IED ID | IndEnz0002002350 |
Enzyme Type ID | protease002350 |
Protein Name |
Methionine aminopeptidase 2-1 MAP 2-1 MetAP 2-1 EC 3.4.11.18 Peptidase M |
Gene Name | HCBG_02311 |
Organism | Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432) (Darling's disease fungus) (Histoplasma capsulatum) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Ajellomycetaceae Histoplasma Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum) Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432) (Darling's disease fungus) (Histoplasma capsulatum) |
Enzyme Sequence | MAAQVIPELQSLNLKTEGGALPQELAPSGAPENEDGDSEDDNGDDQGADESRTIEVLAAKKKKKKKPKKKKKDTQKAQTEPPRVILSALFPNNEYPVGELVEYKDENAYRTTNEEKRYLDRMNNDFLSEYRYAAEVHKQVRQYAQKTIKPGQTLTEIAEGIEDSVRALTGHDGLTEGDNLLGGIAFPTGVNLNNCAAHYSPNAGNKMVLQYEDVMKVDFGVHMNGRIVDSAFTIAFDPVYDNLLAAVKDATNTGIREAGIDVRMSDIGAAIQEAMESYEVEIKGTTYPVKAIRNLNGHTIGQFEIHGGKNGKSVPIVKGGDQSKMEEGEVYAIETFGSTGRGYVRDDMETSHYAKVPDAPNVPLRLSSAKNLLNVITKNFGTLPFCRRYLDRLRQDKYLLGLNNLVANGLVDAYPPLCDIKGSYTAQFEHTILLRPNIKEVISRGDDY |
Enzyme Length | 448 |
Uniprot Accession Number | C0NIQ4 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | BINDING 198; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 306; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175 |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.; EC=3.4.11.18; Evidence={ECO:0000255|HAMAP-Rule:MF_03175}; |
DNA Binding | |
EC Number | 3.4.11.18 |
Enzyme Function | FUNCTION: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). {ECO:0000255|HAMAP-Rule:MF_03175}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Binding site (2); Chain (1); Compositional bias (1); Metal binding (7); Region (1) |
Keywords | Aminopeptidase;Cytoplasm;Hydrolase;Metal-binding;Protease;Reference proteome |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03175}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 49,468 |
Kinetics | |
Metal Binding | METAL 218; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 229; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 229; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 298; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 334; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 429; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 429; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175 |
Rhea ID | |
Cross Reference Brenda |