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P07917 (DPOL_HHV1A) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 80. 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 Angelotti) (HHV-1) (Human herpes simplex virus 1)
Taxonomic identifier10301 [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_0000046512

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
P07917 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 4CDB3B8AE73663BF

FASTA1,235136,603
        10         20         30         40         50         60 
MFSGGGGPLS PGGKSAARAA SGFFVPAGPR 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 VPMAFGTSSD VEFNCTADNL AIEGGMSDLP 

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

       430        440        450        460        470        480 
ESHLTELAAR 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 AALRELDATA PGDEPAPPAA LPCPAKRPRE TPSHADPPGG ASKPRKLLVS 

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

      1210       1220       1230 
DVAARLRAAG FGAVGAGATA EETRRMLHRA FDTLA

« Hide

References

[1]"Nucleotide sequence of the DNA polymerase gene of herpes simplex virus type 1 strain Angelotti."
Knopf C.W.
Nucleic Acids Res. 14:8225-8226(1986) [PubMed: 3022246] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The extended left-handed helix: a simple nucleic acid-binding motif."
Hicks J.M., Hsu V.L.
Proteins 55:330-338(2004) [PubMed: 15048824] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1200-1235.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X04495 Genomic DNA. Translation: CAA28183.1.
PIRDJBEAN. A25552.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DMLX-ray2.70B/D/F/H1200-1235[»]
ProteinModelPortalP07917.
SMRP07917. Positions 59-639, 1200-1235.
ModBaseSearch...

Protein-protein interaction databases

IntActP07917. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

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]
Gene3DG3DSA:3.90.1600.10. DNA_pol_palm_dom. 2 hits.
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...

Entry information

Entry nameDPOL_HHV1A
AccessionPrimary (citable) accession number: P07917
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: December 14, 2011
This is version 80 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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