TFC7_YEAST
ID TFC7_YEAST Reviewed; 435 AA.
AC Q12415; D6W2G9; Q07347; Q6B220;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Transcription factor tau 55 kDa subunit;
DE AltName: Full=TFIIIC 55 kDa subunit;
DE AltName: Full=Transcription factor C subunit 7;
GN Name=TFC7; OrderedLocusNames=YOR110W; ORFNames=O3234, YOR3234w;
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], PROTEIN SEQUENCE OF 62-66; 81-85;
RP 183-188; 227-237; 341-346 AND 347-352, FUNCTION, AND IDENTIFICATION IN
RP TFIIIC.
RX PubMed=9584160; DOI=10.1128/mcb.18.6.3191;
RA Manaud N., Arrebola R., Buffin-Meyer B., Lefebvre O., Voss H., Riva M.,
RA Conesa C., Sentenac A.;
RT "A chimeric subunit of yeast transcription factor IIIC forms a subcomplex
RT with tau95.";
RL Mol. Cell. Biol. 18:3191-3200(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 222-435.
RX PubMed=8904341;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<281::aid-yea904>3.0.co;2-o;
RA Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C.,
RA Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.;
RT "Sequencing and analysis of 51 kb on the right arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 30 open reading frames.";
RL Yeast 12:281-288(1996).
RN [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND IDENTIFICATION BY
RP 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 [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 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).
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 tauA domain of TFIIIC that binds boxA DNA promoter sites of tRNA and
CC similar genes. {ECO:0000269|PubMed:9584160}.
CC -!- SUBUNIT: Component of the TFIIIC complex composed of TFC1, TFC3, TFC4,
CC TFC6, TFC7 and TFC8. The subunits are organized in two globular
CC domains, tauA and tauB, connected by a proteolysis-sensitive and
CC flexible linker. {ECO:0000269|PubMed:9584160}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2660 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X94335; CAA64030.1; -; Genomic_DNA.
DR EMBL; Z75018; CAA99308.1; -; Genomic_DNA.
DR EMBL; AY692910; AAT92929.1; -; Genomic_DNA.
DR EMBL; X90518; CAA62104.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10885.1; -; Genomic_DNA.
DR PIR; S61668; S61668.
DR RefSeq; NP_014753.1; NM_001183529.1.
DR PDB; 2YN0; X-ray; 1.50 A; A=3-272.
DR PDB; 6YJ6; EM; 3.10 A; C=1-435.
DR PDBsum; 2YN0; -.
DR PDBsum; 6YJ6; -.
DR AlphaFoldDB; Q12415; -.
DR SMR; Q12415; -.
DR BioGRID; 34506; 32.
DR ComplexPortal; CPX-1656; Transcription factor TFIIIC complex.
DR DIP; DIP-2309N; -.
DR IntAct; Q12415; 18.
DR MINT; Q12415; -.
DR STRING; 4932.YOR110W; -.
DR iPTMnet; Q12415; -.
DR MaxQB; Q12415; -.
DR PaxDb; Q12415; -.
DR PRIDE; Q12415; -.
DR EnsemblFungi; YOR110W_mRNA; YOR110W; YOR110W.
DR GeneID; 854277; -.
DR KEGG; sce:YOR110W; -.
DR SGD; S000005636; TFC7.
DR VEuPathDB; FungiDB:YOR110W; -.
DR eggNOG; ENOG502RYP8; Eukaryota.
DR GeneTree; ENSGT00940000167071; -.
DR HOGENOM; CLU_042838_0_0_1; -.
DR InParanoid; Q12415; -.
DR OMA; FRANWAP; -.
DR BioCyc; YEAST:G3O-33639-MON; -.
DR PRO; PR:Q12415; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12415; 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:0016791; F:phosphatase activity; IDA: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 CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR014623; Tfc7/tau55.
DR InterPro; IPR019481; TFIIIC_triple_barrel.
DR Pfam; PF00300; His_Phos_1; 1.
DR Pfam; PF10419; TFIIIC_sub6; 1.
DR PIRSF; PIRSF036802; Tau55_TFC7; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
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..435
FT /note="Transcription factor tau 55 kDa subunit"
FT /id="PRO_0000072499"
FT REGION 362..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CONFLICT 9
FT /note="A -> V (in Ref. 5; AAT92929)"
FT /evidence="ECO:0000305"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:2YN0"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:2YN0"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:2YN0"
FT HELIX 38..52
FT /evidence="ECO:0007829|PDB:2YN0"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2YN0"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:2YN0"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2YN0"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:2YN0"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:2YN0"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2YN0"
FT HELIX 136..157
FT /evidence="ECO:0007829|PDB:2YN0"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:2YN0"
FT HELIX 170..181
FT /evidence="ECO:0007829|PDB:2YN0"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:2YN0"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:2YN0"
FT STRAND 236..243
FT /evidence="ECO:0007829|PDB:2YN0"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:2YN0"
FT STRAND 292..299
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 334..340
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 344..349
FT /evidence="ECO:0007829|PDB:6YJ6"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:6YJ6"
FT STRAND 421..431
FT /evidence="ECO:0007829|PDB:6YJ6"
SQ SEQUENCE 435 AA; 49146 MW; D778B81F31B83C45 CRC64;
MVVNTIYIAR HGYRSNWLPE GPYPDPLTGI DSDVPLAEHG VQQAKELAHY LLSLDNQPEA
AFASPFYRCL ETVQPIAKLL EIPVYLERGI GEWYRPDRKP VIPVPAGYEI LSKFFPGVIS
QEWDSTLTPN EKGETEQEMY MRFKKFWPLF IERVEKEYPN VECILLVTHA ASKIALGMSL
LGYDNPRMSL NENGDKIRSG SCSLDKYEIL KKSYDTIDET DDQTSFTYIP FSDRKWVLTM
NGNTEFLSSG EEMNWNFDCV AEAGSDADIK KRQMTKKTSS PIPEADDQTE VETVYISVDI
PSGNYKERTE IAKSAILQYS GLETDAPLFR IGNRLYEGSW ERLVGTELAF PNAAHVHKKT
AGLLSPTEEN ETTNAGQSKG SSTANDPNIQ IQEEDVGLPD STNTSRDHTG DKEEVQSEKI
YRIKERIVLS NVRPM
