ID   RPC5_YEAST              Reviewed;         282 AA.
AC   P36121; D6VX90;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=DNA-directed RNA polymerase III subunit RPC5;
DE            Short=RNA polymerase III subunit C5;
DE   AltName: Full=DNA-directed RNA polymerase III 37 kDa polypeptide;
DE   AltName: Full=RNA polymerase III subunit C37;
GN   Name=RPC37; OrderedLocusNames=YKR025W;
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=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
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   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   [4]
RP   REVIEW ON THE RNA POL III COMPLEX.
RX   PubMed=10384303; DOI=10.1101/sqb.1998.63.381;
RA   Chedin S., Ferri M.L., Peyroche G., Andrau J.-C., Jourdain S., Lefebvre O.,
RA   Werner M., Carles C., Sentenac A.;
RT   "The yeast RNA polymerase III transcription machinery: a paradigm for
RT   eukaryotic gene activation.";
RL   Cold Spring Harb. Symp. Quant. Biol. 63:381-389(1998).
RN   [5]
RP   IDENTIFICATION IN THE RNA POL III COMPLEX, AND INTERACTION WITH RPC4.
RX   PubMed=10393904; DOI=10.1073/pnas.96.14.7815;
RA   Flores A., Briand J.-F., Gadal O., Andrau J.-C., Rubbi L., Van Mullem V.,
RA   Boschiero C., Goussot M., Marck C., Carles C., Thuriaux P., Sentenac A.,
RA   Werner M.;
RT   "A protein-protein interaction map of yeast RNA polymerase III.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:7815-7820(1999).
RN   [6]
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   [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   FUNCTION OF THE RPC53-RPC37 SUBCOMPLEX.
RX   PubMed=16362040; DOI=10.1038/sj.emboj.7600915;
RA   Landrieux E., Alic N., Ducrot C., Acker J., Riva M., Carles C.;
RT   "A subcomplex of RNA polymerase III subunits involved in transcription
RT   termination and reinitiation.";
RL   EMBO J. 25:118-128(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-61, AND IDENTIFICATION BY
RP   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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-61, AND IDENTIFICATION BY
RP   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).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       Specific peripheric component of RNA polymerase III which synthesizes
CC       small RNAs, such as 5S rRNA and tRNAs. The RPC53/RPC4-RPC37/RPC5
CC       subcomplex is required for terminator recognition and reinitiation.
CC       {ECO:0000269|PubMed:16362040}.
CC   -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC       consisting of 17 subunits. Interacts with RPC53/RPC4. RPC53/RPC4,
CC       RPC37/RPC5 and RPC11/RPC10 probably form a Pol III subcomplex.
CC       {ECO:0000269|PubMed:10393904}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 1590 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; Z28250; CAA82097.1; -; Genomic_DNA.
DR   EMBL; AY692886; AAT92905.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09180.1; -; Genomic_DNA.
DR   PIR; S38094; S38094.
DR   RefSeq; NP_012950.3; NM_001179815.3.
DR   PDB; 5FJ8; EM; 3.90 A; M=1-282.
DR   PDB; 5FJ9; EM; 4.60 A; M=1-282.
DR   PDB; 5FJA; EM; 4.65 A; M=1-282.
DR   PDB; 6CNB; EM; 4.10 A; M=1-282.
DR   PDB; 6CNC; EM; 4.10 A; M=1-282.
DR   PDB; 6CND; EM; 4.80 A; M=1-282.
DR   PDB; 6CNF; EM; 4.50 A; M=1-282.
DR   PDB; 6EU0; EM; 4.00 A; M=1-282.
DR   PDB; 6EU1; EM; 3.40 A; M=1-282.
DR   PDB; 6EU2; EM; 3.40 A; M=1-282.
DR   PDB; 6EU3; EM; 3.30 A; M=1-282.
DR   PDB; 6F40; EM; 3.70 A; M=1-282.
DR   PDB; 6F41; EM; 4.30 A; M=1-282.
