ID   DPOL_VACCW              Reviewed;        1006 AA.
AC   P06856; Q76ZV6;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 5.
DT   29-SEP-2021, entry version 125.
DE   RecName: Full=DNA polymerase;
DE            EC=2.7.7.7;
DE   Includes:
DE     RecName: Full=3'-5' exodeoxyribonuclease;
DE              Short=3'-5' exonuclease;
DE              EC=3.1.11.-;
GN   Name=POL; OrderedLocusNames=VACWR065; ORFNames=E9L;
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 [GENOMIC DNA].
RX   PubMed=2398897; DOI=10.1128/mcb.10.10.5433-5441.1990;
RA   Ahn B.-Y., Gershon P.D., Jones E.V., Moss B.;
RT   "Identification of rpo30, a vaccinia virus RNA polymerase gene with
RT   structural similarity to a eucaryotic transcription elongation factor.";
RL   Mol. Cell. Biol. 10:5433-5441(1990).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 40-962.
RX   PubMed=3012524; DOI=10.1073/pnas.83.11.3659;
RA   Earl P.L., Jones E.V., Moss B.;
RT   "Homology between DNA polymerases of poxviruses, herpesviruses, and
RT   adenoviruses: nucleotide sequence of the vaccinia virus DNA polymerase
RT   gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:3659-3663(1986).
RN   [4]
RP   MUTANTS TS42; NG26 AND PAARVG.
RX   PubMed=2911123; DOI=10.1128/jvi.63.2.841-846.1989;
RA   Traktman P., Kelvin M., Pacheco S.;
RT   "Molecular genetic analysis of vaccinia virus DNA polymerase mutants.";
RL   J. Virol. 63:841-846(1989).
RN   [5]
RP   INTERACTION WITH A20.
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   [6]
RP   FUNCTION.
RX   PubMed=15843688; DOI=10.1093/nar/gki525;
RA   Hamilton M.D., Evans D.H.;
RT   "Enzymatic processing of replication and recombination intermediates by the
RT   vaccinia virus DNA polymerase.";
RL   Nucleic Acids Res. 33:2259-2268(2005).
RN   [7]
RP   IDENTIFICATION IN A COMPLEX WITH UDG/D4 AND A20.
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   [8]
RP   IDENTIFICATION IN A COMPLEX WITH D4 AND A20.
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: Catalyzes DNA synthesis. Acquires processivity by associating
CC       with a heterodimeric processivity factor comprised of the viral A20 and
CC       D4 proteins, thereby forming the DNA polymerase holoenzyme. Displays
CC       3'- to 5' exonuclease activity. Might participate in viral DNA
CC       recombination. Does not perform translesion synthesis across an abasic
CC       site. {ECO:0000269|PubMed:15843688}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC   -!- SUBUNIT: Interacts with A20. Component of the Uracil-DNA
CC       glycosylase(UDG)-A20-polymerase complex; A20 and UDG form a
CC       heterodimeric processivity factor that associates with E9 to form the
CC       processive polymerase holoenzyme. {ECO:0000269|PubMed:11711620,
CC       ECO:0000269|PubMed:16326701, ECO:0000269|PubMed:21572084}.
CC   -!- INTERACTION:
CC       P06856; Q49PH7: A20R; Xeno; NbExp=3; IntAct=EBI-984665, EBI-8039061;
CC   -!- MISCELLANEOUS: Ts42 is a temperature-sensitive mutant. PAArVg is a
CC       mutant resistant to the drug phosphonoacetic acid (PAA). NG26 is a
CC       double mutant with a temperature-sensitive lesion and a mutation
CC       rendering the virus resistant to PAA.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA98419.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAA98419.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M36339; AAB59829.1; -; Genomic_DNA.
DR   EMBL; AY243312; AAO89344.1; -; Genomic_DNA.
DR   EMBL; M13213; AAA98419.1; ALT_SEQ; Genomic_DNA.
DR   PIR; A24878; A24878.
DR   PIR; A25270; DJVZZW.
DR   SMR; P06856; -.
