CID12_SCHPO
ID CID12_SCHPO Reviewed; 336 AA.
AC O74518;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Poly(A) RNA polymerase cid12;
DE Short=PAP;
DE EC=2.7.7.19;
DE AltName: Full=Caffeine-induced death protein 12;
DE AltName: Full=Polynucleotide adenylyltransferase cid12;
GN Name=cid12; ORFNames=SPCC663.12;
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 [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 [2]
RP FUNCTION, COMPOSITION OF THE RDRC AND RITS COMPLEXES, SUBCELLULAR LOCATION,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15607976; DOI=10.1016/j.cell.2004.11.034;
RA Motamedi M.R., Verdel A., Colmenares S.U., Gerber S.A., Gygi S.P.,
RA Moazed D.;
RT "Two RNAi complexes, RITS and RDRC, physically interact and localize to
RT noncoding centromeric RNAs.";
RL Cell 119:789-802(2004).
RN [3]
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325; THR-327 AND SER-329, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Has a role in the RNA interference (RNAi) pathway which is
CC important for heterochromatin formation and accurate chromosome
CC segregation. A member of the RNA-directed RNA polymerase complex (RDRC)
CC which is involved in the generation of small interfering RNAs (siRNAs)
CC and mediate their association with the RNA-induced transcriptional
CC silencing (RITS) complex. RITS acts as a priming complex for dsRNA
CC synthesis at the site of non-coding centromeric RNA.
CC {ECO:0000269|PubMed:15607976}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173115; EC=2.7.7.19;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Cid12, hrr1 and rdp1 interact forming the RNA-directed RNA
CC polymerase complex (RDRC). The RDRC complex interacts with the RITS
CC complex via interaction between ago1 and hrr1. Clr4 has a role in
CC mediating this interaction.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:15607976, ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000305}.
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DR EMBL; CU329672; CAA20372.1; -; Genomic_DNA.
DR PIR; T41543; T41543.
DR RefSeq; NP_588273.1; NM_001023263.2.
DR AlphaFoldDB; O74518; -.
DR SMR; O74518; -.
DR BioGRID; 275988; 128.
DR DIP; DIP-60035N; -.
DR IntAct; O74518; 2.
DR STRING; 4896.SPCC663.12.1; -.
DR iPTMnet; O74518; -.
DR MaxQB; O74518; -.
DR PaxDb; O74518; -.
DR PRIDE; O74518; -.
DR EnsemblFungi; SPCC663.12.1; SPCC663.12.1:pep; SPCC663.12.
DR GeneID; 2539423; -.
DR KEGG; spo:SPCC663.12; -.
DR PomBase; SPCC663.12; cid12.
DR VEuPathDB; FungiDB:SPCC663.12; -.
DR eggNOG; KOG1906; Eukaryota.
DR HOGENOM; CLU_845088_0_0_1; -.
DR InParanoid; O74518; -.
DR OMA; TLMCISF; -.
DR PhylomeDB; O74518; -.
DR PRO; PR:O74518; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0031380; C:nuclear RNA-directed RNA polymerase complex; IDA:PomBase.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0031379; C:RNA-directed RNA polymerase complex; IDA:PomBase.
DR GO; GO:0031499; C:TRAMP complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; ISM:PomBase.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; IMP:PomBase.
DR GO; GO:0031508; P:pericentric heterochromatin assembly; IMP:PomBase.
DR GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0043631; P:RNA polyadenylation; ISM:PomBase.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR045862; Trf4-like.
DR InterPro; IPR045100; TUTase_dom.
DR PANTHER; PTHR23092; PTHR23092; 1.
DR Pfam; PF03828; PAP_assoc; 1.
DR Pfam; PF19088; TUTase; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Chromosome partition; Cytoplasm; Magnesium;
KW Manganese; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; RNA-mediated gene silencing; Transferase.
FT CHAIN 1..336
FT /note="Poly(A) RNA polymerase cid12"
FT /id="PRO_0000256156"
FT DOMAIN 209..263
FT /note="PAP-associated"
FT BINDING 77
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 327
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 336 AA; 38558 MW; BF56B701691F8737 CRC64;
MGKVLLELHS VPWNEEGLSD NARLYSFLEF VSPKIEELKY RKLLLEKLQT HIREVVLDAE
LQVYGSMYIG TTLSISDVDV SLKSPRVGEL EKRRVTMVLR KYLDADADFH SSARVPRINL
VDVSGIGVDL TFGNDKACRT AELQKAYNEE HPIFGRLLML LKHWLFERDL ENVHHGGIAS
CALSYMLIGW LEMRFHKKGI DSEVQPIRAL LQKFFYFWGV EWTYELFVLR PLTGQIVPKL
QKGWLNEVQP NLLSIEDPID RNNDIGKQSF QISMIKAAFV ASANELLSDK TWFSTFAITE
DEMFLCKQFE NVINTKRSLV EGYDSDTESD ELQAGG
