ID   DPOL_ADE05              Reviewed;        1056 AA.
AC   P04495;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 110.
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 C serotype 5 (HAdV-5) (Human adenovirus 5).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus.
OX   NCBI_TaxID=28285;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6325298; DOI=10.1016/0378-1119(84)90244-0;
RA   Dekker B.M.M., van Ormondt H.;
RT   "The nucleotide sequence of fragment HindIII-C of human adenovirus type 5
RT   DNA (map positions 17.1-31.7).";
RL   Gene 27:115-120(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1727603; DOI=10.1016/0042-6822(92)90082-z;
RA   Chroboczek J., Bieber F., Jacrot B.;
RT   "The sequence of the genome of adenovirus type 5 and its comparison with
RT   the genome of adenovirus type 2.";
RL   Virology 186:280-285(1992).
RN   [3]
RP   INTERACTION WITH HOST NFIA.
RX   PubMed=2211726; DOI=10.1016/s0021-9258(17)44799-5;
RA   Chen M., Mermod N., Horwitz M.S.;
RT   "Protein-protein interactions between adenovirus DNA polymerase and nuclear
RT   factor I mediate formation of the DNA replication preinitiation complex.";
RL   J. Biol. Chem. 265:18634-18642(1990).
RN   [4]
RP   FUNCTION, AND IDENTIFICATION IN THE INITIATION COMPLEX.
RX   PubMed=12747549; DOI=10.1007/978-3-662-05597-7_5;
RA   Liu H., Naismith J.H., Hay R.T.;
RT   "Adenovirus DNA replication.";
RL   Curr. Top. Microbiol. Immunol. 272:131-164(2003).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH THE TERMINAL PROTEIN.
RX   PubMed=15273278; DOI=10.1093/nar/gkh726;
RA   Mysiak M.E., Holthuizen P.E., van der Vliet P.C.;
RT   "The adenovirus priming protein pTP contributes to the kinetics of
RT   initiation of DNA replication.";
RL   Nucleic Acids Res. 32:3913-3920(2004).
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:0000255|HAMAP-Rule:MF_04055,
CC       ECO:0000269|PubMed:12747549, ECO:0000269|PubMed:15273278}.
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 (PubMed:15273278). Forms a complex with
CC       viral pTP, DBP and hosts NFIA and POU2F1/OCT1 for initiation of
CC       replication (PubMed:2211726, PubMed:12747549). {ECO:0000255|HAMAP-
CC       Rule:MF_04055, ECO:0000269|PubMed:15273278, ECO:0000269|PubMed:2211726,
CC       ECO:0000305|PubMed:12747549}.
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; X02996; CAA26749.1; -; Genomic_DNA.
DR   EMBL; M73260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A00712; DJAD51.
DR   Proteomes; UP000004992; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR   GO; GO:0039693; P:viral DNA genome replication; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   DNA replication; DNA-binding; DNA-directed DNA polymerase; Host nucleus;
KW   Nucleotidyltransferase; Transferase; Viral DNA replication.
FT   CHAIN           1..1056
FT                   /note="DNA polymerase"
FT                   /id="PRO_0000046494"
FT   REGION          37..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          762..788
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1056 AA;  120401 MW;  AE7BBC107A334E99 CRC64;
     MDSSHLRDVV IKLRPPRADI WTLGSRGVVV RSTVTPLEQP DGQGQAAEVE DHQPNPPGEG
     LKFPLCFLVR GRQVNLVQDV QPVHRCQYCA RFYKSQHECS ARRRDFYFHH INSHSSNWWR
     EIQFFPIGSH PRTERLFVTY DVETYTWMGA FGKQLVPFML VMKFGGDEPL VTAARDLAAN
     LGWDRWEQDP LTFYCITPEK MAIGRQFRTF RDHLQMLMAR DLWSSFVASN PHLADWALSE
     HGLSSPEELT YEELKKLPSI KGIPRFLELY IVGHNINGFD EIVLAAQVIN NRSEVPGPFR
     ITRNFMPRAG KILFNDVTFA LPNPRSKKRT DFLLWEQGGC DDTDFKYQYL KVMVRDTFAL
     THTSLRKAAQ AYALPVEKGC CAYQAVNQFY MLGSYRSEAD GFPIQEYWKD REEFVLNREL
     WKKKGQDKYD IIKETLDYCA LDVQVTAELV NKLRDSYASF VRDAVGLTDA SFNVFQRPTI
     SSNSHAIFRQ IVFRAEQPAR SNLGPDLLAP SHELYDYVRA SIRGGRCYPT YLGILREPLY
     VYDICGMYAS ALTHPMPWGP PLNPYERALA ARAWQQALDL QGCKIDYFDA RLLPGVFTVD
     ADPPDETQLD PLPPFCSRKG GRLCWTNERL RGEVATSVDL VTLHNRGWRV HLVPDERTTV
     FPEWRCVARE YVQLNIAAKE RADRDKNQTL RSIAKLLSNA LYGSFATKLD NKKIVFSDQM
     DAATLKGITA GQVNIKSSSF LETDNLSAEV MPAFQREYSP QQLALADSDA EESEDERAPT
     PFYSPPSGTP GHVAYTYKPI TFLDAEEGDM CLHTLERVDP LVDNDRYPSH LASFVLAWTR
     AFVSEWSEFL YEEDRGTPLE DRPLKSVYGD TDSLFVTERG HRLMETRGKK RIKKHGGNLV
     FDPERPELTW LVECETVCGA CGADAYSPES VFLAPKLYAL KSLHCPSCGA SSKGKLRAKG
     HAAEGLDYDT MVKCYLADAQ GEDRQRFSTS RTSLKRTLAS AQPGAHPFTV TQTTLTRTLR
     PWKDMTLARL DEHRLLPYSE SRPNPRNEEI CWIEMP