ID   DPOL_ADEB2              Reviewed;        1017 AA.
AC   O72539;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=DNA polymerase {ECO:0000255|HAMAP-Rule:MF_04055};
DE            EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_04055};
GN   Name=POL {ECO:0000255|HAMAP-Rule:MF_04055};
OS   Bovine adenovirus 2 (BAdV-2) (Mastadenovirus bos2).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Ovine mastadenovirus A.
OX   NCBI_TaxID=114429;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=19;
RX   PubMed=9820840; DOI=10.1159/000024917;
RA   Yagubi A., Ojkic D., Bautista D., Haj-Ahmad Y.;
RT   "Sequencing analysis of the region encoding the DNA polymerase of bovine
RT   adenovirus serotypes 2 and 3.";
RL   Intervirology 41:69-79(1998).
CC   -!- FUNCTION: Eukaryotic-type DNA polymerase involved in viral genomic
CC       replication. DNA synthesis is protein primed, and acts in a strand
CC       displacement replication. Assembles in complex with viral pTP, DBP,
CC       host NFIA and host POU2F1/OCT1 on viral origin of replication. The
CC       polymerase covalently transfers dCMP onto pTP, thereby initiating
CC       complementary strand synthesis. {ECO:0000250|UniProtKB:P03261,
CC       ECO:0000250|UniProtKB:P04495, ECO:0000255|HAMAP-Rule:MF_04055}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_04055};
CC   -!- SUBUNIT: Heterodimer with the terminal protein; this heterodimer binds
CC       to bp 9 to 18 of the genome. Forms a complex with viral pTP, DBP and
CC       hosts NFIA and POU2F1/OCT1 for initiation of replication.
CC       {ECO:0000250|UniProtKB:P04495, ECO:0000255|HAMAP-Rule:MF_04055}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:P03261,
CC       ECO:0000255|HAMAP-Rule:MF_04055}.
CC   -!- MISCELLANEOUS: This DNA polymerase requires a protein as a primer.
CC       {ECO:0000255|HAMAP-Rule:MF_04055}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000255|HAMAP-Rule:MF_04055, ECO:0000305}.
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DR   EMBL; AF252854; AAC16239.1; -; Genomic_DNA.
DR   RefSeq; NP_064286.1; NC_002513.1.
DR   GeneID; 1732721; -.
DR   KEGG; vg:1732721; -.
DR   Proteomes; UP000154597; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.1600.10; -; 2.
DR   HAMAP; MF_04055; ADV_DPOL; 1.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR014382; DNA-dir_DNA_pol_B_adenovir.
DR   InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR   InterPro; IPR004868; DNA-dir_DNA_pol_B_mt/vir.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   Pfam; PF03175; DNA_pol_B_2; 1.
DR   PIRSF; PIRSF000788; DPol_ADV; 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; Host nucleus;
KW   Nucleotidyltransferase; Reference proteome; Transferase;
KW   Viral DNA replication.
FT   CHAIN           1..1017
FT                   /note="DNA polymerase"
FT                   /id="PRO_0000046490"
SQ   SEQUENCE   1017 AA;  117003 MW;  86BBC666A1C6E902 CRC64;
     MLEALKPAEG ATFTYIKGRL IKQQAAVENP ILPFPIFFLI KQNKVFLIKS FQSSQKCEFC
     GDFFANSHTC SVRRRDFYFH HINFKSSEWW SQISFQPIGS CDDTKRFFLT YDVETYTWHG
     KHGKQLVPFM LVFHLSGELE LVSLSANIAE QQRWLAWDTP HTYYYVSPIK GEIGKAFKDL
     RYEIQKQVTR LLWDNFVGEN PELAEIQERH HVNHIDDITA EMHKIKTKGS PQFIEIYVIG
     HNICGFDEIV LAAQVIHNRT DVLPAFKINR NFMPRNGKIL FNDISFCLPN PKYEKRKDFA
     DWECGKLTAA DHKYQFVKFM VRDTFALTHT SLRNAAGAYE LPVEKGSCPY EAVNEFYRIG
     SYQQDEDGFP SLRYWKSSEE YQLNKALWRE KNVGAYDIIQ QTLHYCVQDV LVTSALVNKL
     QESYKNFIAS QVNLPDASFN IFQRPTISSN SHAIFKQILY REVRPNKANL DNVLLAPSHE
     MYDYVRQSIR GGRCYPTYIG IMEQPIYVYD ICGMYASALT HPFPSGQPLN PYERALAATE
     WIRKLENLEQ KIDYFDECLL PGIFTIDADP PDELFLDELP PFCSRKGGRL CWANEPLRGE
     VATSIDLITL HNRGWAVRIL PDERTTIFPE WKCVAKEYVQ LNIGAKEKAD KEKNQTMRSI
     AKLLSNALYG SFATKLDNKK IVFSDQLEAS ASKTIARGNF SIKSSSFIET DNFSAEIMPE
     FVVTYPPAPS AELDESDENE EHTLFIPKDS HVTYKYKPIT FLETEDDDIC LHTLENNSPL
     IENNRYASHI ASFVLAWTRV FVSEWAEFLY AEDRGKPLHQ RTIKSVYGDT DSLFVTEEGH
     RLMEQRGKHR IKKNGGKLVF DPKNPSITWL VECETQCEKC KSDAFSSESV FLAPKLYALK
     NTVCTCCGHV GKGKLRAKGH ATTELCYDTL AKCYLSDAQQ GSQRFHTSRL SLKRTLATNQ
     SNAAPFTVTE TTLTRTVRPW KDKTLVDIDG HRLMPYSKSN PNPRNNDVCW MTLPWNM