TFC8_YEAST
ID TFC8_YEAST Reviewed; 588 AA.
AC Q12308; D6W405;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Transcription factor tau 60 kDa subunit;
DE AltName: Full=TFIIIC 60 kDa subunit;
DE AltName: Full=Transcription factor C subunit 8;
GN Name=TFC8; OrderedLocusNames=YPL007C;
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=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 [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 TFC6.
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 PROTEIN SEQUENCE OF 28-36, FUNCTION, IDENTIFICATION IN THE TFIIIC COMPLEX,
RP AND INTERACTION WITH SPT15.
RX PubMed=10567530; DOI=10.1128/mcb.19.12.8042;
RA Deprez E., Arrebola R., Conesa C., Sentenac A.;
RT "A subunit of yeast TFIIIC participates in the recruitment of TATA-binding
RT protein.";
RL Mol. Cell. Biol. 19:8042-8051(1999).
RN [5]
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 [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN COMPLEX WITH TFC6, INTERACTION
RP WITH SPT15, AND SITE.
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. Plays a role in TFIIB assembly through its interaction
CC with SPT15/TBP. Essential for cell viability.
CC {ECO:0000269|PubMed:10567530}.
CC -!- SUBUNIT: Heterodimer with TFC6. 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 SPT15 and
CC directly with TFC6. {ECO:0000269|PubMed:10567530,
CC ECO:0000269|PubMed:16115780, ECO:0000269|PubMed:17052456}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2070 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z71255; CAA95034.1; -; Genomic_DNA.
DR EMBL; Z48483; CAA88379.1; -; Genomic_DNA.
DR EMBL; U33335; AAB68098.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11421.1; -; Genomic_DNA.
DR PIR; S52524; S52524.
DR RefSeq; NP_015318.1; NM_001183821.1.
DR PDB; 2J04; X-ray; 3.20 A; A/C=1-588.
DR PDBsum; 2J04; -.
DR AlphaFoldDB; Q12308; -.
DR SMR; Q12308; -.
DR BioGRID; 36170; 184.
DR ComplexPortal; CPX-1656; Transcription factor TFIIIC complex.
DR DIP; DIP-6743N; -.
DR IntAct; Q12308; 7.
DR MINT; Q12308; -.
DR STRING; 4932.YPL007C; -.
DR MaxQB; Q12308; -.
DR PaxDb; Q12308; -.
DR PRIDE; Q12308; -.
DR TopDownProteomics; Q12308; -.
DR EnsemblFungi; YPL007C_mRNA; YPL007C; YPL007C.
DR GeneID; 856100; -.
DR KEGG; sce:YPL007C; -.
DR SGD; S000005928; TFC8.
DR VEuPathDB; FungiDB:YPL007C; -.
DR eggNOG; ENOG502RFBH; Eukaryota.
DR HOGENOM; CLU_033367_0_0_1; -.
DR InParanoid; Q12308; -.
DR OMA; NEYGWFT; -.
DR BioCyc; YEAST:G3O-33926-MON; -.
DR EvolutionaryTrace; Q12308; -.
DR PRO; PR:Q12308; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12308; 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: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; IPR024764; TFIIIC_Znf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12660; zf-TFIIIC; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..588
FT /note="Transcription factor tau 60 kDa subunit"
FT /id="PRO_0000252484"
FT REGION 399..588
FT /note="Sufficient for SPT15-binding"
FT SITE 358
FT /note="Involved in the interaction with TFC6"
FT CONFLICT 36
FT /note="D -> T (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:2J04"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:2J04"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:2J04"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:2J04"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 244..251
FT /evidence="ECO:0007829|PDB:2J04"
FT TURN 252..255
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 289..301
FT /evidence="ECO:0007829|PDB:2J04"
FT HELIX 307..316
FT /evidence="ECO:0007829|PDB:2J04"
FT TURN 317..322
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 330..338
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 342..352
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 366..375
FT /evidence="ECO:0007829|PDB:2J04"
FT HELIX 386..394
FT /evidence="ECO:0007829|PDB:2J04"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:2J04"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:2J04"
FT HELIX 423..432
FT /evidence="ECO:0007829|PDB:2J04"
FT HELIX 434..442
FT /evidence="ECO:0007829|PDB:2J04"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:2J04"
FT HELIX 452..464
FT /evidence="ECO:0007829|PDB:2J04"
FT HELIX 465..468
FT /evidence="ECO:0007829|PDB:2J04"
FT HELIX 472..484
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 495..500
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 503..509
FT /evidence="ECO:0007829|PDB:2J04"
FT HELIX 510..512
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 516..520
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 526..529
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:2J04"
FT TURN 546..548
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 551..553
FT /evidence="ECO:0007829|PDB:2J04"
FT HELIX 555..557
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 559..561
FT /evidence="ECO:0007829|PDB:2J04"
FT HELIX 565..573
FT /evidence="ECO:0007829|PDB:2J04"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:2J04"
FT TURN 579..581
FT /evidence="ECO:0007829|PDB:2J04"
SQ SEQUENCE 588 AA; 67683 MW; BDBD7BBE947BAC63 CRC64;
MKLLKDLLVD RKEFEDWKNN LTWARDGTLY LTTFPDISIG QPKYAKDINC NSKNLFHVKE
FPLEFENKLD FELAQQNGLL NSQPVCYPRV CKPSPIDDWM AVLSNNGNVS VFKDNKMLTN
LDSKGNLSSR TYHCFEWNPI ESSIVVGNED GELQFFSIRK NSENTPEFYF ESSIRLSDAG
SKDWVTHIVW YEDVLVAALS NNSVFSMTVS ASSHQPVSRM IQNASRRKIT DLKIVDYKVV
LTCPGYVHKI DLKNYSISSL KTGSLENFHI IPLNHEKEST ILLMSNKTSY KVLLEDELHV
TADNIIAPYL EKKFKKWSTI WNEFNNYETT LVIHGISLSP DGYSIAIVYD MERVAFKYKI
ASEQSFNIMF APLYHTWTIS ERAVGLAWYQ TYQIYNQSLP KLPENFSMNK KLLNGNYPIS
LDFQSYLNAL MKSEEMRIIM FLNMTIDKPS ILSFLEALYE YAINKKSELT NSFDLACVLS
IAAILKREAP IYNGTLLMKN SFLEETFNLE SFTADPETVT STTNNTWKRC GVTLLPILTT
HVKICPVSKQ RVIDIKRDDL NDYGWFTRGL LERFNEISVY CGTTLEVM
