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Protein

Shutoff alkaline exonuclease

Gene

BGLF5

Organism
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in processing non linear or branched viral DNA intermediates in order to promote the production of mature packaged unit-length linear progeny viral DNA molecules. Exhibits endonuclease and exonuclease activities and accepts both double-stranded and single-stranded DNA as substrate. Exonuclease digestion of DNA is in the 5'-> 3' direction and the products are 5'-monophosphate nucleosides. Additionally, forms a recombinase with the major DNA-binding protein, which displays strand exchange activity. Also acts as a cytoplasmic RNA endonuclease that induces degradation of the majority of the cellular messenger RNAs during early lytic infection. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and evasion from host immune response. Internally cleaves host mRNAs which are then degraded by the cellular exonuclease XRN1. Bypasses therefore the regulatory steps of deadenylation and decapping normally required for XRN1 activation.UniRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei166Required for functionUniRule annotation1
Sitei203Required for functionUniRule annotation1
Sitei225Required for functionUniRule annotation1
Sitei227Required for functionUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Decay of host mRNAs by virus, Eukaryotic host gene expression shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Shutoff alkaline exonucleaseUniRule annotation (EC:3.1.-.-UniRule annotation)
Short name:
SOXUniRule annotation
Gene namesi
ORF Names:BGLF5
OrganismiEpstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Taxonomic identifieri10377 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeLymphocryptovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000007640 Componenti: Genome

Subcellular locationi

  • Host nucleus UniRule annotation
  • Host cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi452F → A: 98% loss of nuclease activity. 1 Publication1
Mutagenesisi458V → A: 80% loss of nuclease activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001157001 – 470Shutoff alkaline exonucleaseAdd BLAST470

Expressioni

Keywords - Developmental stagei

Early protein

Interactioni

Subunit structurei

Forms a complex with the DNA polymerase BALF5, the DNA polymerase processivity factor BMRF1, and the major DNA binding protein BALF2.UniRule annotation1 Publication

Protein-protein interaction databases

BioGridi971815. 1 interactor.

Structurei

Secondary structure

1470
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi12 – 14Combined sources3
Helixi19 – 23Combined sources5
Helixi26 – 33Combined sources8
Beta strandi36 – 38Combined sources3
Helixi43 – 56Combined sources14
Turni57 – 59Combined sources3
Helixi64 – 71Combined sources8
Helixi84 – 92Combined sources9
Helixi96 – 110Combined sources15
Helixi117 – 123Combined sources7
Beta strandi127 – 129Combined sources3
Helixi132 – 138Combined sources7
Helixi141 – 144Combined sources4
Helixi158 – 175Combined sources18
Turni176 – 180Combined sources5
Turni193 – 195Combined sources3
Beta strandi196 – 200Combined sources5
Beta strandi203 – 211Combined sources9
Beta strandi214 – 228Combined sources15
Helixi230 – 232Combined sources3
Helixi243 – 251Combined sources9
Helixi255 – 262Combined sources8
Beta strandi265 – 267Combined sources3
Beta strandi269 – 272Combined sources4
Beta strandi284 – 287Combined sources4
Helixi290 – 292Combined sources3
Helixi307 – 316Combined sources10
Beta strandi320 – 326Combined sources7
Turni329 – 334Combined sources6
Beta strandi338 – 345Combined sources8
Helixi353 – 370Combined sources18
Turni371 – 373Combined sources3
Beta strandi384 – 393Combined sources10
Beta strandi397 – 399Combined sources3
Beta strandi404 – 406Combined sources3
Beta strandi413 – 415Combined sources3
Beta strandi417 – 425Combined sources9
Helixi430 – 449Combined sources20
Helixi460 – 462Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2W45X-ray3.00A/B1-470[»]
2W4BX-ray3.50A/B1-470[»]
ProteinModelPortaliP03217.
SMRiP03217.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03217.

Family & Domainsi

Sequence similaritiesi

Belongs to the herpesviridae alkaline nuclease family.UniRule annotation

Family and domain databases

Gene3Di3.90.320.10. 1 hit.
HAMAPiMF_04009. HSV_AN. 1 hit.
InterProiIPR011604. Exonuc_phg/RecB_C.
IPR001616. Herpes_alk_exo.
IPR011335. Restrct_endonuc-II-like.
[Graphical view]
PfamiPF01771. Herpes_alk_exo. 1 hit.
[Graphical view]
PRINTSiPR00924. ALKEXNUCLASE.
SUPFAMiSSF52980. SSF52980. 1 hit.

Sequencei

Sequence statusi: Complete.

P03217-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADVDELEDP MEEMTSYTFA RFLRSPETEA FVRNLDRPPQ MPAMRFVYLY
60 70 80 90 100
CLCKQIQEFS GETGFCDFVS SLVQENDSKD GPSLKSIYWG LQEATDEQRT
110 120 130 140 150
VLCSYVESMT RGQSENLMWD ILRNGIISSS KLLSTIKNGP TKVFEPAPIS
160 170 180 190 200
TNHYFGGPVA FGLRCEDTVK DIVCKLICGD ASANRQFGFM ISPTDGIFGV
210 220 230 240 250
SLDLCVNVES QGDFILFTDR SCIYEIKCRF KYLFSKSEFD PIYPSYTALY
260 270 280 290 300
KRPCKRSFIR FINSIARPTV EYVPDGRLPS EGDYLLTQDE AWNLKDVRKR
310 320 330 340 350
KLGPGHDLVA DSLAANRGVE SMLYVMTDPS ENAGRIGIKD RVPVNIFINP
360 370 380 390 400
RHNYFYQVLL QYKIVGDYVR HSGGGKPGRD CSPRVNIVTA FFRKRSPLDP
410 420 430 440 450
ATCTLGSDLL LDASVEIPVA VLVTPVVLPD SVIRKTLSTA AGSWKAYADN
460 470
TFDTAPWVPS GLFADDESTP
Length:470
Mass (Da):52,667
Last modified:July 21, 1986 - v1
Checksum:i81C2048E8A65CE80
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24827.1.
AJ507799 Genomic DNA. Translation: CAD53437.1.
PIRiA03779. QQBE37.
RefSeqiYP_401687.1. NC_007605.1.

Genome annotation databases

GeneIDi3783773.
KEGGivg:3783773.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24827.1.
AJ507799 Genomic DNA. Translation: CAD53437.1.
PIRiA03779. QQBE37.
RefSeqiYP_401687.1. NC_007605.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2W45X-ray3.00A/B1-470[»]
2W4BX-ray3.50A/B1-470[»]
ProteinModelPortaliP03217.
SMRiP03217.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi971815. 1 interactor.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3783773.
KEGGivg:3783773.

Miscellaneous databases

EvolutionaryTraceiP03217.

Family and domain databases

Gene3Di3.90.320.10. 1 hit.
HAMAPiMF_04009. HSV_AN. 1 hit.
InterProiIPR011604. Exonuc_phg/RecB_C.
IPR001616. Herpes_alk_exo.
IPR011335. Restrct_endonuc-II-like.
[Graphical view]
PfamiPF01771. Herpes_alk_exo. 1 hit.
[Graphical view]
PRINTSiPR00924. ALKEXNUCLASE.
SUPFAMiSSF52980. SSF52980. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAN_EBVB9
AccessioniPrimary (citable) accession number: P03217
Secondary accession number(s): Q777D2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.