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Reviewed, UniProtKB/Swiss-Prot P04293 (DPOL_HHV11)

Last modified November 3, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    DNA polymerase catalytic subunit
    EC=2.7.7.7
    EC=3.1.26.4
Gene names
ORF Names: UL30
OrganismHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Taxonomic identifier10299 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length1235 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

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. Ref.5

Catalytic activity

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Endonucleolytic cleavage to 5'-phosphomonoester.

Subunit structure

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.

Subcellular location

Host nucleus Potential. Note: The protein is present at discrete sites in nuclei, called replication compartments where viral DNA replication occurs By similarity.

Sequence similarities

Belongs to the DNA polymerase type-B family.

Sequence caution

The sequence CAA26941.1 differs from that shown. Reason: Frameshift at position 114.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12351235DNA polymerase catalytic subunit
PRO_0000046511

Regions

Compositional bias4 – 74Poly-Gly
Compositional bias659 – 68830Glu-rich
Compositional bias986 – 9916Poly-Ala
Compositional bias1101 – 112828Pro-rich

Natural variations

Natural variant331S → G in strain: Nonneuroinvasive mutant HF10.
Natural variant1021A → T in strain: Nonneuroinvasive mutant HF10.
Natural variant3301A → R in strain: Nonneuroinvasive mutant HF10 and 17 syn+.
Natural variant6461A → T in strain: Nonneuroinvasive mutant HF10.
Natural variant8021L → F in strain: Nonneuroinvasive mutant HF10.
Natural variant9051V → M in strain: Nonneuroinvasive mutant HF10.
Natural variant12031A → T in strain: Nonneuroinvasive mutant HF10.
Natural variant1208 – 12092TA → AT in strain: Nonneuroinvasive mutant HF10.

Sequences

Sequence LengthMass (Da)Tools
P04293-1 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: E8CD41D6EDED8343

FASTA1,235136,421
        10         20         30         40         50         60 
MFSGGGGPLS PGGKSAARAA SGFFAPAGPR GASRGPPPCL RQNFYNPYLA PVGTQQKPTG 

        70         80         90        100        110        120 
PTQRHTYYSE CDEFRFIAPR VLDEDAPPEK RAGVHDGHLK RAPKVYCGGD ERDVLRVGSG 

       130        140        150        160        170        180 
GFWPRRSRLW GGVDHAPAGF NPTVTVFHVY DILENVEHAY GMRAAQFHAR FMDAITPTGT 

       190        200        210        220        230        240 
VITLLGLTPE GHRVAVHVYG TRQYFYMNKE EVDRHLQCRA PRDLCERMAA ALRESPGASF 

       250        260        270        280        290        300 
RGISADHFEA EVVERTDVYY YETRPALFYR VYVRSGRVLS YLCDNFCPAI KKYEGGVDAT 

       310        320        330        340        350        360 
TRFILDNPGF VTFGWYRLKP GRNNTLAQPA APMAFGTSSD VEFNCTADNL AIEGGMSDLP 

       370        380        390        400        410        420 
AYKLMCFDIE CKAGGEDELA FPVAGHPEDL VIQISCLLYD LSTTALEHVL LFSLGSCDLP 

       430        440        450        460        470        480 
ESHLNELAAR GLPTPVVLEF DSEFEMLLAF MTLVKQYGPE FVTGYNIINF DWPFLLAKLT 

       490        500        510        520        530        540 
DIYKVPLDGY GRMNGRGVFR VWDIGQSHFQ KRSKIKVNGM VNIDMYGIIT DKIKLSSYKL 

       550        560        570        580        590        600 
NAVAEAVLKD KKKDLSYRDI PAYYAAGPAQ RGVIGEYCIQ DSLLVGQLFF KFLPHLELSA 

       610        620        630        640        650        660 
VARLAGINIT RTIYDGQQIR VFTCLLRLAD QKGFILPDTQ GRFRGAGGEA PKRPAAARED 

       670        680        690        700        710        720 
EERPEEEGED EDEREEGGGE REPEGARETA GRHVGYQGAR VLDPTSGFHV NPVVVFDFAS 

       730        740        750        760        770        780 
LYPSIIQAHN LCFSTLSLRA DAVAHLEAGK DYLEIEVGGR RLFFVKAHVR ESLLSILLRD 

