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DNA polymerase catalytic subunit (EC 2.7.7.7) (EC 3.1.26.4)

 DPOL_HHV11              Reviewed;        1235 AA.
P04293; B9VQF8; Q09IA3;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 2.
22-NOV-2017, entry version 118.
RecName: Full=DNA polymerase catalytic subunit;
EC=2.7.7.7;
EC=3.1.26.4;
ORFNames=UL30;
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus
1).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Alphaherpesvirinae; Simplexvirus.
NCBI_TaxID=10299;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C.,
McNab D., Perry L.J., Scott J.E., Taylor P.;
"The complete DNA sequence of the long unique region in the genome of
herpes simplex virus type 1.";
J. Gen. Virol. 69:1531-1574(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2999714; DOI=10.1093/nar/13.22.8143;
Quinn J.P., McGeoch D.J.;
"DNA sequence of the region in the genome of herpes simplex virus type
1 containing the genes for DNA polymerase and the major DNA binding
protein.";
Nucleic Acids Res. 13:8143-8163(1985).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Nonneuroinvasive mutant HF10;
PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019;
Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.;
"Determination and analysis of the DNA sequence of highly attenuated
herpes simplex virus type 1 mutant HF10, a potential oncolytic
virus.";
Microbes Infect. 9:142-149(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=17 syn+;
Cunningham C., Davison A.J.;
"Herpes simplex virus type 1 bacterial artificial chromosome.";
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION.
PubMed=2553735;
Crute J.J., Lehman I.R.;
"Herpes simplex-1 DNA polymerase. Identification of an intrinsic
5'----3' exonuclease with ribonuclease H activity.";
J. Biol. Chem. 264:19266-19270(1989).
[6]
INTERACTION WITH UL8.
PubMed=9261356;
Marsden H.S., McLean G.W., Barnard E.C., Francis G.J., MacEachran K.,
Murphy M., McVey G., Cross A., Abbotts A.P., Stow N.D.;
"The catalytic subunit of the DNA polymerase of herpes simplex virus
type 1 interacts specifically with the C terminus of the UL8 component
of the viral helicase-primase complex.";
J. Virol. 71:6390-6397(1997).
-!- FUNCTION: Replicates viral genomic DNA. The replication complex is
composed of six viral proteins: the DNA polymerase, processivity
factor, primase, primase-associated factor, helicase, and ssDNA-
binding protein. Additionally, the polymerase contains an
intrinsic ribonuclease H (RNase H) activity that specifically
degrades RNA/DNA heteroduplexes or duplex DNA substrates in the 5'
to 3' direction. Therefore, it can catalyze the excision of the
RNA primers that initiate the synthesis of Okazaki fragments at a
replication fork during viral DNA replication.
{ECO:0000269|PubMed:2553735}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1).
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphomonoester.
-!- SUBUNIT: Forms a complex with the ssDNA-binding protein UL29, the
DNA polymerase processivity factor, and the alkaline exonuclease.
Interacts with the putative helicase-primase complex subunit UL8;
this interaction may coordinate leading and lagging strand DNA
synthesis at the replication fork (By similarity). {ECO:0000250}.
-!- INTERACTION:
P10226:UL42; NbExp=3; IntAct=EBI-8615017, EBI-1029310;
P10192:UL8; NbExp=4; IntAct=EBI-8615017, EBI-7185538;
-!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000305}. Note=The protein
is present at discrete sites in nuclei, called replication
compartments where viral DNA replication occurs. {ECO:0000250}.
-!- SIMILARITY: Belongs to the DNA polymerase type-B family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA26941.1; Type=Frameshift; Positions=114; Evidence={ECO:0000305};
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EMBL; X14112; CAA32323.1; -; Genomic_DNA.
EMBL; X03181; CAA26941.1; ALT_FRAME; Genomic_DNA.
EMBL; DQ889502; ABI63492.1; -; Genomic_DNA.
EMBL; FJ593289; ACM62253.1; -; Genomic_DNA.
PIR; A00715; DJBEV1.
PIR; C30085; DJBEH7.
RefSeq; YP_009137105.1; NC_001806.2.
ProteinModelPortal; P04293; -.
SMR; P04293; -.
BioGrid; 971473; 3.
IntAct; P04293; 2.
MINT; MINT-6732532; -.
BindingDB; P04293; -.
ChEMBL; CHEMBL1872; -.
DrugBank; DB00787; Aciclovir.
DrugBank; DB00426; Famciclovir.
DrugBank; DB00529; Foscarnet.
DrugBank; DB01004; Ganciclovir.
DrugBank; DB00299; Penciclovir.
DrugBank; DB00577; Valaciclovir.
PRIDE; P04293; -.
GeneID; 2703462; -.
KEGG; vg:2703462; -.
KO; K18964; -.
OrthoDB; VOG0900001M; -.
PRO; PR:P04293; -.
Proteomes; UP000009294; Genome.
Proteomes; UP000180652; Genome.
GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
GO; GO:0008409; F:5'-3' exonuclease activity; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0034061; F:DNA polymerase activity; IDA:AgBase.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IDA:UniProtKB.
GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; IDA:UniProtKB.
Gene3D; 3.30.420.10; -; 1.
Gene3D; 3.90.1600.10; -; 1.
InterPro; IPR006172; DNA-dir_DNA_pol_B.
InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
InterPro; IPR023211; DNA_pol_palm_dom_sf.
InterPro; IPR021639; DNAPolymera_Pol_C.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR036397; RNaseH_sf.
Pfam; PF00136; DNA_pol_B; 1.
Pfam; PF03104; DNA_pol_B_exo1; 1.
Pfam; PF11590; DNAPolymera_Pol; 1.
PRINTS; PR00106; DNAPOLB.
SMART; SM00486; POLBc; 1.
SUPFAM; SSF53098; SSF53098; 2.
PROSITE; PS00116; DNA_POLYMERASE_B; 1.
1: Evidence at protein level;
Complete proteome; DNA replication; DNA-binding;
DNA-directed DNA polymerase; Endonuclease; Host nucleus; Hydrolase;
Multifunctional enzyme; Nuclease; Nucleotidyltransferase;
Reference proteome; Transferase; Viral DNA replication.
CHAIN 1 1235 DNA polymerase catalytic subunit.
/FTId=PRO_0000046511.
COMPBIAS 4 7 Poly-Gly.
COMPBIAS 659 688 Glu-rich.
COMPBIAS 986 991 Poly-Ala.
COMPBIAS 1101 1128 Pro-rich.
VARIANT 33 33 S -> G (in strain: Nonneuroinvasive
mutant HF10).
VARIANT 102 102 A -> T (in strain: Nonneuroinvasive
mutant HF10).
VARIANT 330 330 A -> R (in strain: Nonneuroinvasive
mutant HF10 and 17 syn+).
VARIANT 646 646 A -> T (in strain: Nonneuroinvasive
mutant HF10).
VARIANT 802 802 L -> F (in strain: Nonneuroinvasive
mutant HF10).
VARIANT 905 905 V -> M (in strain: Nonneuroinvasive
mutant HF10).
VARIANT 1203 1203 A -> T (in strain: Nonneuroinvasive
mutant HF10).
VARIANT 1208 1209 TA -> AT (in strain: Nonneuroinvasive
mutant HF10).
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


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