ID   CYM1_SCHPO              Reviewed;         882 AA.
AC   O42908;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Mitochondrial presequence protease;
DE            EC=3.4.24.-;
GN   Name=cym1; ORFNames=SPBC119.17;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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}.
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; CU329671; CAA17932.3; -; Genomic_DNA.
DR   PIR; T39315; T39315.
DR   RefSeq; NP_595299.2; NM_001021206.3.
DR   AlphaFoldDB; O42908; -.
DR   SMR; O42908; -.
DR   STRING; 4896.SPBC119.17.1; -.
DR   MEROPS; M16.A19; -.
DR   MaxQB; O42908; -.
DR   PaxDb; O42908; -.
DR   GeneID; 2540111; -.
DR   KEGG; spo:SPBC119.17; -.
DR   PomBase; SPBC119.17; cym1.
DR   eggNOG; KOG2019; Eukaryota.
DR   InParanoid; O42908; -.
DR   PhylomeDB; O42908; -.
DR   Reactome; R-SPO-1268020; Mitochondrial protein import.
DR   PRO; PR:O42908; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISO:PomBase.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
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:0006627; P:protein processing involved in protein targeting to mitochondrion; ISO:PomBase.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISO:PomBase.
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; 1.
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..882
FT                   /note="Mitochondrial presequence protease"
FT                   /id="PRO_0000178015"
FT   ACT_SITE        94
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         192
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   882 AA;  98971 MW;  6F1DA9A346717C60 CRC64;
     MNYAKLSIAF SKKTIKTHNC RLFQRWLHVG DKVHDFRVVD TKKVPELQLN YTRLKHEPTN
     ADMIHLDRED PNSVFSIGFQ TPAENDEGIP HILEHTTLCG SNKYPVRDPF FKMLNRSLAT
     FMNAFTASDF TFYPFATVNT TDYKNLRDVY LDATLFPKLR KLDFLQEGWR FEHADVNDKK
     SPIIFNGVVY NEMKGQVSDS SYIFYMLFQQ HLFQGTAYGF NSGGDPLAIP DLKYEELVKF
     HRSHYHPSNA KILSYGSFPL EDNLSALSET FRPFSKRELN LPNTFLKEFD QEKRVVEYGP
     LDPVMAPGRQ VKTSISFLAN DTSNVYETFA LKVLSKLCFD GFSSPFYKAL IESGLGTDFA
     PNSGYDSTTK RGIFSVGLEG ASEESLAKIE NLVYSIFNDL ALKGFENEKL EAILHQMEIS
     LKHKSAHFGI GLAQSLPFNW FNGADPADWL SFNKQIEWLK QKNSDGKLFQ KLIKKYILEN
     KSRFVFTMLP SSTFPQRLQE AEAKKLQERT SKLTDEDIAE IEKTSVKLLE AQSTPADTSC
     LPTLSVSDIP ETIDETKLKF LDIAGMKAQW YDLAAGLTYI RLLLPLKNFP ESLIPYLPVY
     CDACLNLGTH SESIGDLEHQ IRRYTGGISI SPSAVTNNSD VSKYELGIAI SGYALDKNVG
     KLVELINKAF WNTNLSNTDK LAIMLKTSVS GITDGIAEKG HSFAKVSSAS GLTEKTSITE
     QLGGLTQVKL LSQLSREESF GPLVEKLTAI REILRGTSGF KAAINASPTQ HEVVEKALQK
     FMKSRGVNQQ TQTKSTSKER NGINSIKTYH ELPFQTYFAA KSCLGVPYTH PDGAPLQILS
     SLLTHKYLHG EIREKGGAYG AGLSYSGIDG VLSFFTYRDS DP