RPC3_SCHPO
ID RPC3_SCHPO Reviewed; 591 AA.
AC Q9C106;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=DNA-directed RNA polymerase III subunit rpc3;
DE Short=RNA polymerase III subunit C3;
DE AltName: Full=RNA polymerase III subunit C82;
GN Name=rpc82; Synonyms=rpc3; ORFNames=SPAPB1E7.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=16877568; DOI=10.1093/nar/gkl421;
RA Proshkina G.M., Shematorova E.K., Proshkin S.A., Zaros C., Thuriaux P.,
RA Shpakovski G.V.;
RT "Ancient origin, functional conservation and fast evolution of DNA-
RT dependent RNA polymerase III.";
RL Nucleic Acids Res. 34:3615-3624(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, AND INTERACTION WITH MAF1.
RX PubMed=15590667; DOI=10.1074/jbc.m412375200;
RA Desai N., Lee J., Upadhya R., Chu Y., Moir R.D., Willis I.M.;
RT "Two steps in Maf1-dependent repression of transcription by RNA polymerase
RT III.";
RL J. Biol. Chem. 280:6455-6462(2005).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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 ECO:0000269|PubMed:15590667}.
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits (By similarity). Interacts with maf1.
CC {ECO:0000250, ECO:0000269|PubMed:15590667}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
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DR EMBL; DQ156225; ABA54853.1; -; mRNA.
DR EMBL; CU329670; CAC36920.1; -; Genomic_DNA.
DR RefSeq; NP_594129.1; NM_001019553.2.
DR AlphaFoldDB; Q9C106; -.
DR SMR; Q9C106; -.
DR BioGRID; 279839; 3.
DR STRING; 4896.SPAPB1E7.03.1; -.
DR iPTMnet; Q9C106; -.
DR MaxQB; Q9C106; -.
DR PaxDb; Q9C106; -.
DR PRIDE; Q9C106; -.
DR EnsemblFungi; SPAPB1E7.03.1; SPAPB1E7.03.1:pep; SPAPB1E7.03.
DR GeneID; 2543417; -.
DR KEGG; spo:SPAPB1E7.03; -.
DR PomBase; SPAPB1E7.03; rpc82.
DR VEuPathDB; FungiDB:SPAPB1E7.03; -.
DR eggNOG; KOG2587; Eukaryota.
DR HOGENOM; CLU_023294_0_0_1; -.
DR InParanoid; Q9C106; -.
DR OMA; QLKMVNE; -.
DR PhylomeDB; Q9C106; -.
DR Reactome; R-SPO-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-SPO-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR PRO; PR:Q9C106; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005666; C:RNA polymerase III complex; ISO:PomBase.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0006383; P:transcription by RNA polymerase III; ISO:PomBase.
DR Gene3D; 1.10.10.10; -; 3.
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 PANTHER; PTHR12949; PTHR12949; 1.
DR Pfam; PF08221; HTH_9; 1.
DR Pfam; PF05645; RNA_pol_Rpc82; 1.
PE 1: Evidence at protein level;
KW DNA-directed RNA polymerase; Nucleus; Reference proteome; Transcription;
KW Zinc.
FT CHAIN 1..591
FT /note="DNA-directed RNA polymerase III subunit rpc3"
FT /id="PRO_0000351041"
FT REGION 220..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..538
FT /note="Leucine-zipper"
SQ SEQUENCE 591 AA; 68368 MW; 90BDF2AA69402994 CRC64;
MSQYAVELCE ILVEEFFGDC CSAVASALLR HGRLTIPMLQ KRTSLPGPKI RQALVSLMQH
HMVLYVTVIE NVREVTYYET QWKEIYNILR KGKDVYLISQ KLNQEAASVV KYLSTQGRAR
VLEVFNAFDK KVDGSDEESR MMQKNLTELI YQKFLLVVQP RHLIPVGDQE MQLRIKHLDR
RKSENVSEIK KNREVDDSVA LEMLELRAAD MSELQGLTRK PKESIPHPTK RRKRAVGSAP
SVSTDLNNIL DDDNSILVPD LSAHVRINSG KLSVLSKNAR LTHWVERRIG KSTSLVYSHV
LSMLEPRLFS ISNQSPVFTL TTMELTRNFP NDIDVESSIV DKQYSVNSAS NELRVMEKLN
ELDELAEEDN YEESVDENAN RKSKVLAQHL ELLADCSLKF ISKIGNRGMG EWAVNFTHLT
DMLRAIEYEN FIEQKFGERA IRLLRIIKDK GKIEEKQLAN IALLRQRDLR TVLQAMAEIG
ALELQEVPRS SDRAPSKTFF LWFHRPDRAY SLLLDELYHV IARLYMRLRD ARAQRAQLIE
KAERIDIKGN EEQYLQKFEQ AELKKLYSYE EKLLLQASRL DDMVLVFRDN L
