RPAC1_YEAST
ID RPAC1_YEAST Reviewed; 335 AA.
AC P07703; D6W4A9;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=DNA-directed RNA polymerases I and III subunit RPAC1 {ECO:0000305};
DE Short=RNA polymerases I and III subunit AC1 {ECO:0000305};
DE AltName: Full=C37;
DE AltName: Full=DNA-directed RNA polymerases I and III 40 kDa polypeptide {ECO:0000303|PubMed:3815519};
DE Short=AC40 {ECO:0000303|PubMed:3815519};
DE Short=C40 {ECO:0000305};
GN Name=RPC40 {ECO:0000303|PubMed:3815519};
GN Synonyms=RPC5 {ECO:0000312|SGD:S000006314};
GN OrderedLocusNames=YPR110C {ECO:0000312|SGD:S000006314}; ORFNames=P8283.18;
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].
RX PubMed=3815519; DOI=10.1016/0092-8674(87)90241-8;
RA Mann C., Buhler J.-M., Treich I., Sentenac A.;
RT "RPC40, a unique gene for a subunit shared between yeast RNA polymerases A
RT and C.";
RL Cell 48:627-637(1987).
RN [2]
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 [3]
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 [4]
RP ASSOCIATION WITH AC19.
RX PubMed=8516295; DOI=10.1073/pnas.90.12.5524;
RA Lalo D., Carles C., Sentenac A., Thuriaux P.;
RT "Interactions between three common subunits of yeast RNA polymerases I and
RT III.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5524-5528(1993).
RN [5]
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 [6]
RP INTERACTION WITH C53.
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 [7]
RP IDENTIFICATION IN THE RNA POL I COMPLEX.
RX PubMed=11717393; DOI=10.1073/pnas.231181398;
RA Fath S., Milkereit P., Peyroche G., Riva M., Carles C., Tschochner H.;
RT "Differential roles of phosphorylation in the formation of transcriptional
RT active RNA polymerase I.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14334-14339(2001).
RN [8]
RP IDENTIFICATION IN THE RNA POL I COMPLEX.
RX PubMed=12407181; DOI=10.1073/pnas.232580799;
RA Peyroche G., Levillain E., Siaut M., Callebaut I., Schultz P., Sentenac A.,
RA Riva M., Carles C.;
RT "The A14-A43 heterodimer subunit in yeast RNA pol I and their relationship
RT to Rpb4-Rpb7 pol II subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14670-14675(2002).
RN [9]
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 [10]
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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, 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).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [14]
RP INTERACTION WITH TY1 INTEGRASE, AND FUNCTION.
RX PubMed=25931562; DOI=10.1126/science.1259114;
RA Bridier-Nahmias A., Tchalikian-Cosson A., Baller J.A., Menouni R.,
RA Fayol H., Flores A., Saib A., Werner M., Voytas D.F., Lesage P.;
RT "An RNA polymerase III subunit determines sites of retrotransposon
RT integration.";
RL Science 348:585-588(2015).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (12.00 ANGSTROMS) OF THE POL I COMPLEX,
RP FUNCTION, AND SUBUNIT.
RX PubMed=18160037; DOI=10.1016/j.cell.2007.10.051;
RA Kuhn C.D., Geiger S.R., Baumli S., Gartmann M., Gerber J., Jennebach S.,
RA Mielke T., Tschochner H., Beckmann R., Cramer P.;
RT "Functional architecture of RNA polymerase I.";
RL Cell 131:1260-1272(2007).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, AND
RP SUBUNIT.
RX PubMed=24153184; DOI=10.1038/nature12636;
RA Fernandez-Tornero C., Moreno-Morcillo M., Rashid U.J., Taylor N.M.,
RA Ruiz F.M., Gruene T., Legrand P., Steuerwald U., Muller C.W.;
RT "Crystal structure of the 14-subunit RNA polymerase I.";
RL Nature 502:644-649(2013).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, AND
RP SUBUNIT.
RX PubMed=24153182; DOI=10.1038/nature12712;
RA Engel C., Sainsbury S., Cheung A.C., Kostrewa D., Cramer P.;
RT "RNA polymerase I structure and transcription regulation.";
RL Nature 502:650-655(2013).
