PAPO3_XENLA
ID PAPO3_XENLA Reviewed; 400 AA.
AC P51006; Q91602;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Poly(A) polymerase type 3;
DE Short=PAP;
DE EC=2.7.7.19;
DE AltName: Full=Polynucleotide adenylyltransferase;
DE Flags: Fragment;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=7489490;
RA Ballantyne S., Bilger A., Astrom J., Virtanen A., Wickens M.;
RT "Poly(A) polymerases in the nucleus and cytoplasm of frog oocytes: dynamic
RT changes during oocyte maturation and early development.";
RL RNA 1:64-78(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-394.
RC TISSUE=Ovary;
RX PubMed=7862135; DOI=10.1128/mcb.15.3.1422;
RA Gebauer F., Richter J.D.;
RT "Cloning and characterization of a Xenopus poly(A) polymerase.";
RL Mol. Cell. Biol. 15:1422-1430(1995).
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 (CPSF).
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 -!- 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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the poly(A) polymerase family. {ECO:0000305}.
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DR EMBL; U19975; AAC59747.1; -; mRNA.
DR EMBL; U23456; AAA64708.1; -; mRNA.
DR PIR; I51681; I51681.
DR AlphaFoldDB; P51006; -.
DR SMR; P51006; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043631; P:RNA polyadenylation; IEA:InterPro.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR007012; PolA_pol_cen_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 PIRSF; PIRSF018425; PolyA_polymerase; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Magnesium; Manganese; Metal-binding; mRNA processing;
KW Nucleotide-binding; Nucleus; Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..>400
FT /note="Poly(A) polymerase type 3"
FT /id="PRO_0000051616"
FT MOTIF 382..390
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT BINDING 97..99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 110..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 243..244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 61
FT /note="S -> I (in Ref. 2; AAA64708)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="L -> F (in Ref. 2; AAA64708)"
FT /evidence="ECO:0000305"
FT NON_TER 400
SQ SEQUENCE 400 AA; 46020 MW; AB4347C074E60CA3 CRC64;
MPFPLASQGS QQSQKTYGIT SPISLATPKD TDCTLTQKLI ETLKPYGVFE EEDELQHRIL
SLGKLNNLVK EWIREISELK NLPQSVIENV GGKIFTFGSY RLGVHTKGAD IDALCVAPRH
VDRSDLFSSF YEKLKQQEEV KDLRSVEEAF VPVIKLCFDG IEIDILFARL ALQTIPEDLD
LRDDSLLKNL DIRCIRSLNG CRVTDEILHL VPNIDSFRLT LRAIKLWAKR HNIYSNILGF
LGGVSWAMLV ARTCQLYPNA IASTLVHKFF LVFSKWEWPN PVLLKQPEEC NLNLPVWDPR
VNPSDRYHLM PIITPAYPQQ NSTYNVSVST RAVMVEEFKQ GLAITDEILL LKAEWSKLFD
APNFFQKYKY VFYNLLAMFA WGEIINKNKK RCYTLKKKKK
