ID DPOL_VACCC Reviewed; 1006 AA. AC P20509; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 02-SEP-2026, entry version 118. 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; ORFNames=E9L; OS Vaccinia virus (strain Copenhagen) (VACV). OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes; OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus. OX NCBI_TaxID=10249; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2; RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P., RA Paoletti E.; RT "The complete DNA sequence of vaccinia virus."; RL Virology 179:247-266(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P., RA Paoletti E.; RT "Appendix to 'The complete DNA sequence of vaccinia virus'."; RL Virology 179:517-563(1990). CC -!- FUNCTION: Catalyzes DNA synthesis. Acquires processivity by associating CC with a heterodimeric processivity factor comprised of the viral OPG148 CC and OPG116 proteins, thereby forming the DNA polymerase holoenzyme. CC Displays 3'- to 5' exonuclease activity. Might participate in viral DNA CC recombination. Does not perform OPG116/D4synthesis across an abasic CC site. {ECO:0000250|UniProtKB:P06856}. CC -!- CATALYTIC ACTIVITY: CC Reaction=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + CC diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA- CC COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; CC EC=2.7.7.7; Evidence={ECO:0000250|UniProtKB:P06856}; CC -!- SUBUNIT: Interacts with OPG148. Component of the Uracil-DNA CC glycosylase(UDG)-OPG148-polymerase complex; OPG148 and OPG116/UDG form CC a heterodimeric processivity factor that associates with OPG071 to form CC the processive polymerase holoenzyme. {ECO:0000250|UniProtKB:P06856}. CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle. CC {ECO:0000250|UniProtKB:P06856}. CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {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; M35027; AAA48049.1; -; Genomic_DNA. DR PIR; D42509; DJVZ4I. DR PDB; 5N2E; X-ray; 2.74 A; A=2-1006. DR PDB; 5N2G; X-ray; 2.78 A; A=2-1005. DR PDB; 5N2H; X-ray; 2.81 A; A=2-1005. DR PDB; 8Q3R; EM; 3.80 A; E=2-1006. DR EMDB; EMD-18134; -. DR SASBDB; P20509; -. DR SMR; P20509; -. DR IntAct; P20509; 1. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0034061; F:DNA polymerase activity; ISS:UniProtKB. 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:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW. DR FunFam; 1.10.287.690:FF:000010; DNA polymerase; 1. 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; IPR050240; DNA_pol_type-B. 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. DR PDBsum; 5N2E; -. DR PDBsum; 5N2G; -. DR PDBsum; 5N2H; -. DR PDBsum; 8Q3R; -. PE 1: Evidence at protein level; KW 3D-structure; DNA recombination; DNA replication; DNA-binding; KW DNA-directed DNA polymerase; Early protein; Hydrolase; KW Multifunctional enzyme; Nucleotidyltransferase; Transferase; KW Viral DNA replication. FT CHAIN 1..1006 FT /note="DNA polymerase" FT /id="PRO_0000046532" FT STRAND 2..10 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 13..15 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 17..27 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 29..35 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 38..43 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 44..48 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 55..67 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 72..76 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 79..82 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 83..95 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 109..116 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 129..131 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 132..134 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 136..143 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 145..148 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 151..153 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 162..169 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 172..174 FT /evidence="ECO:0007829|PDB:5N2E" FT TURN 178..180 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 183..191 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 197..204 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 205..207 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 210..219 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 227..229 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 235..239 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 241..253 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 257..263 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 264..268 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 269..279 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 282..284 FT /evidence="ECO:0007829|PDB:5N2G" FT STRAND 285..287 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 294..296 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 300..303 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 316..319 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 327..330 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 331..338 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 346..353 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 354..362 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 368..373 FT /evidence="ECO:0007829|PDB:5N2E" FT TURN 374..376 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 381..389 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 394..397 FT /evidence="ECO:0007829|PDB:5N2E" FT TURN 398..400 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 401..410 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 415..419 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 427..432 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 440..445 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 449..472 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 475..486 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 490..493 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 498..501 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 503..512 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 515..518 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 522..524 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 545..552 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 553..561 FT /evidence="ECO:0007829|PDB:5N2E" FT TURN 565..567 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 568..576 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 577..590 FT /evidence="ECO:0007829|PDB:5N2E" FT TURN 593..595 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 596..600 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 609..616 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 622..643 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 647..671 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 674..676 FT /evidence="ECO:0007829|PDB:5N2G" FT HELIX 681..702 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 706..708 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 711..713 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 721..723 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 732..734 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 743..751 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 754..760 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 764..777 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 778..782 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 789..814 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 822..825 FT /evidence="ECO:0007829|PDB:5N2G" FT HELIX 837..855 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 862..882 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 887..890 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 892..895 FT /evidence="ECO:0007829|PDB:5N2G" FT HELIX 905..917 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 918..920 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 930..935 FT /evidence="ECO:0007829|PDB:5N2E" FT TURN 947..950 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 951..953 FT /evidence="ECO:0007829|PDB:5N2E" FT STRAND 964..966 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 968..980 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 986..997 FT /evidence="ECO:0007829|PDB:5N2E" FT HELIX 1000..1002 FT /evidence="ECO:0007829|PDB:5N2H" SQ SEQUENCE 1006 AA; 116903 MW; 9D68FE95A93AE536 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 KKEAVHLCIY 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 //