ID   DPOL_ADE07              Reviewed;        1122 AA.
AC   P05664;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 94.
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 B serotype 7 (HAdV-7) (Human adenovirus 7).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus B.
OX   NCBI_TaxID=10519;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6301944; DOI=10.1016/0378-1119(83)90156-7;
RA   Engler J.A., Hoppe M.S., van Bree M.P.;
RT   "The nucleotide sequence of the genes encoded in early region 2b of human
RT   adenovirus type 7.";
RL   Gene 21:145-159(1983).
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; X03000; CAA26770.1; -; 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..1122
FT                   /note="DNA polymerase"
FT                   /id="PRO_0000046495"
SQ   SEQUENCE   1122 AA;  128635 MW;  49B72129847F507A CRC64;
     MQEATEPPPP KRKNKGTVVA PKGHGTLQAI DISTNGPVEI KYHLNLPHAL EKIMQVNLLT
     LPTNLTPQRL RTLDSSGLRA LVLELRPCRA EVWTCLPRGL VSMTTIETED GHADADNIVE
     REVQAPSLNF PLKFLVKGSQ VQLIHEVHPV NRCEYCGRLY KHKHECSARR REFYFHHINS
     HSSNWWQEIQ FFPIGSHPRT ERLFLTYDVE TYTWMGSFGK QLIPFMLVMK LSGDQRLVNI
     AYDIAMKLKW DRWRQDPQTF YCITPEKMAV GQHFRQYRDQ LQTALAVDLW SSFLKANPHM
     HEWALEHYAL TDPTDLTFEE LKKLPHVRGT PRFLELYIVG HNINGFDEIV LAAQVINNRA
     EVPQPFKITR NFMPRAGEIL FNDVTFALPN PAYKKRADFQ LWEQGACDDI DFKYQFLKVM
     VRDTFALTHT SLRNAAQAYS LPVEKGCCPY KAVNQFYMLG SYRAEKDGFP LEEYWKDHEE
     YLLNRELWEK KSQPRYDIIQ ETLNYCALDV LVTAELVAKL QESYAHFIRD SVGLPHVHFN
     IFQRPTISSN SHAIFRQIVY RAEKPNRTNL GPGLLAPSHE LYDYVRASIR GGRCYPTYIG
     ILEEPLYVYD ICGMYASALT HPMPWGTPLN PYERALAVRE WQMTLDDPAT ISYFDKDLLP
     GIFTIDADPP DEFMLDPLPP FCSRKGGRLC WTNEPLRGEV ATTVDLITLH NRGWRVRIVP
     DELTTIFPEW KCVAREYVQL NIAAKERADK EKNQTMRSIA KLLSNALYGS FATKLDNKKI
     VFSDQMDESL IKGISAGTVN IKSSSFLETD NLSAEVMPAF EREYLPQQLA LLDSDPEDSE
     DEQRSAPFYT PPAGTPGHVA YTYKPITFLD VEEGDMCLHT VEKVDPLVDN DRYPSHVASF
     VLAWTRAFVS EWAGFLYEED RGTPLEDRPI KSVYGDTDSL FVTQRGHELM ETKGKKRIKK
     HGGKLVFDPD EPDLTWLVEC ETVCVSCGAD AYSPESIFLA PKLYALKCIY CPACHKTSKG
     KLRAKGHAAE ALNYELMVNC YLADMQGADR QRFSTSRMSL KRTLASAQPG AHPFTVTETT
     LTRTLRPWKD RTLAALDAHR LIPYSRSRPN PRNEEVCWIE MP