| IED ID | IndEnz0002011191 |
| Enzyme Type ID | protease011191 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like EoMP06 EC 3.4.24.- Prothrombin activator EoMP06 Snake venom metalloprotease SVMP Fragment |
| Gene Name | |
| Organism | Echis ocellatus (Ocellated saw-scaled viper) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Lepidosauria (lepidosaurs) Squamata (squamates) Bifurcata (split-tongued squamates) Unidentata Episquamata Toxicofera Serpentes (snakes) Colubroidea Viperidae Viperinae (vipers) Echis Echis ocellatus (Ocellated saw-scaled viper) |
| Enzyme Sequence | VEDHCYYHGRVQNDAESTASISACNGLKGHFKLQGETYFIEPLKIPNSEAHAVYKYENIEKEDEAPKMCGVTQTNWESDEPIKKTLGLIVPPHGQKFEKKFIELIIVVDHSMVTKYNNDLTAVRTEIYERLNTVNEIYLPLNIHVALVGIVFWSNRDLINVTSSAADTLHSFGEWRGSDLLNQKRHDHAQLLTNVTLDGTTLGITFVFGMCKSDRSVELIRDYSNITFNMAYIMAHEMGHSLGMLHDTKSCTCGDKPCIMFSKESVPPPKEFSSCSYDQYNKYLLKYNPKCIVDPPLRKDIASPAVCGNGVWEEGEECDCGSPEDCENPCCDAATCKLKPGAECGNGECCDNCKIRKAGTECRPARDDCDVAEHCTGQSAECPRNEFQRNGQPCLNNSGYCYNGDCPIMLNQCIALFSPSATVAQDSCFQRNLQGSYYGHCRKEIGHYGKRFPCAAQDVKCGRLYCLDNSFKKNMRCKKDFSYSDENKGIVEPGTKCEDGKVCINRKCVDVNTAY |
| Enzyme Length | 515 |
| Uniprot Accession Number | Q6X1T6 |
| Absorption | |
| Active Site | ACT_SITE 237; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc metalloproteinase that catalyzes the conversion of prothrombin (F2) to alpha-thrombin. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (17); Domain (2); Glycosylation (3); Metal binding (12); Modified residue (1); Motif (1); Non-terminal residue (1); Propeptide (1) |
| Keywords | Blood coagulation cascade activating toxin;Calcium;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Prothrombin activator;Pyrrolidone carboxylic acid;Secreted;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | MOD_RES 95; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 368..370; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 57,658 |
| Kinetics | |
| Metal Binding | METAL 103; /note=Calcium 1; /evidence=ECO:0000250; METAL 187; /note=Calcium 1; /evidence=ECO:0000250; METAL 236; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 240; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 246; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 291; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 294; /note=Calcium 1; /evidence=ECO:0000250; METAL 306; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 309; /note=Calcium 2; /evidence=ECO:0000250; METAL 313; /note=Calcium 2; /evidence=ECO:0000250; METAL 316; /note=Calcium 2; /evidence=ECO:0000250; METAL 319; /note=Calcium 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |