ID   A0A4Q9LVT9_9MICR        Unreviewed;       467 AA.
AC   A0A4Q9LVT9;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 11.
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=CWI38_0737p0030 {ECO:0000313|EMBL:TBU12487.1};
OS   Hamiltosporidium tvaerminnensis.
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Dubosqiidae;
OC   Hamiltosporidium.
OX   NCBI_TaxID=1176355 {ECO:0000313|EMBL:TBU12487.1, ECO:0000313|Proteomes:UP000292282};
RN   [1] {ECO:0000313|EMBL:TBU12487.1, ECO:0000313|Proteomes:UP000292282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL-G-3 {ECO:0000313|EMBL:TBU12487.1};
RA   Pombert J.-F., Haag K.L., Ebert D.;
RL   Submitted (DEC-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TBU12487.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; PITK01000737; TBU12487.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Q9LVT9; -.
DR   STRING; 1176355.A0A4Q9LVT9; -.
DR   VEuPathDB; MicrosporidiaDB:CWI38_0737p0030; -.
DR   Proteomes; UP000292282; 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; 1.
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; 1.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000292282}.
FT   DOMAIN          25..161
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          167..218
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   467 AA;  54717 MW;  C586713B306CF389 CRC64;
     MLASILDISI NKIKKGPIIL TKCVQNDDSV ISIFVKNGSS NENQNNNGIS HFIEHMVFNG
     SKKFPKNITN EILNKKFSYY SAYTTREYTN FLFKTKNLLE TISFIFNILR FPRFNTKDIE
     NEAKTILKEH ESVNSNLIEK KLDFVHKKLF KNALGYPILG PVSNIKSFSK NQLKKFHLTT
     YKPENFLICV SSKYTHNQIL EIIANTFYKS KKSKKFESNI FLDKNIKFDN IVNSIKSIYK
     DLKKINNEGD NENNNCEKLK ELYFVEGKEY KEIEENKGIN KAGDSNNEGN IDDKNKFYTD
     ESNLKNLNEI KNSKFLKNSE ISKVENEVIN KKRMIIKKND IVGIKIGGYK NILHLHILIL
     CKILREKHNL NIFYIPYEKR GILLFFKEDD NLDIKNKIIT FNELESTKKV FLNDIYSIFN
     SSKDFFDFFG PEILFKMNLL LYSPHIINYI NLKHINLFKE KIVEIVK
//