ID   RPC3_KLULA              Reviewed;         657 AA.
AC   Q6CWJ7;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=DNA-directed RNA polymerase III subunit RPC3;
DE            Short=RNA polymerase III subunit C3;
GN   Name=RPC82; Synonyms=RPC3; OrderedLocusNames=KLLA0B03542g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       Specific core component of RNA polymerase III which synthesizes small
CC       RNAs, such as 5S rRNA and tRNAs (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC       consisting of 17 subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000305}.
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DR   EMBL; CR382122; CAH02085.1; -; Genomic_DNA.
DR   RefSeq; XP_451692.1; XM_451692.1.
DR   AlphaFoldDB; Q6CWJ7; -.
DR   SMR; Q6CWJ7; -.
DR   STRING; 28985.XP_451692.1; -.
DR   EnsemblFungi; CAH02085; CAH02085; KLLA0_B03542g.
DR   GeneID; 2896978; -.
DR   KEGG; kla:KLLA0_B03542g; -.
DR   eggNOG; KOG2587; Eukaryota.
DR   HOGENOM; CLU_010734_0_0_1; -.
DR   InParanoid; Q6CWJ7; -.
DR   OMA; QLKMVNE; -.
DR   Proteomes; UP000000598; Chromosome B.
DR   GO; GO:0005666; C:RNA polymerase III complex; IEA:EnsemblFungi.
DR   GO; GO:0001056; F:RNA polymerase III activity; IEA:EnsemblFungi.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR   GO; GO:0006386; P:termination of RNA polymerase III transcription; IEA:EnsemblFungi.
DR   GO; GO:0006384; P:transcription initiation from RNA polymerase III promoter; IEA:EnsemblFungi.
DR   GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IEA:EnsemblFungi.
DR   Gene3D; 1.10.10.10; -; 2.
DR   InterPro; IPR013197; RNA_pol_III_RPC82-rel_HTH.
DR   InterPro; IPR008806; RNA_pol_III_Rpc82_C.
DR   InterPro; IPR039748; RPC3.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR12949; PTHR12949; 1.
DR   Pfam; PF08221; HTH_9; 1.
DR   Pfam; PF05645; RNA_pol_Rpc82; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Nucleus; Reference proteome; Transcription;
KW   Zinc.
FT   CHAIN           1..657
FT                   /note="DNA-directed RNA polymerase III subunit RPC3"
FT                   /id="PRO_0000351035"
FT   REGION          390..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          584..605
FT                   /note="Leucine-zipper"
FT   COMPBIAS        402..416
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..445
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   657 AA;  74071 MW;  E01FDA712B42A2E5 CRC64;
     MSAAQAALIP DAAVPNGGAS VVSAAEPSTS TSPEPIDISS LEQRTLNPDS FLYSELARSH
     LGERASTVLS VLVNKGRLST REIHSFIPEL SLSSIKTVLV SLIQLRCVQY LEETSLSGRK
     TLYYYFNEEG LFLMLYAGDI SDRIVQYFNQ DEEQHLVNIA QQIIHNVLAL GSLTVKDYLA
     SESNSNDTDI FNIHQAFVRL ADLEFLVPLQ GIHYTPIVDL WNMLYLREYK KLPKNTTQSD
     LKKRNEAKAK AKLEFNRIVS SPSQDSNGKI FLTDSGTGFK KVNESVSLTF NLERYLKSRR
     SNQLVQFAKS RIGTTSSKIY AVALSMTEQH SNGLSHPLSK TGLFQDLDER TSLEEDLKLD
     EENVKGVSFT ALDVARRLPS NLDLRGTLVH SNQSLKRKQK HNQSPPQFEK RIKTEDGFVV
     PPLPTVMEES EEENEEGDAN LDLDEDDSDP RSVSLVNGHL RLLLTANIPF IKESKPGQFF
     VPYSSLIPIL KSSTYDSIIA STLGPSSHRV LRCIRDNGLC TERTITTTSL MREKDVRTVI
     GTLVKYNAIE IQEVPRTVDR AASRAVFLFR IKEKHAFNTM KLNLTWNLAR LISKLETLKE
     ENATLLKKAN RDDVKGREME LLLASEINQL KVVNDRELNG LVRRHRLLSL WEVFKLF