ID   CYM1_CANGA              Reviewed;         990 AA.
AC   Q6FUI7;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Mitochondrial presequence protease;
DE            EC=3.4.24.-;
GN   Name=CYM1; OrderedLocusNames=CAGL0F03157g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380952; CAG59031.1; -; Genomic_DNA.
DR   RefSeq; XP_446107.1; XM_446107.1.
DR   AlphaFoldDB; Q6FUI7; -.
DR   SMR; Q6FUI7; -.
DR   STRING; 5478.XP_446107.1; -.
DR   MEROPS; M16.013; -.
DR   PRIDE; Q6FUI7; -.
DR   EnsemblFungi; CAG59031; CAG59031; CAGL0F03157g.
DR   GeneID; 2887720; -.
DR   KEGG; cgr:CAGL0F03157g; -.
DR   CGD; CAL0129172; CAGL0F03157g.
DR   VEuPathDB; FungiDB:CAGL0F03157g; -.
DR   eggNOG; KOG2019; Eukaryota.
DR   HOGENOM; CLU_009165_0_0_1; -.
DR   InParanoid; Q6FUI7; -.
DR   OMA; MTYPDKT; -.
DR   Proteomes; UP000002428; Chromosome F.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:EnsemblFungi.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR013578; Peptidase_M16C_assoc.
DR   Pfam; PF08367; M16C_assoc; 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; Zinc.
FT   CHAIN           1..990
FT                   /note="Mitochondrial presequence protease"
FT                   /id="PRO_0000249944"
FT   ACT_SITE        87
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   990 AA;  111695 MW;  F5AAC8E63BD08EF8 CRC64;
     MLRFQRFAST YNQRAVLRKY PVGGIIHGFQ VRRAVPVPEL KLTAVDLIHE QTGAEHLHID
     RDDKNNVFSI AFRTLPPDAT GVPHILEHTT LCGSEKYPVR DPFFKMLNKS LANFMNAMTG
     PDYTFFPFAT TNARDFVNLR DVYLNSTLRP LLKEQDFYQE GWRLEHSEVT NPKSDIIFKG
     VVFNEMKGQV SNADYHFWSQ FQQNIYPSLN NSGGDPQKIT DLHYQDLVDF HHANYHPSNA
     RTFTYGSFPL EDTLKKVNEE FRAYGKRIIN KKLPKPLELI ETKELTLEGQ IDPMLPAEKQ
     TKTSLTWKCG EPTDLYETFL LKILGNLLLD GHDSIMYKGL IESGLGHDFS VNTGVESMTA
     ANFLTVGIQG SQNVEEFKSK VFDLFKEFIE NDVDSNKVDA IIHQLELSKK DQKADFGLQI
     LYSILPGWTN GIDPIEGLEF DELIGRLKSD FKENGTKIFK NILDKYIIDQ PYFHFTMKGS
     EEFSSKLAAE ESTKLDKKLK ELDETDRKAI FERGLLLEAA QNHKEDLSCL PTLGVADISR
     KVDTYDLNTN ANITVRNTAT NGISYIRGKK LINDMIPLEL YPFLSLFAAS LTHLGTKTTP
     YGAIDNEIKL HTGGISTNIS VNADPTTLQP NLYFDMSGFS LNEKSDYIFN FLKTILMETD
     FSTHKDKLKV LINSIASSNT SHIADSGHTV ARSFASGHLS TVAAIQEHIS GVEHYKLISR
     LCSIMNDDKL FQSEVIDKLV MLQRIIVNSQ NMEFFASVDC QAQENKIRKE VDYFVSTLPN
     TSSDISGAIQ TACVPRYSDS QVLNLIKFPF QVHYTAQAYN GVSYTHKDGA ALQVLANMLT
     FKHLHKEIRE KGGAYGGGAT FSALSGIFSY YSYRDPNPLA SIQTFEKSAS YVLNDAKWTQ
     SDLDESKLSI FQQVDAPISP KSEGSTFFNL GVTDEMRQVR REQLLDTSLL DIHRVAERYI
     LPNKSIATVV GPGIDGETVS PKWHIEDIKV