RPA12_SCHPO
ID RPA12_SCHPO Reviewed; 119 AA.
AC O94703;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=DNA-directed RNA polymerase I subunit RPA12;
DE AltName: Full=DNA-directed RNA polymerase I 13.1 kDa polypeptide;
GN Name=rpa12; ORFNames=SPCC1259.03;
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].
RA Shematorova E.K., Bobik T.V., Shpakovski G.V.;
RT "Molecular cloning and functional characterization of the fission yeast
RT rpa12+ cDNA encoding the specific subunit of Schizosaccharomyces pombe RNA
RT polymerase I.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RX PubMed=11254133; DOI=10.1007/s004380000375;
RA Imazawa Y., Imai K., Yao Y., Yamamoto K., Hisatake K., Muramatsu M.,
RA Nogi Y.;
RT "Isolation and characterization of the fission yeast gene Sprpa12+ reveals
RT that the conserved C-terminal zinc-finger region is dispensable for the
RT function of its product.";
RL Mol. Gen. Genet. 264:852-859(2001).
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 I which synthesizes ribosomal RNA
CC precursors. Required for growth at higher temperatures.
CC {ECO:0000269|PubMed:11254133}.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) complex consisting
CC of at least 13 subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P32529}.
CC -!- DOMAIN: The N-terminal zinc-finger domain but not the C-terminal one is
CC required for rpa12 function.
CC -!- SIMILARITY: Belongs to the archaeal RpoM/eukaryotic RPA12/RPB9/RPC11
CC RNA polymerase family. {ECO:0000305}.
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DR EMBL; AF219943; AAF80580.1; -; mRNA.
DR EMBL; AB023403; BAA87928.1; -; Genomic_DNA.
DR EMBL; AB023817; BAA87930.1; -; mRNA.
DR EMBL; CU329672; CAA22541.1; -; Genomic_DNA.
DR PIR; T40892; T40892.
DR RefSeq; NP_588059.1; NM_001023051.2.
DR PDB; 7AOC; EM; 3.84 A; I=1-119.
DR PDB; 7AOD; EM; 4.50 A; I/U=1-119.
DR PDB; 7AOE; EM; 3.90 A; I=1-119.
DR PDBsum; 7AOC; -.
DR PDBsum; 7AOD; -.
DR PDBsum; 7AOE; -.
DR AlphaFoldDB; O94703; -.
DR SMR; O94703; -.
DR BioGRID; 275483; 228.
DR STRING; 4896.SPCC1259.03.1; -.
DR MaxQB; O94703; -.
DR PaxDb; O94703; -.
DR PRIDE; O94703; -.
DR EnsemblFungi; SPCC1259.03.1; SPCC1259.03.1:pep; SPCC1259.03.
DR GeneID; 2538906; -.
DR KEGG; spo:SPCC1259.03; -.
DR PomBase; SPCC1259.03; rpa12.
DR VEuPathDB; FungiDB:SPCC1259.03; -.
DR eggNOG; KOG2907; Eukaryota.
DR HOGENOM; CLU_093932_1_1_1; -.
DR InParanoid; O94703; -.
DR OMA; EMQYHTL; -.
DR PhylomeDB; O94703; -.
DR Reactome; R-SPO-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-SPO-73772; RNA Polymerase I Promoter Escape.
DR PRO; PR:O94703; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005736; C:RNA polymerase I complex; IGI:PomBase.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006379; P:mRNA cleavage; IEA:InterPro.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IGI:PomBase.
DR CDD; cd10507; Zn-ribbon_RPA12; 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; IPR034004; Zn_ribbon_RPA12_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; PS00466; ZF_TFIIS_1; 1.
DR PROSITE; PS51133; ZF_TFIIS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Zinc; Zinc-finger.
FT CHAIN 1..119
FT /note="DNA-directed RNA polymerase I subunit RPA12"
FT /id="PRO_0000121464"
FT ZN_FING 10..30
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT ZN_FING 76..116
FT /note="TFIIS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
SQ SEQUENCE 119 AA; 13116 MW; 2ECB4C895533A6F3 CRC64;
MSAIGSLIFC SECGNLLEST TAQWTTCDQC QSVYPSEQFA NLVVETKSSA SAFPSALKLK
HSIVQVESQK EEAATIEEKC PKCGNDHMTF HTLQLRSADE GSTVFYECPR CAYKFSTNN
