IED ID | IndEnz0002011670 |
Enzyme Type ID | protease011670 |
Protein Name |
Genome polyprotein Cleaved into: Capsid protein C Core protein ; Protein prM; Peptide pr; Small envelope protein M Matrix protein ; Envelope protein E Fragment |
Gene Name | |
Organism | Langat virus (strain Yelantsev) |
Taxonomic Lineage | Viruses Riboviria Orthornavirae Kitrinoviricota Flasuviricetes Amarillovirales Flaviviridae Flavivirus (arboviruses group B) Langat virus Langat virus (strain Yelantsev) |
Enzyme Sequence | MAGKAVLKGKGGGPPRRASKVAPKKTRQLRVQMPNGLVLMRMLGVLWHALTGTARSPVLKAFWKVVPLKQATLALRKIKRTVSTLMVGLHRRGSRRTTIDWMTPLLITVMLGMCLTATVRRERDGSMVIRAEGRDAATQVRVENGTCVILATDMGSWCDDSLAYECVTIDQGEEPVDVDCFCRGVEKVTLEYGRCGRREGSRSRRSVLIPSHAQRDLTGRGHQWLEGEAVKAHLTRVEGWVWKNKLFTLSLVMVAWLMVDGLLPRILIVVVALALVPAYASRCTHLENRDFVTGVQGTTRLTLVLELGGCVTVTADGKPSLDVWLDSIYQESPAQTREYCLHAKLTGTKVAARCPTMGPATLPEEHQSGTVCKRDQSDRGWGNHCGLFGKGSIVTCVKFTCEDKKKATGHVYDVNKITYTIKVEPHTGEFVAANETHSGRKSASFTVSSEKTILTLGDYGDVSLLCRVASGVDLAQTVVLALDKTHEHLPTAWQVHRDWFNDLALPWKHDGAEAWNEAGRLVEFGTPHAVKMDVFNLGDQTGVLLKSLAGVPVASIEGTKYHLKSGHVTCEVGLEKLKMKGLTYTVCDKTKFTWKRAPTDSGHDTVVMEVGFSGTRPCRIPVRAVAHGVPEVNVAMLITPNPTMENNGGGFIEMQLPPGDNIIYVGDLNHQWFQKGSSIGRVLQKTRKGIERLTVLGEHAWDFGSVGGVMTSIGRAMHTVLGGAFNTLLGGVGFLPKILLGVAMAWLGLNMRNPTLSMGFLLSGGLVLAMTLGVGA |
Enzyme Length | 776 |
Uniprot Accession Number | P29838 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA (By similarity). {ECO:0000250}.; FUNCTION: prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated (By similarity). {ECO:0000250}.; FUNCTION: Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity). {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (6); Disulfide bond (6); Glycosylation (2); Intramembrane (2); Non-terminal residue (1); Propeptide (1); Region (2); Site (4); Topological domain (5); Transmembrane (3) |
Keywords | 3D-structure;Capsid protein;Clathrin-mediated endocytosis of virus by host;Cleavage on pair of basic residues;Disulfide bond;Fusion of virus membrane with host endosomal membrane;Fusion of virus membrane with host membrane;Glycoprotein;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Membrane;Secreted;Transmembrane;Transmembrane helix;Viral attachment to host cell;Viral envelope protein;Viral penetration into host cytoplasm;Virion;Virus endocytosis by host;Virus entry into host cell |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Host endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | PTM: Specific enzymatic cleavages in vivo yield mature proteins Peptide 2K acts as a signal sequence and is removed from the N-terminus of NS4B by the host signal peptidase in the ER lumen. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site (By similarity). {ECO:0000250}. |
Signal Peptide | |
Structure 3D | NMR spectroscopy (1) |
Cross Reference PDB | 1Z66; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 84,537 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |