ID   DPOL_ADES1              Reviewed;        1085 AA.
AC   Q8QNT0;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   03-AUG-2022, entry version 77.
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   Snake adenovirus serotype 1 (SnAdV-1).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Atadenovirus.
OX   NCBI_TaxID=189830;
OH   NCBI_TaxID=94885; Pantherophis guttatus (Corn snake) (Elaphe guttata).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12237421; DOI=10.1099/0022-1317-83-10-2403;
RA   Farkas S.L., Benko M., Elo P.T., Ursu K., Dan A., Ahne W., Harrach B.;
RT   "Genetic analysis of an adenovirus isolated from corn snake (Elaphe
RT   guttata) implies common origin with the members of the proposed new genus
RT   Atadenovirus.";
RL   J. Gen. Virol. 83:2403-2410(2002).
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.
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   -!- 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:0000255|HAMAP-Rule:MF_04055}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {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; DQ106414; AAL89790.2; -; Genomic_DNA.
DR   RefSeq; YP_001552247.1; NC_009989.1.
DR   GeneID; 10973889; -.
DR   KEGG; vg:10973889; -.
DR   Proteomes; UP000136605; Genome.
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   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; Reference proteome; Transferase;
KW   Viral DNA replication.
FT   CHAIN           1..1085
FT                   /note="DNA polymerase"
FT                   /id="PRO_0000425910"
FT   REGION          1059..1085
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1085 AA;  123880 MW;  12AF20437FAF6465 CRC64;
     MEASTTTVKA RSTHYICGHA GDSFVKIIYY KDKVKAVVSY LNMNDYLNTY ALKCVIPEKI
     TKDFFSSCPD DLLYSTLASI QRGYSPKKKE ELGGKWEPLL LLYHRGEEYI IRAVVPQRRC
     EDCGKQFVSS HQCNVRRREF YHHAVLPDTK TWWKPIKFSP IGALSNAKRL FIIYDIETYT
     FHSGYGKQLV PYLLVMQFKG DSRLRCEAEK IALECGFQPY RQCFMMLNKA RDVIGHKFKD
     MRVQLQKRAA SDIWSRYREK HDILSEEGVS YAQLEAMAKD NLLKTDAEPE FTEIIVVGHN
     ITGFDEIVLA SHVLEGLPKD EELQMFKITR NFMPRAGKLL FNDVIMALPN AAFQKPKQST
     FQRWKTGDLR PEDLKWEGVR FMVRDTVLLT HSSLRNAAQA YQLEVSKGHC PYDALNQYFM
     VGTYLCDENM YPAREYWSSD EEYLENKPPD GEKYDLVQKA VDYCVNDVKV TVALVKKLCS
     GYQQFCDEVL KLDCTFNVFQ RPTISSTTHA MFKQMFYKSE PSAVGKFLPN LEAPSEVMYE
     HIRKSVRGGR CYPSFLGVFT EPHLCYDICG MYASALSHPM PYGPTLSPFD SAVAIAEFQR
     KLDGQSELSY FDPDIFPMIV VADAFPPSLH CLDVLPPLCS KRSGKLCWTN EPLLGEVLTT
     VDLIMLKNRG WRVKLIQNAE CYAVWREWRP LCREYVSINI AAKEKADREK NQTQRSISKL
     LSNALYGSFA TRLDNKQVVF MDDMSSTTQS ELRSGKASIV SMTSVCSRSL PQKDTSFWER
     YFNLPQVEDS ISAELNDEPE TEPFIGGERS HVIYKPITFL SAECDNLLLA TVQSNSDWVK
     NDRYATQVAS FVLAWSRAFM SEWATILYGE DIGVPYEQRK LKSVYGDTDS LFLTGEGHRL
     MITKGRHKLK SSGNSLVYRD DGNLAWLVEC ETSCPSCKSD SFSSESCFLA PKLYALKDTT
     CPSCGLVSGG KLRAKGHAKS CITYDVLKSC FLDHYLLERP TEQYQSERTP IKRTLANGSA
     NSAPFTVVEK QLARVIRPWN DPTMARGTDL SQGFLLFPYD QKRPNPRPQE PLLENPFWDD
     SSQTA