ID   DPOL_ADE04              Reviewed;        1193 AA.
AC   P87503;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 79.
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 E serotype 4 (HAdV-4) (Human adenovirus 4).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus E.
OX   NCBI_TaxID=28280;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Stanglmaier M., Winnacker E.L.;
RL   Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
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; X74672; CAA52739.1; -; Genomic_DNA.
DR   EMBL; X74508; CAA52739.1; JOINED; Genomic_DNA.
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..1193
FT                   /note="DNA polymerase"
FT                   /id="PRO_0000046493"
FT   REGION          1..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1193 AA;  135210 MW;  7C6690E364D09105 CRC64;
     MALVQTHGSR GLHPEASDPG RQPSRRRSRQ SSPGAVPEPA RARRRRAPAT TASGSRAAPT
     ARRASSPPLL TMEAKPLPPA KKKRGTVVTP QGHGTLQAID VATNGAVEIK YHLDLPRALE
     KLLQVNRAPP LPTDLTPQRL RTLDSSGLRA LVLALRPVRA EVWTCLPRGL VSMTTIEAEE
     GQADHHDVVQ HQMQAPRLHF PLKFLVKGTQ VQLVQHVHPV QRCEHCGRLY KHKHECSARR
     RHFYFHHINS HSSNWWQEIQ FFPIGSHPRT ERLFLTYDVE TYTWMGSFGK QLVPFMLVMK
     LSGDDRLVEL ALDLALQLKW DRWHGDPRTF YCVTPEKMAV GQQFRQYRDR LQTALAVDLW
     TSFLRANPHL ADWALEQHGL SDPDELTYEE LKKLPHVKGR PRFVELYIVG HNINGFDEIV
     LAAQVINNRA EVPQPFRITR NFMPRAGKIL FNDVTFALPN PAYKKRTDFQ LWEQGGCDDI
     DFKHQFLKVM VRDTFALTHT SLRKAAQAYA LPVEKGCCAY KAVNQFYMLG SYRADQDGFP
     LEEYWKDREE FLLNRELWKQ KGQLKYDIIQ ETLDYCALDV LVTAELVAKL QDSYAHFIRD
     SVGLPHAHFN IFQRPTISSN SHAIFRQIVY RAEKPSRANL GAGLLAPSHE LYDYVRATIR
     GGRCYPTYIG ILDEPLYVYD ICGMYASALT HPMPWGTPLS PYERALAVRE WQASLDDLGT
     CISYFDPDLL PGIFTIDADP PDELMLDPLP PFCSRKGGRL CWTNEPLRGE VATSVDLITL
     HNRGWQVRIV PDELTTVFPE WKCVAREYVQ LNIAAKERAD KEKNQTMRSI AKLLSNALYG
     SFATKLDNKK IVFSDQMDEG LLKGISAGTV NIKSSSFLET DNLSAEVMPA FEREYLPQHV
     ALLDSDPEDS EDEQRPAPFY TPPAGTPGHV AYTYKPITFL DVDEGDMCLH TLEKVDPLVD
     NDRYPSHVAS FVLAWTRAFV SEWSGFLYDE DRGVPLEDRP IKSVYGDTDS LFVTQRGHEL
     METRGKKRIK KNGGKLVFDP NQPDLTWLVE CETVCAHCGA DAYAPESVFL APKLYALKSL
     LCPACGQTSK GNVRAKGHAA EALNYELMVN CYLADAQGAD RERFSTSRMS LKRTLASAQP
     GAHPFTVTET TLTRTLRPWK DRTLAALDAH RLAPYSRSRP NPRNEEVCWI EMP