ID   PAP1_CWPXG              Reviewed;         479 AA.
AC   Q80E12;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   29-SEP-2021, entry version 50.
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; ORFNames=F1L;
OS   Cowpox virus (strain GRI-90 / Grishak) (CPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=265871;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH   NCBI_TaxID=29092; Microtus agrestis (Short-tailed field vole).
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
OH   NCBI_TaxID=447135; Myodes glareolus (Bank vole) (Clethrionomys glareolus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Shchelkunov S.N., Safronov P.F., Totmenin A.V., Miheev M.V.,
RA   Ryazankina O.I., Petrov N.A., Gutorov V.V., Kotwal G.J., Sandakhchiev L.S.;
RT   "Structure-function and organization of cowpox virus strain GRI-90 complete
RT   genome.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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; X94355; CAD90606.1; -; Genomic_DNA.
DR   SMR; Q80E12; -.
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_0000308928"
FT   ACT_SITE        202
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        204
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   479 AA;  55532 MW;  79FE3A151EC51A77 CRC64;
     MNRNPDQNTL PNITLKIIET YLGRVPSVNE YHMLKLQARN IQKITVFNKD IFVSLVKKNK
     KRFFSDVDTS ASEIKDRILS YFSKQTQTYN IGKLFTIIEL QSVLVTTYTD ILGVLTIKAP
     NVISSKISYN VTSMEELARD MLNSMNVAVI DKAKVMGRHN VSSLVKNVNK LMEEYLRRHN
     KSCICYGSYS LYLINPNIRY 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