ID   DPOL_FOWPN              Reviewed;         988 AA.
AC   P21402; Q9J5C6;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 2.
DT   29-SEP-2021, entry version 100.
DE   RecName: Full=DNA polymerase;
DE            EC=2.7.7.7;
GN   Name=POL; OrderedLocusNames=FPV094;
OS   Fowlpox virus (strain NVSL) (FPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus.
OX   NCBI_TaxID=928301;
OH   NCBI_TaxID=7742; Vertebrata.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FP-9 / Isolate HP-444;
RX   PubMed=2819823; DOI=10.1093/nar/15.16.6563;
RA   Binns M.M., Stenzler L., Tomley F.M., Campbell J., Boursnell M.E.G.;
RT   "Identification by a random sequencing strategy of the fowlpoxvirus DNA
RT   polymerase gene, its nucleotide sequence and comparison with other viral
RT   DNA polymerases.";
RL   Nucleic Acids Res. 15:6563-6573(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA   Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT   "The genome of fowlpox virus.";
RL   J. Virol. 74:3815-3831(2000).
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; M31638; AAA43821.1; -; Genomic_DNA.
DR   EMBL; AF198100; AAF44438.1; -; Genomic_DNA.
DR   RefSeq; NP_039057.1; NC_002188.1.
DR   SMR; P21402; -.
DR   PRIDE; P21402; -.
DR   GeneID; 1486642; -.
DR   KEGG; vg:1486642; -.
DR   Proteomes; UP000008597; 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:0000166; F:nucleotide binding; IEA:InterPro.
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 replication; DNA-binding; DNA-directed DNA polymerase;
KW   Nucleotidyltransferase; Reference proteome; Transferase;
KW   Viral DNA replication.
FT   CHAIN           1..988
FT                   /note="DNA polymerase"
FT                   /id="PRO_0000046535"
FT   CONFLICT        840
FT                   /note="E -> Q (in Ref. 1; AAA43821)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   988 AA;  116661 MW;  53A3E0AD4A71A328 CRC64;
     MDIRCVNWFE NKGETKYIYL KAINRESNVI FIRFNYYYHY VYDASKELEY KPNECIDLGP
     FKIINIDEKL STDIRYVEPR NYYTSELVLV KDLKRNREKQ YLQEYLDITW FYLLNNITPD
     GCYKIDIEHL TPIKKDCYHC DDVSKVFIQE IPIFEVKFTY LLFDIECQFD KKFPSVFVNP
     ISHISCWIID KVTEYKFTLI NTDILPDKEP SILHHKDFSP KDRITYCTEI VMLLIMKKIL
     EHRFDFVITF NGNNFDIRYI SGRLEILEKS FIYFSLPDAT ETVKLKIFER FVTGGTFTNK
     TYHINNNNGV MFFDLYAFIQ KTERLDSYKL DSISKNIFNC NVAIKEIDDT ILTLEATVKD
     NSKDKLSIFS RVLETGNYIT IGDNNVSKIV YKDINQDSFI IKVISNRDYE IGSVHNISFG
     KDDVDLKDMY KNYNLEIALD MERYCIHDAC LCKYIWDYYR VPSKINAASS TYLLPQSLAL
     EYRASTLIKG PLLKLLLEER VIYTRKITKV RYPYIGGKVF LPSQKTFENN VMIFDYNSLY
     PNVCIYGNLS PEKLVCILLN SNKLESEINM RTIKSKYPYP EYVCVSCESR LSDYYSEIIV
     YDRREKGIIP KLLEMFIGKR KEYKNLLKTA STTIESTLYD SLQYIYKIIA NSVYGLMGFS
     NSTLYSYSSA KTCTTIGRNM ITYLDSIMNG AVWENDKLIL ADFPRNIFSG ETMFNKELEV
     PNMNESFKFR SVYGDTDSIF SEISTKDIEK TAKIAKHLEH IINTKILHAN FKIEFEAIYT
     QLILQSKKKY TTIKYLANYK PGDKPIRVNK GTSETRRDVA LFHKHMIQRY KDMLMKLLME
     SKGQQEITRL ILQSLETDMI SEFTHNREFE KYLLSRKHHN NYKSATHSNF ELVKRYNLEN
     TEKIEIGERY YYIYICDISL PWQKKLCNIL SYEVIADSKF YLPKDKRIFY EIYFKRIASE
     VVNLLTDKTQ CMLFFSRLFG TKPVFSSD