Detail Information for IndEnz0002011747
IED ID IndEnz0002011747
Enzyme Type ID protease011747
Protein Name Gag-Pro polyprotein
Pr76Gag-Pro

Cleaved into: Matrix protein p19
MA
; Capsid protein p24
CA
; Nucleocapsid protein p15-pro
NC'
NC-pro
; Protease
PR
EC 3.4.23.-
; p1; Transframe peptide
TFP
p8
pX
Gene Name gag-pro
Organism Human T-cell leukemia virus 3 (strain 2026ND) (HTLV-3)
Taxonomic Lineage Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Deltaretrovirus Primate T-lymphotropic virus 3 Human T-cell leukemia virus 3 (HTLV-3) (Human T-lymphotropic virus 3) Human T-cell leukemia virus 3 (strain 2026ND) (HTLV-3)
Enzyme Sequence MGKTYSSPINPIPKAPKGLAIHHWLNFLQAAYRLQPGPSEFDFHQLRKFLKLAIKTPVWLNPINYSVLAGLIPKNYPGRVHEIVAILIQETPAREAPPSAPLAEDPQKPPPYPEQAQEASQCLPILHPHGAPAAHRPWQMKDLQAIKQEVSSSAPGSPQFMQTIRLAVQQFDPTAKDLHDLLQYLCSSLVASLHHQQLETLIAQAETQGITGYNPLAGPLRIQANNPNQQGLRKEYQNLWLSAFSALPGNTKDPTWAAILQGPEEPFGSFVERLNVALDNGLPEGTPKDPILRSLAYSNANKECQKLLQARGQTNSPLGEMLRACQTWTPRDKNKILMVQPKKTPPPNQPCFRCGQVGHWSRDCKQPRPPPGPCPVCQDPTHWKRDCPQLKTDTRDSEDLLLDLPCEAPNVRERKNLLRGGGLASPRTILPLIPLSQQKQPTLHIQVSFSNTPPVSVQALLDTGADITVLPACLCPPDSNLQDTTVLGAGGPSTNKFKILPCPVHIHLPFRRQPVTLTACLIDINNQWTILGRDALQQCQSSLYLADQPSKVLPVLAPKLIGLEHLPPPPEVSQFPLNQSASRL
Enzyme Length 584
Uniprot Accession Number Q0R5R3
Absorption
Active Site ACT_SITE 462; /note=For protease activity; shared with dimeric partner; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.23.-
Enzyme Function FUNCTION: Matrix protein p19 targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex (By similarity). {ECO:0000250}.; FUNCTION: Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.; FUNCTION: Nucleocapsid protein p15 is involved in the packaging and encapsidation of two copies of the genome. {ECO:0000250}.; FUNCTION: The aspartyl protease mediates proteolytic cleavages of Gag, Gag-Pro and Gag-Pro-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. Hydrolyzes host EIF4GI in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (6); Domain (1); Initiator methionine (1); Lipidation (1); Motif (2); Peptide (1); Region (1); Site (5); Zinc finger (2)
Keywords Aspartyl protease;Capsid protein;Eukaryotic host gene expression shutoff by virus;Eukaryotic host translation shutoff by virus;Host gene expression shutoff by virus;Host-virus interaction;Hydrolase;Lipoprotein;Metal-binding;Myristate;Protease;Reference proteome;Repeat;Ribosomal frameshifting;Viral nucleoprotein;Virion;Zinc;Zinc-finger
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p15-pro]: Virion {ECO:0000305}.
Modified Residue
Post Translational Modification PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation. The protease is autoproteolytically processed at its N- and C-termini (By similarity). {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 98..101; /note=PTAP/PSAP motif; MOTIF 109..112; /note=PPXY motif
Gene Encoded By
Mass 64,421
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda