ID   CYM1_YARLI              Reviewed;         990 AA.
AC   Q6C0U8;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Mitochondrial presequence protease;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=CYM1; OrderedLocusNames=YALI0F21615g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: ATP-independent protease that degrades mitochondrial transit
CC       peptides after their cleavage. Also degrades other unstructured
CC       peptides (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. PreP subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR382132; CAG78525.1; -; Genomic_DNA.
DR   RefSeq; XP_505714.1; XM_505714.1.
DR   AlphaFoldDB; Q6C0U8; -.
DR   SMR; Q6C0U8; -.
DR   STRING; 4952.CAG78525; -.
DR   PRIDE; Q6C0U8; -.
DR   EnsemblFungi; CAG78525; CAG78525; YALI0_F21615g.
DR   GeneID; 2907820; -.
DR   KEGG; yli:YALI0F21615g; -.
DR   VEuPathDB; FungiDB:YALI0_F21615g; -.
DR   HOGENOM; CLU_009165_0_0_1; -.
DR   InParanoid; Q6C0U8; -.
DR   OMA; MTYPDKT; -.
DR   Proteomes; UP000001300; Chromosome F.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0016485; P:protein processing; IBA:GO_Central.
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   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; SSF63411; 4.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease;
KW   Reference proteome; Transit peptide; Zinc.
FT   TRANSIT         1..25
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..990
FT                   /note="Mitochondrial presequence protease"
FT                   /id="PRO_0000249950"
FT   ACT_SITE        92
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   990 AA;  110840 MW;  F9927E03CB8CD80B CRC64;
     MLRLKSLKKP VQAVVRRFAT TSAPTLSVGD NIHGFNVLRT KEIPEFDLQA TLLEHSTGAQ
     HLHIARDDSN NVFSIGFKTN PPDRTGVPHI LEHTTLCGSE KYQVRDPFFK MLNRSLANFM
     NAMTAQDYTF YPFATTNATD MKNLRDVYLD ATLKPLLREL DFSQEGWRLE NEDSKDKTSP
     IILKGVVFNE MKGQMSNAAY AFYIRYLEKI YPSLNNSGGD PLVIPELTYE GLKKFHADHY
     NPSNAKTFSY GDISVADHLE ALNAKFENCE ISKTPGNTER LPLEFSSAAE NTRIVEEGPI
     DTLLDTSKQH KMSMSWLMGS PKDIYESFCV KIISSLLIDG HSSPLHQKLI DSGLGSSYSP
     NTGLDSAPGA NIFSVGLQGV TESDLTKVET VILDTIKTTV AEGFDKGRID GLLHQTELAR
     KDQNAKFGMA LMNGVLPGWF NQVDPLEALE WNSVLDRFNK DMEADPEFLQ KVMKKYLLDN
     KYFHFQMNPN PDYEKNVQEK EDEILTDKLA KLTESDKEEI FETGANLEKM QEEPENLDCL
     PTLHVSDIPR SKPRVALEHT KNPYPIQWRL APTNGLTYFH SISSLEGLPH EYYPFLPLFT
     SSLTFLGTKD KTMGQLEDEI KLNTGGLDFS VSCSSSPLSL PSSQLNFAMD GVALDKNVET
     MFGLFQELLR NTDFTNVEKL KTMIAASTAN LSNALAQSGH SFAMLRAASD ISPVKKIDDI
     LGGVAQVRFL SELAAKSEQQ LVDEVIPKLQ EIAKFALTRE QRFAVTCGQD MQTKNDELVR
     KFAESFETNE SPFNISSLSI PMTTPTSTLF KLPFQVNYAG IAIPGVPYTH ADGAPLQVLA
     NMLTHKHLHR EIREKGGAYG GGASYNPTDG FFSYYSYRDP NLERTLQTCQ EAGEWSVKKD
     WSSSDLQEAK LSLFQRIDAP ISVKSEGMAL YANGLTYEQR EKRRRQLLDV AVDDVKRVAK
     QYLVNPSGYS VAALGPGYET MDKKKWTVLE