ID DPOL_VACCW Reviewed; 1006 AA. AC P06856; Q76ZV6; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 5. DT 29-MAY-2024, entry version 128. DE RecName: Full=DNA polymerase; DE EC=2.7.7.7; DE Includes: DE RecName: Full=3'-5' exodeoxyribonuclease; DE Short=3'-5' exonuclease; DE EC=3.1.11.-; GN Name=OPG071; Synonyms=POL; OrderedLocusNames=VACWR065; ORFNames=E9L; OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain OS WR)). OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes; OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus. OX NCBI_TaxID=10254; OH NCBI_TaxID=9913; Bos taurus (Bovine). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2398897; DOI=10.1128/mcb.10.10.5433-5441.1990; RA Ahn B.-Y., Gershon P.D., Jones E.V., Moss B.; RT "Identification of rpo30, a vaccinia virus RNA polymerase gene with RT structural similarity to a eucaryotic transcription elongation factor."; RL Mol. Cell. Biol. 10:5433-5441(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J., RA Wohlhueter R.; RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold RT redundancy and an error rate of 0.16/10kb."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 40-962. RX PubMed=3012524; DOI=10.1073/pnas.83.11.3659; RA Earl P.L., Jones E.V., Moss B.; RT "Homology between DNA polymerases of poxviruses, herpesviruses, and RT adenoviruses: nucleotide sequence of the vaccinia virus DNA polymerase RT gene."; RL Proc. Natl. Acad. Sci. U.S.A. 83:3659-3663(1986). RN [4] RP MUTANTS TS42; NG26 AND PAARVG. RX PubMed=2911123; DOI=10.1128/jvi.63.2.841-846.1989; RA Traktman P., Kelvin M., Pacheco S.; RT "Molecular genetic analysis of vaccinia virus DNA polymerase mutants."; RL J. Virol. 63:841-846(1989). RN [5] RP INTERACTION WITH A20. RX PubMed=11711620; DOI=10.1128/jvi.75.24.12298-12307.2001; RA Klemperer N., McDonald W., Boyle K., Unger B., Traktman P.; RT "The A20R protein is a stoichiometric component of the processive form of RT vaccinia virus DNA polymerase."; RL J. Virol. 75:12298-12307(2001). RN [6] RP FUNCTION. RX PubMed=15843688; DOI=10.1093/nar/gki525; RA Hamilton M.D., Evans D.H.; RT "Enzymatic processing of replication and recombination intermediates by the RT vaccinia virus DNA polymerase."; RL Nucleic Acids Res. 33:2259-2268(2005). RN [7] RP IDENTIFICATION IN A COMPLEX WITH UDG/D4 AND A20. RX PubMed=16326701; DOI=10.1074/jbc.m511239200; RA Stanitsa E.S., Arps L., Traktman P.; RT "Vaccinia virus uracil DNA glycosylase interacts with the A20 protein to RT form a heterodimeric processivity factor for the viral DNA polymerase."; RL J. Biol. Chem. 281:3439-3451(2006). RN [8] RP IDENTIFICATION IN A COMPLEX WITH OPG116/D4 AND OPG148/A20. RX PubMed=21572084; DOI=10.1074/jbc.m111.222216; RA Boyle K.A., Stanitsa E.S., Greseth M.D., Lindgren J.K., Traktman P.; RT "Evaluation of the role of the vaccinia virus uracil DNA glycosylase and RT A20 proteins as intrinsic components of the DNA polymerase holoenzyme."; RL J. Biol. Chem. 286:24702-24713(2011). RN [9] RP INDUCTION. RX PubMed=25903347; DOI=10.1128/jvi.00528-15; RA Yang Z., Cao S., Martens C.A., Porcella S.F., Xie Z., Ma M., Shen B., RA Moss B.; RT "Deciphering poxvirus gene expression by RNA sequencing and ribosome RT profiling."; RL J. Virol. 89:6874-6886(2015). CC -!- FUNCTION: Catalyzes DNA synthesis. Acquires processivity by associating CC with a heterodimeric processivity factor comprised of the viral CC OPG148/A20 and OPG116/D4 proteins, thereby forming the DNA polymerase CC holoenzyme. Displays 3'- to 5' exonuclease activity. Might participate CC in viral DNA recombination. Does not perform OPG116/D4synthesis across CC an abasic site. {ECO:0000269|PubMed:15843688}. 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: Interacts with OPG148/A20. Component of the Uracil-DNA CC glycosylase(UDG)-OPG148/A20-polymerase complex; OPG148/A20 and CC OPG116/UDG form a heterodimeric processivity factor that associates CC with OPG071/E9 to form the processive polymerase holoenzyme. CC {ECO:0000269|PubMed:11711620, ECO:0000269|PubMed:16326701, CC ECO:0000269|PubMed:21572084}. CC -!- INTERACTION: CC P06856; Q49PH7: A20R; Xeno; NbExp=3; IntAct=EBI-984665, EBI-8039061; CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle. CC {ECO:0000269|PubMed:25903347}. CC -!