| 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 |