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HAMAP rule MF_04059

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General rule information [?]

Accession MF_04059
Dates 16-MAR-2017 (Created)
4-JUN-2021 (Last updated, Version 7)
Scope(s) Viruses
Template(s) P03252 (PRO_ADE02); [ Recover all ]
Triggered by HAMAP; MF_04059 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier PRO
Protein name RecName: Full=Protease;
AltName: Full=Adenain;
AltName: Full=Adenovirus protease;
AltName: Full=Adenovirus proteinase;
AltName: Full=Endoprotease;
Gene name Name=L3;

Comments [?]

FUNCTIONCleaves viral precursor proteins (pTP, pIIIa, pVI, pVII, pVIII, and pX) inside newly assembled particles giving rise to mature virions. Protease complexed to its cofactor slides along the viral DNA to specifically locate and cleave the viral precursors. Mature virions have a weakened organization compared to the unmature virions, thereby facilitating subsequent uncoating. Without maturation, the particle lacks infectivity and is unable to uncoat. Late in adenovirus infection, in the cytoplasm, may participate in the cytoskeleton destruction. Cleaves host cell cytoskeletal keratins K7 and K18.
CATALYTIC ACTIVITY Reaction=Cleaves proteins of the adenovirus and its host cell at two consensus sites: -Yaa-Xaa-Gly-Gly-|-Xaa- and -Yaa-Xaa-Gly-Xaa-|- Gly- (in which Yaa is Met, Ile or Leu, and Xaa is any amino acid).; EC=;
ACTIVITY REGULATIONRequires DNA and protease cofactor for maximal activation. Inside nascent virions, becomes partially activated by binding to the viral DNA, allowing it to cleave the cofactor that binds to the protease and fully activates it. Actin, like the viral protease cofactor, seems to act as a cofactor in the cleavage of cytokeratin 18 and of actin itself.
SUBUNITInteracts with protease cofactor pVI-C; this interaction is necessary for protease activation.
SUBCELLULAR LOCATIONVirion. Host nucleus. Note=Present in about 10 copies per virion.
INDUCTIONExpressed in the late phase of the viral replicative cycle.
MISCELLANEOUSAll late proteins expressed from the major late promoter are produced by alternative splicing and alternative polyadenylation of the same gene giving rise to non-overlapping ORFs. A leader sequence is present in the N-terminus of all these mRNAs and is recognized by the viral shutoff protein to provide expression although conventional translation via ribosome scanning from the cap has been shut off in the host cell.
SIMILARITYBelongs to the peptidase C5 family.

Keywords [?]

Gene Ontology [?]

GO:0042025; Cellular component:host cell nucleus
GO:0044423; Cellular component:virion component
GO:0004197; Molecular function:cysteine-type endopeptidase activity
GO:0008234; Molecular function:cysteine-type peptidase activity
GO:0003677; Molecular function:DNA binding

Cross-references [?]

Pfam PF00770; Peptidase_C5; 1;
PIRSF PIRSF001218; Protease_ADV; 1;

Features [?]

From: PRO_ADE02 (P03252)
Key From To Description Tag Condition FTGroup
ACT_SITE 54 54 H
ACT_SITE 71 71 [DE]
ACT_SITE 122 122 C
SITE 51 52 /note="Cleavage; by autolysis" G-x
DISULFID 104 104 /note="Interchain (with C-10 in cleaved protease cofactor pVI-C)" C

Additional information [?]

Size range 196-214 amino acids
Related rules None
Fusion Nter: None Cter: None

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