AC   MF_04009;
DC   Protein; auto
TR   HAMAP; MF_04009; -; 1; level=0
XX
Names: HSV_AN
XX
ID   AN
case <OC:Gammaherpesvirinae>
DE   RecName: Full=Shutoff alkaline exonuclease;
DE            Short=SOX;
DE            EC=3.1.-.-;
else
DE   RecName: Full=Alkaline nuclease;
DE            EC=3.1.-.-;
end case
XX
case <OC:Gammaherpesvirinae>
CC   -!- FUNCTION: Plays a role in processing non linear or branched viral DNA
CC       intermediates in order to promote the production of mature packaged
CC       unit-length linear progeny viral DNA molecules. Exhibits endonuclease
CC       and exonuclease activities and accepts both double-stranded and single-
CC       stranded DNA as substrate. Exonuclease digestion of DNA is in the 5'->
CC       3' direction and the products are 5'-monophosphate nucleosides.
CC       Additionally, forms a recombinase with the major DNA-binding protein,
CC       which displays strand exchange activity. Also acts as a cytoplasmic RNA
CC       endonuclease that induces degradation of the majority of the cellular
CC       messenger RNAs during early lytic infection. The resulting inhibition
CC       of cellular protein synthesis serves to ensure maximal viral gene
CC       expression and evasion from host immune response. Internally cleaves
CC       host mRNAs which are then degraded by the cellular exonuclease XRN1.
CC       Bypasses therefore the regulatory steps of deadenylation and decapping
CC       normally required for XRN1 activation.
else
CC   -!- FUNCTION: Plays a role in processing non linear or branched viral DNA
CC       intermediates in order to promote the production of mature packaged
CC       unit-length linear progeny viral DNA molecules. Exhibits endonuclease
CC       and exonuclease activities and accepts both double-stranded and single-
CC       stranded DNA as substrate. Exonuclease digestion of DNA is in the 5'->
CC       3' direction and the products are 5'-monophosphate nucleosides.
CC       Additionally, forms a recombinase with the major DNA-binding protein,
CC       which displays strand exchange activity.
end case
case <OC:Gammaherpesvirinae>
CC   -!- SUBUNIT: Forms a complex with the DNA polymerase, the DNA polymerase
CC       processivity factor, and the major DNA binding protein.
else
CC   -!- SUBUNIT: Interacts with major DNA-binding protein; this interaction
CC       increases the nuclease processivity of the alkaline exonuclease.
end case
CC   -!- SUBCELLULAR LOCATION: Host nucleus. Host cytoplasm.
CC   -!- SIMILARITY: Belongs to the herpesviridae alkaline nuclease family.
XX
DR   Pfam; PF01771; Herpes_alk_exo; 1; trigger=no
DR   PRINTS; PR00924; ALKEXNUCLASE; 1; trigger=no
XX
KW   Endonuclease
KW   Exonuclease
KW   Host cytoplasm
KW   Host nucleus
KW   Host-virus interaction
KW   Hydrolase
KW   Nuclease
XX
case <OC:Gammaherpesvirinae>
GO   GO:0030430; C:host cell cytoplasm
GO   GO:0042025; C:host cell nucleus
GO   GO:0003677; F:DNA binding
GO   GO:0004519; F:endonuclease activity
GO   GO:0004527; F:exonuclease activity
GO   GO:0004518; F:nuclease activity
GO   GO:0090304; P:nucleic acid metabolic process
GO   GO:0016032; P:viral process
GO   GO:0003723; F:RNA binding
GO   GO:0039595; P:induction by virus of catabolism of host mRNA
GO   GO:0039657; P:suppression by virus of host gene expression
else
GO   GO:0030430; C:host cell cytoplasm
GO   GO:0042025; C:host cell nucleus
GO   GO:0003677; F:DNA binding
GO   GO:0004519; F:endonuclease activity
GO   GO:0004527; F:exonuclease activity
GO   GO:0004518; F:nuclease activity
GO   GO:0090304; P:nucleic acid metabolic process
GO   GO:0016032; P:viral process
end case
XX
FT   From: AN_HHV11 (P04294)
FT   SITE            280
FT                   /note="Required for function"
FT   Condition: E
FT   SITE            340
FT                   /note="Required for function"
FT   Condition: D
FT   SITE            364
FT                   /note="Required for function"
FT   Condition: E
FT   SITE            366
FT                   /note="Required for function"
FT   Condition: K
XX
Size: 470-626;
Related: None;
Template: P04294; Q2HR95; P03217;
Scope:
 Viruses; Herpesviridae
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.6 2023/12/15
//