TFC5_YEAST
ID TFC5_YEAST Reviewed; 594 AA.
AC P46678; D6W1E0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Transcription factor TFIIIB component B'';
DE AltName: Full=TFIIIB90;
GN Name=BDP1; Synonyms=TFC5; OrderedLocusNames=YNL039W; ORFNames=N2682;
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 [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=7568218; DOI=10.1073/pnas.92.21.9786;
RA Kassavetis G.A., Nguyen S.T., Kobayashi R., Kumar A., Geiduschek E.P.,
RA Pisano M.;
RT "Cloning, expression, and function of TFC5, the gene encoding the B'
RT component of the Saccharomyces cerevisiae RNA polymerase III transcription
RT factor TFIIIB.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9786-9790(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8617241; DOI=10.1002/j.1460-2075.1996.tb00545.x;
RA Rueth J., Conesa C., Dieci G., Lefebvre O., Duesterhoeft A., Ottonello S.,
RA Sentenac A.;
RT "A suppressor of mutations in the class III transcription system encodes a
RT component of yeast TFIIIB.";
RL EMBO J. 15:1941-1949(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8662956; DOI=10.1074/jbc.271.25.14903;
RA Roberts S., Miller S.J., Lane W.S., Lee S., Hahn S.;
RT "Cloning and functional characterization of the gene encoding the TFIIIB90
RT subunit of RNA polymerase III transcription factor TFIIIB.";
RL J. Biol. Chem. 271:14903-14909(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [5]
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 [6]
RP INTERACTION WITH TFC4.
RX PubMed=1922038; DOI=10.1128/mcb.11.10.5181-5189.1991;
RA Bartholomew B., Kassavetis G.A., Geiduschek E.P.;
RT "Two components of Saccharomyces cerevisiae transcription factor IIIB
RT (TFIIIB) are stereospecifically located upstream of a tRNA gene and
RT interact with the second-largest subunit of TFIIIC.";
RL Mol. Cell. Biol. 11:5181-5189(1991).
RN [7]
RP INTERACTION WITH TFC4.
RX PubMed=12930823; DOI=10.1074/jbc.m308354200;
RA Liao Y., Willis I.M., Moir R.D.;
RT "The Brf1 and Bdp1 subunits of transcription factor TFIIIB bind to
RT overlapping sites in the tetratricopeptide repeats of Tfc4.";
RL J. Biol. Chem. 278:44467-44474(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-178, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: General activator of RNA polymerase III transcription.
CC -!- SUBUNIT: TFIIIB comprises the TATA-binding protein (TBP), the B-related
CC factor (BRF) and the B'' component (BDP1). Interacts with TFC4.
CC {ECO:0000269|PubMed:12930823, ECO:0000269|PubMed:1922038}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the TFC5 family. {ECO:0000305}.
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DR EMBL; U31819; AAC49073.1; -; Genomic_DNA.
DR EMBL; U38415; AAC49364.1; -; Genomic_DNA.
DR EMBL; U37533; AAC49348.1; -; Genomic_DNA.
DR EMBL; Z71315; CAA95906.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10506.1; -; Genomic_DNA.
DR PIR; S62141; S62141.
DR RefSeq; NP_014359.3; NM_001182878.3.
DR PDB; 6CNB; EM; 4.10 A; S=1-594.
DR PDB; 6CNC; EM; 4.10 A; S=1-594.
DR PDB; 6CND; EM; 4.80 A; S=1-594.
DR PDB; 6CNF; EM; 4.50 A; S=1-594.
DR PDB; 6EU0; EM; 4.00 A; V=1-594.
DR PDB; 6F40; EM; 3.70 A; W=1-594.
DR PDB; 6F41; EM; 4.30 A; W=1-594.
DR PDB; 6F42; EM; 5.50 A; W=1-594.
DR PDB; 6F44; EM; 4.20 A; W=1-594.
DR PDB; 7Q5B; EM; 3.98 A; X=1-594.
DR PDBsum; 6CNB; -.
DR PDBsum; 6CNC; -.
DR PDBsum; 6CND; -.