CC -!- FUNCTION: DNA-dependent RNA polymerases catalyze the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Common component of RNA polymerases I (Pol I) and III (Pol III) which
CC synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and
CC tRNAs, respectively. RPC40 is part of the polymerase core and may
CC function as a clamp element that moves to open and close the cleft
CC (PubMed:18160037, PubMed:24153182, PubMed:24153184). Plays an important
CC role in targeting retrotransposons Ty integration upstream of pol III-
CC transcribed genes such as tRNA genes, allowing Ty1, Ty2 and Ty4 to
CC proliferate and yet minimizing genetic damage (PubMed:25931562).
CC {ECO:0000269|PubMed:18160037, ECO:0000269|PubMed:24153182,
CC ECO:0000269|PubMed:24153184, ECO:0000269|PubMed:25931562,
CC ECO:0000305|PubMed:10384303}.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8,
CC RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34 (PubMed:8516295,
CC PubMed:11717393, PubMed:12407181, PubMed:18160037, PubMed:24153184,
CC PubMed:24153182). The complex is composed of a horseshoe-shaped core
CC containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10,
CC RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-
CC binding cleft. Outside of the core, RPA14 and RPA43 form the stalk that
CC mediates interactions with transcription initiation factors and newly
CC synthesized RNA. Component of the RNA polymerase III (Pol III) complex
CC consisting of at least 17 subunits (PubMed:8516295, PubMed:10384303,
CC PubMed:10393904). Interacts with the RPC19/RPAC2 (PubMed:8516295) and
CC RPC53/RPC4 (PubMed:10393904). Interacts with retrotransposons Ty
CC integrase, targeting Ty1, Ty2 and Ty4 integration upstream of pol III-
CC transcribed genes (PubMed:25931562). {ECO:0000269|PubMed:10393904,
CC ECO:0000269|PubMed:11717393, ECO:0000269|PubMed:12407181,
CC ECO:0000269|PubMed:18160037, ECO:0000269|PubMed:24153182,
CC ECO:0000269|PubMed:24153184, ECO:0000269|PubMed:25931562,
CC ECO:0000269|PubMed:8516295, ECO:0000305|PubMed:10384303}.
CC -!- INTERACTION:
CC P07703; P10964: RPA190; NbExp=4; IntAct=EBI-15831, EBI-15730;
CC P07703; P08518: RPB2; NbExp=2; IntAct=EBI-15831, EBI-15767;
CC P07703; P20436: RPB8; NbExp=3; IntAct=EBI-15831, EBI-15794;
CC P07703; P28000: RPC19; NbExp=5; IntAct=EBI-15831, EBI-15846;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 13000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase
CC subunit family. {ECO:0000305}.
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DR EMBL; M15499; AAA34999.1; -; Genomic_DNA.
DR EMBL; U32445; AAB68080.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11525.1; -; Genomic_DNA.
DR PIR; A25968; A25968.
DR RefSeq; NP_015435.1; NM_001184207.1.
DR PDB; 4C2M; X-ray; 2.80 A; C/R=1-335.
DR PDB; 4C3H; X-ray; 3.27 A; C=1-335.
DR PDB; 4C3I; X-ray; 3.00 A; C=1-335.
DR PDB; 4C3J; X-ray; 3.35 A; C=1-335.
DR PDB; 4YM7; X-ray; 5.50 A; AC/BC/CC/DC/EC/FC=1-335.
DR PDB; 5FJ8; EM; 3.90 A; C=1-335.
DR PDB; 5FJ9; EM; 4.60 A; C=1-335.
DR PDB; 5FJA; EM; 4.65 A; C=1-335.
DR PDB; 5G5L; EM; 4.80 A; C=1-335.
DR PDB; 5LMX; EM; 4.90 A; C=1-335.
DR PDB; 5M3F; EM; 3.80 A; C=1-335.
DR PDB; 5M3M; EM; 4.00 A; C=1-335.
DR PDB; 5M5W; EM; 3.80 A; C=1-335.
DR PDB; 5M5X; EM; 4.00 A; C=1-335.
DR PDB; 5M5Y; EM; 4.00 A; C=1-335.
DR PDB; 5M64; EM; 4.60 A; C=1-335.
DR PDB; 5N5Y; EM; 7.70 A; C=1-335.
DR PDB; 5N5Z; EM; 7.70 A; C=1-335.
DR PDB; 5N60; EM; 7.70 A; C=1-335.
DR PDB; 5N61; EM; 3.40 A; C=1-335.
DR PDB; 5OA1; EM; 4.40 A; C=1-335.
