TF2B_YEAST
ID TF2B_YEAST Reviewed; 345 AA.
AC P29055; D6W488; E9P939;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Transcription initiation factor IIB;
DE AltName: Full=General transcription factor TFIIB;
DE AltName: Full=Transcription factor E;
GN Name=SUA7; OrderedLocusNames=YPR086W; ORFNames=P9513.4;
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=1547497; DOI=10.1016/0092-8674(92)90040-j;
RA Pinto I., Ware D.E., Hampsey M.;
RT "The yeast SUA7 gene encodes a homolog of human transcription factor TFIIB
RT and is required for normal start site selection in vivo.";
RL Cell 68:977-988(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
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).
CC -!- FUNCTION: General factor that plays a major role in the activation of
CC eukaryotic genes transcribed by RNA polymerase II.
CC -!- SUBUNIT: Associates with TFIID-IIA (DA complex) to form TFIID-IIA-IIB
CC (DAB-complex) which is then recognized by polymerase II.
CC -!- INTERACTION:
CC P29055; P20434: RPB5; NbExp=4; IntAct=EBI-19123, EBI-15781;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 6750 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; M81380; AAA35126.1; -; Genomic_DNA.
DR EMBL; U51033; AAB68135.1; -; Genomic_DNA.
DR EMBL; AY693232; AAT93251.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11504.1; -; Genomic_DNA.
DR PIR; S26707; S26707.
DR RefSeq; NP_015411.1; NM_001184183.1.
DR PDB; 3K1F; X-ray; 4.30 A; M=1-68.
DR PDB; 3K7A; X-ray; 3.80 A; M=1-345.
DR PDB; 4BBR; X-ray; 3.40 A; M=1-345.
DR PDB; 4BBS; X-ray; 3.60 A; M=1-345.
DR PDB; 4V1N; EM; 7.80 A; M=1-345.
DR PDB; 4V1O; EM; 9.70 A; M=1-345.
DR PDB; 5FMF; EM; 6.00 A; P=1-345.
DR PDB; 5FYW; EM; 4.35 A; M=1-345.
DR PDB; 5FZ5; EM; 8.80 A; M=1-345.
DR PDB; 5OQJ; EM; 4.70 A; M=1-345.
DR PDB; 5OQM; EM; 5.80 A; M=1-345.
DR PDB; 5SVA; EM; 15.30 A; c=1-345.
DR PDB; 6GYK; EM; 5.10 A; M=1-345.
DR PDB; 6GYL; EM; 4.80 A; M=1-345.
DR PDB; 6GYM; EM; 6.70 A; M=1-345.
DR PDB; 7ML0; EM; 3.00 A; M=1-345.
DR PDB; 7ML1; EM; 4.00 A; M=1-345.
DR PDB; 7ML2; EM; 3.40 A; M=1-345.
DR PDB; 7ML4; EM; 3.10 A; M=1-345.
DR PDB; 7O4I; EM; 3.20 A; M=1-345.
DR PDB; 7O4J; EM; 2.90 A; M=1-345.
DR PDB; 7O72; EM; 3.40 A; M=1-345.
DR PDB; 7O73; EM; 3.40 A; M=1-345.
DR PDB; 7O75; EM; 3.20 A; M=1-345.
DR PDBsum; 3K1F; -.
DR PDBsum; 3K7A; -.
DR PDBsum; 4BBR; -.
DR PDBsum; 4BBS; -.
DR PDBsum; 4V1N; -.
DR PDBsum; 4V1O; -.
DR PDBsum; 5FMF; -.
DR PDBsum; 5FYW; -.
DR PDBsum; 5FZ5; -.
DR PDBsum; 5OQJ; -.
DR PDBsum; 5OQM; -.
DR PDBsum; 5SVA; -.
DR PDBsum; 6GYK; -.
DR PDBsum; 6GYL; -.
DR PDBsum; 6GYM; -.
