ID   DPOL_ADECT              Reviewed;        1150 AA.
AC   P87553;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 84.
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   Canine adenovirus serotype 2 (strain Toronto A 26-61) (CAdV-2) (Canine
OS   adenovirus 2 (strain Toronto A 26-61)).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Canine mastadenovirus A.
OX   NCBI_TaxID=69152;
OH   NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Campbell J.B., Zhao Y.;
RT   "Complete DNA sequence and genomic organization of canine adenovirus type
RT   2.";
RL   Submitted (DEC-1996) 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; U77082; AAB38716.1; -; Genomic_DNA.
DR   RefSeq; AP_000613.1; AC_000020.1.
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   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; 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..1150
FT                   /note="DNA polymerase"
FT                   /id="PRO_0000046499"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1150 AA;  130460 MW;  474E0F53705C5873 CRC64;
     MSLVQGHGTS GLFTEPPNPI NQQESSGPSL PAQDAAQAFA SSPRAGATST IVNPPKRKYK
     GAVVVQRATL SISAVLDNGQ CVEIKYHSNL ASALTNLCNT NLYDLPACLN RPITAHNLPA
     LIEEAAAPYS LICYYQRGTV RRVEFQAEVP LLSFPLKFLV KQGKVFLIKD ISQMQKCEFC
     GSFFKVTHTC ALRRRDFYFH HVAAHSADWW EKISFTPIGA PPNTERLFIV YDVETYTWHG
     KFGKQLVPFM LVFQLLGDDH LVNVAKTLAT EQNWEIWNGK EQDTLYYCIT PEKRAIGVKF
     KKFRDTLQQH IAASLWSHVI CQNPQLQEKA TTLGLESPEE LTPDQLKKFK LKGNPRFIEV
     YAVGHNITGF DEILLAAQVV STRAEIPPVF EICRNFMPRA GRLLFNDITY SLPNPSYVPA
     KSYEHWEQGQ VLASDLKSQY IKFMVRDTFS LTHTSLKNAA KAYSLTVSKG CCPYQAVNEF
     YMLGSYQQDA DGFPDLKYWK DQEEYSFNKD LWIKEKKGAY DIIQQTLDYC ALDVQVTAQL
     VNKLIESYQI FIKNSVNLPE TSFNVFQRPT ISSNSHAIFK QILYKAEKPN THHLSTILMA
     PSNEMYEYVR LSIRGGRCYP TYIGVLQEPV FVYDICGMYA SALTHPFPAG SPLNPYERAL
     AIKAYEQKML NHKTISYFDK DLLPGIFTID ADPPAEEFLD VLPPFCSRKG GRLCWTNEPL
     RGEIATSIDV ITLHNRGWKV TLIPDTRTTV FPEWKCLARE YVQLNISAKE EADKSKNQTM
     RSIAKLLSNA LYGSFATKLD NKKTVFSDQI ESNIAKEIAS GAYVVKSSSY IETDNLCAEI
     MPEFVVAYPP VNSDVRQLAP PSCSEEDPTK DPLAEAPFMH NFSMTSYHYK PIMFIDAEDD
     DFCLHTLEKS TPLIANNRYP SQIASFVLAW TRAFVSEWSQ FLYENDAGTP LENRVLKSVY
     GDTDSLFTTM EGYKLMEEKG KKRLKKNGGK LVFDPSNPEL TWLVECETQC EKCGSDAYSS
     ESVYLAPKLY ALKDTTCPKC HHVGKGKLRA KGHATSTLSY DVLKACYYAD MQQGSDVFKT
     SRMSLRRTLT SVQAHVQPFT VTETTLTRKL RPWKDKTLHA LDMHRLIPYS RKHPNPRNTE
     TTWMELQWMT