ID   PAP1_VACCC              Reviewed;         479 AA.
AC   P21079;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   27-MAR-2024, entry version 93.
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;
DE   AltName: Full=VP55;
GN   Name=OPG063; Synonyms=PAPL; ORFNames=E1L;
OS   Vaccinia virus (strain Copenhagen) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10249;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "The complete DNA sequence of vaccinia virus.";
RL   Virology 179:247-266(1990).
RN   [2]
RP   COMPLETE GENOME.
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL   Virology 179:517-563(1990).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M35027; AAA48038.1; -; Genomic_DNA.
DR   PIR; E42508; E42508.
DR   SMR; P21079; -.
DR   Proteomes; UP000008269; Genome.
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_0000099106"
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;  55580 MW;  50AC0C13698BECA7 CRC64;
     MNRNPDQNTF PNITLKIIET YLGRVPSVNE YHMLKLQARN IQKITVFNKD IFVSLVKKNK
     KRFFSDVDTS ASEIKDRILS YFSKQTQTYN IGKLFTIIEL QSVLVTTYTD ILGVLTIKAP
     NVISSKISYN VTSMEELARD MLNSMNVAII 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
//