ID   PAP1_HSPV               Reviewed;         479 AA.
AC   Q0GP30;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   29-SEP-2021, entry version 46.
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=HSPV058;
OS   Horsepox virus (HSPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=397342;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=9796; Equus caballus (Horse).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MNR-76;
RX   PubMed=16940536; DOI=10.1128/jvi.00945-06;
RA   Tulman E.R., Delhon G., Afonso C.L., Lu Z., Zsak L., Sandybaev N.T.,
RA   Kerembekova U.Z., Zaitsev V.L., Kutish G.F., Rock D.L.;
RT   "Genome of horsepox virus.";
RL   J. Virol. 80:9244-9258(2006).
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; DQ792504; ABH08161.1; -; Genomic_DNA.
DR   SMR; Q0GP30; -.
DR   Proteomes; UP000111173; 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; Transcription;
KW   Transferase.
FT   CHAIN           1..479
FT                   /note="Poly(A) polymerase catalytic subunit"
FT                   /id="PRO_0000308933"
FT   ACT_SITE        202
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        204
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   479 AA;  55566 MW;  BEE615306F051AF5 CRC64;
     MNRNPDQNTF PNITLKIIET YLSRVPSVNE YHMLKLQARN IQKITVFNKD IFVSLVKKNK
     KRFFSDVNTS ASEIKDRILS YFSKQTQTYN IGKLFTIIEL QSVLVTTYTD ILGVLTIKAP
     NVISSKISYN VTSMEELARD MLNSMNVAII DKAKVMGRHN VSSLVKNVNK LMEEYLRRHN
     KSCICYGSYS LYLINPNILY GDIDILQTNS RTFLIDLAFL IKFITGNNII LSKIPYLRNY
     MVIKDENDNH IIDSFNIRQD TMNVVPKIFI DNIYIVDPTF QLLNMIKMFS QIDRLEDLSK
     DPEKFNARMA TMLEYVRYTH GIVFDGKRNN MPMKCIIDEN NRIVTVTTKD YFSFKKCLVY
     LDENVLSSDI LDLNADTSCD FESVTNSVYL IHDNIMYTYF SNTILLSDKG KVHEISARGL
     CAHILLYQML TSGEYKQCLS DLLNSMMNRD KIPIYSHTER DKKPGRHGFI NIEKDIIVF