| IED ID | IndEnz0002001485 |
| Enzyme Type ID | protease001485 |
| Protein Name |
Protease EC 3.4.22.39 Adenain Adenovirus protease AVP Adenovirus proteinase Endoprotease |
| Gene Name | L3 |
| Organism | Fowl adenovirus A serotype 1 (strain CELO / Phelps) (FAdV-1) (Avian adenovirus gal1 (strain Phelps)) |
| Taxonomic Lineage | Viruses Varidnaviria Bamfordvirae Preplasmiviricota Tectiliviricetes Rowavirales Adenoviridae Aviadenovirus Fowl aviadenovirus A Fowl adenovirus A serotype 1 (strain CELO / Phelps) (FAdV-1) (Avian adenovirus gal1 (strain Phelps)) |
| Enzyme Sequence | MSGTTETQLRDLLSSMHLRHRFLGVFDKSFPGFLDPHVPASAIVNTGSRASGGMHWIGFAFDPAAGRCYMFDPFGWSDQKLWELYRVKYNAFMRRTGLRQPDRCFTLVRSTEAVQCPCSAACGLFSALFIVSFDRYRSKPMDGNPVIDTVVGVKHENMNSPPYRDILHRNQERTYYWWTKNSAYFRAHQEELRRETALNALPENHV |
| Enzyme Length | 206 |
| Uniprot Accession Number | P42672 |
| Absorption | |
| Active Site | ACT_SITE 55; /evidence=ECO:0000255|HAMAP-Rule:MF_04059; ACT_SITE 72; /evidence=ECO:0000255|HAMAP-Rule:MF_04059; ACT_SITE 122; /evidence=ECO:0000255|HAMAP-Rule:MF_04059 |
| Activity Regulation | ACTIVITY REGULATION: Requires 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. {ECO:0000255|HAMAP-Rule:MF_04059}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | 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=3.4.22.39; Evidence={ECO:0000255|HAMAP-Rule:MF_04059}; |
| DNA Binding | |
| EC Number | 3.4.22.39 |
| Enzyme Function | FUNCTION: Cleaves 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. {ECO:0000255|HAMAP-Rule:MF_04059}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (1); Site (1) |
| Keywords | Autocatalytic cleavage;DNA-binding;Disulfide bond;Host nucleus;Hydrolase;Late protein;Protease;Reference proteome;Thiol protease;Virion |
| Interact With | |
| Induction | INDUCTION: Expressed in the late phase of the viral replicative cycle. {ECO:0000255|HAMAP-Rule:MF_04059}. |
| Subcellular Location | SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04059}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04059}. Note=Present in about 10 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04059}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 23,764 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |