PAP1_CWPXB
ID PAP1_CWPXB Reviewed; 479 AA.
AC Q8QMZ9;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 29-SEP-2021, entry version 64.
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=CPXV067;
OS Cowpox virus (strain Brighton Red) (CPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX NCBI_TaxID=265872;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH NCBI_TaxID=29092; Microtus agrestis (Short-tailed field vole).
OH NCBI_TaxID=10090; Mus musculus (Mouse).
OH NCBI_TaxID=447135; Myodes glareolus (Bank vole) (Clethrionomys glareolus).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dietrich F.S., Ray C.A., Sharma D.A., Allen A., Pickup D.J.;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
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; AF482758; AAM13512.1; -; Genomic_DNA.
DR RefSeq; NP_619854.1; NC_003663.2.
DR SMR; Q8QMZ9; -.
DR GeneID; 1485943; -.
DR KEGG; vg:1485943; -.
DR Proteomes; UP000152733; 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; Transcription;
KW Transferase.
FT CHAIN 1..479
FT /note="Poly(A) polymerase catalytic subunit"
FT /id="PRO_0000308927"
FT ACT_SITE 202
FT /evidence="ECO:0000250"
FT ACT_SITE 204
FT /evidence="ECO:0000250"
SQ SEQUENCE 479 AA; 55519 MW; 7C7CB8EC113620A0 CRC64;
MNRNPDQNTL PNITLKIIET YLGRIPSVNE YHMLKLQARN IQKITVFNKD IFVSLVKKNK
KRFFSDVDTS ASEIKDRILS YFSKQTQTYN IGKLFTIIEL QSVLVTTYTD ILGVLTIKAP
NVISSKISYN VTSMEELARD MLNSMNVAVI DKAKVMGRHN VSSLVKNVNK LMEEYLRRHN
KSCICYGSYS LYLINPNIRY GDIDILQTNS RTFLIDLAFL IKFITGNNII LSKIPYLRNY
MVIKDENDNH IIDSFNIRQD TMNVVPKIFI DNIYIVDPTF QLLNMIKMFS QIDRLEDLSK
DPEKFNARMA TMLEYVRYTH GIVFDGTRNN MPMKCIIDEN NRIVTVTTKD YFSFKKCLVY
LDENVLSSDI LDLNADTSCD FESVTNSVYL IHDNIMYTYF SNTILLSDKG KVHEISARGL
CAHILLYQML TSGEYKQCLS DLLNSMMNRD KIPIYSHTER DKKPGRHGFI NIEKDIIVF
