ID   CYM1_ASHGO              Reviewed;         990 AA.
AC   Q759T9;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Mitochondrial presequence protease;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=CYM1; OrderedLocusNames=ADR184W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 374 AND 377.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS52104.2; -; Genomic_DNA.
DR   RefSeq; NP_984280.2; NM_209633.2.
DR   AlphaFoldDB; Q759T9; -.
DR   SMR; Q759T9; -.
DR   STRING; 33169.AAS52104; -.
DR   MEROPS; M16.013; -.
DR   PRIDE; Q759T9; -.
DR   EnsemblFungi; AAS52104; AAS52104; AGOS_ADR184W.
DR   GeneID; 4620442; -.
DR   KEGG; ago:AGOS_ADR184W; -.
DR   eggNOG; KOG2019; Eukaryota.
DR   HOGENOM; CLU_009165_0_0_1; -.
DR   InParanoid; Q759T9; -.
DR   OMA; MTYPDKT; -.
DR   Proteomes; UP000000591; Chromosome IV.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:EnsemblFungi.
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   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; Transit peptide; Zinc.
FT   TRANSIT         1..56
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           57..990
FT                   /note="Mitochondrial presequence protease"
FT                   /id="PRO_0000249940"
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;  112270 MW;  539FBF8FC260EC8A CRC64;
     MLRFQRTVPR VAIRRLANVY SEGAVLHGYK VRRAQEIPEM RMAAVELEHE MTGARHLHLE
     REDQNNVFSV GFRTPPPDAT GVPHILEHTT LCGSQKYPVR DPFFKMLNRS LANFMNAMTA
     HDHTFYPFAT TNQKDFANLR DLYLDATLRP LLRHADFLQE GWRLEHRDVG DASSELVFKG
     VVYNEMKGQV SNADYYFWIR FQEAIYPALH NSGGDPEHIT DLSYEDLVAF HQNHYHPSNA
     KTFTYGNFPL RDTLRKLDDE FRGFGRRAIP QMHEKPLQLR EAVSVEEPCQ IDPMLPADKQ
     CRTSMTWICG NPNDVYETFL LKILGSLLFD GHSSAFYKKL VEETGLAYEL SVNTGVESQT
     AANFLTVGVQ GCTDVGQVHK VIMETFTALL AQPFEKHRVE AILHQLELSK KDQKSDFGLQ
     LLYGILPGWV NNTDPFDLLS LNSALQRFRA DWDREGDGLF QRLLNKYVIG KPSFTFTMVG
     SSDFNQVKDQ NEQSKLKAKV SSLTESDKEV IYKRGLHLQE LQNSEQDLSK LPTLTTADIP
     HSSGHYFVSR DGPITTRQTD TNGITYIRMK RPLKGAIPYD AYPYIPLYSD GLMNIGTLLE
     DASAIEEQIR LHTGGISVSI GVHPNVETRL SELYLEISAC ALNSKTQYVF DIINKIMNET
     ALSVRSEKMK VLIRAAASSF TSYAAENGHD LARLHTGAHF SQTQAIMEQT AGIEQVRHMN
     NLMSIIEKEA EFNTVLQNLE AMHRKIFVAD GLEVMITTDN RQTSDVVKDQ ALKFIAGVQQ
     SAGAESWLPE KYSRRALEKP YPALLQFPFQ VHYTAQSTQG VSYTHPDGAH LQVLASLLTF
     KHLHREVREK GGAYGGGATY NATDGIFNFF SYRDPQPVRS LNIFRNAGKY VLNEARWTAD
     DLNEAKLSIF QRVDAPISPS SEGLLQFRHN ISDEQRDRRR QQLLKSTLDD VRRVADIYLV
     QPSPSQHMSA VVGPELPREV WSSQWPVIKV