| IED ID | IndEnz0002015518 |
| Enzyme Type ID | protease015518 |
| Protein Name |
Zinc metalloproteinase nas-8 EC 3.4.24.21 Nematode astacin 8 Sc-AST |
| Gene Name | |
| Organism | Steinernema carpocapsae (Entomopathogenic nematode) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Tylenchina Panagrolaimomorpha Strongyloidoidea Steinernematidae Steinernema Steinernema carpocapsae (Entomopathogenic nematode) |
| Enzyme Sequence | MMNRASLCRIAVLLCILHLSHLIDSTYAQSYLTEKDFLAPLYDDDAITLSDDDFDNARKLSTEMVNSQKKRRVLSHQKYYRGDIRGRAAWTSKLKSGVRRNGVTSVIKRWPNGRIPYVISSQYNERERAVLARAFQEYHSRTCIRFVPRTSFDQDYLYIGKIDGCYSDVGRAGGRQELSLDDGCLQYNTAIHELMHSVGFYHEHERWDRDQYITILWNNIDKDAYDQFGRVDLTESSYYGQAYDYYSVMHYDSLAFSKNGFETLVAKRPEMTAVIGSAIDFSPIDLLKINKLYNCPAPNTIDISQISGNGWQGGGMGPRAPLPQVNLPLPPPPPLPTNPAIAIVGECSDRTNLCWRWLDRCRSYFFEKIMKEFCALSCGYCVPTNAVSKAAPAIPLQPTLSIAEGPEGPMPPLYQRFG |
| Enzyme Length | 418 |
| Uniprot Accession Number | D2KBH9 |
| Absorption | |
| Active Site | ACT_SITE 193; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by ethylene glycol-bis(2-aminoethylether)-N,N,N,N-tetraacetic acid (EGTA), ethylenediaminetetraacetic acid (EDTA) and o-phenanthroline. {ECO:0000269|PubMed:20670659}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of peptide bonds in substrates containing five or more amino acids, preferentially with Ala in P1', and Pro in P2'.; EC=3.4.24.21; Evidence={ECO:0000269|PubMed:20670659}; |
| DNA Binding | |
| EC Number | 3.4.24.21 |
| Enzyme Function | FUNCTION: Metalloprotease. {ECO:0000269|PubMed:20670659}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:20670659}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:20670659}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (5); Domain (2); Metal binding (3); Propeptide (1); Signal peptide (1) |
| Keywords | Cleavage on pair of basic residues;Disulfide bond;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | INDUCTION: Induced upon parasitic infection of insects. {ECO:0000269|PubMed:20670659}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 47,458 |
| Kinetics | |
| Metal Binding | METAL 192; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 196; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 202; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.21; |