Protein: Presequence protease, mitochondrial (PreP) (EC 3.4.24.-) (Pitrilysin metalloproteinase) (Q5B6H7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Degrades mitochondrial transit peptides after their cleavage in the intermembrane space or in the matrix, and presequence peptides; clearance of these peptides is required to keep the presequence processing machinery running (By similarity). Preferentially cleaves the N-terminal side of paired basic amino acid residues (By similarity). Also degrades other unstructured peptides (By similarity). May function as an ATP-dependent peptidase as opposed to a metalloendopeptidase (By similarity).
Subcellular location: Mitochondrion intermembrane space {ECO:0000250|UniProtKB:P32898}. Mitochondrion matrix {ECO:0000250|UniProtKB:P32898}.
Sequence: MLRSYLHLGRHRTPAFRQPLGRLLRPTASILQYAQSRTLASVSSLESLPEVGDQLHGFTVQEKKQVPELHLTAIRLRHDKTHADYLHIAREDKNNVFGIGFKTNPPDATGVPHILEHTTLCGSEKYPIRDPFFKMLPRSLSNFMNAFTSSDHTMYPFATTNQQDFQNLLSVYLDATMHPLLKEEDFRQEGWRLGPEDPRAIQTQEGNLKPEDILFKGVVYNEMKGQMSDANYLYWIRFQESIFPAINNSGGDPQHITDLTHKQLVEFSKKNYNPSNAKIITYGDMPLADHLKQVGGVLNDFSKGAVDTTVKLPIELRGPINVTVPGPIDTFVSEDRQFKTSTSWYMGDITDTVETFSAGILSSLLLDGYGSPMYKALIESGLGSSFTPNTGLDTSGKIPIFSIGVTGVSEEQAPRVKEEIQRVLQETLQRGFNDEKVQGFLHQLELALRHKTANFGLGVIQKTFTSWFNGSDPMKELAWNEVINAFKSRYEKGGYLEALMQKYLINDNCLTFTMVGTPSFNKELDDKEMARKEKKFEQLTQQHGSVEKAVTELAKAELQLLEVQEKAQHADLSCLPSLRVEDISRQKEHKPVRESKVEGTDIVWREAPTNGLTYFQAVNAFADLPDDLRLLLPLFNDAIMRLGTPTRTMEQWEDLIKLKTGGVSTSNFHTTSPTEMGKYTEGLQFSGFALDKNVPDMLEILTALVTETDFTSPSAPAMIQELLRLTTNGALDAVAGTGHRYALNAAAAGLSRSFWAQEQTSGLAQLQATANLLRDAETSPERLAELIEKLRLIQSFAISKTSGLRVRLVCEPASSTQNESVLQRWVTGLPKVPSPTSQPQRFDLSTPSKKAFYDLPYKVYYSGLALPTVPFTHSSSATLSVLSQLLTHNYLHPEIREKGGAYGAGASNGPVKGLFAFTSYRDPNPANTLKVFKNSGVFARDRAWSDREINEAKLGIFQGLDAPVSVDEEGSRYFLNGITHEMDQRWREQVLDVTAKDVNEVAQTFLVDGTRRSVCLLGEKKDWAESEGWEVRKLSMNPNGSNIPSGDAA
InterPro domains: - IPR007863: Peptidase M16, C-terminal (domain) [258-439]
- IPR013578: Peptidase M16C associated (domain) [514-772]
- IPR011765: Peptidase M16, N-terminal (domain) [99-188]
- IPR011249: Metalloenzyme, LuxS/M16 peptidase-like (homologous_superfamily) [53-1040]
- IPR055130: Presequence protease, mitochondrial-type, C-terminal domain (domain) [878-1018]
Gene Ontology annotations:
Molecular Function (MF): GO:0003674 (molecular function), GO:0003824 (catalytic activity), GO:0140096 (catalytic activity, acting on a protein), GO:0016787 (hydrolase activity), GO:0008233 (peptidase activity), GO:0004175 (endopeptidase activity), GO:0008237 (metallopeptidase activity), GO:0004222 (metalloendopeptidase activity)
Biological Process (BP): GO:0008150 (biological process), GO:0009987 (cellular process), GO:0050896 (response to stimulus), GO:0051716 (cellular response to stimulus), GO:0042221 (response to chemical), GO:1901700 (response to oxygen-containing compound), GO:0010033 (response to organic substance), GO:0070887 (cellular response to chemical stimulus), GO:0097305 (response to alcohol), GO:0071310 (cellular response to organic substance), GO:1901701 (cellular response to oxygen-containing compound), GO:0033993 (response to lipid), GO:0097306 (cellular response to alcohol), GO:0097307 (response to farnesol), GO:0071396 (cellular response to lipid), GO:0097308 (cellular response to farnesol)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005622 (intracellular anatomical structure), GO:0043226 (organelle), GO:0005737 (cytoplasm), GO:0043229 (intracellular organelle), GO:0005739 (mitochondrion), GO:0043227 (membrane-bounded organelle), GO:0043231 (intracellular membrane-bounded organelle)