ID   CYM1_KLULA              Reviewed;         982 AA.
AC   Q6CWW6;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Mitochondrial presequence protease;
DE            EC=3.4.24.-;
GN   Name=CYM1; OrderedLocusNames=KLLA0B00957g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382122; CAH01966.1; -; Genomic_DNA.
DR   RefSeq; XP_451573.1; XM_451573.1.
DR   AlphaFoldDB; Q6CWW6; -.
DR   SMR; Q6CWW6; -.
DR   STRING; 28985.XP_451573.1; -.
DR   MEROPS; M16.013; -.
DR   EnsemblFungi; CAH01966; CAH01966; KLLA0_B00957g.
DR   GeneID; 2897482; -.
DR   KEGG; kla:KLLA0_B00957g; -.
DR   eggNOG; KOG2019; Eukaryota.
DR   HOGENOM; CLU_009165_0_0_1; -.
DR   InParanoid; Q6CWW6; -.
DR   OMA; MTYPDKT; -.
DR   Proteomes; UP000000598; Chromosome B.
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; 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; Zinc.
FT   CHAIN           1..982
FT                   /note="Mitochondrial presequence protease"
FT                   /id="PRO_0000249948"
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   982 AA;  112030 MW;  E8A490477F9FBFDE CRC64;
     MFQIRNYATK YAQSRALRKY PVGGVFHGYE VKRLLPVPEL KLTAVDLLHN QTGSQHLHID
     RDDNNNVFSI GFKTNPPDST GVPHILEHTT LCGSHKYPVR DPFFKMLNRS LANFMNAMTG
     HDYTFYPFAT TNETDFANLR DVYLDATLNP LLNQQDFLQE GWRLEHTKVD DPNSDIGFKG
     VVYNEMKGQV SNANYYFWIK FQESYYPSLN NSGGDPTKMT DLQYEDLISF HRNNYHPSNA
     KTFTYGNFDL NNTLQRLNKE YQGYGRRGSK KRELLPIQMK EDVSVETEGQ VDPMLPPDKQ
     IKTSVTWICG KPEDTYQTFL LKILGNLLLD GHSSPFYQKL IESGLAYDFS VNTGVESQTA
     ANFITIGVQG CDEVDSIYEV INKVWEEVLQ NPFEESRIQA IIQQLELSKK DQRADFGLQL
     LYSVLPGWVN KTDPFDSLLF DETLERFQED WATKGDNLFK DLIKEFVISK PVFKFTMKGS
     ETFSQKLDAE EQERLERKLK LLDEEDKKVI FERGKQLQEL QDLKEDLSCL PSLQISAIPR
     VSKTYPLLEK DNVLNRITDT NGITYVRGKR LLNHHIPREL YPFLPLYADS LTNLGTSTEE
     FSTIEEQIKL HTGGVSTRVS VNPDAQTGKP MLLFQVDGWA LNSKTDHIFK FWKKLLCETD
     FHKHKEKLKV LIRSLASSNT ASVAETGHAF ARNFGAAHLS VTKAINESLN GIEQLQLINK
     LSQCLDDEAL FEKEVVSKLV ELQSYINGSS DMKFMITSDS QVQIDAVHQQ ITGFLSSLPK
     DSKPCDFYSE NYSMLENPGK PTLLQFPFQV HYTAKCYPGV SYTHPDGAKL QILSNMLTHK
     YLHREIREKG GAYGGGATYS ALDGTFSFYS YRDPHALNSL STFDSVPEFI LNKSSWGEPD
     LNEAKLSVFQ QVDSPMSAKN EGTILFHYDV TDEMKQRRRE QLLDVNLNDI HQVAEEYLKQ
     DKSIASIVGP EIPNFDALVQ TV