ID   W7HQ54_9PEZI            Unreviewed;      1017 AA.
AC   W7HQ54;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Presequence protease, mitochondrial {ECO:0000256|ARBA:ARBA00020167};
DE   AltName: Full=Pitrilysin metalloproteinase {ECO:0000256|ARBA:ARBA00034552};
GN   ORFNames=DRE_04462 {ECO:0000313|EMBL:EWC46291.1};
OS   Drechslerella stenobrocha 248.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Drechslerella.
OX   NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC46291.1, ECO:0000313|Proteomes:UP000024837};
RN   [1] {ECO:0000313|EMBL:EWC46291.1, ECO:0000313|Proteomes:UP000024837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=248 {ECO:0000313|EMBL:EWC46291.1,
RC   ECO:0000313|Proteomes:UP000024837};
RA   Liu X., Zhang W., Liu K.;
RT   "Drechslerella stenobrocha genome reveals carnivorous origination and
RT   mechanical trapping mechanism of predatory fungi.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Degrades mitochondrial transit peptides after their cleavage
CC       in the intermembrane space or in the matrix, and presequence peptides;
CC       clearance of these peptides is required to keep the presequence
CC       processing machinery running (By similarity). Preferentially cleaves
CC       the N-terminal side of paired basic amino acid residues (By
CC       similarity). Also degrades other unstructured peptides (By similarity).
CC       May function as an ATP-dependent peptidase as opposed to a
CC       metalloendopeptidase. {ECO:0000256|ARBA:ARBA00034467}.
CC   -!- SUBUNIT: Monomer and homodimer; homodimerization is induced by binding
CC       of the substrate. {ECO:0000256|ARBA:ARBA00011853}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC       {ECO:0000256|ARBA:ARBA00004569}. Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. PreP subfamily.
CC       {ECO:0000256|ARBA:ARBA00007575}.
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DR   EMBL; KI966419; EWC46291.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7HQ54; -.
DR   HOGENOM; CLU_009165_0_0_1; -.
DR   Proteomes; UP000024837; Unassembled WGS sequence.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR013578; Peptidase_M16C_assoc.
DR   PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR   PANTHER; PTHR43016:SF13; PRESEQUENCE PROTEASE, MITOCHONDRIAL; 1.
DR   Pfam; PF08367; M16C_assoc; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SMART; SM01264; M16C_associated; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000024837}.
FT   DOMAIN          490..741
FT                   /note="Peptidase M16C associated"
FT                   /evidence="ECO:0000259|SMART:SM01264"
SQ   SEQUENCE   1017 AA;  112791 MW;  240DA064AA8A4DC1 CRC64;
     MLRAAIASLR RPPAQRRFLA TAAIDTANLA KLPPSGLKLN GFTLQRAKHV PELELSALQF
     KHDKTGADYI HVARDDSNNV FSIGFKTNPP DATGVPHILE HTTLCGSKKY PVRDPFFKML
     NRSLSNFMNA FTSPDHTMYP FATTNRTDFM NLMDVYLDAT LNPLLKESDF KQEGWRIGPE
     NPAEDGSPLL FKGVVYNEMK GQMSDGSYLF YKRFQDYIIP SVNNSGGDPA FIPDLTLEQL
     RDYHKNHYHP SNAKLFSYGN FPLESTLEKV DGKLSEFEHI SIDTDIKEPI SIDKPISVTV
     EGPVDPLAEL SEQYKTSMSW ITPDTSNVLD SFAFSVLSSL LTDGYGSPMY KALIESNLGA
     EFSPNTGYDG SFKKGIFSVG LQNVKAQNLK DVQSEIVRTL KIARNEGFQQ QKVEGILHQL
     EIALKHKTAN FGLGLMQRLE SGWFNGVDPF DALKWNEIVL QFRERYSQGG YLEELIEKYL
     IDGNALTFTM NPVAQYEANL QSAETARLNV DIEKLGGDEN ARETMVLMEK ELSELQEKAK
     SEDLSSLPTL HVKDIPRETD KVELKATQIN DVNVQWRVAP TNGLTYFRLF VNFDNQPDEL
     RKYLPLYAAS LFRLGTAKVP METLEDEIKL RTGGISCAPF ISADPHDLSK WQEGIVFSGH
     CLDKNVPRML DILRVIIIGT DFSRISKIHT LVKGIASGAI DGVAESGHSY ARGFAAAHLT
     TAAQVNETVN GLAQVKLITD LALSENYPPA MSALSFIAQY PQASGNPMRI AITCGQEAVA
     DNEKHISEYI DGLVPGKTVY EPHDIPPVLG HGTKSFFPLP FQVNYTATAL KTAPFASPDN
     AALTVLGNML THKHLHHEIR EKGGAYGGGA TQGGISGVFS FYSYRDPNPL NTIDVVRNAG
     EFAVNKNWTD RDLEEAKLSI FQGIDAPKSV SSEGMLYFLD GITNEMKQKR REQLLDVTAK
     EVQEVAQKYI VDQFEQGNGA TVVIGGVNEW ATNENGWTTY EMSPEAATAE LPSKVEL
//