ID   PAP1_CWPXB              Reviewed;         479 AA.
AC   Q8QMZ9;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-NOV-2023, entry version 71.
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=OPG063; Synonyms=PAPL; OrderedLocusNames=CPXV067;
OS   Cowpox virus (strain Brighton Red) (CPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Cowpox virus.
OX   NCBI_TaxID=265872;
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   Dietrich F.S., Ray C.A., Sharma D.A., Allen A., Pickup D.J.;
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's.
CC       {ECO:0000250|UniProtKB:P23371}.
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         Evidence={ECO:0000250|UniProtKB:P23371};
CC   -!- SUBUNIT: Heterodimer of a large (catalytic) subunit and a small
CC       (regulatory) subunit. {ECO:0000250|UniProtKB:P23371}.
CC   -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC       {ECO:0000250|UniProtKB:P23371}.
CC   -!- SIMILARITY: Belongs to the poxviridae poly(A) polymerase catalytic
CC       subunit family. {ECO:0000305}.
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DR   EMBL; AF482758; AAM13512.1; -; Genomic_DNA.
DR   RefSeq; NP_619854.1; NC_003663.2.
DR   SMR; Q8QMZ9; -.
DR   GeneID; 1485943; -.
DR   KEGG; vg:1485943; -.
DR   Proteomes; UP000152733; Segment.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1990817; F:poly(A) RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd20919; polyA_pol_Pox; 1.
DR   Gene3D; 1.20.1270.320; Poxvirus poly(A) polymerase, N domain; 1.
DR   Gene3D; 3.30.460.60; Poxvirus poly(A) polymerase, nucleotidyltransferase domain; 1.
DR   InterPro; IPR004976; PolyA_pol_cat_Poxvir.
DR   InterPro; IPR037265; PolyA_pol_cat_sf.
DR   InterPro; IPR024231; PolyA_pol_nucTrfase_Poxvir.
DR   InterPro; IPR038419; PolyA_pol_nucTrfase_sf_Poxvir.
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; Poly(A) polymerase catalytic subunit-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Calcium; Early protein; Metal-binding; mRNA processing;
KW   Nucleotide-binding; Transcription; Transferase.
FT   CHAIN           1..479
FT                   /note="Poly(A) polymerase catalytic subunit"
FT                   /id="PRO_0000308927"
FT   ACT_SITE        202
FT                   /evidence="ECO:0000255|PIRSR:PIRSR015693-50"
FT   ACT_SITE        204
FT                   /evidence="ECO:0000255|PIRSR:PIRSR015693-50"
FT   BINDING         202
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P23371"
FT   BINDING         202
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P23371"
FT   BINDING         204
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P23371"
FT   BINDING         204
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P23371"
FT   BINDING         253
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P23371"
SQ   SEQUENCE   479 AA;  55519 MW;  7C7CB8EC113620A0 CRC64;
     MNRNPDQNTL PNITLKIIET YLGRIPSVNE 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 GIVFDGTRNN MPMKCIIDEN NRIVTVTTKD YFSFKKCLVY
     LDENVLSSDI LDLNADTSCD FESVTNSVYL IHDNIMYTYF SNTILLSDKG KVHEISARGL
     CAHILLYQML TSGEYKQCLS DLLNSMMNRD KIPIYSHTER DKKPGRHGFI NIEKDIIVF
//