TFC6_YEAST
ID TFC6_YEAST Reviewed; 672 AA.
AC Q06339; D6VSZ0;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Transcription factor tau 91 kDa subunit;
DE AltName: Full=TFIIIC 91 kDa subunit;
DE AltName: Full=Transcription factor C subunit 6;
GN Name=TFC6; OrderedLocusNames=YDR362C;
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 N-TERMINUS, CRYSTALLIZATION, AND INTERACTION WITH TFC8.
RX PubMed=16115780; DOI=10.1016/j.pep.2005.06.013;
RA Mylona A., Acker J., Fernandez-Tornero C., Sentenac A., Mueller C.W.;
RT "Expression, proteolytic analysis, reconstitution, and crystallization of
RT the tau60/tau91 subcomplex of yeast TFIIIC.";
RL Protein Expr. Purif. 45:255-261(2006).
RN [4]
RP FUNCTION.
RX PubMed=2651441; DOI=10.1016/s0021-9258(18)83263-x;
RA Gabrielsen O.S., Marzouki N., Ruet A., Sentenac A., Fromageot P.;
RT "Two polypeptide chains in yeast transcription factor tau interact with
RT DNA.";
RL J. Biol. Chem. 264:7505-7511(1989).
RN [5]
RP INTERACTION WITH TFC1; TFC3 AND TFC4.
RX PubMed=7688737; DOI=10.1016/s0021-9258(17)46809-8;
RA Conesa C., Swanson R.N., Schultz P., Oudet P., Sentenac A.;
RT "On the subunit composition, stoichiometry, and phosphorylation of the
RT yeast transcription factor TFIIIC/tau.";
RL J. Biol. Chem. 268:18047-18052(1993).
RN [6]
RP FUNCTION, AND IDENTIFICATION IN THE TFIIIC COMPLEX.
RX PubMed=9418847; DOI=10.1128/mcb.18.1.1;
RA Arrebola R., Manaud N., Rozenfeld S., Marsolier M.C., Lefebvre O.,
RA Carles C., Thuriaux P., Conesa C., Sentenac A.;
RT "Tau91, an essential subunit of yeast transcription factor IIIC, cooperates
RT with tau138 in DNA binding.";
RL Mol. Cell. Biol. 18:1-9(1998).
RN [7]
RP INTERACTION WITH TFC1 AND TFC3.
RX PubMed=12533520; DOI=10.1074/jbc.m213310200;
RA Jourdain S., Acker J., Ducrot C., Sentenac A., Lefebvre O.;
RT "The tau95 subunit of yeast TFIIIC influences upstream and downstream
RT functions of TFIIIC.DNA complexes.";
RL J. Biol. Chem. 278:10450-10457(2003).
RN [8]
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 [9]
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 [10]
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 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).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 159-672 IN COMPLEX WITH TFC8,
RP REGION, AND DISULFIDE BOND.
RX PubMed=17052456; DOI=10.1016/j.molcel.2006.08.013;
RA Mylona A., Fernandez-Tornero C., Legrand P., Haupt M., Sentenac A.,
RA Acker J., Mueller C.W.;
RT "Structure of the tau60/Delta tau91 subcomplex of yeast transcription
RT factor IIIC: insights into preinitiation complex assembly.";
RL Mol. Cell 24:221-232(2006).
CC -!- FUNCTION: TFIIIC mediates tRNA and 5S RNA gene activation by binding to
CC intragenic promoter elements. Upstream of the transcription start site,
CC TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is
CC sufficient for RNA polymerase III recruitment and function. Part of the
CC tauB domain of TFIIIC that binds boxB DNA promoter sites of tRNA and
CC similar genes. Cooperates with TFC3 in DNA binding.
CC {ECO:0000269|PubMed:2651441, ECO:0000269|PubMed:9418847}.
CC -!- SUBUNIT: Heterodimer with TFC8. Component of the TFIIIC complex
CC composed of TFC1, TFC3, TFC4, TFC6, TFC7 and TFC8. The subunits are
CC organized in two globular domains, tauA and tauB, connected by a
CC proteolysis-sensitive and flexible linker. Interacts with TFC1, TFC3,
CC TFC4 and directly with TFC8. {ECO:0000269|PubMed:12533520,
CC ECO:0000269|PubMed:16115780, ECO:0000269|PubMed:17052456,
CC ECO:0000269|PubMed:7688737, ECO:0000269|PubMed:9418847}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1130 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U28372; AAB64796.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12200.1; -; Genomic_DNA.
DR PIR; S61157; S61157.
DR RefSeq; NP_010649.1; NM_001180670.1.
DR PDB; 2J04; X-ray; 3.20 A; B/D=159-672.
DR PDBsum; 2J04; -.
DR AlphaFoldDB; Q06339; -.
DR SMR; Q06339; -.
DR BioGRID; 32417; 510.
