IED ID | IndEnz0002005943 |
Enzyme Type ID | protease005943 |
Protein Name |
Gag polyprotein Cleaved into: Matrix protein p16; Capsid protein p25; Nucleocapsid protein p14 |
Gene Name | gag |
Organism | Maedi visna virus (strain 1514 / clone LV1-1KS1) (MVV) (Visna lentivirus) |
Taxonomic Lineage | Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Lentivirus Visna-maedi virus Visna/maedi virus 1514 Maedi visna virus (strain 1514 / clone LV1-1KS1) (MVV) (Visna lentivirus) |
Enzyme Sequence | MAKQGSKEKKGYPELKEVIKATCKIRVGPGKETLTEGNCLWALKTIDFIFEDLKTEPWTITKMYTVWDRLKGLTPEETSKREFASLQATLACIMCSQMGMKPETVQAAKGIISMKEGLQENKEAKGEKVEQLYPNLEKHREVYPIVNLQAGGRSWKAVESVVFQQLQTVAMQHGLVSEDFERQLAYYATTWTSKDILEVLAMMPGNRAQKELIQGKLNEEAERWVRQNPPGPNVLTVDQIMGVGQTNQQASQANMDQARQICRQWVITALRSVRHMSHRPGNPMLVKQKNTESYEDFIARLLEAIDAEPVTDPIKTYLKVTLSYTNASTDCQKQMDRTLGTRVQQATVEEKMQACRDVGSEGFKMQLLAQALRPQGKAGHKGVNQKCYNCGKPGHLARQCRQGIICHHCGKRGHMQKDCRQKKQQGNNRRGPRVVPSAPPML |
Enzyme Length | 442 |
Uniprot Accession Number | P23424 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence. {ECO:0000250|UniProtKB:P04585}.; FUNCTION: [Matrix protein p16]: Targets the polyprotein to the plasma membrane. {ECO:0000250|UniProtKB:P12497}.; FUNCTION: [Capsid protein p25]: Forms the core that encapsulates the genomic RNA-nucleocapsid complex in the virion. {ECO:0000250|UniProtKB:P04585}.; FUNCTION: [Nucleocapsid protein p14]: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearrangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. {ECO:0000250|UniProtKB:P04585}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (4); Erroneous initiation (1); Motif (1); Region (1); Site (1); Zinc finger (2) |
Keywords | Capsid protein;Host-virus interaction;Metal-binding;Repeat;Ribosomal frameshifting;Viral budding;Viral budding via the host ESCRT complexes;Viral release from host cell;Virion;Zinc;Zinc-finger |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: [Matrix protein p16]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p25]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p14]: Virion {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | PTM: [Gag polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000305}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | MOTIF 436..439; /note=PTAP/PSAP motif |
Gene Encoded By | |
Mass | 49,900 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |