DPOL_PBCVN
ID DPOL_PBCVN Reviewed; 913 AA.
AC P30320;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 29-SEP-2021, entry version 100.
DE RecName: Full=DNA polymerase;
DE EC=2.7.7.7;
GN Name=DPO;
OS Paramecium bursaria Chlorella virus NY2A (PBCV-NY2A).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Algavirales; Phycodnaviridae; Chlorovirus.
OX NCBI_TaxID=46021;
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).
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; M86837; AAA88827.1; -; Genomic_DNA.
DR SMR; P30320; -.
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; Transferase; Viral DNA replication.
FT CHAIN 1..913
FT /note="DNA polymerase"
FT /id="PRO_0000046538"
FT REGION 182..401
FT /note="Contains conserved residues essential for 3' -> 5'
FT exonuclease activities"
SQ SEQUENCE 913 AA; 104956 MW; 7E656423123B02B5 CRC64;
MTELTFFPTD WRSEDVEPDK GEPYFRINIF GKTMDGKTVC VRAKFTPFFL LETPESWSAA
RTNLFITETA MKYDAIRPSC LPTKRKNMWG YDGGKMRPMV QFVFKTLSQM RKAKYRLKNE
YQIYESSVDP IIRIFHLRNI NPADWMHVSK AFPVETRISN SDIEVETSFQ HLGPSDLKEV
PPLIIASWDI ETYSKDRKFP LAENPADYCI QIATTFQKYG EPEPYRRVVV CYKQTASVEG
VEIISCAEEA DVMNTWMTIL QDEITDVSIG YNLWQYDLRY IHGRSMMCVD DITGEDNVRL
KNLGRLLVGG GEVIERDLSS NAFGQNKFFL LDMPGVMQID LLQWFRKNRN LESYSLNNVS
KLYLGDQKND LPAMQIFEKF EGGADDRAII AAYARKDTDL PLKLLKKMAI LEDITEMANA
VKVPVDYINF RGQQVRAFSC LVGKARQMNY AIPDDKMWTV DGKYEGATVL DAKKGAYFTS
IAALDFASLY PSIIRAHNMS PETLVMDKRF ENLPGIEYYE IETGLGTFKY PQKNDETGEG
QGVVPALLDD LAKFRKQAKK HMAEAKKNDD EFREALYDAQ QRSYKIVMNS VYGFLGASRG
FIPCVPIAAS VTATGRKMIE HTAKRVTELL PGSEVIYGDT DSVMIRMKLP DDKIHDMDEQ
FKMAKWLAGE ITKDFKAPND LEFEKIYYPY ILYSKKRYAA IKFEDPDEKG KVDVKGLALV
RRDFSPITRE ILKESLDTIL FKKDTPTAVT ETVECIRKVL DNEYPMEKFT MSKTLKTGYK
NECQPHLHVS NKIFERTGFP VPSGARVPFV YIEDKKNLDT KQSFRAEDPT FAQENDLIVD
RLFYIEHQLM KPICSLFEPL LDDPETEIFG HPLIKGKIDE LKSTFKADLR DAKRTKKNIA
NNQREITSFF KKK