM01395; Tbf5; 1.
DR SUPFAM; SSF142897; SSF142897; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA damage; DNA repair; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..72
FT /note="General transcription and DNA repair factor IIH
FT subunit TFB5"
FT /id="PRO_0000119287"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:3DGP"
FT HELIX 14..27
FT /evidence="ECO:0007829|PDB:3DGP"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:3DGP"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:3DGP"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:3DGP"
FT HELIX 47..59
FT /evidence="ECO:0007829|PDB:3DGP"
SQ SEQUENCE 72 AA; 8232 MW; 9198E5CCFF304239 CRC64;
MARARKGALV QCDPSIKALI LQIDAKMSDI VLEELDDTHL LVNPSKVEFV KHELNRLLSK
NIYNPMDEEE NQ