DR PDBsum; 6CNF; -.
DR PDBsum; 6EU0; -.
DR PDBsum; 6F40; -.
DR PDBsum; 6F41; -.
DR PDBsum; 6F42; -.
DR PDBsum; 6F44; -.
DR PDBsum; 7Q5B; -.
DR AlphaFoldDB; P46678; -.
DR SMR; P46678; -.
DR BioGRID; 35785; 54.
DR ComplexPortal; CPX-1143; Transcription factor TFIIIB complex.
DR DIP; DIP-964N; -.
DR IntAct; P46678; 6.
DR MINT; P46678; -.
DR STRING; 4932.YNL039W; -.
DR iPTMnet; P46678; -.
DR MaxQB; P46678; -.
DR PaxDb; P46678; -.
DR PRIDE; P46678; -.
DR EnsemblFungi; YNL039W_mRNA; YNL039W; YNL039W.
DR GeneID; 855689; -.
DR KEGG; sce:YNL039W; -.
DR SGD; S000004984; BDP1.
DR VEuPathDB; FungiDB:YNL039W; -.
DR eggNOG; KOG2009; Eukaryota.
DR GeneTree; ENSGT00390000012762; -.
DR HOGENOM; CLU_021041_1_0_1; -.
DR OMA; HPVMIEL; -.
DR BioCyc; YEAST:G3O-33075-MON; -.
DR Reactome; R-SCE-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-SCE-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR PRO; PR:P46678; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P46678; protein.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000126; C:transcription factor TFIIIB complex; IDA:SGD.
DR GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; IC:SGD.
DR GO; GO:0001156; F:TFIIIC-class transcription factor complex binding; IDA:SGD.
DR GO; GO:0001112; P:DNA-templated transcription open complex formation; IMP:SGD.
DR GO; GO:0070896; P:positive regulation of transposon integration; IDA:SGD.
DR GO; GO:0006359; P:regulation of transcription by RNA polymerase III; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0070898; P:RNA polymerase III preinitiation complex assembly; IDA:SGD.
DR CDD; cd00167; SANT; 1.
DR InterPro; IPR017174; Bdp1_fungi.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR039467; TFIIIB_B''_Myb.
DR Pfam; PF15963; Myb_DNA-bind_7; 1.
DR PIRSF; PIRSF037327; TFIIIB_Bdp1_fun; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..594
FT /note="Transcription factor TFIIIB component B''"
FT /id="PRO_0000072498"
FT DOMAIN 415..466
FT /note="SANT"
FT REGION 1..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 594 AA; 67688 MW; 7B0115BBB2491175 CRC64;
MSSIVNKSGT RFAPKVRQRR AATGGTPTPK PRTPQLFIPE SKEIEEDNSD NDKGVDENET
AIVEKPSLVG ERSLEGFTLT GTNGHDNEIG DEGPIDASTQ NPKADVIEDN VTLKPAPLQT
HRDQKVPRSS RLASLSKDNE SRPSFKPSFL DSSSNSNGTA RRLSTISNKL PKKIRLGSIT
ENDMNLKTFK RHRVLGKPSS AKKPAGAHRI SIVSKISPPT AMTDSLDRNE FSSETSTSRE
ADENENYVIS KVKDIPKKVR DGESAKYFID EENFTMAELC KPNFPIGQIS ENFEKSKMAK
KAKLEKRRHL RELRMRARQE FKPLHSLTKE EQEEEEEKRK EERDKLLNAD IPESDRKAHT
AIQLKLNPDG TMAIDEETMV VDRHKNASIE NEYKEKVDEN PFANLYNYGS YGRGSYTDPW
TVEEMIKFYK ALSMWGTDFN LISQLYPYRS RKQVKAKFVN EEKKRPILIE LALRSKLPPN
FDEYCCEIKK NIGTVADFNE KLIELQNEHK HHMKEIEEAK NTAKEEDQTA QRLNDANLNK
KGSGGIMTND LKVYRKTEVV LGTIDDLKRK KLKERNNDDN EDNEGSEEEP EIDQ
