PAP_SCHPO
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 03-AUG-2022, entry version 141.
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 AlphaFoldDB; Q10295; -.
DR SMR; Q10295; -.
DR BioGRID; 277614; 14.
DR IntAct; Q10295; 5.
DR MINT; Q10295; -.
DR STRING; 4896.SPBC646.04.1; -.
DR iPTMnet; Q10295; -.
DR MaxQB; Q10295; -.
DR PaxDb; Q10295; -.
DR PRIDE; Q10295; -.
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 Reactome; R-SPO-72187; mRNA 3'-end processing.
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:0004652; F:polynucleotide adenylyltransferase activity; IGI:PomBase.
DR GO; GO:1990817; F:RNA adenylyltransferase activity; IDA:PomBase.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; EXP:PomBase.
DR GO; GO:0006378; P:mRNA polyadenylation; IDA:PomBase.
DR GO; GO:0033621; P:nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts; IMP:PomBase.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR011068; NuclTrfase_I-like_C.
DR InterPro; IPR007012; PolA_pol_cen_dom.
DR InterPro; IPR007010; PolA_pol_RNA-bd_dom.
DR InterPro; IPR014492; PolyA_polymerase.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF04928; PAP_central; 1.
DR Pfam; PF04926; PAP_RNA-bind; 1.
DR PIRSF; PIRSF018425; PolyA_polymerase; 1.
DR SUPFAM; SSF55003; SSF55003; 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..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"
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
