ID   CYM1_NEUCR              Reviewed;        1012 AA.
AC   Q7S7C0;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Mitochondrial presequence protease;
DE            EC=3.4.24.-;
GN   Name=cym-1; ORFNames=B13M13.120, NCU01272;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; BX842618; CAE76121.1; -; Genomic_DNA.
DR   EMBL; CM002240; EAA31514.1; -; Genomic_DNA.
DR   RefSeq; XP_960750.1; XM_955657.2.
DR   AlphaFoldDB; Q7S7C0; -.
DR   SMR; Q7S7C0; -.
DR   STRING; 5141.EFNCRP00000004190; -.
DR   EnsemblFungi; EAA31514; EAA31514; NCU01272.
DR   GeneID; 3876900; -.
DR   KEGG; ncr:NCU01272; -.
DR   VEuPathDB; FungiDB:NCU01272; -.
DR   HOGENOM; CLU_009165_0_0_1; -.
DR   InParanoid; Q7S7C0; -.
DR   OMA; MTYPDKT; -.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
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; Zinc.
FT   CHAIN           1..1012
FT                   /note="Mitochondrial presequence protease"
FT                   /id="PRO_0000249949"
FT   ACT_SITE        88
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
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         196
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1012 AA;  112825 MW;  B8A54F7D28005210 CRC64;
     MLRNATKGAA RRAVTELSQY PKPGEKLHGF TLLRSKHVPE LELTALHLQH DKTGAEHLHI
     ARDDSNNVFS IGFKTNPPDD TGVPHILEHT TLCGSQKYPI RDPFFKMLPR TLSNFMNAFT
     ASDHTFYPFA TTNAQDFKNL MSVYLDATLH PLLKETDFTQ EGWRIGPENP QALVAAEGNA
     KPEDRKLVFK GVVYNEMKGQ MSDAAYLFWI RFQDHIFPDI HNSGGDPQKI TDLTYQQLKK
     FHADHYHPSN AKVFTYGDMP LADHLKEIGA QLDVFEKIRA DVAHHSPIDL SSGPREVKLY
     GPIDPLVDAN KQFKTSVSWV LGETNNVVES FSLALISALL MDGYGSPLYK GLIESGLGTD
     WSPNTGYDSS GKLGIFSIGL SGVQEEDVPK VKAKVQEILR SMRDKGFERS KIDGYLHQLE
     LGLKHKTANF GMSLLHRLKP KWFVGVDPFD SLAWNDTIAA FETELAKGGY LEGLIDKYLI
     NDNTLSFTMA PSPTFSQELA QEEETRLSTK ISEVVKAAGS EEEARAALEA RELKLLAEQS
     KTNTEDLGCL PSVHVKDIPR QKDSVILRHD NTARVKTQWH EAPTNGLTYF RAINQLENLP
     DELRSLIPLF TDSIMRLGTK DMTMEQLEDL IKLKTGGVSV GYHSASHPTD FTRATEGLMF
     SGMALDRHVP TMFDLLRKLV VETDFDSPQA AQQIRQLLQA SADGVVNDIA SSGHAYARRA
     AESGLTWDSF LKEQVSGLSQ VKLVTSLASR PESDPLEDVI AKLKQIQQFA LAGNLRTAIT
     CDSGSVSDNA KALLNFVNSL PSEAVTFPSR GPPNFTRDIK TFYPLPYQVY YGALALPTAS
     YTASVNAPLQ ILSQLLTHKH LHHEIREKGG AYGGGSYARP LDGIFGFYSY RDPNPVNTLK
     IMRNAGQWAV DKEWTDRDLE DAKISVFQGV DAPKAVNEEG MAQFLYGITD EMKQKRREEL
     LDVTKDQVRE VAQEYVVKAL NNGSERVVFL GEKRDWVDKS WAVKEMDING ST