PAP1_ASFK5
ID PAP1_ASFK5 Reviewed; 475 AA.
AC P0C9D5;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 23-FEB-2022, entry version 25.
DE RecName: Full=Putative poly(A) polymerase catalytic subunit {ECO:0000250|UniProtKB:Q65159};
DE EC=2.7.7.19;
GN OrderedLocusNames=Ken-079;
OS African swine fever virus (isolate Pig/Kenya/KEN-50/1950) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=561445;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kutish G.F., Rock D.L.;
RT "African swine fever virus genomes.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's.
CC {ECO:0000305}.
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 -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:Q65159}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the poxviridae poly(A) polymerase catalytic
CC subunit family. Highly divergent. {ECO:0000305}.
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DR EMBL; AY261360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0C9D5; -.
DR PRIDE; P0C9D5; -.
DR Proteomes; UP000000861; 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 InterPro; IPR045355; PolyA_pol_cat_su.
DR Pfam; PF19244; Poly_A_pol_cat; 1.
PE 3: Inferred from homology;
KW ATP-binding; Late protein; mRNA processing; Nucleotide-binding;
KW Transcription; Transferase; Virion.
FT CHAIN 1..475
FT /note="Putative poly(A) polymerase catalytic subunit"
FT /id="PRO_0000373151"
SQ SEQUENCE 475 AA; 54989 MW; A93A036D65150EC5 CRC64;
MSSLPKTDFN VPKYQLIAQK REANAAEIEA ALEVVREFII KKKLILYGGI AIDYALHLKG
SSIYPEGERP DFDMFSPNHV EDAYELADLL YEKGFKQVGT VRAIHVQTMR VRTDFVWVAD
LSYMPSNIFD TIPTLTYKNL KIIHPDYQRA GLHLAFCFPF DNPPREDVFS RFKKDLQRYN
LIEKYYPIPV VPVKSTYENK TFSIPFKRVA IHGFAAYALL YQTLNELRMT CKVPEWKTEF
PQPSYSYHKN DKNITLTVDM PKAYPSLVLA TYNPEEIIKE MGLHLTEICE PYMDYSPPIF
KTKDIHFFST MFKELAISMI QDNIIVVSPQ YLLLYFLYGA FATPADKALF LFYYNATLWI
LEKADSLLNI IQKQTSPEEF MKFANTSPFV LTTRVLRCSQ DRCTFSPAYR ISLANDVQQS
QLPLPKTHFL SNFLPDISTL PYNYYPGKGK DRPTNFSYEK NLLFNIGGKC TQLAM