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Protein

Shutoff alkaline exonuclease

Gene
N/A
Organism
Human herpesvirus 8 type M
Status
Unreviewed-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 annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi184MagnesiumCombined sources1
Sitei184Required for functionUniRule annotation1
Metal bindingi221MagnesiumCombined sources1
Sitei221Required for functionUniRule annotation1
Metal bindingi244MagnesiumCombined sources1
Sitei244Required for functionUniRule annotation1
Metal bindingi245Magnesium; via carbonyl oxygenCombined sources1
Sitei246Required for functionUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionEndonucleaseUniRule annotation, ExonucleaseUniRule annotation, Hydrolase, Nuclease
Biological processHost-virus interactionUniRule annotation
LigandMagnesiumCombined sources, Metal-bindingCombined sources

Names & Taxonomyi

Protein namesi
Recommended name:
Shutoff alkaline exonucleaseUniRule annotation (EC:3.1.-.-UniRule annotation)
Short name:
SOXUniRule annotation
OrganismiHuman herpesvirus 8 type MImported
Taxonomic identifieri435895 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeRhadinovirus

Subcellular locationi

  • Host nucleus UniRule annotation
  • Host cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Host cytoplasmUniRule annotation, Host nucleusUniRule annotation

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi183 ↔ 247Combined sources

Interactioni

Subunit structurei

Forms a complex with the DNA polymerase, the DNA polymerase processivity factor, and the major DNA binding protein.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
P889392EBI-7922402,EBI-7922395

Protein-protein interaction databases

IntActiP88925. 3 interactors.
MINTiMINT-2824695.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FHDX-ray1.85A1-486[»]
3POVX-ray2.50A1-486[»]
5HSWX-ray3.30A1-486[»]
ProteinModelPortaliP88925.
SMRiP88925.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP88925.

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.
InterProiView protein in InterPro
IPR011604. Exonuc_phg/RecB_C.
IPR001616. Herpes_alk_exo.
IPR011335. Restrct_endonuc-II-like.
IPR034720. Viral_alk_exo.
PfamiView protein in Pfam
PF01771. Herpes_alk_exo. 1 hit.
PRINTSiPR00924. ALKEXNUCLASE.
SUPFAMiSSF52980. SSF52980. 1 hit.

Sequencei

Sequence statusi: Complete.

P88925-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEATPTPADL FSEDYLVDTL DGLTVDDQQA VLASLSFSKF LKHAKVRDWC
60 70 80 90 100
AQAKIQPSMP ALRMAYNYFL FSKVGEFIGS EDVCNFFVDR VFGGVRLLDV
110 120 130 140 150
ASVYAACSQM NAHQRHHICC LVERATSSQS LNPVWDALRD GIISSSKFHW
160 170 180 190 200
AVKQQNTSKK IFSPWPITNN HFVAGPLAFG LRCEEVVKTL LATLLHPDET
210 220 230 240 250
NCLDYGFMQS PQNGIFGVSL DFAANVKTDT EGRLQFDPNC KVYEIKCRFK
260 270 280 290 300
YTFAKMECDP IYAAYQRLYE APGKLALKDF FYSISKPAVE YVGLGKLPSE
310 320 330 340 350
SDYLVAYDQE WEACPRKKRK LTPLHNLIRE CILHNSTTES DVYVLTDPQD
360 370 380 390 400
TRGQISIKAR FKANLFVNVR HSYFYQVLLQ SSIVEEYIGL DSGIPRLGSP
410 420 430 440 450
KYYIATGFFR KRGYQDPVNC TIGGDALDPH VEIPTLLIVT PVYFPRGAKH
460 470 480
RLLHQAANFW SRSAKDTFPY IKWDFSYLSA NVPHSP
Length:486
Mass (Da):55,106
Last modified:May 1, 1997 - v1
Checksum:iBC8A46991065AF9E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U75698 Genomic DNA. Translation: AAC57119.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U75698 Genomic DNA. Translation: AAC57119.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FHDX-ray1.85A1-486[»]
3POVX-ray2.50A1-486[»]
5HSWX-ray3.30A1-486[»]
ProteinModelPortaliP88925.
SMRiP88925.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP88925. 3 interactors.
MINTiMINT-2824695.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP88925.

Family and domain databases

Gene3Di3.90.320.10. 1 hit.
HAMAPiMF_04009. HSV_AN. 1 hit.
InterProiView protein in InterPro
IPR011604. Exonuc_phg/RecB_C.
IPR001616. Herpes_alk_exo.
IPR011335. Restrct_endonuc-II-like.
IPR034720. Viral_alk_exo.
PfamiView protein in Pfam
PF01771. Herpes_alk_exo. 1 hit.
PRINTSiPR00924. ALKEXNUCLASE.
SUPFAMiSSF52980. SSF52980. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiP88925_HHV8
AccessioniPrimary (citable) accession number: P88925
Entry historyiIntegrated into UniProtKB/TrEMBL: May 1, 1997
Last sequence update: May 1, 1997
Last modified: May 10, 2017
This is version 74 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.