ID   PAPO2_XENLA             Reviewed;         484 AA.
AC   P51005;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Poly(A) polymerase alpha-B;
DE            Short=PAP-alpha-B;
DE            EC=2.7.7.19;
DE   AltName: Full=Polynucleotide adenylyltransferase alpha-B;
GN   Name=papola-b;
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).
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   -!- 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; U19974; AAC59746.1; -; mRNA.
DR   AlphaFoldDB; P51005; -.
DR   SMR; P51005; -.
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: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:0031123; P:RNA 3'-end processing; IEA:InterPro.
DR   GO; GO:0043631; P:RNA polyadenylation; IEA:InterPro.
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   Pfam; PF04928; PAP_central; 1.
DR   Pfam; PF04926; PAP_RNA-bind; 1.
DR   PIRSF; PIRSF018425; PolyA_polymerase; 1.
DR   SUPFAM; SSF55003; SSF55003; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; mRNA processing; Nucleotide-binding; Nucleus;
KW   Reference proteome; RNA-binding; Transferase.
FT   CHAIN           1..484
FT                   /note="Poly(A) polymerase alpha-B"
FT                   /id="PRO_0000051615"
FT   REGION          276..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          326..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           240..257
FT                   /note="Nuclear localization signal 1"
FT                   /evidence="ECO:0000250"
FT   MOTIF           392..407
FT                   /note="Nuclear localization signal 2"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        375..397
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..440
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   484 AA;  53830 MW;  D81361CF0D79B879 CRC64;
     MLVARTCQLY PNAIASTLVH KFFLVFSKWE WPNPVLLKQP EECNLNLPVW DPRVNPSDRY
     HLMPIITPAY PQQNSTYNVS VSTRAVMVEE FKQGLAITDE ILLVKAEWSK LFDAPNFFQK
     YKHYILLLAS APTEKQRLEW VGLVESKIRI LVGSLEKNEF ITLAHVNPQS FPSPSENSEK
     EEFRTMWVIG LVFKKMENSE NLSVDLTYDI QSFTDTVYRQ AINSKMFETE IKIAAMHVKR
     KQLHQLLPSH VLPKKKKHSV EGVKLVSLND SSIDLSVDSD NSMSVPSPTN ATRTSPLNST
     GLSQGNSPAT PVSLSVTNTQ ATDVMVPQNN STENSGGSLN ESIPETATHP AFSSTPRPLV
     TRVVSSMPLV NQVQKPVTNT VTKMPSPVAG VKRTSSPTNE ESPKKTKTEE DENDSSNSTE
     VDEQNKLEPE ELKEVHSEEK SSSPVPGALP SSQRSSSTDL SDISVLPATP IPVIKNSIKL
     RLNR