ID   DPOL_VARV               Reviewed;        1005 AA.
AC   P0DOO6; P33793; Q85375;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   25-MAY-2022, entry version 12.
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; ORFNames=E9L;
OS   Variola virus.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=10255;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Bangladesh-1975;
RX   PubMed=8264798; DOI=10.1038/366748a0;
RA   Massung R.F., Esposito J.J., Liu L.I., Qi J., Utterback T.R., Knight J.C.,
RA   Aubin L., Yuran T.E., Parsons J.M., Loparev V.N., Selivanov N.A.,
RA   Cavallaro K.F., Kerlavage A.R., Mahy B.W.J., Venter J.C.;
RT   "Potential virulence determinants in terminal regions of variola smallpox
RT   virus genome.";
RL   Nature 366:748-751(1993).
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR   EMBL; L22579; AAA60798.1; -; Genomic_DNA.
DR   PIR; T28488; T28488.
DR   SMR; P0DOO6; -.
DR   DrugBank; DB12151; Brincidofovir.
DR   Proteomes; UP000119805; Genome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   DNA recombination; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Hydrolase; Multifunctional enzyme;
KW   Nucleotidyltransferase; Transferase; Viral DNA replication.
FT   CHAIN           1..1005
FT                   /note="DNA polymerase"
FT                   /id="PRO_0000448103"
SQ   SEQUENCE   1005 AA;  116716 MW;  1B68C53DE8921EA9 CRC64;
     MDVRCINWFE SHGENRFLYL KSRCRNGETV FIRFPHYFYY VVTDEIYQSL APPPFNARPM
     GKMRTIDIDE TISYNLDIKD RKCSVADMWL IEEPKKRNIQ NATMDEFLNI SWFYISNGIS
     PDGCYSLDDQ YLTKINNGCY HCGDPRNCFA KEIPRFDIPR SYLFLDIECH FDKKFPSVFI
     NPISHTSYCY IDLSGKRLLF TLINEEMLTE QEIQEAVDRG CLRIQSLMEM DYERELVLCS
     EIVLLQIAKQ LLELTFDYIV TFNGHNFDLR YITNRLELLT GEKIIFRSPD KKEAVHLCIY
     ERNQSSHKGV GGMANTTFHV NNNNGTIFFD LYSFIQKSEK LDSYKLDSIS KNAFSCMGKV
     LNRGVREMTF IGDDTTDAKG KAAVFAKVLT TGNYVTVDDI ICKVIHKDIW ENGFKVVLSC
     PTLTNDTYKL SFGKDDVDLA QMYKDYNLNI ALDMARYCIH DACLCQYLWE YYGVETKTDA
     GASTYVLPQS MVFEYKASTV IKGPLLKLLL ETKTILVRSE TKQKFPYEGG KVFAPKQKMF
     SNNVLIFDYN SLYPNVCIFG NLSPETLVGV VVSSNRLEEE INNQLLLQKY PPPRYITVHC
     EPRLPNLISE IAIFDRSIEG TIPRLLRTFL AERARYKKML KQATSSTEKA IYDSMQYTYK
     IIANSVYGLM GFRNSALYSY ASAKSCTSIG RRMILYLESV LNGAELSNGM LRFANPLSNP
     FYMDDRDINP IVKTSLPIDY RFRFRSVYGD TDSVFTEIDS QDVDKSIEIA KELERLINSR
     VLFNNFKIEF EAVYKNLIMQ SKKKYTTMKY SASSNSKSVP ERINKGTSET RRDVSKFHKN
     MIKIYKTRLS EMLSEGRMNS NQVCIDILRS LETDLRSEFD SRSSPLELFM LSRMHHLNYK
     SADNPNMYLV TEYNKNNPET IELGERYYFA YICPANVPWT KKLVNIKTYE TIIDRSFKLG
     SDQRIFYEVY FKRLTSEIVN LLDNKVLCIS FFERMFGSRP TFYEA