| IED ID | IndEnz0002008558 |
| Enzyme Type ID | protease008558 |
| Protein Name |
Vacuolar membrane protease EC 3.4.-.- FXNA-related family protease 1 |
| Gene Name | LELG_02615 |
| Organism | Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Lodderomyces Lodderomyces elongisporus Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) |
| Enzyme Sequence | MADNNSSSGSLVIDEQDYDVHEAGQQGQQGQQKHQQRQQERPSLITRVFRSVFGYRKTSLSLFVVATIALCVSLSYIDNSVDFISFPTVESEVNLLNAAWLDLQVIAKEQHPYGSIGNDRVHDFLERRIQELITGANFITWDNDINGNNSFMFESSSNPKTVSYYESNNLLVKIEGKNAKLPGILLSSHFDSVPTSYGVTDDGMGVASMLGILNYFSQQKKQPERTIVMNFNNNEEFGLLGATAFTRHPWFKLVKYFLNLEGTGAGGKAILFRATDYGIAKYFQNVRTPYASSIFQQGFANGLVHSETDYKVYKEAGMRGLDLAFFKPRDYYHTAEDNIRRTSEKSLWHMLSNSLDFIDYLSKDKEFGMNLEEKPNLLEEPAVFASFLNYFFTISTSQLFKINVALLTVFPILNGLLLLYTIRSRKWQVSFSSAISIPVALLVTMFIVVYLVVESYKSFNQYLPSSRPLLLVATITSILLLVFSIILVAFSFFSIIAEENLRLLAIVELSFAYWVGLAFTTHGLSGAESARHSGEFAVSILFTLEAVASFLGLIGWSLCRNRSHLQVAEGESVPLLNGIDARYSSDNDHDHEHRHGHEDNEHGEAHVQQQSQSRHKKQCKETVHSFGYDWSLQYLITVPLSIFIIYNSGWLVLEGVNKTLQESAKAETFVYNLLWIVSVSLVLPLIPFAGKLNRYMVFVLIAIGVLGTLLVHVVQPFNEANPLKLRFLQRIDGKNNASSVHVYARKGLATEVLEQLPSVRQSNETIHCSQLADGMEDCSFVSALAPQILPGYELGNYIEVTNNGSAPSQLFGVNYNQIKIVALKSQSCSLHFGDSKVKAVVVGSSLESAPAFKHLPSGYSFNKDHFYKDTSGIWNLTLNKLDSHSSFDISLYWLPGIDDEANTLQFDVECFWADLSPVALNNTVFEAIPAFNEVQQYSPISVSWANREKGLVAYTKQVHV |
| Enzyme Length | 960 |
| Uniprot Accession Number | A5DZ28 |
| Absorption | |
| Active Site | ACT_SITE 235; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P80561 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.-.- |
| Enzyme Function | FUNCTION: May be involved in vacuolar sorting and osmoregulation. {ECO:0000250|UniProtKB:P38244}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Glycosylation (7); Metal binding (6); Region (2); Site (1); Topological domain (10); Transmembrane (9) |
| Keywords | Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Transmembrane;Transmembrane helix;Vacuole;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P38244}; Multi-pass membrane protein {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 107,646 |
| Kinetics | |
| Metal Binding | METAL 189; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 201; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 201; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 236; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 261; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 333; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561 |
| Rhea ID | |
| Cross Reference Brenda |