ID   DPOL_ADECC              Reviewed;        1149 AA.
AC   Q65946;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 81.
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 1 (strain CLL) (CAdV-1) (Canine adenovirus 1
OS   (strain CLL)).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Canine mastadenovirus A.
OX   NCBI_TaxID=69150;
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   "DNA sequence and genomic organization of canine adenovirus type 1.";
RL   Submitted (AUG-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; U55001; AAB05434.1; -; Genomic_DNA.
DR   PRIDE; Q65946; -.
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..1149
FT                   /note="DNA polymerase"
FT                   /id="PRO_0000046498"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1149 AA;  130939 MW;  A0B686FAEFFA236E CRC64;
     MSLVQSHGTS GLFTEPPNSI NQQESSGPSL PAQDATQASA SSARAGATPA INSTKRKYRG
     AVVAQRATLS ISAILDNGQC VQIKYHSNLA SALTNLCNTN LYDLPACLNK PITVHNLPTL
     IEEAAASYSL IYYYQRGTVR KVEFRAEIPL LSFPLKFLVK HGKVFLIKDI SPMQRCEFCG
     SFFKVTHTCT LRRRDFYFHH VASHSGDWWE KISFSPIGAP ANTERLFIVY DVETYTWHGK
     FGKQLVPFML VFQLLGDEHL VNAAKNLATT QNWDTWNSNE QTALYYCITP EKRAIGVKFK
     TFRDTLQQHF ANNLWSHVLC QNPKLMEEAA ALGLENPEDI TANQLKKFKL QGTPRFIEVY
     VVGHNITGFD EILLAAQVVS TRAEIPPVFD ISRNFMPRAG RLLFNDITYS LPNPSYVPSK
     DYRHWEQGQV LASDLKTQYI KFMVRDTFSL THTSLKNAAK AYSLTVSKGC CPYQAVNEFY
     MLGSYQQDAD GFPDLKYWKD QEEYCFNKDL WKKEKKGAYD IIQQTLDYCA LDVQVTAQLV
     NKLIESYQIF IKNSVNLPET YFNVFQRPTI SSNSHAIFKQ ILYRAEKPNA PHLNTIIMAP
     SNEMYEYVRL SIRGGRCYPT YIGVLQEPVF VYDICGMYAS ALTHPFPAGS PLNPYERAVA
     IKAYEHKMQE HKTISYFDED LLPGIFTIDA DPPAEEFLDV LPPFCSRKGG RLCWTNEPLR
     GEVTTSIDVI TLHNRGWKVT LIPDTRTTVF PEWKCLAREY VQLNINAKEK ADKSKNQTMR
     SIAKLLSNAL YGSFATKLDN KKTVFSDQIE SNIAKEIASG AYVVKSSSYI ETDNLCAEIM
     PEFVVAYPPV NFDVHRLAPP SYSEEYPTEN PHAEGPFMQN FNMTSYRYKP IMFIDAEDDD
     FCLHTLEKST PLITNNRYAS QIASFVLAWT RAFVSEWSQF LYENDAGIPL EKRILKSVYG
     DTDSLFTTME GYRLMEEKGK RRLKKNGGNL VFDPNNPELT WLVECETKCE KCGADAYSSE
     SVYLAPKLYA LKDTTCPECQ YVGKGKLRAK GHATSTLSYD VLKACYYADL QQGSDIFKTS
     RMSLRRTLTS VQTHVQPFTV TETTLTRKLR PWKDKTLHAL DMNRLIPYSR KYPNPRNNET
     TWMELQWMT