Detail Information for IndEnz0002002379
IED ID IndEnz0002002379
Enzyme Type ID protease002379
Protein Name Methionine aminopeptidase 2-2
MAP 2-2
MetAP 2-2
EC 3.4.11.18
Peptidase M
Gene Name ACLA_046220
Organism Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Aspergillus clavatus Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)
Enzyme Sequence MAAQTTEKLQKLDLNGQSGDAKADAPAAGQAEAGEAEEDSDDEKDDGNAAPEAGAGGAAKKKKRKSKKKKKGGAKVQSSPPRVPVSNLFPNNQYPEGEIVEYTNENSYRTTNEEKRYLDRMNNDFLQEYRQAAEVHRQVRQYAQKNIKPGQTLTEIAEGIEDAVRALTGHQGLEEGDNLKGGMGFPCGLSINHCAAHYTPNAGNKMVLQQGDVMKVDFGAQINGRIVDSAFTMTFDPVYDPLLEAVKDATNTGIREAGIDVRMSDIGAAIQEAMESYEIELNGTMYPVKCIRNLNGHNIDQHVIHGGKSVPIVKGGDQTKMEEGETFAIETFGSTGKGYVREDMETSHYALVPDAPSVPLRLSSAKNLLNVINKNFGTLPFCRRYLDRLGQDKYLLGLNNLVSSGIVQDYPPLCDIKGSYTAQFEHVQIPSHSHP
Enzyme Length 435
Uniprot Accession Number A1CH02
Absorption
Active Site
Activity Regulation
Binding Site BINDING 197; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; BINDING 305; /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 47,491
Kinetics
Metal Binding METAL 217; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 228; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 228; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 297; /note=Divalent metal cation 2; catalytic; via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 330; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 425; /note=Divalent metal cation 1; /evidence=ECO:0000255|HAMAP-Rule:MF_03175; METAL 425; /note=Divalent metal cation 2; catalytic; /evidence=ECO:0000255|HAMAP-Rule:MF_03175
Rhea ID
Cross Reference Brenda