IED ID | IndEnz0002019010 |
Enzyme Type ID | protease019010 |
Protein Name |
Intracisternal A-particle Gag-related polyprotein Cleaved into: Phosphorylated protein; Capsid protein; Nucleocapsid protein; Protease EC 3.4.23.- |
Gene Name | gag |
Organism | Mouse intracisternal a-particle MIA14 (IAP-MIA14) |
Taxonomic Lineage | Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae unclassified Retroviridae Intracisternal A-particles Mouse intracisternal a-particle MIAE (IAP-MIAE) Mouse intracisternal a-particle MIA14 (IAP-MIA14) |
Enzyme Sequence | MFGLEFFLVLEALLFLFTCYQVVKAGRILDEIQDKLSEVKRGERVGTKRKYGTQNKYTGLSKGLEPEEKLRLGRNTWREIRRKRGKREKKKDQLAEVSRKRSLCSSLDGLGEPALSSSEADEEFSSEETDWEEEAAHYEKKGYQPGKVLANQLRKPKAAGEGQFADWPQGSRLQGPPYAESPPCVVRQPCAERQCAKRQCADSFIPREEQRKIQQAFPVFEGAEGGRVHAPVEYLQIKELAESVRKYGTNANFTLVQLDRLAGMALTPADWQTVVKAALPMMGKYMEWRALWHETAQAQARANAAALTPEQRDWTFDLLTGQGAYSADQTNYHWGAYAQISSTAIRRWKGLSRAGETTGQLTKVVQGPQESFSDFVARMTEAAERIFGESEQAAPLIEQLIYEQATKECRAAIAPRKNKGLQDWLRVCRELGGPLTNAGLAAAILQSQNRSMSRNDQRTCFNCGKPGHFKKDCRAPDKQGGTLTLCSKCGKGYHRADQCRSVRDIKGRVLPPPDSQSAYVPKNGSSGPRSQGLKDMGTGLSGPRKQSERRPRKTHKVDLRAASDFLLMPQMSIQPVPVEPIPSLPLGTMGLILGRGSASTLQGLVVHPELWIVNIPQKYQVLCSSPKGVFSISKGDRIPQLLLLLPDNTREKSAGPEIKKMGSSGNDSAYLVVSLNDRPKLRLKINGKEFEGILDTGADKSIISTHWWPKAWPTTESSHSLQGLGYQSCPTISSVALTWESSEGQQGKFIPYVLPLPVNLWGRDIMQHLGLILSNENAPSGGYSAKAKNIMAKMGYKEGKGLGHQEQGRIEPISPNGNQDRQGLGFP |
Enzyme Length | 827 |
Uniprot Accession Number | P11365 |
Absorption | |
Active Site | ACT_SITE 695; /note=Protease; shared with dimeric partner; /evidence=ECO:0000255|PROSITE-ProRule:PRU00275 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.23.- |
Enzyme Function | FUNCTION: [Protease]: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. {ECO:0000255|PROSITE-ProRule:PRU00275}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (5); Compositional bias (1); Domain (2); Region (3); Signal peptide (1); Site (4); Zinc finger (2) |
Keywords | Aspartyl protease;Hydrolase;Metal-binding;Protease;Repeat;Signal;Transposable element;Zinc;Zinc-finger |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 91,593 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |