TF3B_YEAST
ID TF3B_YEAST Reviewed; 596 AA.
AC P29056; D6VV26;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Transcription factor IIIB 70 kDa subunit;
DE Short=TFIIIB;
DE AltName: Full=B-related factor 1;
DE Short=BRF-1;
GN Name=BRF1; Synonyms=PCF4, TDS4; OrderedLocusNames=YGR246C;
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].
RX PubMed=1423589; DOI=10.1016/0092-8674(92)90350-l;
RA Lopez-De-Leon A., Librizzi M., Puglia K., Willis I.M.;
RT "PCF4 encodes an RNA polymerase III transcription factor with homology to
RT TFIIB.";
RL Cell 71:211-220(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1423590; DOI=10.1016/0092-8674(92)90351-c;
RA Buratowski S., Zhou H.;
RT "A suppressor of TBP mutations encodes an RNA polymerase III transcription
RT factor with homology to TFIIB.";
RL Cell 71:221-230(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1398071; DOI=10.1101/gad.6.10.1940;
RA Colbert T., Hahn S.;
RT "A yeast TFIIB-related factor involved in RNA polymerase III
RT transcription.";
RL Genes Dev. 6:1940-1949(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9133742;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<373::aid-yea82>3.0.co;2-v;
RA Feroli F., Carignani G., Pavanello A., Guerreiro P., Azevedo D.,
RA Rodrigues-Pousada C., Melchioretto P., Panzeri L., Agostoni Carbone M.L.;
RT "Analysis of a 17.9 kb region from Saccharomyces cerevisiae chromosome VII
RT reveals the presence of eight open reading frames, including BRF1
RT (TFIIIB70) and GCN5 genes.";
RL Yeast 13:373-377(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [6]
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 [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381 AND SER-384, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND IDENTIFICATION BY
RP 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 Interacts with TBP. Binds to Pol III subunit C34 and to the TAU135
CC component of TFIIIC.
CC -!- SUBUNIT: TFIIIB comprises the TATA-binding protein (TBP), the B-related
CC factor (BRF) and the B' component (TFC5).
CC -!- INTERACTION:
CC P29056; P13393: SPT15; NbExp=2; IntAct=EBI-19142, EBI-19129;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 4330 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TFIIB family. {ECO:0000305}.
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DR EMBL; M91073; AAB04945.1; -; Genomic_DNA.
DR EMBL; L00630; AAA35148.1; -; Genomic_DNA.
DR EMBL; Y07703; CAA68968.1; -; Genomic_DNA.
DR EMBL; Z73031; CAA97275.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08337.1; -; Genomic_DNA.
DR PIR; A44072; A44072.
DR RefSeq; NP_011762.1; NM_001181375.1.
DR PDB; 1NGM; X-ray; 2.95 A; B/F/J/N=437-506.
DR PDB; 6CNB; EM; 4.10 A; R=1-382, R=438-596.
DR PDB; 6CNC; EM; 4.10 A; R=1-382, R=438-596.
DR PDB; 6CND; EM; 4.80 A; R=1-382, R=438-596.
DR PDB; 6CNF; EM; 4.50 A; R=1-382, R=438-596.
DR PDB; 6EU0; EM; 4.00 A; Z=1-596.
DR PDB; 6F40; EM; 3.70 A; V=1-596.
DR PDB; 6F41; EM; 4.30 A; V=1-596.
DR PDB; 6F42; EM; 5.50 A; V=1-596.
DR PDB; 6F44; EM; 4.20 A; V=1-596.
DR PDB; 7Q5B; EM; 3.98 A; Z=1-596.
DR PDBsum; 1NGM; -.
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; P29056; -.
DR SMR; P29056; -.
DR BioGRID; 33497; 201.
DR ComplexPortal; CPX-1143; Transcription factor TFIIIB complex.
DR DIP; DIP-191N; -.
DR IntAct; P29056; 13.
DR MINT; P29056; -.
DR STRING; 4932.YGR246C; -.
DR iPTMnet; P29056; -.
DR MaxQB; P29056; -.
DR PaxDb; P29056; -.
DR PRIDE; P29056; -.
DR EnsemblFungi; YGR246C_mRNA; YGR246C; YGR246C.
DR GeneID; 853161; -.
DR KEGG; sce:YGR246C; -.
DR SGD; S000003478; BRF1.
DR VEuPathDB; FungiDB:YGR246C; -.
DR eggNOG; KOG1598; Eukaryota.
DR GeneTree; ENSGT00390000010349; -.
DR HOGENOM; CLU_010293_3_3_1; -.
DR InParanoid; P29056; -.
DR OMA; NYEALDM; -.
DR BioCyc; YEAST:G3O-30921-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 EvolutionaryTrace; P29056; -.
DR PRO; PR:P29056; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P29056; protein.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000126; C:transcription factor TFIIIB complex; IDA:SGD.
DR GO; GO:0097550; C:transcription preinitiation complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000994; F:RNA polymerase III core binding; IDA:SGD.
DR GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; IBA:GO_Central.
DR GO; GO:0001006; F:RNA polymerase III type 3 promoter sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0017025; F:TBP-class protein binding; IDA: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:0006352; P:DNA-templated transcription, initiation; IBA:GO_Central.
DR GO; GO:0006359; P:regulation of transcription by RNA polymerase III; IDA:ComplexPortal.
DR GO; GO:0070898; P:RNA polymerase III preinitiation complex assembly; IDA:SGD.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IBA:GO_Central.
DR GO; GO:0070893; P:transposon integration; IDA:SGD.
DR CDD; cd00043; CYCLIN; 2.
DR InterPro; IPR029529; Brf1.
DR InterPro; IPR011665; BRF1_TBP-bd_dom.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR000812; TFIIB.
DR InterPro; IPR023486; TFIIB_CS.
DR InterPro; IPR013150; TFIIB_cyclin.
DR InterPro; IPR013137; Znf_TFIIB.
DR PANTHER; PTHR11618; PTHR11618; 1.
DR PANTHER; PTHR11618:SF4; PTHR11618:SF4; 1.
DR Pfam; PF07741; BRF1; 1.
DR Pfam; PF08271; TF_Zn_Ribbon; 1.
DR Pfam; PF00382; TFIIB; 2.
DR PRINTS; PR00685; TIFACTORIIB.
DR SMART; SM00385; CYCLIN; 2.
DR SUPFAM; SSF47954; SSF47954; 2.
DR PROSITE; PS00782; TFIIB; 2.
DR PROSITE; PS51134; ZF_TFIIB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..596
FT /note="Transcription factor IIIB 70 kDa subunit"
FT /id="PRO_0000119346"
FT REPEAT 90..166
FT /note="1"
FT REPEAT 185..264
FT /note="2"
FT ZN_FING 1..33
FT /note="TFIIB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT REGION 363..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 4
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT HELIX 442..444
FT /evidence="ECO:0007829|PDB:1NGM"
FT HELIX 448..452
FT /evidence="ECO:0007829|PDB:1NGM"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:1NGM"
FT HELIX 477..490
FT /evidence="ECO:0007829|PDB:1NGM"
FT TURN 491..493
FT /evidence="ECO:0007829|PDB:1NGM"
FT HELIX 494..500
FT /evidence="ECO:0007829|PDB:1NGM"
FT TURN 501..505
FT /evidence="ECO:0007829|PDB:1NGM"
SQ SEQUENCE 596 AA; 66906 MW; 489207643A66B796 CRC64;
MPVCKNCHGT EFERDLSNAN NDLVCKACGV VSEDNPIVSE VTFGETSAGA AVVQGSFIGA
GQSHAAFGGS SALESREATL NNARRKLRAV SYALHIPEYI TDAAFQWYKL ALANNFVQGR
RSQNVIASCL YVACRKEKTH HMLIDFSSRL QVSVYSIGAT FLKMVKKLHI TELPLADPSL
FIQHFAEKLD LADKKIKVVK DAVKLAQRMS KDWMFEGRRP AGIAGACILL ACRMNNLRRT
HTEIVAVSHV AEETLQQRLN EFKNTKAAKL SVQKFRENDV EDGEARPPSF VKNRKKERKI
KDSLDKEEMF QTSEEALNKN PILTQVLGEQ ELSSKEVLFY LKQFSERRAR VVERIKATNG
IDGENIYHEG SENETRKRKL SEVSIQNEHV EGEDKETEGT EEKVKKVKTK TSEEKKENES
GHFQDAIDGY SLETDPYCPR NLHLLPTTDT YLSKVSDDPD NLEDVDDEEL NAHLLNEEAS
KLKERIWIGL NADFLLEQES KRLKQEADIA TGNTSVKKKR TRRRNNTRSD EPTKTVDAAA
AIGLMSDLQD KSGLHAALKA AEESGDFTTA DSVKNMLQKA SFSKKINYDA IDGLFR
