Detail Information for IndEnz0002012960
IED ID IndEnz0002012960
Enzyme Type ID protease012960
Protein Name Endogenous retrovirus group K member 6 Pro protein
HERV-K
C7
Pro protein
HERV-K
HML-2.HOM
Pro protein
HERV-K108 Pro protein
HERV-K_7p22.1 provirus ancestral Pro protein
EC 3.4.23.50
Protease
Proteinase
PR
Gene Name ERVK-6 ERVK6
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence WASQVSENRPVCKAIIQGKQFEGLVDTGADVSIIALNQWPKNWPKQKAVTGLVGIGTASEVYQSTEILHCLGPDNQESTVQPMITSIPLNLWGRDLLQQWGAEITMPAPSYSPTSQKIMTKMGYIPGKGLGKNEDGIKIPVEAKINQEREGIGNPC
Enzyme Length 156
Uniprot Accession Number Q9Y6I0
Absorption
Active Site ACT_SITE 26; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Processing at the authentic HIV-1 PR recognition site and release of the mature p17 matrix and the p24 capsid protein, as a result of the cleavage of the -SQNY-|-PIVQ- cleavage site.; EC=3.4.23.50;
DNA Binding
EC Number 3.4.23.50
Enzyme Function FUNCTION: Retroviral proteases have roles in the processing of the primary translation products and the maturation of the viral particle. Endogenous Pro proteins may have kept, lost or modified their original function during evolution.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Domain (2); Erroneous initiation (2); Sequence conflict (1)
Keywords Aspartyl protease;Autocatalytic cleavage;ERV;Hydrolase;Protease;Reference proteome;Ribosomal frameshifting;Transposable element
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification PTM: Autoproteolytically processed at the N-terminus. Expected C-terminal autoprocessing not detected. The sequence shown is that of the processed Pro protein (By similarity). {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 16,972
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda