A20_VACCW
ID A20_VACCW Reviewed; 426 AA.
AC P68710; O57228; Q80HV4;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 02-JUN-2021, entry version 34.
DE RecName: Full=DNA polymerase processivity factor component A20;
GN OrderedLocusNames=VACWR141; ORFNames=A20R;
OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS WR)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10254;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA Wohlhueter R.;
RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT redundancy and an error rate of 0.16/10kb.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND INTERACTION WITH PROTEIN E9.
RX PubMed=11711620; DOI=10.1128/jvi.75.24.12298-12307.2001;
RA Klemperer N., McDonald W., Boyle K., Unger B., Traktman P.;
RT "The A20R protein is a stoichiometric component of the processive form of
RT vaccinia virus DNA polymerase.";
RL J. Virol. 75:12298-12307(2001).
RN [3]
RP FUNCTION, AND INTERACTION WITH PROTEIN UDG/D4.
RX PubMed=16326701; DOI=10.1074/jbc.m511239200;
RA Stanitsa E.S., Arps L., Traktman P.;
RT "Vaccinia virus uracil DNA glycosylase interacts with the A20 protein to
RT form a heterodimeric processivity factor for the viral DNA polymerase.";
RL J. Biol. Chem. 281:3439-3451(2006).
RN [4]
RP INTERACTION WITH D5.
RX PubMed=12490386; DOI=10.1006/viro.2002.1721;
RA Ishii K., Moss B.;
RT "Mapping interaction sites of the A20R protein component of the vaccinia
RT virus DNA replication complex.";
RL Virology 303:232-239(2002).
RN [5]
RP IDENTIFICATION IN A COMPLEX WITH UDG/D4 AND THE DNA POLYMERASE.
RX PubMed=21572084; DOI=10.1074/jbc.m111.222216;
RA Boyle K.A., Stanitsa E.S., Greseth M.D., Lindgren J.K., Traktman P.;
RT "Evaluation of the role of the vaccinia virus uracil DNA glycosylase and
RT A20 proteins as intrinsic components of the DNA polymerase holoenzyme.";
RL J. Biol. Chem. 286:24702-24713(2011).
CC -!- FUNCTION: Plays an essential role in viral DNA replication by acting as
CC the polymerase processivity factor together with protein D4. May serve
CC as a bridge which links the DNA polymerase E9 and the uracil DNA
CC glycosylase. {ECO:0000269|PubMed:11711620,
CC ECO:0000269|PubMed:16326701}.
CC -!- SUBUNIT: Interacts with the DNA polymerase catalytic subunit E9.
CC Interacts with UDG. Component of the Uracil-DNA glycosylase(UDG)-A20-
CC polymerase complex; A20 and UDG form a heterodimeric processivity
CC factor that associates with E9 to form the processive polymerase
CC holoenzyme. Interacts with D5. {ECO:0000269|PubMed:11711620,
CC ECO:0000269|PubMed:12490386, ECO:0000269|PubMed:16326701,
CC ECO:0000269|PubMed:21572084}.
CC -!- SIMILARITY: Belongs to the poxviruses A20 family. {ECO:0000305}.
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DR EMBL; AY243312; AAO89420.1; -; Genomic_DNA.
DR RefSeq; YP_233023.1; NC_006998.1.
DR SMR; P68710; -.
DR DNASU; 3707671; -.
DR GeneID; 3707671; -.
DR KEGG; vg:3707671; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR InterPro; IPR010267; Chordopox_A20R.
DR Pfam; PF05941; Chordopox_A20R; 1.
PE 1: Evidence at protein level;
KW DNA replication; Reference proteome.
FT CHAIN 1..426
FT /note="DNA polymerase processivity factor component A20"
FT /id="PRO_0000099268"
SQ SEQUENCE 426 AA; 49074 MW; 650D8EE38CC76A78 CRC64;
MTSSADLTNL KELLSLYKSL KFSDSAAIEK YNSLVEWGTS TYWKIGVQKV ANVETSISDY
YDEVKNKPFN IDPGYYIFLP VYFGSVFIYS KGKNMVELGS GNSFQIPDDM RSACNKVLDS
DNGIDFLRFV LLNNRWIMED AISKYQSPVN IFKLASEYGL NIPKYLEIEI EEDTLFDDEL
YSIIERSFDD KFPKISISYI KLGELRRQVV DFFKFSFMYI ESIKVDRIGD NIFIPSVITK
SGKKILVKDV DHLIRSKVRE HTFVKVKKKN TFSILYDYDG NGTETRGEVI KRIIDTIGRD
YYVNGKYFSK VGSAGLKQLT NKLDINECAT VDELVDEINK SGTVKRKIKN QSAFDLSREC
LGYPEADFIT LVNNMRFKIE NCKVVNFNIE NTNCLNNPSI ETIYGNFNQF VSIFNIVTDV
KKRLFE