ID   PAP_SCHPO               Reviewed;         566 AA.
AC   Q10295; Q9UU09;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 149.
DE   RecName: Full=Poly(A) polymerase pla1;
DE            Short=PAP;
DE            EC=2.7.7.19 {ECO:0000269|PubMed:8692700};
DE   AltName: Full=Polynucleotide adenylyltransferase;
GN   Name=pla1; ORFNames=SPBC646.04;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=8692700; DOI=10.1093/nar/24.13.2585;
RA   Ohnacker M., Minivielle-Sebastia L., Keller W.;
RT   "The Schizosaccharomyces pombe pla1 gene encodes a poly(A) polymerase and
RT   can functionally replace its Saccharomyces cerevisiae homologue.";
RL   Nucleic Acids Res. 24:2585-2591(1996).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 233-436, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
CC   -!- FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's. May
CC       acquire specificity through interaction with a cleavage and
CC       polyadenylation factor (CF I). {ECO:0000269|PubMed:8692700}.
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:8692700};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11333;
CC         Evidence={ECO:0000305|PubMed:8692700};
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       Note=Binds 2 magnesium ions. Also active with manganese. {ECO:0000250};
CC   -!- INTERACTION:
CC       Q10295; O74958: mmi1; NbExp=3; IntAct=EBI-7997221, EBI-7997069;
CC       Q10295; Q9UTR8: red1; NbExp=3; IntAct=EBI-7997221, EBI-1117407;
CC       Q10295; O13799: SPAC17H9.02; NbExp=2; IntAct=EBI-7997221, EBI-8993901;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889}.
CC   -!- SIMILARITY: Belongs to the poly(A) polymerase family. {ECO:0000305}.
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DR   EMBL; X79705; CAA56141.1; -; mRNA.
DR   EMBL; CU329671; CAA22808.1; -; Genomic_DNA.
DR   EMBL; AB027883; BAA87187.1; -; Genomic_DNA.
DR   PIR; JC6058; JC6058.
DR   RefSeq; NP_595362.1; NM_001021270.2.
DR   PDB; 7Q72; X-ray; 2.80 A; A/B=1-566.
DR   PDB; 7Q73; X-ray; 1.90 A; A=1-566.
DR   PDB; 7Q74; X-ray; 2.60 A; A/B=1-542.
DR   PDBsum; 7Q72; -.
DR   PDBsum; 7Q73; -.
DR   PDBsum; 7Q74; -.
DR   AlphaFoldDB; Q10295; -.
DR   SASBDB; Q10295; -.
DR   SMR; Q10295; -.
DR   BioGRID; 277614; 14.
DR   IntAct; Q10295; 5.
DR   MINT; Q10295; -.
DR   STRING; 284812.Q10295; -.
DR   iPTMnet; Q10295; -.
DR   MaxQB; Q10295; -.
DR   PaxDb; 4896-SPBC646-04-1; -.
DR   EnsemblFungi; SPBC646.04.1; SPBC646.04.1:pep; SPBC646.04.
DR   GeneID; 2541099; -.
DR   KEGG; spo:SPBC646.04; -.
DR   PomBase; SPBC646.04; pla1.
DR   VEuPathDB; FungiDB:SPBC646.04; -.
DR   eggNOG; KOG2245; Eukaryota.
DR   HOGENOM; CLU_011511_4_1_1; -.
DR   InParanoid; Q10295; -.
DR   OMA; PAYPAMC; -.
DR   PhylomeDB; Q10295; -.
DR   PRO; PR:Q10295; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; IDA:PomBase.
DR   GO; GO:0033620; C:Mei2 nuclear dot complex; IDA:PomBase.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IGI:PomBase.
DR   GO; GO:1990251; C:nuclear exosome focus; IDA:PomBase.
DR   GO; GO:0005654; C:nucleoplasm; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; 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:1990817; F:poly(A) RNA polymerase activity; IDA:PomBase.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0180010; P:co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway; IC:PomBase.
DR   GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR   GO; GO:0033621; P:nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts; IMP:PomBase.
DR   CDD; cd05402; NT_PAP_TUTase; 1.
DR   Gene3D; 1.10.1410.10; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 3.30.70.590; Poly(A) polymerase predicted RNA binding domain; 1.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR011068; NuclTrfase_I-like_C.
