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
//