T2FA_YEAST
ID T2FA_YEAST Reviewed; 735 AA.
AC P41895; D6VUW9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Transcription initiation factor IIF subunit alpha;
DE Short=TFIIF-alpha;
DE AltName: Full=TFIIF large subunit;
DE AltName: Full=Transcription factor G 105 kDa subunit;
DE Short=P105;
GN Name=TFG1; Synonyms=SSU71; OrderedLocusNames=YGR186W; ORFNames=G7526;
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 PROTEIN SEQUENCE OF 125-142 AND
RP 143-161.
RC STRAIN=ATCC 208279 / BJ926;
RX PubMed=7995524; DOI=10.1101/gad.8.23.2868;
RA Henry N.L., Campbell A.M., Feaver W.J., Poon D., Weil P.A., Kornberg R.D.;
RT "TFIIF-TAF-RNA polymerase II connection.";
RL Genes Dev. 8:2868-2878(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7724527; DOI=10.1073/pnas.92.8.3127;
RA Sun Z.W., Hampsey M.;
RT "Identification of the gene (SSU71/TFG1) encoding the largest subunit of
RT transcription factor TFIIF as a suppressor of a TFIIB mutation in
RT Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3127-3131(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9133739;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<357::aid-yea77>3.0.co;2-j;
RA Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez-Perez M.,
RA Nombela C.;
RT "DNA sequence analysis of a 23,002 bp DNA fragment of the right arm of
RT Saccharomyces cerevisiae chromosome VII.";
RL Yeast 13:357-363(1997).
RN [4]
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 [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 FUNCTION.
RX PubMed=1331085; DOI=10.1016/s0021-9258(18)50103-4;
RA Henry N.L., Sayre M.H., Kornberg R.D.;
RT "Purification and characterization of yeast RNA polymerase II general
RT initiation factor g.";
RL J. Biol. Chem. 267:23388-23392(1992).
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 THR-200; SER-515 AND SER-655, AND
RP IDENTIFICATION BY 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-571, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198; SER-515 AND SER-655, AND
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198; THR-200; SER-515;
RP SER-560 AND SER-562, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: TFIIF is a general transcription initiation factor that binds
CC to RNA polymerase II. Its functions include the recruitment of RNA
CC polymerase II to the promoter bound DNA-TBP-TFIIB complex, decreasing
CC the affinity of RNA polymerase II for non-specific DNA, allowing for
CC the subsequent recruitment of TFIIE and TFIIH, and facilitating RNA
CC polymerase II elongation. {ECO:0000269|PubMed:1331085}.
CC -!- SUBUNIT: TFIIF is composed of three different subunits: TFG1/RAP74,
CC TFG2/RAP30 and TAF14.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Phosphorylated on Ser and other residues by TAF1 and casein kinase
CC II-like kinases. {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 1920 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TFIIF alpha subunit family. {ECO:0000305}.
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DR EMBL; U13015; AAA61640.1; -; Genomic_DNA.
DR EMBL; U14527; AAA68478.1; -; Genomic_DNA.
DR EMBL; X99074; CAA67530.1; -; Genomic_DNA.
DR EMBL; Z72971; CAA97212.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08280.1; -; Genomic_DNA.
DR PIR; S64504; S64504.
DR RefSeq; NP_011702.1; NM_001181315.1.
DR PDB; 5FMF; EM; 6.00 A; U=94-150, U=323-417.
DR PDB; 5FYW; EM; 4.35 A; Q=1-735.
DR PDB; 5FZ5; EM; 8.80 A; Q=1-735.
DR PDB; 5IP7; X-ray; 3.52 A; Q=21-35.
DR PDB; 5IP9; X-ray; 3.90 A; Q=21-35.
DR PDB; 5OQJ; EM; 4.70 A; Q=1-735.
DR PDB; 5OQM; EM; 5.80 A; Q=1-735.
DR PDB; 5SVA; EM; 15.30 A; f=1-735.
DR PDB; 6GYK; EM; 5.10 A; Q=1-735.
DR PDB; 6GYL; EM; 4.80 A; Q=1-735.
DR PDB; 6GYM; EM; 6.70 A; Q=1-735.
DR PDB; 7MEI; EM; 3.54 A; Q=1-735.
DR PDB; 7ML0; EM; 3.00 A; Q=1-735.
DR PDB; 7ML1; EM; 4.00 A; Q=1-735.
DR PDB; 7ML2; EM; 3.40 A; Q=1-735.
DR PDB; 7ML4; EM; 3.10 A; Q=1-735.
DR PDB; 7O4I; EM; 3.20 A; Q=1-735.
DR PDB; 7O4J; EM; 2.90 A; Q=1-735.
DR PDB; 7O72; EM; 3.40 A; Q=1-735.
DR PDB; 7O73; EM; 3.40 A; Q=1-735.
DR PDB; 7O75; EM; 3.20 A; Q=1-735.
DR PDBsum; 5FMF; -.
DR PDBsum; 5FYW; -.
DR PDBsum; 5FZ5; -.
