Detail Information for IndEnz0002002623
IED ID IndEnz0002002623
Enzyme Type ID protease002623
Protein Name Mitochondrial presequence protease
EC 3.4.24.-
Gene Name cym1 AN3853
Organism Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Enzyme Sequence MLRSYLHLGRHRTPAFRQPLGRLLRPTASILQYAQSRTLASVSSLESLPEVGDQLHGFTVQEKKQVPELHLTAIRLRHDKTHADYLHIAREDKNNVFGIGFKTNPPDATGVPHILEHTTLCGSEKYPIRDPFFKMLPRSLSNFMNAFTSSDHTMYPFATTNQQDFQNLLSVYLDATMHPLLKEEDFRQEGWRLGPEDPRAIQTQEGNLKPEDILFKGVVYNEMKGQMSDANYLYWIRFQESIFPAINNSGGDPQHITDLTHKQLVEFSKKNYNPSNAKIITYGDMPLADHLKQVGGVLNDFSKGAVDTTVKLPIELRGPINVTVPGPIDTFVSEDRQFKTSTSWYMGDITDTVETFSAGILSSLLLDGYGSPMYKALIESGLGSSFTPNTGLDTSGKIPIFSIGVTGVSEEQAPRVKEEIQRVLQETLQRGFNDEKVQGFLHQLELALRHKTANFGLGVIQKTFTSWFNGSDPMKELAWNEVINAFKSRYEKGGYLEALMQKYLINDNCLTFTMVGTPSFNKELDDKEMARKEKKFEQLTQQHGSVEKAVTELAKAELQLLEVQEKAQHADLSCLPSLRVEDISRQKEHKPVRESKVEGTDIVWREAPTNGLTYFQAVNAFADLPDDLRLLLPLFNDAIMRLGTPTRTMEQWEDLIKLKTGGVSTSNFHTTSPTEMGKYTEGLQFSGFALDKNVPDMLEILTALVTETDFTSPSAPAMIQELLRLTTNGALDAVAGTGHRYALNAAAAGLSRSFWAQEQTSGLAQLQATANLLRDAETSPERLAELIEKLRLIQSFAISKTSGLRVRLVCEPASSTQNESVLQRWVTGLPKVPSPTSQPQRFDLSTPSKKAFYDLPYKVYYSGLALPTVPFTHSSSATLSVLSQLLTHNYLHPEIREKGGAYGAGASNGPVKGLFAFTSYRDPNPANTLKVFKNSGVFARDRAWSDREINEAKLGIFQGLDAPVSVDEEGSRYFLNGITHEMDQRWREQVLDVTAKDVNEVAQTFLVDGTRRSVCLLGEKKDWAESEGWEVRKLSMNPNGSNIPSGDAA
Enzyme Length 1049
Uniprot Accession Number Q5B6H7
Absorption
Active Site ACT_SITE 116; /note=Proton acceptor; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: ATP-independent protease that degrades mitochondrial transit peptides after their cleavage. Also degrades other unstructured peptides (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Metal binding (3); Transit peptide (1)
Keywords Hydrolase;Metal-binding;Metalloprotease;Mitochondrion;Protease;Reference proteome;Transit peptide;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 117,040
Kinetics
Metal Binding METAL 113; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 117; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 222; /note=Zinc; catalytic; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda