ID PAP1_DPV83 Reviewed; 470 AA. AC Q08FW1; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 1. DT 08-NOV-2023, entry version 63. 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=DpV83gp040; OS Deerpox virus (strain Mule deer/United States/W-848-83/1983) (DPV). OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes; OC Chitovirales; Poxviridae; Chordopoxvirinae; Cervidpoxvirus; OC Mule deerpox virus. OX NCBI_TaxID=305674; OH NCBI_TaxID=9872; Odocoileus hemionus (Mule deer) (Cervus hemionus). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15613325; DOI=10.1128/jvi.79.2.966-977.2005; RA Afonso C.L., Delhon G., Tulman E.R., Lu Z., Zsak A., Becerra V.M., Zsak L., RA Kutish G.F., Rock D.L.; RT "Genome of deerpox virus."; RL J. Virol. 79:966-977(2005). 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}. 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; AY689436; ABI99196.1; -; Genomic_DNA. DR RefSeq; YP_227416.1; NC_006966.1. DR SMR; Q08FW1; -. DR GeneID; 3346388; -. DR KEGG; vg:3346388; -. DR OrthoDB; 3428at10239; -. DR Proteomes; UP000000866; Genome. 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..470 FT /note="Poly(A) polymerase catalytic subunit" FT /id="PRO_0000308931" FT ACT_SITE 192 FT /evidence="ECO:0000250" FT ACT_SITE 194 FT /evidence="ECO:0000250" SQ SEQUENCE 470 AA; 54186 MW; D290C021F12E25C2 CRC64; MNRHISEILE KYLGRIPSLT EYHTLKSQYK NIHRVNIFNK DIFISLIKKN KKKFFSDIDT SVSEIKKLVF DYFTKQEQTY SIGKLYTIIE LQTILVTTYT DILGVLTTKG PDIFSSNVQY NTSSMQKIAN DALNSMNIAT ISDKVMGRHN VSSLVCNVNS LMEEYLRRHN KSCICYGSYS LHLLNPEIKY GDIDILQTNS RTFLIDLAFL IKFITGYNVI LLKVPYLKNY MVLKDQNDSH IIDSFNIRQE TMQHIPKILI DNIYIVDPTI QLLSMLKMLS QIDRLEDLAK NPDKLTIRFA TLLEYVRNKY GIILNGNSNN MPMPSTIDIK KRIITVDTKY YNFAYDKCYV YLDENSLSSD ILSLNADDAV DFENVSNSAF LVNDKTLYTY FSNTILLSGN DKIHEISSRG ISAHILIYQA LMKYDISIPL TDIVNSLIGR NKQPIYEIIP RDKKTGKHGI IDIEKDIITH //