AC   PRU00275;
DC   Domain;
TR   PROSITE; PS50175; ASP_PROT_RETROV; 1; level=0
XX
Names: Eukaryotic and viral aspartyl proteases
Function: Belongs to peptidase family A2
XX
case <OS:Human immunodeficiency virus 1> and <FTTag:act_site>
DE   + RecName: EC=3.4.23.16;
else case <OS:Human immunodeficiency virus 2> and <FTTag:act_site>
DE   + RecName: EC=3.4.23.47;
else case <FTTag:act_site>
DE   + RecName: EC=3.4.23.-;
end case
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case <OS:Human immunodeficiency virus 1>
CC   -!- FUNCTION: The aspartyl protease mediates proteolytic cleavages of Gag
CC       and Gag-Pol polyproteins during or shortly after the release of the
CC       virion from the plasma membrane. Cleavages take place as an ordered,
CC       step-wise cascade to yield mature proteins. This process is called
CC       maturation. Displays maximal activity during the budding process just
CC       prior to particle release from the cell. Also cleaves Nef and Vif,
CC       probably concomitantly with viral structural proteins on maturation of
CC       virus particles.
else case <OC:Retroviridae>
CC   -!- FUNCTION: The aspartyl protease mediates proteolytic cleavages of Gag
CC       and Gag-Pol polyproteins during or shortly after the release of the
CC       virion from the plasma membrane. Cleavages take place as an ordered,
CC       step-wise cascade to yield mature proteins. This process is called
CC       maturation. Displays maximal activity during the budding process just
CC       prior to particle release from the cell.
end case
case <OS:Human immunodeficiency virus 1> and <FTTag:act_site>
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Specific for a P1 residue that is hydrophobic, and P1'
CC         variable, but often Pro.; EC=3.4.23.16;
else case <OS:Human immunodeficiency virus 2> and <FTTag:act_site>
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endopeptidase for which the P1 residue is preferably
CC         hydrophobic.; EC=3.4.23.47;
end case
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DR   PROSITE; PS00141; ASP_PROTEASE; 1; trigger=no
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case <FTTag:act_site>
GO   GO:0004190; F:aspartic-type endopeptidase activity
GO   GO:0016787; F:hydrolase activity
GO   GO:0008233; F:peptidase activity
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KW   Aspartyl protease
KW   Hydrolase
KW   Protease
end case
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FT   From: PS50175
FT   DOMAIN          from..to
FT                   /note="Peptidase A2 #"
case <OC:Retroviridae>
FT   ACT_SITE        6
FT                   /note="Protease; shared with dimeric partner"
FT   Tag: act_site; Condition: D
else
FT   ACT_SITE        6
FT                   /note="@TARGET_ACTIVITY_VISIBILITY|For protease activity@"
FT   Tag: act_site; Condition: D
end case
XX
Chop: Nter=0; Cter=0;
Size: 40-82;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P51518;
Scope:
 Eukaryota
 Viruses
Comments: None
XX
# Revision 1.20 2019/11/21
//