DPOL_VACCC
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 03-AUG-2022, entry version 102.
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; 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 A20 and
CC D4 proteins, thereby forming the DNA polymerase holoenzyme. Displays
CC 3'- to 5' exonuclease activity. Might participate in viral DNA
CC recombination. Does not perform translesion synthesis across an abasic
CC site (By similarity). {ECO:0000250}.
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 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 the
CC processive polymerase holoenzyme (By similarity). {ECO:0000250}.
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 PDBsum; 5N2E; -.
DR PDBsum; 5N2G; -.
DR PDBsum; 5N2H; -.
DR SASBDB; P20509; -.
DR SMR; P20509; -.
DR IntAct; P20509; 1.
DR PRIDE; P20509; -.
DR Proteomes; UP000008269; 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: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 Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.90.1600.10; -; 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; 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 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; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA recombination; DNA replication; DNA-binding;
KW DNA-directed DNA polymerase; Hydrolase; Multifunctional enzyme;
KW Nucleotidyltransferase; Reference proteome; 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 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 TURN 264..267
FT /evidence="ECO:0007829|PDB:5N2E"
FT HELIX 268..279
FT /evidence="ECO:0007829|PDB:5N2E"
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 TURN 490..495
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 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..780
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"
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