DR   InterPro; IPR007012; PolA_pol_cen_dom.
DR   InterPro; IPR048840; PolA_pol_NTPase.
DR   InterPro; IPR007010; PolA_pol_RNA-bd_dom.
DR   InterPro; IPR014492; PolyA_polymerase.
DR   PANTHER; PTHR10682; POLY A POLYMERASE; 1.
DR   PANTHER; PTHR10682:SF10; POLYNUCLEOTIDE ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF04928; PAP_central; 1.
DR   Pfam; PF20750; PAP_NTPase; 1.
DR   Pfam; PF04926; PAP_RNA-bind; 1.
DR   PIRSF; PIRSF018425; PolyA_polymerase; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF55003; PAP/Archaeal CCA-adding enzyme, C-terminal domain; 1.
DR   SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Magnesium; Manganese; Metal-binding;
KW   mRNA processing; Nucleotide-binding; Nucleus; Reference proteome;
KW   RNA-binding; Transferase.
FT   CHAIN           1..566
FT                   /note="Poly(A) polymerase pla1"
FT                   /id="PRO_0000051620"
FT   REGION          437..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        437..461
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..557
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         86..88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         99..101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         232..233
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            144
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            313
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            314
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            385
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   SITE            500
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250"
FT   STRAND          7..9
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   HELIX           19..34
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   HELIX           41..68
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   HELIX           73..78
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   STRAND          82..86
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   HELIX           87..91
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   STRAND          100..106
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   HELIX           112..117
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   HELIX           119..124
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   STRAND          129..135
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   STRAND          138..140
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   STRAND          142..147
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   STRAND          150..158
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   STRAND          160..162
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   HELIX           173..176
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   HELIX           181..199
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   HELIX           203..219
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   HELIX           225..227
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   HELIX           232..245
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   HELIX           251..263
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   TURN            288..290
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   HELIX           292..295
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   STRAND          304..307
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   TURN            311..314
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   HELIX           317..338
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   HELIX           344..348
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   HELIX           353..356
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   STRAND          358..369
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   HELIX           370..382
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   HELIX           384..393
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   STRAND          397..402
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   STRAND          407..415
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   HELIX           416..423
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   STRAND          432..435
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   HELIX           437..446
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   STRAND          468..481
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   STRAND          491..493
FT                   /evidence="ECO:0007829|PDB:7Q72"
FT   HELIX           495..505
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   TURN            513..515
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   STRAND          516..524
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   HELIX           525..527
FT                   /evidence="ECO:0007829|PDB:7Q73"
FT   HELIX           530..532
FT                   /evidence="ECO:0007829|PDB:7Q73"
SQ   SEQUENCE   566 AA;  64109 MW;  E8E0E4165AAFD3D5 CRC64;
     MTTKQWGITP PISTAPATEQ ENALNTALIN ELKNQNLFES PAESEKRVKV LDELQQITTE
     FVKKVSLAKH MNEKMANEAG GKIFTYGSYR LGVYGPGSDI DTLVVVPKHV SRDNFFQDLE
     PMLREREEVT DLAAVPDAYV PIIKFKFLGI SIDLIFARLS VPRVPRDLEL SDNNLLKGVE
     ERCVLSLNGT RVTDQILQLV PNRAVFKHAL RAIKFWAQRR AIYANVVGFP GGVAWAMMVA
     RICQLYPNAV SSVIVAKFFR ILHQWNWPQP ILLKPIEDGP LQVRIWNPKL YPSDKAHRMP
     IITPAYPSMC ATHNITLSTQ TIILREMVRA GEIADQIMVK ALPWSALFQK HDFFHRYKHY
     LTITAAAKTA EAQLKWAGLV ESKLRHLVTR LELVDAIALA HPFNKGFDKV YNCSSEEEAQ
     QVASGVTLEV AYESTDHEKL ANDTVNEEKA DNTESKADGS ENGEKQIFPV YTTTCYIGLE
     LEKKKGHPIK RLDISWPTQE FYELCKKWDK YDDTLMNVFI KNTKNTALPD EVFEPGEERP
     KATKKRSTAD TAHSTEQLKR QKVSTA
//