DPOL_HHV11
ID DPOL_HHV11 Reviewed; 1235 AA.
AC P04293; B9VQF8; Q09IA3;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=DNA polymerase catalytic subunit;
DE EC=2.7.7.7;
DE EC=3.1.26.4;
GN ORFNames=UL30;
OS Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10299;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
RA McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D.,
RA Perry L.J., Scott J.E., Taylor P.;
RT "The complete DNA sequence of the long unique region in the genome of
RT herpes simplex virus type 1.";
RL J. Gen. Virol. 69:1531-1574(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2999714; DOI=10.1093/nar/13.22.8143;
RA Quinn J.P., McGeoch D.J.;
RT "DNA sequence of the region in the genome of herpes simplex virus type 1
RT containing the genes for DNA polymerase and the major DNA binding
RT protein.";
RL Nucleic Acids Res. 13:8143-8163(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nonneuroinvasive mutant HF10;
RX PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019;
RA Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.;
RT "Determination and analysis of the DNA sequence of highly attenuated herpes
RT simplex virus type 1 mutant HF10, a potential oncolytic virus.";
RL Microbes Infect. 9:142-149(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17 syn+;
RA Cunningham C., Davison A.J.;
RT "Herpes simplex virus type 1 bacterial artificial chromosome.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=2553735; DOI=10.1016/s0021-9258(19)47296-7;
RA Crute J.J., Lehman I.R.;
RT "Herpes simplex-1 DNA polymerase. Identification of an intrinsic 5'----3'
RT exonuclease with ribonuclease H activity.";
RL J. Biol. Chem. 264:19266-19270(1989).
RN [6]
RP INTERACTION WITH UL8.
RX PubMed=9261356; DOI=10.1128/jvi.71.9.6390-6397.1997;
RA Marsden H.S., McLean G.W., Barnard E.C., Francis G.J., MacEachran K.,
RA Murphy M., McVey G., Cross A., Abbotts A.P., Stow N.D.;
RT "The catalytic subunit of the DNA polymerase of herpes simplex virus type 1
RT interacts specifically with the C terminus of the UL8 component of the
RT viral helicase-primase complex.";
RL J. Virol. 71:6390-6397(1997).
CC -!- FUNCTION: Replicates viral genomic DNA. The replication complex is
CC composed of six viral proteins: the DNA polymerase, processivity
CC factor, primase, primase-associated factor, helicase, and ssDNA-binding
CC protein. Additionally, the polymerase contains an intrinsic
CC ribonuclease H (RNase H) activity that specifically degrades RNA/DNA
CC heteroduplexes or duplex DNA substrates in the 5' to 3' direction.
CC Therefore, it can catalyze the excision of the RNA primers that
CC initiate the synthesis of Okazaki fragments at a replication fork
CC during viral DNA replication. {ECO:0000269|PubMed:2553735}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC -!- SUBUNIT: Forms a complex with the ssDNA-binding protein UL29, the DNA
CC polymerase processivity factor, and the alkaline exonuclease. Interacts
CC with the putative helicase-primase complex subunit UL8; this
CC interaction may coordinate leading and lagging strand DNA synthesis at
CC the replication fork (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P04293; P10226: UL42; NbExp=3; IntAct=EBI-8615017, EBI-1029310;
CC P04293; P10192: UL8; NbExp=4; IntAct=EBI-8615017, EBI-7185538;
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000305}. Note=The protein is
CC present at discrete sites in nuclei, called replication compartments
CC where viral DNA replication occurs. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA26941.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X14112; CAA32323.1; -; Genomic_DNA.
DR EMBL; X03181; CAA26941.1; ALT_FRAME; Genomic_DNA.
DR EMBL; DQ889502; ABI63492.1; -; Genomic_DNA.
DR EMBL; FJ593289; ACM62253.1; -; Genomic_DNA.
DR PIR; A00715; DJBEV1.
DR PIR; C30085; DJBEH7.
DR RefSeq; YP_009137105.1; NC_001806.2.
DR PDB; 7LUF; X-ray; 3.50 A; A/B=43-1197.
DR PDBsum; 7LUF; -.
DR SMR; P04293; -.
DR BioGRID; 971473; 3.
DR IntAct; P04293; 2.
DR MINT; P04293; -.
DR BindingDB; P04293; -.
DR ChEMBL; CHEMBL1872; -.
DR DrugBank; DB00787; Acyclovir.
DR DrugBank; DB00426; Famciclovir.
DR DrugBank; DB00529; Foscarnet.
DR DrugBank; DB01004; Ganciclovir.
DR DrugBank; DB00299; Penciclovir.
DR DrugBank; DB13896; Talimogene laherparepvec.
DR DrugBank; DB00577; Valaciclovir.
DR DrugBank; DB00194; Vidarabine.
DR DrugCentral; P04293; -.
DR PRIDE; P04293; -.
DR GeneID; 2703462; -.
DR KEGG; vg:2703462; -.
DR PRO; PR:P04293; -.
DR Proteomes; UP000009294; Genome.
DR Proteomes; UP000180652; Genome.
DR GO; GO:0042575; C:DNA polymerase complex; IDA:GO_Central.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034061; F:DNA polymerase activity; IDA:AgBase.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IDA:UniProtKB.
DR GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; IDA:UniProtKB.
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; IPR021639; DNAPolymera_Pol_C.
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 Pfam; PF11590; DNAPolymera_Pol; 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 replication; DNA-binding; DNA-directed DNA polymerase;
KW Endonuclease; Host nucleus; Hydrolase; Multifunctional enzyme; Nuclease;
KW Nucleotidyltransferase; Reference proteome; Transferase;
KW Viral DNA replication.
