ID   DPOL_ADE12              Reviewed;        1061 AA.
AC   P06538;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   03-AUG-2022, entry version 115.
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   Human adenovirus A serotype 12 (HAdV-12) (Human adenovirus 12).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus A.
OX   NCBI_TaxID=28282;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3803925; DOI=10.1016/0378-1119(86)90403-8;
RA   Shu L., Hong J.S., Wei Y.-F., Engler J.A.;
RT   "Nucleotide sequence of the genes encoded in early region 2b of human
RT   adenovirus type 12.";
RL   Gene 46:187-195(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8254750; DOI=10.1128/jvi.68.1.379-389.1994;
RA   Sprengel J., Schmitz B., Heuss-Neitzel D., Zock C., Doerfler W.;
RT   "Nucleotide sequence of human adenovirus type 12 DNA: comparative
RT   functional analysis.";
RL   J. Virol. 68:379-389(1994).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA42478.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M14785; AAA42478.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X73487; CAA51882.1; -; Genomic_DNA.
DR   PIR; S33933; DJAD12.
DR   Proteomes; UP000004993; 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; -; 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..1061
FT                   /note="DNA polymerase"
FT                   /id="PRO_0000046496"
FT   REGION          773..792
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        32
FT                   /note="R -> S (in Ref. 1; AAA42478)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        162
FT                   /note="V -> L (in Ref. 1; AAA42478)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        181..182
FT                   /note="LQ -> YN (in Ref. 1; AAA42478)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        461
FT                   /note="S -> T (in Ref. 1; AAA42478)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        575
FT                   /note="L -> F (in Ref. 1; AAA42478)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        892
FT                   /note="S -> T (in Ref. 1; AAA42478)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1030
FT                   /note="K -> M (in Ref. 1; AAA42478)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1061 AA;  121728 MW;  33FBA89C33065C08 CRC64;
     MLFSLTDTMD SSRLYALISR FRPSRAEIWT CRSRGTVTLS VLAFEDPNGS GNAAEEEEDE
     RQLPSGIDFP ICFLVRGRQV HLIQQIQPVQ RCEHCARFYK HQHECSVRRR DFYFHHINSH
     SSNWWQEIHF FPIGSHPRTE RLFITYDVET YTWMGAFGKQ LVPFMLVMKL SGDDNLVKHA
     LQLALELGWD QWEKDSTTFY CLTPEKMKVG QQFRTYRNRL QTSLATDLWM TFLQKNPHLS
     QWAQEENGLV ALEDLSYEDL KRAPAIKGEP RFVELYIVGH NINGFDEIVL AAQVINNRLD
     VPGPFKISRN FIPRAGKILF NDITFALPNP HYKKRTNFLL WEHGGCDDQD FKYQYLKVMV
     RDTFALTHTS LRKAAQAYAL PVEKGCCPYK AVNQFYMLGS YRADANGFPL EEYWKDKEEY
     LLNQELWKKK GEKNYNLIGE TLNYCALDVL VTASLVEKLR SSYAQFVTDA VGLDAAHFNV
     FQRPTISSNS HAIFRQILYR AEKPQRTHLG PNILAPSHEL YDYVRASIRG GRCYPTYIGV
     LKEPIYVYDI CGMYASALTH PMPWGPPLNP YERALAVRQW QVALENYTCK IDYFDKNLCP
     GIFTIDADPP DENQLDVLPP FCSRKGGRLA WTNESLRGEV VTSVDLVTLH NRGWRLRLLS
     DERTTIFPTW KCLAREYVQL NIAAKERADR DKNQTLRSIA KLLSNALYGS FATKLDNKKI
     VFSDQMEESL MKEIAAGRLN IKSSSFIETD TLSTEVMPAF ERVYSPNQLA LVNSEAEESD
     EDQGPAPFYS PPPENCEHVT YTYKPITFMD AEEGDMCLHT LESSNPLINN DRYPSHVASF
     VLAWTRAFVS EWSEFLYEED RGIPLKDRPL KSVYGDTDSL FVTEKGRRLM ESQGKKRIKK
     YGGKLVFDPS CPELTWSVEC ETVCSYCGAD AYSPESVFLA PKLYALKCLQ CPHCGSTSKG
     KIRAKGHATE ALSYDLMLKC YLAEAQGEDT RFSTSRLSLK RTLASAQPGA HPFTVTETTL
     TRTLRPWKDK TLVHLDAHRL VPYSNSQPNP RNEEVCWIEM A