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 08-NOV-2023, entry version 67.
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;
OC Nile crocodilepox virus.
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 GeneID; 4363317; -.
DR KEGG; vg:4363317; -.
DR Proteomes; UP000011300; Segment.
DR GO; GO:0005524; F:ATP 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; 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
//
