ID   DPOL_ADET1              Reviewed;         214 AA.
AC   Q88469;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   29-SEP-2021, entry version 77.
DE   RecName: Full=DNA polymerase;
DE            EC=2.7.7.7;
DE   Flags: Fragment;
GN   Name=POL;
OS   Tree shrew adenovirus serotype 1 (TSAdV-1) (Tupaia adenovirus 1).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Tree shrew mastadenovirus A.
OX   NCBI_TaxID=47680;
OH   NCBI_TaxID=9393; Tupaiidae (tree shrews).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8661390; DOI=10.1006/viro.1996.0327;
RA   Song B., Hu S.L., Darai G., Spindler K.R., Young C.S.;
RT   "Conservation of DNA sequence in the predicted major late promoter regions
RT   of selected mastadenoviruses.";
RL   Virology 220:390-401(1996).
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}.
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;
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}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:P03261}.
CC   -!- MISCELLANEOUS: This DNA polymerase requires a protein as a primer.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR   EMBL; U57337; AAB01337.1; -; Genomic_DNA.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
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   Pfam; PF03175; DNA_pol_B_2; 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..>214
FT                   /note="DNA polymerase"
FT                   /id="PRO_0000046501"
FT   NON_TER         1
FT   NON_TER         214
SQ   SEQUENCE   214 AA;  23869 MW;  8ABEEFCA2B4A458F CRC64;
     EWKCIAQEYV KLNIAAKEKA DKEKNQTIRS IAKLLSNALY GSFATKLDNK KTVFADQLDS
     STAKGIANGE FSVKSSSFIE TDCLSAEIMS ELVVAYSPDT LLHPQQEGAT EANTQETPTF
     IGPTDHVTYT YKPITFLEAE EDEICLQTIE KNSPLIPNDR YPSHIASFVL AWTRAFVSEW
     ASLLYSEDLG TPMERRCLKS VYGDTDSLFL TEEG