FT CHAIN 1..1235
FT /note="DNA polymerase catalytic subunit"
FT /id="PRO_0000046511"
FT REGION 640..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..678
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1129
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 33
FT /note="S -> G (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 102
FT /note="A -> T (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 330
FT /note="A -> R (in strain: Nonneuroinvasive mutant HF10 and
FT 17 syn+)"
FT VARIANT 646
FT /note="A -> T (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 802
FT /note="L -> F (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 905
FT /note="V -> M (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 1203
FT /note="A -> T (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 1208..1209
FT /note="TA -> AT (in strain: Nonneuroinvasive mutant HF10)"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:7LUF"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 146..157
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 179..187
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 209..215
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 221..233
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 249..259
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 266..274
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 276..285
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 299..306
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 312..318
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 340..346
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 363..372
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 386..400
FT /evidence="ECO:0007829|PDB:7LUF"
FT TURN 401..404
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 405..415
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 421..429
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 436..442
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 443..457
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 460..466
FT /evidence="ECO:0007829|PDB:7LUF"
FT TURN 467..470
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 471..481
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 490..496
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 499..502
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 514..517
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 520..524
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 525..532
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 540..547
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 557..559
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 560..565
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 568..592
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 594..605
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 609..614
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 618..632
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 707..709
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 713..720
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 721..728
FT /evidence="ECO:0007829|PDB:7LUF"
FT TURN 733..735
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 736..738
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 740..743
FT /evidence="ECO:0007829|PDB:7LUF"
FT TURN 749..751
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 752..757
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 760..765
FT /evidence="ECO:0007829|PDB:7LUF"
FT TURN 767..769
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 773..789
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 797..821
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 826..828
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 831..855
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 856..858
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 859..865
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 870..872
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 881..885
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 887..893
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 899..901
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 902..917
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 924..937
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 940..945
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 950..955
FT /evidence="ECO:0007829|PDB:7LUF"
FT TURN 956..958
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 964..979
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 981..992
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 997..999
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 1005..1007
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 1008..1022
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 1023..1026
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 1029..1031
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 1033..1036
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 1050..1060
FT /evidence="ECO:0007829|PDB:7LUF"
FT STRAND 1070..1075
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 1081..1094
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 1146..1151
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 1158..1173
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 1174..1177
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 1181..1188
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 1189..1191
FT /evidence="ECO:0007829|PDB:7LUF"
FT HELIX 1194..1196
FT /evidence="ECO:0007829|PDB:7LUF"
SQ SEQUENCE 1235 AA; 136421 MW; E8CD41D6EDED8343 CRC64;
MFSGGGGPLS PGGKSAARAA SGFFAPAGPR GASRGPPPCL RQNFYNPYLA PVGTQQKPTG
PTQRHTYYSE CDEFRFIAPR VLDEDAPPEK RAGVHDGHLK RAPKVYCGGD ERDVLRVGSG
GFWPRRSRLW GGVDHAPAGF NPTVTVFHVY DILENVEHAY GMRAAQFHAR FMDAITPTGT
VITLLGLTPE GHRVAVHVYG TRQYFYMNKE EVDRHLQCRA PRDLCERMAA ALRESPGASF
RGISADHFEA EVVERTDVYY YETRPALFYR VYVRSGRVLS YLCDNFCPAI KKYEGGVDAT
TRFILDNPGF VTFGWYRLKP GRNNTLAQPA APMAFGTSSD VEFNCTADNL AIEGGMSDLP
AYKLMCFDIE CKAGGEDELA FPVAGHPEDL VIQISCLLYD LSTTALEHVL LFSLGSCDLP
ESHLNELAAR GLPTPVVLEF DSEFEMLLAF MTLVKQYGPE FVTGYNIINF DWPFLLAKLT
DIYKVPLDGY GRMNGRGVFR VWDIGQSHFQ KRSKIKVNGM VNIDMYGIIT DKIKLSSYKL
NAVAEAVLKD KKKDLSYRDI PAYYAAGPAQ RGVIGEYCIQ DSLLVGQLFF KFLPHLELSA
VARLAGINIT RTIYDGQQIR VFTCLLRLAD QKGFILPDTQ GRFRGAGGEA PKRPAAARED
EERPEEEGED EDEREEGGGE REPEGARETA GRHVGYQGAR VLDPTSGFHV NPVVVFDFAS
LYPSIIQAHN LCFSTLSLRA DAVAHLEAGK DYLEIEVGGR RLFFVKAHVR ESLLSILLRD
WLAMRKQIRS RIPQSSPEEA VLLDKQQAAI KVVCNSVYGF TGVQHGLLPC LHVAATVTTI
GREMLLATRE YVHARWAAFE QLLADFPEAA DMRAPGPYSM RIIYGDTDSI FVLCRGLTAA
GLTAVGDKMA SHISRALFLP PIKLECEKTF TKLLLIAKKK YIGVIYGGKM LIKGVDLVRK
NNCAFINRTS RALVDLLFYD DTVSGAAAAL AERPAEEWLA RPLPEGLQAF GAVLVDAHRR
ITDPERDIQD FVLTAELSRH PRAYTNKRLA HLTVYYKLMA RRAQVPSIKD RIPYVIVAQT
REVEETVARL AALRELDAAA PGDEPAPPAA LPSPAKRPRE TPSPADPPGG ASKPRKLLVS
ELAEDPAYAI AHGVALNTDY YFSHLLGAAC VTFKALFGNN AKITESLLKR FIPEVWHPPD
DVAARLRTAG FGAVGAGATA EETRRMLHRA FDTLA