DR PDBsum; 7ML0; -.
DR PDBsum; 7ML1; -.
DR PDBsum; 7ML2; -.
DR PDBsum; 7ML4; -.
DR PDBsum; 7O4I; -.
DR PDBsum; 7O4J; -.
DR PDBsum; 7O72; -.
DR PDBsum; 7O73; -.
DR PDBsum; 7O75; -.
DR AlphaFoldDB; P29055; -.
DR SMR; P29055; -.
DR BioGRID; 36257; 412.
DR DIP; DIP-701N; -.
DR IntAct; P29055; 61.
DR MINT; P29055; -.
DR STRING; 4932.YPR086W; -.
DR MoonDB; P29055; Predicted.
DR iPTMnet; P29055; -.
DR MaxQB; P29055; -.
DR PaxDb; P29055; -.
DR PRIDE; P29055; -.
DR EnsemblFungi; YPR086W_mRNA; YPR086W; YPR086W.
DR GeneID; 856201; -.
DR KEGG; sce:YPR086W; -.
DR SGD; S000006290; SUA7.
DR VEuPathDB; FungiDB:YPR086W; -.
DR eggNOG; KOG1597; Eukaryota.
DR GeneTree; ENSGT00390000006671; -.
DR HOGENOM; CLU_043736_1_0_1; -.
DR InParanoid; P29055; -.
DR OMA; DHDQRMK; -.
DR BioCyc; YEAST:G3O-34230-MON; -.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-6807505; RNA polymerase II transcribes snRNA genes.
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-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR EvolutionaryTrace; P29055; -.
DR PRO; PR:P29055; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P29055; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0097550; C:transcription preinitiation complex; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IDA:SGD.
DR GO; GO:0001139; F:RNA polymerase II complex recruiting activity; IDA:SGD.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IBA:GO_Central.
DR GO; GO:0017025; F:TBP-class protein binding; IDA:SGD.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IBA:GO_Central.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IDA:SGD.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IDA:SGD.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0001113; P:transcription open complex formation at RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0001174; P:transcriptional start site selection at RNA polymerase II promoter; IMP:SGD.
DR CDD; cd00043; CYCLIN; 2.
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 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; 1.
DR PROSITE; PS51134; ZF_TFIIB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..345
FT /note="Transcription initiation factor IIB"
FT /id="PRO_0000119308"
FT REPEAT 136..212
FT /note="1"
FT REPEAT 242..318
FT /note="2"
FT ZN_FING 20..53
FT /note="TFIIB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT REGION 65..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT CONFLICT 10
FT /note="R -> L (in Ref. 4; AAT93251)"
FT /evidence="ECO:0000305"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:4BBR"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:4BBR"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:4BBR"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:7O73"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 121..139
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:7O4I"
FT HELIX 168..182
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 189..193
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 200..219
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 250..262
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 274..288
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 295..301
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 306..315
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 316..319
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 326..331
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:7O4J"
SQ SEQUENCE 345 AA; 38200 MW; 8F1F6D24602436E2 CRC64;
MMTRESIDKR AGRRGPNLNI VLTCPECKVY PPKIVERFSE GDVVCALCGL VLSDKLVDTR
SEWRTFSNDD HNGDDPSRVG EASNPLLDGN NLSTRIGKGE TTDMRFTKEL NKAQGKNVMD
KKDNEVQAAF AKITMLCDAA ELPKIVKDCA KEAYKLCHDE KTLKGKSMES IMAASILIGC
RRAEVARTFK EIQSLIHVKT KEFGKTLNIM KNILRGKSED GFLKIDTDNM SGAQNLTYIP
RFCSHLGLPM QVTTSAEYTA KKCKEIKEIA GKSPITIAVV SIYLNILLFQ IPITAAKVGQ
TLQVTEGTIK SGYKILYEHR DKLVDPQLIA NGVVSLDNLP GVEKK
