ID   PAP1_CPRVZ              Reviewed;         473 AA.
AC   Q070J7;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 60.
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=CRV054;
OS   Nile crocodilepox virus (isolate Crocodylus niloticus/Zimbabwe/Ume/2001)
OS   (CRV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Crocodylidpoxvirus.
OX   NCBI_TaxID=1289473;
OH   NCBI_TaxID=184234; Crocodylus johnsoni (Australian freshwater crocodile).
OH   NCBI_TaxID=8501; Crocodylus niloticus (Nile crocodile) (African crocodile).
OH   NCBI_TaxID=8502; Crocodylus porosus (Saltwater crocodile) (Estuarine crocodile).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641289; DOI=10.1128/jvi.80.10.4978-4991.2006;
RA   Afonso C.L., Tulman E.R., Delhon G., Lu Z., Viljoen G.J., Wallace D.B.,
RA   Kutish G.F., Rock D.L.;
RT   "Genome of crocodilepox virus.";
RL   J. Virol. 80:4978-4991(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; DQ356948; ABJ08945.1; -; Genomic_DNA.
DR   RefSeq; YP_784244.1; NC_008030.1.
DR   SMR; Q070J7; -.
DR   PRIDE; Q070J7; -.
DR   GeneID; 4363317; -.
DR   KEGG; vg:4363317; -.
DR   Proteomes; UP000011300; 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..473
FT                   /note="Poly(A) polymerase catalytic subunit"
FT                   /id="PRO_0000308929"
FT   ACT_SITE        193
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        195
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   473 AA;  54062 MW;  2145D9F31671CCA1 CRC64;
     MNNRELINRY LGKTADQPIY YALFHKVGKI KQILNFDLNV FLKLLLKNRD RFLRENKQPT
     AEIKRRLTHY FTKQHRVRKV GKILSIVEFQ HVIVTTFTRV LGVLTIDNRR VSKMYSSTAI
     LDYAAHEDYV EAMLRSYRVT DGAGPPKGRN KVSDLVGYVI SMLKEYLKRH NKSAFCHGSY
     SLHLLNPAIE YGDIDMLQTN SRTFLINLAF LIYCNTGRVT TMMKIPYLLN YIVMFDEEQA
     HIVDSFQVSQ EIFDRIPKIL INDIYIIDPC VQLLNGIKMF SQVDRLDDLH TKFEKLRARF
     CTLLEYVLYD YDMRIGEGSG AGALRRSRFA YSERVATVEA GALGEDLSPA RWVAFMDNAA
     LDARIGASTR QAADFGPVTN SRFLEEDGCL YGYFSNTLLL TPDGAPHPVS CNALAAHFLM
     YFVMTGAPCK PQLACLLNSL VVPEAREFTL VPRDKKLGDH VILSIDHDVF IDF