DR   PDB; 6F42; EM; 5.50 A; M=1-282.
DR   PDB; 6F44; EM; 4.20 A; M=1-282.
DR   PDB; 6TUT; EM; 3.25 A; M=1-282.
DR   PDB; 7Z0H; EM; 2.60 A; M=1-282.
DR   PDB; 7Z1L; EM; 2.80 A; M=1-282.
DR   PDB; 7Z1M; EM; 3.40 A; M=1-282.
DR   PDB; 7Z1O; EM; 2.70 A; M=1-282.
DR   PDB; 7Z2Z; EM; 3.07 A; M=1-282.
DR   PDB; 7Z30; EM; 2.90 A; M=1-282.
DR   PDB; 7Z31; EM; 2.76 A; M=1-282.
DR   PDB; 8BWS; EM; 3.20 A; M=1-282.
DR   PDBsum; 5FJ8; -.
DR   PDBsum; 5FJ9; -.
DR   PDBsum; 5FJA; -.
DR   PDBsum; 6CNB; -.
DR   PDBsum; 6CNC; -.
DR   PDBsum; 6CND; -.
DR   PDBsum; 6CNF; -.
DR   PDBsum; 6EU0; -.
DR   PDBsum; 6EU1; -.
DR   PDBsum; 6EU2; -.
DR   PDBsum; 6EU3; -.
DR   PDBsum; 6F40; -.
DR   PDBsum; 6F41; -.
DR   PDBsum; 6F42; -.
DR   PDBsum; 6F44; -.
DR   PDBsum; 6TUT; -.
DR   PDBsum; 7Z0H; -.
DR   PDBsum; 7Z1L; -.
DR   PDBsum; 7Z1M; -.
DR   PDBsum; 7Z1O; -.
DR   PDBsum; 7Z2Z; -.
DR   PDBsum; 7Z30; -.
DR   PDBsum; 7Z31; -.
DR   PDBsum; 8BWS; -.
DR   AlphaFoldDB; P36121; -.
DR   EMDB; EMD-10595; -.
DR   EMDB; EMD-14421; -.
DR   EMDB; EMD-14447; -.
DR   EMDB; EMD-14448; -.
DR   EMDB; EMD-14451; -.
DR   EMDB; EMD-14468; -.
DR   EMDB; EMD-14469; -.
DR   EMDB; EMD-14470; -.
DR   EMDB; EMD-16299; -.
DR   EMDB; EMD-3955; -.
DR   EMDB; EMD-3956; -.
DR   EMDB; EMD-3957; -.
DR   EMDB; EMD-3958; -.
DR   EMDB; EMD-4180; -.
DR   EMDB; EMD-4181; -.
DR   EMDB; EMD-4182; -.
DR   EMDB; EMD-4183; -.
DR   EMDB; EMD-7530; -.
DR   EMDB; EMD-7531; -.
DR   EMDB; EMD-7532; -.
DR   EMDB; EMD-7533; -.
DR   SMR; P36121; -.
DR   BioGRID; 34157; 84.
DR   ComplexPortal; CPX-2660; DNA-directed RNA polymerase III complex.
DR   DIP; DIP-761N; -.
DR   IntAct; P36121; 11.
DR   MINT; P36121; -.
DR   STRING; 4932.YKR025W; -.
DR   iPTMnet; P36121; -.
DR   MaxQB; P36121; -.
DR   PaxDb; 4932-YKR025W; -.
DR   PeptideAtlas; P36121; -.
DR   EnsemblFungi; YKR025W_mRNA; YKR025W; YKR025W.
DR   GeneID; 853895; -.
DR   KEGG; sce:YKR025W; -.
DR   AGR; SGD:S000001733; -.
DR   SGD; S000001733; RPC37.
DR   VEuPathDB; FungiDB:YKR025W; -.
DR   eggNOG; KOG2354; Eukaryota.
DR   GeneTree; ENSGT00390000016123; -.
DR   HOGENOM; CLU_072845_1_0_1; -.
