ID   PAP1_YMTV5              Reviewed;         470 AA.
AC   Q6TUY0;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   29-SEP-2021, entry version 64.
DE   RecName: Full=Poly(A) polymerase catalytic subunit;
DE            EC=2.7.7.19;
DE   AltName: Full=Poly(A) polymerase large subunit;
DE            Short=PAP-L;
GN   Name=PAPL; OrderedLocusNames=32L;
OS   Yaba monkey tumor virus (strain VR587) (YMTV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Yatapoxvirus.
OX   NCBI_TaxID=928314;
OH   NCBI_TaxID=9538; Erythrocebus patas (Red guenon) (Cercopithecus patas).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9539; Macaca (macaques).
OH   NCBI_TaxID=9557; Papio hamadryas (Hamadryas baboon).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14645589; DOI=10.1128/jvi.77.24.13335-13347.2003;
RA   Brunetti C.R., Amano H., Ueda Y., Qin J., Miyamura T., Suzuki T., Li X.,
RA   Barrett J.W., McFadden G.;
RT   "Complete genomic sequence and comparative analysis of the tumorigenic
RT   poxvirus Yaba monkey tumor virus.";
RL   J. Virol. 77:13335-13347(2003).
CC   -!- FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's.
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: Heterodimer of a large (catalytic) subunit and a small
CC       (regulatory) subunit. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the poxviridae poly(A) polymerase catalytic
CC       subunit family. {ECO:0000305}.
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DR   EMBL; AY386371; AAR07389.1; -; Genomic_DNA.
DR   RefSeq; NP_938288.1; NC_005179.1.
DR   SMR; Q6TUY0; -.
DR   GeneID; 2943665; -.
DR   KEGG; vg:2943665; -.
DR   Proteomes; UP000008596; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1270.320; -; 1.
DR   Gene3D; 3.30.460.60; -; 1.
DR   InterPro; IPR037265; PolyA_pol_cat_sf.
DR   InterPro; IPR024231; Pox_polyA_pol_nucTrfase.
DR   InterPro; IPR038419; Pox_polyA_pol_nucTrfase_sf.
DR   InterPro; IPR004976; Poxviridae_polyA_pol_cat.
DR   InterPro; IPR024397; Poxvirus_polyA_pol_cat_C.
DR   InterPro; IPR024398; Poxvirus_polyA_pol_cat_N.
DR   InterPro; IPR038337; Poxvirus_polyA_pol_cat_N_sf.
DR   Pfam; PF03296; Pox_polyA_pol; 1.
DR   Pfam; PF12629; Pox_polyA_pol_C; 1.
DR   Pfam; PF12630; Pox_polyA_pol_N; 1.
DR   PIRSF; PIRSF015693; VAC-48L_nuct; 1.
DR   SUPFAM; SSF160957; SSF160957; 1.
PE   3: Inferred from homology;
KW   ATP-binding; mRNA processing; Nucleotide-binding; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..470
FT                   /note="Poly(A) polymerase catalytic subunit"
FT                   /id="PRO_0000308942"
FT   ACT_SITE        192
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        194
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   470 AA;  54614 MW;  523D828081B1669B CRC64;
     MNNSITLTLK NYLGRMPTVN EYYMLKSQVR NIQKIMFFNK DIFISLIKKN KKKFFYEIKS
     SPSEMRLHIL EYFMKQQKTS SIGKLYAIIE LQTILVSTYT DVLGVLTTKA PYVFPSNVRY
     EPRSMKKIAH DILTTINVAT VSEKVMGRHN VSELVTNVNL LMEEYLRRHN KSCICYGSYS
     LYLLNPSIEY GDIDIMQTNS RIFLINLAFL IKFITGHNVM LLKVPYLKNY MVLRDDEDKH
     IIDSFNVRQD TMHSIPKILI DNIYIVDPTF QLLSMIKMFS QVDRLEDLAR NQEKATIKLA
     TLLEYVRVKH GIIFNGKVTN MPMPSSFDHE KRIITVDTSR YNFSFKKCFV YLDENSLSSD
     ILNLNADDAI DFENVSNSVF LINDEIMYTY FSNTILMSSK DEIHEISARG VSAHILMYQI
     LTDGDYLIPL SDIVNSLMFK EKIPIFSIIP RDKKTGKHGI INIEKDIITH