ID   CID11_SCHPO             Reviewed;         478 AA.
AC   O74326;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Poly(A) RNA polymerase cid11;
DE            Short=PAP;
DE            EC=2.7.7.19;
DE   AltName: Full=Caffeine-induced death protein 11;
DE   AltName: Full=Polynucleotide adenylyltransferase cid11;
GN   Name=cid11; ORFNames=SPBC1685.06;
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   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   -!- 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAA20054.1; -; Genomic_DNA.
DR   PIR; T39522; T39522.
DR   RefSeq; NP_595210.1; NM_001021117.2.
DR   AlphaFoldDB; O74326; -.
DR   SMR; O74326; -.
DR   STRING; 4896.SPBC1685.06.1; -.
DR   SwissPalm; O74326; -.
DR   PaxDb; O74326; -.
DR   EnsemblFungi; SPBC1685.06.1; SPBC1685.06.1:pep; SPBC1685.06.
DR   GeneID; 2539762; -.
DR   KEGG; spo:SPBC1685.06; -.
DR   PomBase; SPBC1685.06; cid11.
DR   VEuPathDB; FungiDB:SPBC1685.06; -.
DR   eggNOG; KOG2277; Eukaryota.
DR   HOGENOM; CLU_033943_0_0_1; -.
DR   InParanoid; O74326; -.
DR   OMA; ESRLAIH; -.
DR   PhylomeDB; O74326; -.
DR   PRO; PR:O74326; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR   GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006378; P:mRNA polyadenylation; ISS:PomBase.
DR   GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR   GO; GO:0071050; P:sno(s)RNA polyadenylation; ISS:PomBase.
DR   GO; GO:0016180; P:snRNA processing; ISS:PomBase.
DR   Gene3D; 3.30.460.10; -; 1.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002058; PAP_assoc.
DR   InterPro; IPR045100; TUTase_dom.
DR   Pfam; PF03828; PAP_assoc; 1.
DR   Pfam; PF19088; TUTase; 1.
DR   SUPFAM; SSF81301; SSF81301; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Magnesium; Manganese; Metal-binding;
KW   mRNA processing; Nucleotide-binding; Nucleus; Reference proteome;
KW   RNA-binding; Transferase.
FT   CHAIN           1..478
FT                   /note="Poly(A) RNA polymerase cid11"
FT                   /id="PRO_0000256154"
FT   DOMAIN          263..317
FT                   /note="PAP-associated"
FT   REGION          428..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         106
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   478 AA;  54543 MW;  5D769C049DCC0CF0 CRC64;
     MELLTFTCCP FEGQMQQKKR RFDANLVQLQ ESEHRNDQIN ETVDAELTNE CWKLYMRLKP
     SNEEVSRRQQ FVDKLRTILS TEIKDAKLDL FVFGSTENNL AIQQSDVDVC IITNGSKYLN
     STCQLAQLLY SYGMKQIVCV SRARVPIVKI WDPQFDIHCD LNINNDVAKI NTKMLRLFVS
     IDPRVRPLGL IIKYWAKQRA LCDAAGSGTI TSYTISCMLV NFLQTRNPPI LPAMLDLMSN
     DDNKMFVDDI VGFKEKATLN KTSLGRLLID FFYYYGFSFN YLDSVVSVRS GTVLNKQEKG
     WAMEVNNSLC VEEPFNTARN LANTADNPSV KGLQSEFQRA FRLMSENNAC ERLCKICEEY
     QFLDITNEAN YGNTNTPFNT AYESFGCNHT VLPEAAAYPK PYYPPQITLS DGGNMNFLYY
     IPDESNHQSY ENKANRDSDF QGQTSLTQGS APPWHYIPCQ SWLVWYPSED ASNPASGN