ID   DPOL_PBCV1              Reviewed;         913 AA.
AC   P30321; Q84505;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   29-SEP-2021, entry version 115.
DE   RecName: Full=DNA polymerase;
DE            EC=2.7.7.7;
GN   Name=DPO; OrderedLocusNames=A185R;
OS   Paramecium bursaria Chlorella virus 1 (PBCV-1).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Algavirales; Phycodnaviridae; Chlorovirus.
OX   NCBI_TaxID=10506;
OH   NCBI_TaxID=114055; Chlorella.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1585643; DOI=10.1016/0042-6822(92)90527-v;
RA   Grabherr R., Strasser P., van Etten J.L.;
RT   "The DNA polymerase gene from chlorella viruses PBCV-1 and NY-2A contains
RT   an intron with nuclear splicing sequences.";
RL   Virology 188:721-731(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RX   PubMed=8614977; DOI=10.1006/viro.1996.0038;
RA   Lu Z., Li Y., Que Q., Kutish G.F., Rock D.L., van Etten J.L.;
RT   "Analysis of 94 kb of the chlorella virus PBCV-1 330-kb genome: map
RT   positions 88 to 182.";
RL   Virology 216:102-123(1996).
CC   -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC       potentially exhibits 3' to 5' exonuclease activity.
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   -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR   EMBL; M86836; AAC00532.1; -; Genomic_DNA.
DR   EMBL; JF411744; AAC96553.1; -; Genomic_DNA.
DR   PIR; A42543; A42543.
DR   PIR; T17675; T17675.
DR   RefSeq; NP_048532.2; NC_000852.5.
DR   SMR; P30321; -.
DR   PRIDE; P30321; -.
DR   GeneID; 917871; -.
DR   KEGG; vg:917871; -.
DR   Proteomes; UP000000862; Genome.
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:0004527; F:exonuclease 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   Gene3D; 1.10.132.60; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.90.1600.10; -; 1.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR   InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR042087; DNA_pol_B_thumb.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 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; Early protein;
KW   Exonuclease; Hydrolase; Multifunctional enzyme; Nuclease;
KW   Nucleotidyltransferase; Reference proteome; Transferase;
KW   Viral DNA replication.
FT   CHAIN           1..913
FT                   /note="DNA polymerase"
FT                   /id="PRO_0000046539"
FT   REGION          182..401
FT                   /note="Contains conserved residues essential for 3' -> 5'
FT                   exonuclease activities"
SQ   SEQUENCE   913 AA;  104686 MW;  4B5EC5492249EC2B CRC64;
     MTDITIFPTD WRAEDVVPDK GESFFRINIF GKTAEGKTVC VQTKFTPYFL LEVPESWSPA
     RTNLFITETA MKYDAVRPMC LSTKRKNMWG FDGGKMRNMV QFVFKTQAQL RKAKYRLKDQ
     YQIYESSVDP IIRVFHLRNI NPADWIRVSK AYPAQTRISN SDIEVETSFQ HLGPVEDKTV
     PPLVIASWDI ETYSKDRKFP LAENPTDYCI QIATTFQKYG EPEPYRRVVV CYKQTAPVEG
     VEIISCLEES DVMNTWMKIL QDEKTDVSIG YNTWQYDLRY VHGRTQMCVD DMTGEDKVKL
     SNLGRLLSGG GEVVERDLSS NAFGQNKFFL LDMPGVMQID LLQWFRKNRN LESYSLNNVS
     KLYLGDQKND LPAMQIFEKF EGNAEDRAII AAYAAKDTDL PLKLLKKMAI LEDLTEMANA
     VKVPVDYINF RGQQIRAFSC LVGKARQMNY AIPDDKAWAT EGKYEGATVL DAKKGAYFTP
     IAALDFASLY PSIIRAHNMS PETLVMEKRF ENVPGVEYYE IETGLGKFKY AQKNDETGEG
     QGVVPALLDD LAKFRKLAKK HMAEAKRNGD DFKEALYDAQ QRSFKVVMNS VYGFLGASKG
     FIPCVPIAAS VTATGRKMIE HTAKRAVELL PGSEVIYGDT DSVMVKMKLP DDKVHDMDEQ
     FKMAKWLAGE ITKDFRAPND LEFEKIYYPY ILYSKKRYAA VKFEEPDEKG KVDVKGLALV
     RRDFSPITRD ILKESLDTIL YKKDTPTAVS ETLERIRKVL DNEYPMEKFM MSKLLKTGYK
     NECQPHLHVA NKIYERTGFP VPSGARVPFV YIEDKKNPDI KQSFKAEDPT FAQDNGLIVD
     RLFYIEHQLL KPICSLFEPL LDDPEKEIFG HRLIKEKIEN LKNVFKADLK VAKRVKKNIA
     NNQREITSFF KKK