ID   CYM1_ASPOR              Reviewed;        1025 AA.
AC   Q2UGN1;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Mitochondrial presequence protease;
DE            EC=3.4.24.-;
GN   Name=cym1; ORFNames=AO090023000781;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007157; BAE59284.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2UGN1; -.
DR   SMR; Q2UGN1; -.
DR   STRING; 510516.Q2UGN1; -.
DR   EnsemblFungi; BAE59284; BAE59284; AO090023000781.
DR   HOGENOM; CLU_009165_0_0_1; -.
DR   OMA; MTYPDKT; -.
DR   Proteomes; UP000006564; Chromosome 3.
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; 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..1025
FT                   /note="Mitochondrial presequence protease"
FT                   /id="PRO_0000249942"
FT   ACT_SITE        93
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1025 AA;  114432 MW;  93B2F0BB226DCC16 CRC64;
     MAADDIVGCY QVDKARRSLT NVESYPKVGE QLHGFTVQEK KHVPELHLTA VRLKHDKTDA
     DYLHVAREDK NNVFGVGFKT NPPDATGVPH ILEHTTLCGS EKYPVRDPFF KMLPRSLSNF
     MNAFTSADHT TYPFATTNQQ DFQNLLSVYL DATLHPLLKE EDFRQEGWRL GPEDPRASDA
     LDGKPEDVLF KGVVYNEMKG QISDANYLYY IKYRESIFPA LNNSGGDPQY ITDLTHKQLV
     EFSKRNYHPS NAKFLTYGDM PLSTHLKQIG DVLDGFGKGE ADTSVKLPID LSRGPSNVTV
     PGPIDTFADA DKQYKTSTSW YLGDTSEVVE TFSAGILSSL LLDGYGSPMY RALIESGLGS
     SFTPNTGLDT SGRVPVLSVG LTGVSEEDAP KVKEAIQKVY QDSLSAGFSD EKVQGFLHQL
     ELALRHKTAN FGIGVMEKTI SSWFNGVDPM KELAWNDVIN EFKRRYQQGG YLESLMQKYL
     MNDRCLTFTM VGTPTFHQEL DQQEMVRKEK KLSQLVEQHG SMEKAISSLR EQELQLLKTQ
     EEAQHADLGC LPSLRVEDIS REKERKPVRE SKVDDVDVVW REAPTNGLTY FQALNAFEDL
     PDDLRLLMPL FNDSVMRLGT ANKTMEQWED LIKLKTGGVS SSAFHTSSPT ELGKFNEGLQ
     FSGFALDKNI PDMLEILTTL ITETDFTSPY APAMIQELLR LTTNGALDSV AASGHRFALN
     AAAAGLSRSF WVQEQQSGLA QLQATANLLR DAETSPERLA ELIEKLRLIQ SFAISKSSSL
     RVRMVCEPSS AHQNEVVLQK WLAGLPQIRS PTSVDARSMQ QVSSKAFYDM PYKVYYSGLA
     MQTVPFVHKS SAPLSVLSQL LTHNYLHPEI REKGGAYGAA ASNGPVKGIF ALTSYRDPNP
     LNTLKVFQNS GIFARDRSWS ERELNEAKLG IFQGLDAPVS VDEEGSRYFM SGVTHEMDQR
     WREQLLDVTA RDVNEVAQTF LVDGPRQSVC LLGEKKDWAE DWDVRKLSMN AGEAEAYPED
     ASTTA