DR PDB; 5W5Y; EM; 3.80 A; C=1-335.
DR PDB; 5W64; EM; 4.20 A; C=1-335.
DR PDB; 5W65; EM; 4.30 A; C=1-335.
DR PDB; 5W66; EM; 3.90 A; C=1-335.
DR PDB; 6CNB; EM; 4.10 A; C=1-335.
DR PDB; 6CNC; EM; 4.10 A; C=1-335.
DR PDB; 6CND; EM; 4.80 A; C=1-335.
DR PDB; 6CNF; EM; 4.50 A; C=1-335.
DR PDB; 6EU0; EM; 4.00 A; C=1-335.
DR PDB; 6EU1; EM; 3.40 A; C=1-335.
DR PDB; 6EU2; EM; 3.40 A; C=1-335.
DR PDB; 6EU3; EM; 3.30 A; C=1-335.
DR PDB; 6F40; EM; 3.70 A; C=1-335.
DR PDB; 6F41; EM; 4.30 A; C=1-335.
DR PDB; 6F42; EM; 5.50 A; C=1-335.
DR PDB; 6F44; EM; 4.20 A; C=1-335.
DR PDB; 6H67; EM; 3.60 A; C=1-335.
DR PDB; 6H68; EM; 4.60 A; C=1-335.
DR PDB; 6HKO; EM; 3.42 A; C=1-335.
DR PDB; 6HLQ; EM; 3.18 A; C=1-335.
DR PDB; 6HLR; EM; 3.18 A; C=1-335.
DR PDB; 6HLS; EM; 3.21 A; C=1-335.
DR PDB; 6RQH; EM; 3.70 A; C=1-335.
DR PDB; 6RQL; EM; 2.90 A; C=1-335.
DR PDB; 6RQT; EM; 4.00 A; C=1-335.
DR PDB; 6RRD; EM; 3.10 A; C=1-335.
DR PDB; 6RUI; EM; 2.70 A; C=1-335.
DR PDB; 6RUO; EM; 3.50 A; C=1-335.
DR PDB; 6RWE; EM; 3.00 A; C=1-335.
DR PDB; 6TPS; EM; 3.54 A; C=1-335.
DR PDB; 6TUT; EM; 3.25 A; C=1-335.
DR PDBsum; 4C2M; -.
DR PDBsum; 4C3H; -.
DR PDBsum; 4C3I; -.
DR PDBsum; 4C3J; -.
DR PDBsum; 4YM7; -.
DR PDBsum; 5FJ8; -.
DR PDBsum; 5FJ9; -.
DR PDBsum; 5FJA; -.
DR PDBsum; 5G5L; -.
DR PDBsum; 5LMX; -.
DR PDBsum; 5M3F; -.
DR PDBsum; 5M3M; -.
DR PDBsum; 5M5W; -.
DR PDBsum; 5M5X; -.
DR PDBsum; 5M5Y; -.
DR PDBsum; 5M64; -.
DR PDBsum; 5N5Y; -.
DR PDBsum; 5N5Z; -.
DR PDBsum; 5N60; -.
DR PDBsum; 5N61; -.
DR PDBsum; 5OA1; -.
DR PDBsum; 5W5Y; -.
DR PDBsum; 5W64; -.
DR PDBsum; 5W65; -.
DR PDBsum; 5W66; -.
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; 6H67; -.
DR PDBsum; 6H68; -.
DR PDBsum; 6HKO; -.
DR PDBsum; 6HLQ; -.
DR PDBsum; 6HLR; -.
DR PDBsum; 6HLS; -.
DR PDBsum; 6RQH; -.
DR PDBsum; 6RQL; -.
DR PDBsum; 6RQT; -.
DR PDBsum; 6RRD; -.
DR PDBsum; 6RUI; -.
DR PDBsum; 6RUO; -.
DR PDBsum; 6RWE; -.
DR PDBsum; 6TPS; -.
DR PDBsum; 6TUT; -.
DR AlphaFoldDB; P07703; -.
DR SMR; P07703; -.
DR BioGRID; 36277; 252.
DR ComplexPortal; CPX-1664; DNA-directed RNA Polymerase I complex.
DR ComplexPortal; CPX-2660; DNA-directed RNA polymerase III complex.
DR DIP; DIP-17N; -.
DR IntAct; P07703; 148.
DR MINT; P07703; -.
DR STRING; 4932.YPR110C; -.
DR iPTMnet; P07703; -.
