ID   W7I549_9PEZI            Unreviewed;       516 AA.
AC   W7I549;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=mitochondrial processing peptidase {ECO:0000256|ARBA:ARBA00012299};
DE            EC=3.4.24.64 {ECO:0000256|ARBA:ARBA00012299};
DE   AltName: Full=Beta-MPP {ECO:0000256|ARBA:ARBA00031018};
GN   ORFNames=DRE_07257 {ECO:0000313|EMBL:EWC43880.1};
OS   Drechslerella stenobrocha 248.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Drechslerella.
OX   NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC43880.1, ECO:0000313|Proteomes:UP000024837};
RN   [1] {ECO:0000313|EMBL:EWC43880.1, ECO:0000313|Proteomes:UP000024837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=248 {ECO:0000313|EMBL:EWC43880.1,
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal transit peptides from precursor proteins
CC         imported into the mitochondrion, typically with Arg in position P2.;
CC         EC=3.4.24.64; Evidence={ECO:0000256|ARBA:ARBA00001098};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; KI966449; EWC43880.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7I549; -.
DR   MEROPS; M16.003; -.
DR   HOGENOM; CLU_009902_4_2_1; -.
DR   Proteomes; UP000024837; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000024837}.
FT   DOMAIN          91..238
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          243..431
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   516 AA;  56929 MW;  995A607EA78313BB CRC64;
     MALGVLCPRL ELNWRLQSLA CDITTLTSFP RLAAPNTLLS HDGCHPGAGL TRSLLKPSRS
     ARAFATPATT APATWTPNKT ETTTLSNGFT IATETNPGQQ TATVGVWIDA GSRSETDANN
     GTAHFLEHLA FKGTKNRTQN QLELEIENMG GHLNAYTSRE NTVYYAKAFK NDVAKSVEIL
     SDILQNSRLD EGAIEREREV ILREQEEVDK QLEEVVFDHL HATAFQGQAL GRTILGPKEN
     IMSIQRADLT NYIQNNYTSD RMVLVGAGGV SHEELVKLAE KHFGGLKPSP TPTVFGAARS
     EPPDFVGSEV RLRDDAYPTA HIAIAVEGVS WKDDNYFTAL VAQAIVGNWD RAMGNASHLG
     SRLASYVHEH HLANSFMSFS TSYNDTGLWG IYLVTDKLQE IDDLVHFSLR EWTRLAISVD
     ESEVERAKAQ LKASLLLSLD GTTAIAEDIG RQLITTGRRM TPAEVERVVG AITPDDVMKF
     ASKHIWDQDI AISCFGSVEG MFDYQRVRND MSRMFS
//