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 11-JUN-2014, entry version 87. 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=POL; OrderedLocusNames=VACWR065; ORFNames=E9L; OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain OS WR)). OC Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae; OC Orthopoxvirus; Vaccinia virus. OX NCBI_TaxID=10254; OH NCBI_TaxID=9913; Bos taurus (Bovine). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2398897; 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 RT 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., RA Osborne J., 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; RA Traktman P., Kelvin M., Pacheco S.; RT "Molecular genetic analysis of vaccinia virus DNA polymerase RT 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 RT of 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 RT by the 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 RT to form a heterodimeric processivity factor for the viral DNA RT polymerase."; RL J. Biol. Chem. 281:3439-3451(2006). RN [8] RP IDENTIFICATION IN A COMPLEX WITH D4 AND 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 RT and A20 proteins as intrinsic components of the DNA polymerase RT holoenzyme."; RL J. Biol. Chem. 286:24702-24713(2011). CC -!- FUNCTION: Catalyzes DNA synthesis. Acquires processivity by CC associating with a heterodimeric processivity factor comprised of CC the viral A20 and D4 proteins, thereby forming the DNA polymerase CC holoenzyme. Displays 3'- to 5' exonuclease activity. Might CC participate in viral DNA recombination. Does not perform CC translesion synthesis across an abasic site. CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). CC -!- SUBUNIT: Interacts with A20. Component of the Uracil-DNA CC glycosylase(UDG)-A20-polymerase complex; A20 and UDG form a CC heterodimeric processivity factor that associates with E9 to form CC the processive polymerase holoenzyme. CC -!- INTERACTION: CC Q49PH7:W86/88-1-137 (xeno); NbExp=3; IntAct=EBI-984665, EBI-8039061; 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. CC -!- SEQUENCE CAUTION: CC Sequence=AAA98419.1; Type=Erroneous initiation; CC Sequence=AAA98419.1; Type=Frameshift; Positions=1; 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 ProteinModelPortal; P06856; -. DR IntAct; P06856; 2. DR MINT; MINT-6740349; -. 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR Gene3D; 3.30.420.10; -; 2. 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; IPR013660; DNApol_B_exo_N. DR InterPro; IPR012337; RNaseH-like_dom. 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; SSF53098; SSF53098; 3. DR PROSITE; PS00116; DNA_POLYMERASE_B; 1. PE 1: Evidence at protein level; KW Complete proteome; DNA recombination; DNA replication; DNA-binding; KW DNA-directed DNA polymerase; Hydrolase; Multifunctional enzyme; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1 1006 DNA polymerase. FT /FTId=PRO_0000046533. FT COMPBIAS 321 324 Poly-Asn. FT VARIANT 338 338 S -> F (in PAA-R mutant; FT phosphonoacetate-resistant). FT VARIANT 372 372 G -> D (in PAA-R, NG26 and PAArVg FT mutants; phosphonoacetate-resistant). FT VARIANT 392 392 G -> D (in NG26 mutant; temperature- FT sensitivity). FT VARIANT 611 611 E -> K (in ts42 mutant; temperature- FT sensitivity). FT CONFLICT 296 296 Y -> H (in Ref. 2; AAO89344). 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 //