CID13_SCHPO
ID CID13_SCHPO Reviewed; 578 AA.
AC Q9UT49;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Poly(A) RNA polymerase cid13;
DE Short=PAP;
DE EC=2.7.7.19 {ECO:0000269|PubMed:12062100};
DE AltName: Full=Caffeine-induced death protein 13;
DE AltName: Full=Polynucleotide adenylyltransferase cid13;
GN Name=cid13; ORFNames=SPAC821.04c;
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, CATALYTIC ACTIVITY, INTERACTION WITH PAB1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12062100; DOI=10.1016/s0092-8674(02)00753-5;
RA Saitoh S., Chabes A., McDonald W.H., Thelander L., Yates J.R. III,
RA Russell P.;
RT "Cid13 is a cytoplasmic poly(A) polymerase that regulates ribonucleotide
RT reductase mRNA.";
RL Cell 109:563-573(2002).
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).
CC -!- FUNCTION: Polymerase that creates the 3' poly(A) tail of suc22 mRNA.
CC {ECO:0000269|PubMed:12062100}.
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 Evidence={ECO:0000269|PubMed:12062100};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11333;
CC Evidence={ECO:0000269|PubMed:12062100};
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: Interacts with pab1. {ECO:0000269|PubMed:12062100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12062100,
CC ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB57438.1; -; Genomic_DNA.
DR PIR; T41715; T41715.
DR RefSeq; NP_593157.1; NM_001018555.2.
DR AlphaFoldDB; Q9UT49; -.
DR SMR; Q9UT49; -.
DR BioGRID; 279633; 16.
DR IntAct; Q9UT49; 6.
DR STRING; 4896.SPAC821.04c.1; -.
DR MaxQB; Q9UT49; -.
DR PaxDb; Q9UT49; -.
DR EnsemblFungi; SPAC821.04c.1; SPAC821.04c.1:pep; SPAC821.04c.
DR GeneID; 2543204; -.
DR KEGG; spo:SPAC821.04c; -.
DR PomBase; SPAC821.04c; cid13.
DR VEuPathDB; FungiDB:SPAC821.04c; -.
DR eggNOG; KOG2277; Eukaryota.
DR HOGENOM; CLU_476635_0_0_1; -.
DR InParanoid; Q9UT49; -.
DR OMA; ISCMVIN; -.
DR PhylomeDB; Q9UT49; -.
DR PRO; PR:Q9UT49; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
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:0003730; F:mRNA 3'-UTR binding; IC:PomBase.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:1990817; F:RNA adenylyltransferase activity; IDA:PomBase.
DR GO; GO:0006378; P:mRNA polyadenylation; IDA:PomBase.
DR GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Magnesium; Manganese; Metal-binding;
KW mRNA processing; Nucleotide-binding; Nucleus; Reference proteome;
KW RNA-binding; Transferase.
FT CHAIN 1..578
FT /note="Poly(A) RNA polymerase cid13"
FT /id="PRO_0000120313"
FT DOMAIN 275..330
FT /note="PAP-associated"
FT REGION 495..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 578 AA; 65771 MW; A572D21E13552351 CRC64;
MDNANCVGGC KFETRSFQYR RRIPYSLGAD PLPPVHPLSL KNLVDIDTDL ISSQLYELYD
SIILNDSGLE RRYAFVQKLE QILKKEFPYK NIKTSLFGST QSLLASNASD IDLCIITDPP
QCAPTTCEVS AAFARNGLKK VVCISTAKVP IVKVWDSELQ LSCDCNINKT ISTLNTRLMR
SYVLCDPRVR PLIVMIKYWA KRRCLNDAAE GGTLTSYTIS CMVINFLQKR DPPILPSLQM
LPHLQDSSTM TDGLDVSFFD DPDLVHGFGD KNEESLGILF VEFFRFFGYL FDYEHFVLSI
RHGTFLSKRA KGWQFQLNNF LCVEEPFHTS RNLANTADEI TMKGIQLEFR RVFRLLAYNC
NVDDACSQFT FPSLTDTSFM DDYVNELQLE IVPGFSHGRD SSDTSCTESP PEPSHFAWAF
DPYNATASPY YNQNINSSID YSSIYSNDVP AIPPNVPYTF VDPYTYACYI NNNSYLPPSY
MDFYTWYNSP YPKSSHHFDE RHGGDRHEKN LSNSRRYSRN KFHKKKQSSG PFQYYPDAFS
FTPTDNNSPP SNSSSSEVVS PVSLHSEPVL STVQAFKS
