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P04292 (DPOL_HHV1K) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 KOS) (HHV-1) (Human herpes simplex virus 1)
Taxonomic identifier10306 [NCBI]
Taxonomic lineageViruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Simplexvirus ›
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length1235 AA.
Sequence statusComplete.
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 By similarity.

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12351235DNA polymerase catalytic subunit
PRO_0000046513

Regions

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

Secondary structure

1 .................................................................................................................................................................. 1235
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04292 [UniParc].

Last modified March 20, 1987. Version 1.
Checksum: 90415EF72ED2A607

FASTA1,235136,520
        10         20         30         40         50         60 
MFSGGGGPLS PGGKSAARAA SGFFAPAGPR GAGRGPPPCL 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 GRNNTLAQPR 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 PAYYATGPAQ RGVIGEYCIQ DSLLVGQLFF KFLPHLELSA 

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

       670        680        690        700        710        720 
EERPEEEGED EDEREEGGGE REPEGARETA GRHVGYQGAK 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 
GLTAMGDKMA 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 TPSHADPPGG ASKPRKLLVS 

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

      1210       1220       1230 
DVAARLRAAG FGAVGAGATA EETRRMLHRA FDTLA

« Hide

References

[1]"Sequence and mapping analyses of the herpes simplex virus DNA polymerase gene predict a C-terminal substrate binding domain."
Gibbs J.S., Chiou H.C., Hall J.D., Mount D.W., Retondo M.J., Weller S.K., Coen D.M.
Proc. Natl. Acad. Sci. U.S.A. 82:7969-7973(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A point mutation in a herpesvirus polymerase determines neuropathogenicity."
Goodman L.B., Loregian A., Perkins G.A., Nugent J., Buckles E.L., Mercorelli B., Kydd J.H., Palu G., Smith K.C., Osterrieder N., Davis-Poynter N.
PLoS Pathog. 3:E160-E160(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 43-1235.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M10792 Genomic DNA. Translation: AAA66438.1.
PIRDJBEK1. A00714.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GV9X-ray2.68A/B43-1235[»]
ProteinModelPortalP04292.
SMRP04292. Positions 59-639, 1200-1235.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.90.1600.10. 2 hits.
InterProIPR006172. DNA-dir_DNA_pol_B.
IPR017964. DNA-dir_DNA_pol_B_CS.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR023211. DNA_pol_palm_dom.
IPR021639. DNAPolymera_Pol_C.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamPF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
PF11590. DNAPolymera_Pol. 1 hit.
[Graphical view]
PRINTSPR00106. DNAPOLB.
SMARTSM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMSSF53098. RNaseH_fold. 1 hit.
PROSITEPS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP04292.
ChEMBLCHEMBL5944.
EvolutionaryTraceP04292.

Entry information

Entry nameDPOL_HHV1K
AccessionPrimary (citable) accession number: P04292
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: April 3, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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