DR MaxQB; P07703; -.
DR PaxDb; P07703; -.
DR PRIDE; P07703; -.
DR EnsemblFungi; YPR110C_mRNA; YPR110C; YPR110C.
DR GeneID; 856226; -.
DR KEGG; sce:YPR110C; -.
DR SGD; S000006314; RPC40.
DR VEuPathDB; FungiDB:YPR110C; -.
DR eggNOG; KOG1521; Eukaryota.
DR GeneTree; ENSGT00950000183100; -.
DR HOGENOM; CLU_038421_0_1_1; -.
DR InParanoid; P07703; -.
DR OMA; ECLRHPE; -.
DR BioCyc; YEAST:G3O-34250-MON; -.
DR Reactome; R-SCE-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-SCE-73772; RNA Polymerase I Promoter Escape.
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 PRO; PR:P07703; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P07703; protein.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0005736; C:RNA polymerase I complex; IDA:UniProtKB.
DR GO; GO:0005666; C:RNA polymerase III complex; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0001054; F:RNA polymerase I activity; IDA:UniProtKB.
DR GO; GO:0001056; F:RNA polymerase III activity; IEA:InterPro.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:ComplexPortal.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IDA:ComplexPortal.
DR GO; GO:0006386; P:termination of RNA polymerase III transcription; IDA:ComplexPortal.
DR GO; GO:0006360; P:transcription by RNA polymerase I; IDA:UniProtKB.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IDA:ComplexPortal.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IDA:ComplexPortal.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; IDA:ComplexPortal.
DR GO; GO:0006384; P:transcription initiation from RNA polymerase III promoter; IDA:ComplexPortal.
DR GO; GO:0070893; P:transposon integration; IMP:SGD.
DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IDA:SGD.
DR CDD; cd07032; RNAP_I_II_AC40; 1.
DR Gene3D; 2.170.120.12; -; 1.
DR Gene3D; 3.30.1360.10; -; 1.
DR HAMAP; MF_00320; RNApol_arch_Rpo3; 1.
DR InterPro; IPR001514; DNA-dir_RNA_pol_30-40kDasu_CS.
DR InterPro; IPR011262; DNA-dir_RNA_pol_insert.
DR InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
DR InterPro; IPR036603; RBP11-like.
DR InterPro; IPR022842; RNAP_Rpo3/Rpb3/RPAC1.
DR InterPro; IPR033901; RNAPI/III_AC40.
DR InterPro; IPR036643; RNApol_insert_sf.
DR PANTHER; PTHR11800:SF13; PTHR11800:SF13; 1.
DR Pfam; PF01000; RNA_pol_A_bac; 1.
DR Pfam; PF01193; RNA_pol_L; 1.
DR SMART; SM00662; RPOLD; 1.
DR SUPFAM; SSF55257; SSF55257; 1.
DR SUPFAM; SSF56553; SSF56553; 1.
DR PROSITE; PS00446; RNA_POL_D_30KD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; DNA-directed RNA polymerase; Nucleus;
KW Phosphoprotein; Reference proteome; Ribosome biogenesis; Transcription.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..335
FT /note="DNA-directed RNA polymerases I and III subunit
FT RPAC1"
FT /id="PRO_0000132742"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 34..39
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 77..88
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 94..102
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:6EU3"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:4C2M"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 201..211
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 225..235
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 242..248
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:4C2M"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:4C2M"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:4C2M"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 285..302
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 312..329
FT /evidence="ECO:0007829|PDB:6RUI"
SQ SEQUENCE 335 AA; 37687 MW; 76A5D6784403E990 CRC64;
MSNIVGIEYN RVTNTTSTDF PGFSKDAENE WNVEKFKKDF EVNISSLDAR EANFDLINID
TSIANAFRRI MISEVPSVAA EYVYFFNNTS VIQDEVLAHR IGLVPLKVDP DMLTWVDSNL
PDDEKFTDEN TIVLSLNVKC TRNPDAPKGS TDPKELYNNA HVYARDLKFE PQGRQSTTFA
DCPVVPADPD ILLAKLRPGQ EISLKAHCIL GIGGDHAKFS PVSTASYRLL PQINILQPIK
GESARRFQKC FPPGVIGIDE GSDEAYVKDA RKDTVSREVL RYEEFADKVK LGRVRNHFIF
NVESAGAMTP EEIFFKSVRI LKNKAEYLKN CPITQ