DR   InParanoid; P36121; -.
DR   OMA; KPKTGWM; -.
DR   OrthoDB; 1355725at2759; -.
DR   BioCyc; YEAST:G3O-32001-MONOMER; -.
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   BioGRID-ORCS; 853895; 7 hits in 10 CRISPR screens.
DR   PRO; PR:P36121; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P36121; Protein.
DR   GO; GO:0005634; C:nucleus; NAS:ComplexPortal.
DR   GO; GO:0005666; C:RNA polymerase III complex; IDA:SGD.
DR   GO; GO:0006386; P:termination of RNA polymerase III transcription; IDA:ComplexPortal.
DR   GO; GO:0006383; P:transcription by RNA polymerase III; IDA:ComplexPortal.
DR   GO; GO:0006384; P:transcription initiation at RNA polymerase III promoter; IDA:ComplexPortal.
DR   GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IDA:SGD.
DR   InterPro; IPR006886; RNA_pol_III_Rpc5.
DR   PANTHER; PTHR12069:SF0; DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC5; 1.
DR   PANTHER; PTHR12069; DNA-DIRECTED RNA POLYMERASES III 80 KDA POLYPEPTIDE RNA POLYMERASE III SUBUNIT 5; 1.
DR   Pfam; PF04801; RPC5; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-directed RNA polymerase; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription.
FT   CHAIN           1..282
FT                   /note="DNA-directed RNA polymerase III subunit RPC5"
FT                   /id="PRO_0000203203"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..33
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..70
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         61
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   STRAND          70..74
FT                   /evidence="ECO:0007829|PDB:6TUT"
FT   STRAND          86..101
FT                   /evidence="ECO:0007829|PDB:6TUT"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:6TUT"
FT   TURN            114..117
FT                   /evidence="ECO:0007829|PDB:6TUT"
FT   STRAND          118..124
FT                   /evidence="ECO:0007829|PDB:6TUT"
FT   STRAND          127..131
FT                   /evidence="ECO:0007829|PDB:6TUT"
FT   HELIX           134..139
FT                   /evidence="ECO:0007829|PDB:6TUT"
FT   STRAND          145..154
FT                   /evidence="ECO:0007829|PDB:6TUT"
FT   STRAND          158..164
FT                   /evidence="ECO:0007829|PDB:6TUT"
FT   STRAND          167..172
FT                   /evidence="ECO:0007829|PDB:6TUT"
FT   STRAND          175..182
FT                   /evidence="ECO:0007829|PDB:6TUT"
FT   HELIX           184..191
FT                   /evidence="ECO:0007829|PDB:6TUT"
FT   TURN            192..197
FT                   /evidence="ECO:0007829|PDB:6TUT"
FT   HELIX           230..238
FT                   /evidence="ECO:0007829|PDB:6TUT"
FT   STRAND          246..249
FT                   /evidence="ECO:0007829|PDB:6TUT"
FT   HELIX           253..257
FT                   /evidence="ECO:0007829|PDB:6TUT"
FT   HELIX           259..261
FT                   /evidence="ECO:0007829|PDB:6TUT"
FT   TURN            262..264
FT                   /evidence="ECO:0007829|PDB:6EU1"
SQ   SEQUENCE   282 AA;  32142 MW;  9E948BDDECE9D15E CRC64;
     MSIDNKLFVT EEDEEDRTQD RADVEDESND IDMIADENGT NSAIANEQEE KSEEVKAEDD
     TGEEEEDDPV IEEFPLKISG EEESLHVFQY ANRPRLVGRK PAEHPFISAA RYKPKSHLWE
     IDIPLDEQAF YNKDKAESEW NGVNVQTLKG VGVENNGQYA AFVKDMQVYL VPIERVAQLK
     PFFKYIDDAN VTRKQEDARR NPNPSSQRAQ VVTMSVKSVN DPSQNRLTGS LLAHKVADEE
     ANIELTWAEG TFEQFKDTIV KEAEDKTLVA LEKQEDYIDN LV
//