DR   IntAct; P06856; 2.
DR   MINT; P06856; -.
DR   BindingDB; P06856; -.
DR   ChEMBL; CHEMBL3988586; -.
DR   Proteomes; UP000000344; Genome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0039693; P:viral DNA genome replication; IDA:UniProtKB.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.90.1600.10; -; 2.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR   InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR013617; DNA-dir_DNA_pol_B_vir_insert.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR013660; DNApol_B_exo_N.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF08408; DNA_pol_B_3; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   Pfam; PF08452; DNAP_B_exo_N; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   1: Evidence at protein level;
KW   DNA recombination; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Hydrolase; Multifunctional enzyme;
KW   Nucleotidyltransferase; Reference proteome; Transferase;
KW   Viral DNA replication.
FT   CHAIN           1..1006
FT                   /note="DNA polymerase"
FT                   /id="PRO_0000046533"
FT   VARIANT         338
FT                   /note="S -> F (in PAA-R mutant; phosphonoacetate-
FT                   resistant)"
FT   VARIANT         372
FT                   /note="G -> D (in PAA-R, NG26 and PAArVg mutants;
FT                   phosphonoacetate-resistant)"
FT   VARIANT         392
FT                   /note="G -> D (in NG26 mutant; temperature-sensitivity)"
FT   VARIANT         611
FT                   /note="E -> K (in ts42 mutant; temperature-sensitivity)"
FT   CONFLICT        296
FT                   /note="Y -> H (in Ref. 2; AAO89344)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1006 AA;  116929 MW;  BB663635CC82446F CRC64;
     MDVRCINWFE SHGENRFLYL KSRCRNGETV FIRFPHYFYY VVTDEIYQSL SPPPFNARPL
     GKMRTIDIDE TISYNLDIKD RKCSVADMWL IEEPKKRSIQ NATMDEFLNI SWFYISNGIS
     PDGCYSLDEQ YLTKINNGCY HCDDPRNCFA KKIPRFDIPR SYLFLDIECH FDKKFPSVFI
     NPISHTSYCY IDLSGKRLLF TLINEEMLTE QEIQEAVDRG CLRIQSLMEM DYERELVLCS
     EIVLLRIAKQ LLELTFDYVV TFNGHNFDLR YITNRLELLT GEKIIFRSPD KKEAVYLCIY
     ERNQSSHKGV GGMANTTFHV NNNNGTIFFD LYSFIQKSEK LDSYKLDSIS KNAFSCMGKV
     LNRGVREMTF IGDDTTDAKG KAAAFAKVLT TGNYVTVDED IICKVIRKDI WENGFKVVLL
     CPTLPNDTYK LSFGKDDVDL AQMYKDYNLN IALDMARYCI HDACLCQYLW EYYGVETKTD
     AGASTYVLPQ SMVFEYRAST VIKGPLLKLL LETKTILVRS ETKQKFPYEG GKVFAPKQKM
     FSNNVLIFDY NSLYPNVCIF GNLSPETLVG VVVSTNRLEE EINNQLLLQK YPPPRYITVH
     CEPRLPNLIS EIAIFDRSIE GTIPRLLRTF LAERARYKKM LKQATSSTEK AIYDSMQYTY
     KIVANSVYGL MGFRNSALYS YASAKSCTSI GRRMILYLES VLNGAELSNG MLRFANPLSN
     PFYMDDRDIN PIVKTSLPID YRFRFRSVYG DTDSVFTEID SQDVDKSIEI AKELERLINN
     RVLFNNFKIE FEAVYKNLIM QSKKKYTTMK YSASSNSKSV PERINKGTSE TRRDVSKFHK
     NMIKTYKTRL SEMLSEGRMN SNQVCIDILR SLETDLRSEF DSRSSPLELF MLSRMHHSNY
     KSADNPNMYL VTEYNKNNPE TIELGERYYF AYICPANVPW TKKLVNIKTY ETIIDRSFKL
     GSDQRIFYEV YFKRLTSEIV NLLDNKVLCI SFFERMFGSK PTFYEA