DR ComplexPortal; CPX-1656; Transcription factor TFIIIC complex.
DR DIP; DIP-2952N; -.
DR IntAct; Q06339; 6.
DR MINT; Q06339; -.
DR STRING; 4932.YDR362C; -.
DR iPTMnet; Q06339; -.
DR MaxQB; Q06339; -.
DR PaxDb; Q06339; -.
DR PRIDE; Q06339; -.
DR EnsemblFungi; YDR362C_mRNA; YDR362C; YDR362C.
DR GeneID; 851964; -.
DR KEGG; sce:YDR362C; -.
DR SGD; S000002770; TFC6.
DR VEuPathDB; FungiDB:YDR362C; -.
DR eggNOG; ENOG502S1WJ; Eukaryota.
DR HOGENOM; CLU_023122_0_0_1; -.
DR InParanoid; Q06339; -.
DR OMA; RLWKWDY; -.
DR BioCyc; YEAST:G3O-29912-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; Q06339; -.
DR PRO; PR:Q06339; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06339; protein.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000127; C:transcription factor TFIIIC complex; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; ISA:SGD.
DR GO; GO:0042791; P:5S class rRNA transcription by RNA polymerase III; IDA:SGD.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IDA:SGD.
DR GO; GO:0006384; P:transcription initiation from RNA polymerase III promoter; IC:ComplexPortal.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; DNA-binding;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..672
FT /note="Transcription factor tau 91 kDa subunit"
FT /id="PRO_0000252483"
FT DNA_BIND 6..18
FT /note="A.T hook"
FT REGION 1..158
FT /note="Required for DNA-binding"
FT REGION 24..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..672
FT /note="Sufficient for interaction with TFC8"
FT /evidence="ECO:0000269|PubMed:16115780"
FT COMPBIAS 70..96
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 375..383
FT /evidence="ECO:0000269|PubMed:17052456"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:2J04"
FT HELIX 178..191
FT /evidence="ECO:0007829|PDB:2J04"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:2J04"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:2J04"
FT TURN 226..230
FT /evidence="ECO:0007829|PDB:2J04"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:2J04"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 308..318
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 339..347
FT /evidence="ECO:0007829|PDB:2J04"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 353..361
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 365..371
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 383..388
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 393..397
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 402..409
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:2J04"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 425..440
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 443..449
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 457..461
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 467..473
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 481..486
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 489..494
FT /evidence="ECO:0007829|PDB:2J04"
FT HELIX 496..498
FT /evidence="ECO:0007829|PDB:2J04"
FT HELIX 499..502
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 504..508
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 517..520
FT /evidence="ECO:0007829|PDB:2J04"
FT TURN 521..524
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 525..529
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 531..539
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 547..551
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 556..560
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 569..572
FT /evidence="ECO:0007829|PDB:2J04"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 576..578
FT /evidence="ECO:0007829|PDB:2J04"
FT TURN 586..588
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 601..604
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 609..611
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 613..616
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 645..647
FT /evidence="ECO:0007829|PDB:2J04"
FT TURN 651..655
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 656..660
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 664..670
FT /evidence="ECO:0007829|PDB:2J04"
SQ SEQUENCE 672 AA; 74709 MW; 744D6D6A1923B076 CRC64;
MAVIPAKKRG RPRKSVVAEV PYDSLASPVS ENSGSKRPRR NASKKAVANF AQLVHAGRDD
VINTTQVNNV DDTDDDDFVL NDEGDGEESD NVEIEFENEL ESTKNEVADL NSSGSGASVR
PSGRRNTVQK LRLKKNSTKN MKSSSPGSSL GQKGRPIRLL KDLSSARDKI ERIYGLNKEK
LLLLAKVKEG FETSVFDFPF KNIQPDSPYF VCLDPPCKKE SAYNKVIGDK NRTVYHEINK
TEFENMIKLR TKRLKLLIGE VDAEVSTGDK IEFPVLANGK RRGFIYNVGG LVTDIAWLNI
EENTDIGKDI QYLAVAVSQY MDEPLNEHLE MFDKEKHSSC IQIFKMNTST LHCVKVQTIV
HSFGEVWDLK WHEGCHAPHL VGCLSFVSQE GTINFLEIID NATDVHVFKM CEKPSLTLSL
ADSLITTFDF LSPTTVVCGF KNGFVAEFDL TDPEVPSFYD QVHDSYILSV STAYSDFEDT
VVSTVAVDGY FYIFNPKDIA TTKTTVSRFR GSNLVPVVYC PQIYSYIYSD GASSLRAVPS
RAAFAVHPLV SRETTITAIG VSRLHPMVLA GSADGSLIIT NAARRLLHGI KNSSATQKSL
RLWKWDYSIK DDKYRIDSSY EVYPLTVNDV SKAKIDAHGI NITCTKWNET SAGGKCYAFS
NSAGLLTLEY LS
