RPC10_SCHPO
ID RPC10_SCHPO Reviewed; 109 AA.
AC O13896;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC10;
DE Short=RNA polymerase III subunit C10;
DE AltName: Full=DNA-directed RNA polymerases III 12.5 kDa polypeptide;
DE AltName: Full=RNA polymerase III subunit C11;
GN Name=rpc11; ORFNames=SPAC22A12.05;
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;
RA Shpakovski G.V., Lebedenko E.N.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9869639; DOI=10.1101/gad.12.24.3857;
RA Chedin S., Riva M., Schultz P., Sentenac A., Carles C.;
RT "The RNA cleavage activity of RNA polymerase III is mediated by an
RT essential TFIIS-like subunit and is important for transcription
RT termination.";
RL Genes Dev. 12:3857-3871(1998).
RN [3]
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).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Component of RNA polymerase III which synthesizes small RNAs, such as
CC 5S rRNA and tRNAs.
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P32529}.
CC -!- SIMILARITY: Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11
CC RNA polymerase family. {ECO:0000305}.
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DR EMBL; AF027823; AAD03488.1; -; mRNA.
DR EMBL; AF126532; AAD31425.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB16575.1; -; Genomic_DNA.
DR PIR; T38145; T38145.
DR RefSeq; NP_593235.1; NM_001018632.2.
DR AlphaFoldDB; O13896; -.
DR SMR; O13896; -.
DR BioGRID; 278022; 3.
DR DIP; DIP-29537N; -.
DR IntAct; O13896; 1.
DR STRING; 4896.SPAC22A12.05.1; -.
DR MaxQB; O13896; -.
DR PaxDb; O13896; -.
DR PRIDE; O13896; -.
DR EnsemblFungi; SPAC22A12.05.1; SPAC22A12.05.1:pep; SPAC22A12.05.
DR GeneID; 2541521; -.
DR KEGG; spo:SPAC22A12.05; -.
DR PomBase; SPAC22A12.05; rpc11.
DR VEuPathDB; FungiDB:SPAC22A12.05; -.
DR eggNOG; KOG2906; Eukaryota.
DR HOGENOM; CLU_093932_3_0_1; -.
DR InParanoid; O13896; -.
DR OMA; MVKFCPK; -.
DR PhylomeDB; O13896; -.
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:O13896; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005666; C:RNA polymerase III complex; IDA:PomBase.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006386; P:termination of RNA polymerase III transcription; IMP:PomBase.
DR GO; GO:0042779; P:tRNA 3'-trailer cleavage; IMP:PomBase.
DR CDD; cd10509; Zn-ribbon_RPC11; 1.
DR InterPro; IPR019761; DNA-dir_RNA_pol-M_15_CS.
DR InterPro; IPR001529; DNA-dir_RNA_pol_M/15kDasu.
DR InterPro; IPR012164; Rpa12/Rpb9/Rpc10/TFS.
DR InterPro; IPR034014; Zn_ribbon_RPC11_C.
DR InterPro; IPR001222; Znf_TFIIS.
DR PANTHER; PTHR11239; PTHR11239; 1.
DR Pfam; PF02150; RNA_POL_M_15KD; 1.
DR Pfam; PF01096; TFIIS_C; 1.
DR PIRSF; PIRSF005586; RNApol_RpoM; 1.
DR SMART; SM00661; RPOL9; 1.
DR SMART; SM00440; ZnF_C2C2; 1.
DR PROSITE; PS01030; RNA_POL_M_15KD; 1.
DR PROSITE; PS51133; ZF_TFIIS_2; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Zinc; Zinc-finger.
FT CHAIN 1..109
FT /note="DNA-directed RNA polymerase III subunit RPC10"
FT /id="PRO_0000121477"
FT ZN_FING 4..28
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT ZN_FING 65..107
FT /note="TFIIS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
SQ SEQUENCE 109 AA; 12815 MW; D17DA46D3AAE5B0A CRC64;
MQFCPTCGNH LIVAVDEEGR NAFDCRTCPY HFPISTFLYS RHEFAQKEVD DVLGGEEAFE
SNQQTEVTCE NTKCDNNRAY FFQLQIRSAD EPMSTFYRCT KCKFQWREN