- MISCELLANEOUS: Ts42 is a temperature-sensitive mutant. PAArVg is a CC mutant resistant to the drug phosphonoacetic acid (PAA). NG26 is a CC double mutant with a temperature-sensitive lesion and a mutation CC rendering the virus resistant to PAA. CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA98419.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAA98419.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M36339; AAB59829.1; -; Genomic_DNA. DR EMBL; AY243312; AAO89344.1; -; Genomic_DNA. DR EMBL; M13213; AAA98419.1; ALT_SEQ; Genomic_DNA. DR PIR; A24878; A24878. DR PIR; A25270; DJVZZW. DR SMR; P06856; -. DR IntAct; P06856; 2. DR MINT; P06856; -. DR BindingDB; P06856; -. DR ChEMBL; CHEMBL3988586; -. DR Proteomes; UP000000344; Genome. DR GO; GO:0008408; F:3'-5' exonuclease activity; IDA:UniProtKB. DR GO; GO:0008296; F:3'-5'-DNA exonuclease activity; IEA:TreeGrafter. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:UniProtKB. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0006287; P:base-excision repair, gap-filling; IEA:TreeGrafter. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0045004; P:DNA replication proofreading; IEA:TreeGrafter. DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IEA:TreeGrafter. DR GO; GO:0009432; P:SOS response; IEA:TreeGrafter. DR GO; GO:0039693; P:viral DNA genome replication; IDA:UniProtKB. DR Gene3D; 1.10.287.690; Helix hairpin bin; 1. DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 2. DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; IPR013617; DNA-dir_DNA_pol_B_vir_insert. DR InterPro; IPR043502; DNA/RNA_pol_sf. DR InterPro; IPR023211; DNA_pol_palm_dom_sf. DR InterPro; IPR013660; DNApol_B_exo_N. DR InterPro; IPR012337; RNaseH-like_sf. DR InterPro; IPR036397; RNaseH_sf. DR PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1. DR PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1. DR Pfam; PF00136; DNA_pol_B; 1. DR Pfam; PF08408; DNA_pol_B_3; 1. DR Pfam; PF03104; DNA_pol_B_exo1; 1. DR Pfam; PF08452; DNAP_B_exo_N; 1. DR PRINTS; PR00106; DNAPOLB. DR SMART; SM00486; POLBc; 1. DR SUPFAM; SSF56672; DNA/RNA polymerases; 1. DR SUPFAM; SSF53098; Ribonuclease H-like; 1. DR PROSITE; PS00116; DNA_POLYMERASE_B; 1. PE 1: Evidence at protein level; KW DNA recombination; DNA replication; DNA-binding; KW DNA-directed DNA polymerase; Early protein; Hydrolase; KW Multifunctional enzyme; Nucleotidyltransferase; Reference proteome; KW Transferase; Viral DNA replication. FT CHAIN 1..1006 FT /note="DNA polymerase" FT /id="PRO_0000046533" FT VARIANT 338 FT /note="S -> F (in PAA-R mutant; phosphonoacetate- FT resistant)" FT VARIANT 372 FT /note="G -> D (in PAA-R, NG26 and PAArVg mutants; FT phosphonoacetate-resistant)" FT VARIANT 392 FT /note="G -> D (in NG26 mutant; temperature-sensitivity)" FT VARIANT 611 FT /note="E -> K (in ts42 mutant; temperature-sensitivity)" FT CONFLICT 296 FT /note="Y -> H (in Ref. 2; AAO89344)" FT /evidence="ECO:0000305" SQ SEQUENCE 1006 AA; 116929 MW; BB663635CC82446F CRC64; MDVRCINWFE SHGENRFLYL KSRCRNGETV FIRFPHYFYY VVTDEIYQSL SPPPFNARPL GKMRTIDIDE TISYNLDIKD RKCSVADMWL IEEPKKRSIQ NATMDEFLNI SWFYISNGIS PDGCYSLDEQ YLTKINNGCY HCDDPRNCFA KKIPRFDIPR SYLFLDIECH FDKKFPSVFI NPISHTSYCY IDLSGKRLLF TLINEEMLTE QEIQEAVDRG CLRIQSLMEM DYERELVLCS EIVLLRIAKQ LLELTFDYVV TFNGHNFDLR YITNRLELLT GEKIIFRSPD KKEAVYLCIY ERNQSSHKGV GGMANTTFHV NNNNGTIFFD LYSFIQKSEK LDSYKLDSIS KNAFSCMGKV LNRGVREMTF IGDDTTDAKG KAAAFAKVLT TGNYVTVDED IICKVIRKDI WENGFKVVLL CPTLPNDTYK LSFGKDDVDL AQMYKDYNLN IALDMARYCI HDACLCQYLW EYYGVETKTD AGASTYVLPQ SMVFEYRAST VIKGPLLKLL LETKTILVRS ETKQKFPYEG GKVFAPKQKM FSNNVLIFDY NSLYPNVCIF GNLSPETLVG VVVSTNRLEE EINNQLLLQK YPPPRYITVH CEPRLPNLIS EIAIFDRSIE GTIPRLLRTF LAERARYKKM LKQATSSTEK AIYDSMQYTY KIVANSVYGL MGFRNSALYS YASAKSCTSI GRRMILYLES VLNGAELSNG MLRFANPLSN PFYMDDRDIN PIVKTSLPID YRFRFRSVYG DTDSVFTEID SQDVDKSIEI AKELERLINN RVLFNNFKIE FEAVYKNLIM QSKKKYTTMK YSASSNSKSV PERINKGTSE TRRDVSKFHK NMIKTYKTRL SEMLSEGRMN SNQVCIDILR SLETDLRSEF DSRSSPLELF MLSRMHHSNY KSADNPNMYL VTEYNKNNPE TIELGERYYF AYICPANVPW TKKLVNIKTY ETIIDRSFKL GSDQRIFYEV YFKRLTSEIV NLLDNKVLCI SFFERMFGSK PTFYEA //