DR PDBsum; 5IP7; -.
DR PDBsum; 5IP9; -.
DR PDBsum; 5OQJ; -.
DR PDBsum; 5OQM; -.
DR PDBsum; 5SVA; -.
DR PDBsum; 6GYK; -.
DR PDBsum; 6GYL; -.
DR PDBsum; 6GYM; -.
DR PDBsum; 7MEI; -.
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; P41895; -.
DR BMRB; P41895; -.
DR SMR; P41895; -.
DR BioGRID; 33438; 160.
DR ComplexPortal; CPX-1149; Transcription factor TFIIF complex.
DR DIP; DIP-1151N; -.
DR IntAct; P41895; 16.
DR MINT; P41895; -.
DR STRING; 4932.YGR186W; -.
DR iPTMnet; P41895; -.
DR MaxQB; P41895; -.
DR PaxDb; P41895; -.
DR PRIDE; P41895; -.
DR EnsemblFungi; YGR186W_mRNA; YGR186W; YGR186W.
DR GeneID; 853098; -.
DR KEGG; sce:YGR186W; -.
DR SGD; S000003418; TFG1.
DR VEuPathDB; FungiDB:YGR186W; -.
DR eggNOG; KOG2393; Eukaryota.
DR GeneTree; ENSGT00440000038032; -.
DR HOGENOM; CLU_020322_0_0_1; -.
DR InParanoid; P41895; -.
DR OMA; FEEFYPW; -.
DR BioCyc; YEAST:G3O-30876-MON; -.
DR Reactome; R-SCE-113418; Formation of the Early Elongation Complex.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SCE-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-SCE-72086; mRNA Capping.
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 Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
DR PRO; PR:P41895; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P41895; protein.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0005674; C:transcription factor TFIIF complex; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0072542; F:protein phosphatase activator activity; IDA:SGD.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IBA:GO_Central.
DR GO; GO:0001096; F:TFIIF-class transcription factor complex binding; IBA:GO_Central.
DR GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IDA:SGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:InterPro.
DR GO; GO:0001111; P:promoter clearance from RNA polymerase II promoter; IC:SGD.
DR GO; GO:0080163; P:regulation of protein serine/threonine phosphatase activity; IDA:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IPI:ComplexPortal.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:SGD.
DR GO; GO:0001174; P:transcriptional start site selection at RNA polymerase II promoter; IMP:SGD.
DR InterPro; IPR008851; TFIIF-alpha.
DR InterPro; IPR011039; TFIIF_interaction.
DR PANTHER; PTHR13011; PTHR13011; 1.
DR Pfam; PF05793; TFIIF_alpha; 1.
DR SUPFAM; SSF50916; SSF50916; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..735
FT /note="Transcription initiation factor IIF subunit alpha"
FT /id="PRO_0000211234"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 200
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT CONFLICT 238
FT /note="V -> I (in Ref. 1; AAA61640)"
FT /evidence="ECO:0000305"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 153..167
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 337..345
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 360..366
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 370..378
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 391..397
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 406..413
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 424..431
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 437..449
FT /evidence="ECO:0007829|PDB:7O4J"
SQ SEQUENCE 735 AA; 82194 MW; A6D4685F187BB593 CRC64;
MSRRNPPGSR NGGGPTNASP FIKRDRMRRN FLRMRMGQNG SNSSSPGVPN GDNSRGSLVK
KDDPEYAEER EKMLLQIGVE ADAGRSNVKV KDEDPNEYNE FPLRAIPKED LENMRTHLLK
FQSKKKINPV TDFHLPVRLH RKDTRNLQFQ LTRAEIVQRQ KEISEYKKKA EQERSTPNSG
GMNKSGTVSL NNTVKDGSQT PTVDSVTKDN TANGVNSSIP TVTGSSVPPA SPTTVSAVES
NGLSNGSTSA ANGLDGNAST ANLANGRPLV TKLEDAGPAE DPTKVGMVKY DGKEVTNEPE
FEEGTMDPLA DVAPDGGGRA KRGNLRRKTR QLKVLDENAK KLRFEEFYPW VMEDFDGYNT
WVGSYEAGNS DSYVLLSVED DGSFTMIPAD KVYKFTARNK YATLTIDEAE KRMDKKSGEV
PRWLMKHLDN IGTTTTRYDR TRRKLKAVAD QQAMDEDDRD DNSEVELDYD EEFADDEEAP
IIDGNEQENK ESEQRIKKEM LQANAMGLRD EEAPSENEED ELFGEKKIDE DGERIKKALQ
KTELAALYSS DENEINPYLS ESDIENKENE SPVKKEEDSD TLSKSKRSSP KKQQKKATNA
HVHKEPTLRV KSIKNCVIIL KGDKKILKSF PEGEWNPQTT KAVDSSNNAS NTVPSPIKQE
EGLNSTVAER EETPAPTITE KDIIEAIGDG KVNIKEFGKF IRRKYPGAEN KKLMFAIVKK
LCRKVGNDHM ELKKE
