PAP1_ASFP4
ID PAP1_ASFP4 Reviewed; 475 AA.
AC P0C9D3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Putative poly(A) polymerase catalytic subunit {ECO:0000250|UniProtKB:Q65159};
DE EC=2.7.7.19;
GN OrderedLocusNames=Pret-079;
OS African swine fever virus (isolate Tick/South Africa/Pretoriuskop Pr4/1996)
OS (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=561443;
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}.
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; AY261363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0C9D3; -.
DR Proteomes; UP000000859; 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_0000373149"
SQ SEQUENCE 475 AA; 54736 MW; 549043CF8995E2CC CRC64;
MSSLLKTDFN VSKYRLIAQK REANAVEIEA ALEVVREFII KKKLILYGGI AIDYALHLKG
SSIYPEGERP DFDMFSPNHV EDAYELADIL YEKGFKQVGT VRAIHVQTMR VRTDFVWVAD
LSYMPPNIFD TIPTLTYKNL KIIHPDYQRA GLHLAFCFPF DNPPREDVFS RFKKDLQRYN
LIEKYYPIPV VPVKSTYESK TFSIPFKQVA IHGFAAYALL YQTLNELRIT CKVPEWKTEF
PQPSYSYHKN DKNITLTVDM PRAYPALVLA TYNPEGVIKE MGLHLTEICE PYMDYSPPIF
KTNDIHFFST MFKELAISII QDNLIVVSPQ YLLLYFLYGA FATPADKSLF LFYYNATLWI
LEKADSLLNI IQKQTSPEEF TRFANTSPFV LTTRVLSCSQ ERCTFSPAYR ISLANDVQQS
QLPLPKTHFL SNSLPDISTL PYNYYPGKGK EKPTNFNYEK NLLFNIGGKC TPSAM