RPC9_YEAST
ID RPC9_YEAST Reviewed; 161 AA.
AC P47076; D6VWG6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC9;
DE Short=RNA polymerase III subunit C9;
DE AltName: Full=RNA polymerase III subunit C17;
GN Name=RPC17; OrderedLocusNames=YJL011C; ORFNames=J1349;
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=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 159.
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, AND PHOSPHORYLATION.
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 POLYMERASE III COMPLEX, AND INTERACTION WITH
RP TDS4.
RX PubMed=10611227; DOI=10.1128/mcb.20.2.488-495.2000;
RA Ferri M.L., Peyroche G., Siaut M., Lefebvre O., Carles C., Conesa C.,
RA Sentenac A.;
RT "A novel subunit of yeast RNA polymerase III interacts with the TFIIB-
RT related domain of TFIIIB70.";
RL Mol. Cell. Biol. 20:488-495(2000).
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 SUBCELLULAR LOCATION, AND INTERACTION WITH RPC25.
RX PubMed=12482973; DOI=10.1128/mcb.23.1.195-205.2003;
RA Siaut M., Zaros C., Levivier E., Ferri M.L., Court M., Werner M.,
RA Callebaut I., Thuriaux P., Sentenac A., Conesa C.;
RT "An Rpb4/Rpb7-like complex in yeast RNA polymerase III contains the
RT orthologue of mammalian CGRP-RCP.";
RL Mol. Cell. Biol. 23:195-205(2003).
RN [9]
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 [10]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH RPC25, AND
RP 3D-STRUCTURE MODELING OF THE POL III CORE COMPLEX.
RX PubMed=16818233; DOI=10.1016/j.molcel.2006.05.013;
RA Jasiak A.J., Armache K.J., Martens B., Jansen R.P., Cramer P.;
RT "Structural biology of RNA polymerase III: subcomplex C17/25 X-ray
RT structure and 11 subunit enzyme model.";
RL Mol. Cell 23:71-81(2006).
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 RPC25/RPC8-RPC17/RPC9
CC subcomplex may bind Pol III transcripts emerging from the adjacent exit
CC pore during elongation.
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits. Forms a Pol III subcomplex with RPC25/RPC8.
CC Interacts with BURF1/TDS4. {ECO:0000269|PubMed:10611227,
CC ECO:0000269|PubMed:12482973, ECO:0000269|PubMed:16818233}.
CC -!- INTERACTION:
CC P47076; P20436: RPB8; NbExp=2; IntAct=EBI-25782, EBI-15794;
CC P47076; P32910: RPC34; NbExp=2; IntAct=EBI-25782, EBI-15835;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12482973,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2930 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPC9 RNA polymerase subunit
CC family. {ECO:0000305}.
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DR EMBL; Z49286; CAA89302.1; -; Genomic_DNA.
DR EMBL; AY558346; AAS56672.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08782.2; -; Genomic_DNA.
DR PIR; S56782; S56782.
DR RefSeq; NP_012523.2; NM_001181445.2.
DR PDB; 2CKZ; X-ray; 3.20 A; A/C=1-161.
DR PDB; 5FJ8; EM; 3.90 A; D=1-161.
DR PDB; 5FJ9; EM; 4.60 A; D=1-161.
DR PDB; 5FJA; EM; 4.65 A; D=1-161.
DR PDB; 6CNB; EM; 4.10 A; D=1-161.
DR PDB; 6CNC; EM; 4.10 A; D=1-161.
DR PDB; 6CND; EM; 4.80 A; D=1-161.
DR PDB; 6CNF; EM; 4.50 A; D=1-161.
DR PDB; 6EU0; EM; 4.00 A; D=1-161.
DR PDB; 6EU1; EM; 3.40 A; D=1-161.
DR PDB; 6EU2; EM; 3.40 A; D=1-161.
DR PDB; 6EU3; EM; 3.30 A; D=1-161.
DR PDB; 6F40; EM; 3.70 A; D=1-161.
DR PDB; 6F41; EM; 4.30 A; D=1-161.
DR PDB; 6F42; EM; 5.50 A; D=1-161.
DR PDB; 6F44; EM; 4.20 A; D=1-161.
DR PDB; 6TUT; EM; 3.25 A; D=1-161.
DR PDBsum; 2CKZ; -.
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 AlphaFoldDB; P47076; -.
DR SMR; P47076; -.
DR BioGRID; 33744; 209.
DR ComplexPortal; CPX-2660; DNA-directed RNA polymerase III complex.
DR DIP; DIP-6745N; -.
DR IntAct; P47076; 15.
DR MINT; P47076; -.
DR STRING; 4932.YJL011C; -.
DR MaxQB; P47076; -.
DR PaxDb; P47076; -.
DR PRIDE; P47076; -.
DR EnsemblFungi; YJL011C_mRNA; YJL011C; YJL011C.
DR GeneID; 853442; -.
DR KEGG; sce:YJL011C; -.
DR SGD; S000003548; RPC17.
DR VEuPathDB; FungiDB:YJL011C; -.
DR eggNOG; KOG4168; Eukaryota.
DR GeneTree; ENSGT00390000014189; -.
DR HOGENOM; CLU_092529_3_0_1; -.
DR InParanoid; P47076; -.
DR OMA; PTNMVHL; -.
DR BioCyc; YEAST:G3O-31487-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; P47076; -.
DR PRO; PR:P47076; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47076; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005666; C:RNA polymerase III complex; IDA:SGD.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
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 from RNA polymerase III promoter; IDA:ComplexPortal.
DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IDA:SGD.
DR Gene3D; 1.20.1250.40; -; 1.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR005574; Rpb4/RPC9.
DR InterPro; IPR038324; Rpb4/RPC9_sf.
DR InterPro; IPR038846; RPC9.
DR PANTHER; PTHR15561; PTHR15561; 1.
DR Pfam; PF03874; RNA_pol_Rpb4; 1.
DR SUPFAM; SSF47819; SSF47819; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription.
FT CHAIN 1..161
FT /note="DNA-directed RNA polymerase III subunit RPC9"
FT /id="PRO_0000203077"
FT REGION 75..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 159
FT /note="G -> A (in Ref. 1; CAA89302 and 3; AAS56672)"
FT /evidence="ECO:0000305"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:2CKZ"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:2CKZ"
FT HELIX 31..35
FT /evidence="ECO:0007829|PDB:2CKZ"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:6EU1"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:2CKZ"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:2CKZ"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:2CKZ"
FT HELIX 131..135
FT /evidence="ECO:0007829|PDB:2CKZ"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2CKZ"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:2CKZ"
FT HELIX 147..158
FT /evidence="ECO:0007829|PDB:2CKZ"
SQ SEQUENCE 161 AA; 18596 MW; BA1FF62FE3676C51 CRC64;
MKVLEERNAF LSDYEVLKFL TDLEKKHLWD QKSLAALKKS RSKGKQNRPY NHPELQGITR
NVVNYLSINK NFINQEDEGE ERESSGAKDA EKSGISKMSD ESFAELMTKL NSFKLFKAEK
LQIVNQLPAN MVHLYSIVEE CDARFDEKTI EEMLEIISGY A
