CID14_SCHPO
ID CID14_SCHPO Reviewed; 684 AA.
AC Q9UTN3; Q09876; Q565C4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Poly(A) RNA polymerase cid14;
DE Short=PAP;
DE EC=2.7.7.19 {ECO:0000305|PubMed:16478992};
DE AltName: Full=Caffeine-induced death protein 14;
DE AltName: Full=Polynucleotide adenylyltransferase cid14;
GN Name=cid14; ORFNames=SPAC12G12.13c;
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, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=16478992; DOI=10.1128/mcb.26.5.1710-1721.2006;
RA Win T.Z., Draper S., Read R.L., Pearce J., Norbury C.J., Wang S.-W.;
RT "Requirement of fission yeast Cid14 in polyadenylation of rRNAs.";
RL Mol. Cell. Biol. 26:1710-1721(2006).
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 INTERACTION WITH AIR1.
RX PubMed=17512405; DOI=10.1016/j.cell.2007.03.038;
RA Buehler M., Haas W., Gygi S.P., Moazed D.;
RT "RNAi-dependent and -independent RNA turnover mechanisms contribute to
RT heterochromatic gene silencing.";
RL Cell 129:707-721(2007).
CC -!- FUNCTION: Required for 3' polyadenylation of the 5.8S and 25S rRNAs as
CC a prelude to their degradation in the exosome. Involved in the
CC nucleolar organization to ensure faithful chromosome segregation during
CC mitosis. {ECO:0000269|PubMed:16478992}.
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:0000305|PubMed:16478992};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11333;
CC Evidence={ECO:0000305|PubMed:16478992};
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: Heterooligomer. Interacts with air1.
CC {ECO:0000269|PubMed:16478992, ECO:0000269|PubMed:17512405}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16478992,
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; CU329670; CAI79317.1; -; Genomic_DNA.
DR PIR; S62544; S62544.
DR RefSeq; NP_001018181.1; NM_001018285.2.
DR AlphaFoldDB; Q9UTN3; -.
DR SMR; Q9UTN3; -.
DR BioGRID; 280460; 153.
DR STRING; 4896.SPAC12G12.13c.1; -.
DR iPTMnet; Q9UTN3; -.
DR MaxQB; Q9UTN3; -.
DR PaxDb; Q9UTN3; -.
DR PRIDE; Q9UTN3; -.
DR EnsemblFungi; SPAC12G12.13c.1; SPAC12G12.13c.1:pep; SPAC12G12.13c.
DR GeneID; 3361384; -.
DR KEGG; spo:SPAC12G12.13c; -.
DR PomBase; SPAC12G12.13c; cid14.
DR VEuPathDB; FungiDB:SPAC12G12.13c; -.
DR eggNOG; KOG1906; Eukaryota.
DR HOGENOM; CLU_013572_4_0_1; -.
DR InParanoid; Q9UTN3; -.
DR OMA; VGIAVHN; -.
DR PhylomeDB; Q9UTN3; -.
DR BRENDA; 2.7.7.19; 5613.
DR PRO; PR:Q9UTN3; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0031499; C:TRAMP complex; IDA: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:0004652; F:polynucleotide adenylyltransferase activity; IMP:PomBase.
DR GO; GO:0043023; F:ribosomal large subunit binding; IDA:PomBase.
DR GO; GO:1990817; F:RNA adenylyltransferase activity; IDA:PomBase.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043630; P:ncRNA polyadenylation involved in polyadenylation-dependent ncRNA catabolic process; IMP:PomBase.
DR GO; GO:0071046; P:nuclear polyadenylation-dependent ncRNA catabolic process; IMP:PomBase.
DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IMP:PomBase.
DR GO; GO:0031123; P:RNA 3'-end processing; IMP:PomBase.
DR GO; GO:0016077; P:sno(s)RNA catabolic process; ISO:PomBase.
DR GO; GO:0016078; P:tRNA catabolic process; ISO:PomBase.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR InterPro; IPR045862; Trf4-like.
DR PANTHER; PTHR23092; PTHR23092; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF03828; PAP_assoc; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Magnesium; Manganese; Metal-binding; mRNA processing;
KW Nucleotide-binding; Nucleus; Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..684
FT /note="Poly(A) RNA polymerase cid14"
FT /id="PRO_0000089746"
FT DOMAIN 434..492
FT /note="PAP-associated"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 684 AA; 78298 MW; C2CF653A51C8D39B CRC64;
MGKKSVSFNR NNYKKRKNER TEPLPRRIFK NDKPSKFKSK RKEKDKNSDA YDEMLLNNNF
TLLDQEEPMV EIGSKKSRND NDSEGIRDKG GVEISNKNDP YIQFGKADPL EPLEKPDLPE
EAIKRGEPTI LLGIPKREGR KTNPVHDKAV ENNSDFIKFD WNSDEDEDSV SNDKSKNNES
LKKSSKNEIP GFMRQRGRFF HEANEKSDSN RKRKRQAYEL DSQSCPWHRQ YKVEREVSRI
FHQDILHFID YITPTPEEHA VRKTLVSRIN QAVLQKWPDV SLYVFGSFET KLYLPTSDLD
LVIISPEHHY RGTKKDMFVL AHHLKKLKLA SEVQVITTAN VPIIKFVDPL TKVHVDISFN
QPGGLKTCLV VNGFMKKYPA LRPLVIIIKH FLNMRALNEV FLGGLSSYAI VCLVVSFLQL
HPRLSTGSMR EEDNFGVLLL EFLELYGKQF YYDAVGIAVH NGGFYFSKKK MGWLKPNQPY
LLSIQDPVDF QNDVSKSSRG LLRVKATFAN GFDLLTSKLY ALASRIEREG VNRVKDFPSI
LSTILSVDEG VRQHREHMLK CYKNNPVPLE PLVEVDALAS IDVDKLPLQD VGLQYVEDES
DSDETDAAKD DLFKVNESIE TNGHENFQKQ ALTSTGEQSS SNSRANPSKL FNISSDDSED
EVPIIEDTTA SDEESRAKKI RKRF