       790        800        810        820        830        840 
WLAMRKQIRS RIPQSSPEEA VLLDKQQAAI KVVCNSVYGF TGVQHGLLPC LHVAATVTTI 

       850        860        870        880        890        900 
GREMLLATRE YVHARWAAFE QLLADFPEAA DMRAPGPYSM RIIYGDTDSI FVLCRGLTAA 

       910        920        930        940        950        960 
GLTAVGDKMA SHISRALFLP PIKLECEKTF TKLLLIAKKK YIGVIYGGKM LIKGVDLVRK 

       970        980        990       1000       1010       1020 
NNCAFINRTS RALVDLLFYD DTVSGAAAAL AERPAEEWLA RPLPEGLQAF GAVLVDAHRR 

      1030       1040       1050       1060       1070       1080 
ITDPERDIQD FVLTAELSRH PRAYTNKRLA HLTVYYKLMA RRAQVPSIKD RIPYVIVAQT 

      1090       1100       1110       1120       1130       1140 
REVEETVARL AALRELDAAA PGDEPAPPAA LPSPAKRPRE TPSPADPPGG ASKPRKLLVS 

      1150       1160       1170       1180       1190       1200 
ELAEDPAYAI AHGVALNTDY YFSHLLGAAC VTFKALFGNN AKITESLLKR FIPEVWHPPD 

      1210       1220       1230 
DVAARLRTAG FGAVGAGATA EETRRMLHRA FDTLA 

« Hide

References

« Hide 'large scale' references
[1]"The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1."
McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D., Perry L.J., Scott J.E., Taylor P.
J. Gen. Virol. 69:1531-1574(1988) [PubMed: 2839594] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"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."
Quinn J.P., McGeoch D.J.
Nucleic Acids Res. 13:8143-8163(1985) [PubMed: 2999714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Determination and analysis of the DNA sequence of highly attenuated herpes simplex virus type 1 mutant HF10, a potential oncolytic virus."
Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.
Microbes Infect. 9:142-149(2007) [PubMed: 17218138] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Nonneuroinvasive mutant HF10.
[4]"Herpes simplex virus type 1 bacterial artificial chromosome."
Cunningham C., Davison A.J.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 17 syn+.
[5]"Herpes simplex-1 DNA polymerase. Identification of an intrinsic 5'----3' exonuclease with ribonuclease H activity."
Crute J.J., Lehman I.R.
J. Biol. Chem. 264:19266-19270(1989) [PubMed: 2553735] [Abstract]
Cited for: FUNCTION.
[6]"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."
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.
J. Virol. 71:6390-6397(1997) [PubMed: 9261356] [Abstract]
Cited for: INTERACTION WITH UL8.

Cross-references

Sequence databases

X14112 Genomic DNA. Translation: CAA32323.1.
X03181 Genomic DNA. Translation: CAA26941.1. Frameshift.
DQ889502 Genomic DNA. Translation: ABI63492.1.
FJ593289 Genomic DNA. Translation: ACM62253.1.
PIRDJBEV1. A00715.
DJBEH7. C30085.
RefSeqNP_044632.1.

3D structure databases

SMRP04293. Positions 60-640, 700-1110.
ModBaseSearch...

Genome annotation databases

GeneID2703462.

Family and domain databases

InterProIPR006172. DNA-dir_DNA_pol_B.
IPR006134. DNA-dir_DNA_pol_B_cons-reg.
IPR017966. DNA-dir_DNA_pol_B_cons_reg2.
IPR017964. DNA-dir_DNA_pol_B_CS.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
[Graphical view]
PANTHERPTHR10322. DNA_pol_B. 1 hit.
PfamPF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo. 1 hit.
[Graphical view]
PRINTSPR00106. DNAPOLB.
SMARTSM00486. POLBc. 1 hit.
[Graphical view]
PROSITEPS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00787. Aciclovir.
DB00426. Famciclovir.
DB00529. Foscarnet.
DB01004. Ganciclovir.
DB00249. Idoxuridine.
DB00299. Penciclovir.
DB00432. Trifluridine.
DB00577. Valaciclovir.
DB01610. Valganciclovir.

Entry information

Entry nameDPOL_HHV11
AccessionPrimary (citable) accession number: P04293
Secondary accession number(s): B9VQF8, Q09IA3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: July 1, 1989
Last modified: November 3, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectVirus (Virus annotation project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents