ID   DPOL_ADEB3              Reviewed;        1023 AA.
AC   O72540;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 85.
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 B serotype 3 (BAdV-3) (Mastadenovirus bos3).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Bovine mastadenovirus B.
OX   NCBI_TaxID=10510;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WBR-1;
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; AF061654; AAC16240.1; -; Genomic_DNA.
DR   PRIDE; O72540; -.
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; -; 1.
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; Transferase; Viral DNA replication.
FT   CHAIN           1..1023
FT                   /note="DNA polymerase"
FT                   /id="PRO_0000046491"
FT   REGION          726..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..748
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1023 AA;  117729 MW;  193998701764957A CRC64;
     MCVYKTYKGK LKITSIPARA DRPRLPFPLN FLIHKRKLYL IDTIAEVQRC ADCGSYFKQT
     HTCSTRRRDF YFHHINTQSS DWWEEIKFFP LGAHPDTRRL FVVYDVETYT WHGSFGKQLM
     PFMLVFTLFG DAQLCEQAVN IAKKQKWSSW PKQANTFYYL NPQRNKVGSL FKQYRDALQE
     AASTLLWRQF LADNPCLENL CLKLGYVHAS DIPFEELCTL ELKGQPTFLE VYVVGHNING
     FDEIVLAAQV INNKQGIPAA FKVSRNFMPR CGKILFNDLT FALPNPTHAA RKDFKDWEEG
     TPTSADYKFQ FVKFMVRDTF ALTHTSLRNA AAAYALPVEK GCCPYKAVNE FYMLGTYRTD
     ADSFPQRDYW SSDEEYLLNK SLWLQENSGA YDIVQRTLDY CAMDVLVTAE LVKKLQASYL
     DFVHTSVGLP HCNFNVLQRP TISSNSHAIF RQVVYRSQRP NRSSLGNFLL APSNEMYDYV
     RESIRGGRCY PTYIGVLTEA IYVYDICGMY ASALTHPFPA GKPLNPFDRA LAIKNWQDRL
     TQLHRPIDYF DRTLLPAIFT IDADPPPEAF LDVIPPFCSR KGGRLCWTNE TLRGEVVTCL
     DAITLHNRGW RVQILNDPRT TVFPQWECLA RDYVQLNIAA KERADKEKNQ TLRSIAKLLS
     NALYGSFATK LDNRVTVFSD QMEDKYVRGI SDGTYDIKST AFVETDNLSS SVMAELKITY
     SPVKQQTDAT RKHRQCTPTS NSSSDEDAPF YTLGDPQNHH VTYTYKPITF LEADDSALCL
     HTLQKKSSLI FNNRYPSHIA SFVLAWTRAF VSEWADILYL EDRGTPLEDR ILKFVYGDTD
     SMFLTQRGKE LMDTRGKHRL KGNNRPLVFD PTNPQLTWLV ECETQCPRCH GDAHSQESVF
     LAPKLYALKN IYCPSCRAES SGKLRAKGHA TSQLSYDLLV TCYYSTEQLG DEKFGTSRLS
     LRRSLVSRQT HQQPFTVTET TLARTLRPWK DRTLRAIDRH RLAPYSNSHP NPRNKELCWM
     EMY