ID   CYM1_ASPFU              Reviewed;        1065 AA.
AC   Q4WP38;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Mitochondrial presequence protease;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=cym1; ORFNames=AFUA_4G07910;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(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; AAHF01000005; EAL89996.1; -; Genomic_DNA.
DR   RefSeq; XP_752034.1; XM_746941.1.
DR   AlphaFoldDB; Q4WP38; -.
DR   SMR; Q4WP38; -.
DR   STRING; 746128.CADAFUBP00006327; -.
DR   PRIDE; Q4WP38; -.
DR   EnsemblFungi; EAL89996; EAL89996; AFUA_4G07910.
DR   GeneID; 3508886; -.
DR   KEGG; afm:AFUA_4G07910; -.
DR   VEuPathDB; FungiDB:Afu4g07910; -.
DR   eggNOG; KOG2019; Eukaryota.
DR   HOGENOM; CLU_009165_0_0_1; -.
DR   InParanoid; Q4WP38; -.
DR   OMA; MTYPDKT; -.
DR   OrthoDB; 107079at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
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; 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; Transit peptide; Zinc.
FT   TRANSIT         1..42
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           43..1065
FT                   /note="Mitochondrial presequence protease"
FT                   /id="PRO_0000249941"
FT   ACT_SITE        120
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         230
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1065 AA;  118563 MW;  E139B99443CAAF83 CRC64;
     MLRSFSGAGK CKCRIPVSRQ PVCGRSLRIS STLTPWNQSR RAASTVTSLD SFPNVGEKLH
     GFTVQEKKHV PELHLTAVRL KHDKTDADYL HVAREDKNNV FGIGFKTNPP DATGVPHILE
     HTTLCGSEKY PIRDPFFKML PRSLSNFMNA FTSADHTTYP FATTNRQDFQ NLLSVYLDAT
     LHPLLKEEDF RQEGWRLGPE DPRSILTQGE QSKGNLQSED VVFKGVVYNE MKGQISDANY
     LYYIKYRESI CPSLNNSGGD PQYITDLTHQ QLVDFSKRNY HPSNAKILTY GDMPLSVHLK
     QIGEVLDGFE KGQADTDVKL PLDLSRGPLN VTVPGPIDTF ASEDKQYKTS TSWYMGDTTD
     VVETFSVGIL SSLLLDGYGS PMYRALIEGG LGSSFTPNTG LDSSGRVPIF SVGLTGVSEA
     DAPKVKSTIK RVFEESLSSG FNDEKVQGFL HQLELALRHK TANFGIGVME KTLSSWFNGS
     NPMKELSWNE VIDEFKKKYE QGGYLESLMQ KYLMNDNCLT FTMVGTPSYN KDLDDQEMVR
     KEKKLSELVE RHGSVEQAVS ALAEEELQLL KIQEEAQNAD LSCLPSLRVE DISREKERKP
     VRESKMDDID VVWREAPTNG LTYFQALNSF EELPDDLRLL LPLFNDCIMR LGTGDKTMEQ
     WEDLIKLKTG GITTSTLHTS SPTELGKFRE GLQFSGYALD NNIPDMLQIL TTLVTETDFT
     SPHAPAMIQE LLRMTTNGAL DAVAGSGHRY ALNAAAAGLS RSFWVQEQQS GLAQLQATAN
     LLRDAESSPE RLAELIDKLR LIQSFAISKG SGLRVRMVCE PSSASQNEIV LQKWLAGLPR
     NRSPTSPLDH TSVNSVANRV FYDLPYKVYY SGLAMQTVPF IDPSSAPLSV LSQLLTHKYL
     HPEIREKGGA YGAGASNGPI KGFFAFTSYR DPNPVNSLKV FQNSGIFARD RAWSDRELAE
     AKLGIFQGLD APMSVDEEGA RYFMSGVTHE MDQRWREQVL DVTAKDVNEV AQKFLVEGSR
     QSICLLGEKK DWADSDDWEV RKLSMNASGE PVIDPLSQDG AVASA