ID   CYM1_EMENI              Reviewed;        1049 AA.
AC   Q5B6H7; C8V6H9;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Mitochondrial presequence protease;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=cym1; ORFNames=AN3853;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000062; EAA59118.1; -; Genomic_DNA.
DR   EMBL; BN001302; CBF75238.1; -; Genomic_DNA.
DR   RefSeq; XP_661457.1; XM_656365.1.
DR   AlphaFoldDB; Q5B6H7; -.
DR   SMR; Q5B6H7; -.
DR   STRING; 162425.CADANIAP00004852; -.
DR   EnsemblFungi; CBF75238; CBF75238; ANIA_03853.
DR   EnsemblFungi; EAA59118; EAA59118; AN3853.2.
DR   GeneID; 2873276; -.
DR   KEGG; ani:AN3853.2; -.
DR   VEuPathDB; FungiDB:AN3853; -.
DR   eggNOG; KOG2019; Eukaryota.
DR   HOGENOM; CLU_009165_0_0_1; -.
DR   InParanoid; Q5B6H7; -.
DR   OMA; MTYPDKT; -.
DR   OrthoDB; 107079at2759; -.
DR   Proteomes; UP000000560; Chromosome II.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
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:0097308; P:cellular response to farnesol; IEP:AspGD.
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..39
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..1049
FT                   /note="Mitochondrial presequence protease"
FT                   /id="PRO_0000249946"
FT   ACT_SITE        116
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
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         222
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1049 AA;  117040 MW;  17233EE9F5E2D091 CRC64;
     MLRSYLHLGR HRTPAFRQPL GRLLRPTASI LQYAQSRTLA SVSSLESLPE VGDQLHGFTV
     QEKKQVPELH LTAIRLRHDK THADYLHIAR EDKNNVFGIG FKTNPPDATG VPHILEHTTL
     CGSEKYPIRD PFFKMLPRSL SNFMNAFTSS DHTMYPFATT NQQDFQNLLS VYLDATMHPL
     LKEEDFRQEG WRLGPEDPRA IQTQEGNLKP EDILFKGVVY NEMKGQMSDA NYLYWIRFQE
     SIFPAINNSG GDPQHITDLT HKQLVEFSKK NYNPSNAKII TYGDMPLADH LKQVGGVLND
     FSKGAVDTTV KLPIELRGPI NVTVPGPIDT FVSEDRQFKT STSWYMGDIT DTVETFSAGI
     LSSLLLDGYG SPMYKALIES GLGSSFTPNT GLDTSGKIPI FSIGVTGVSE EQAPRVKEEI
     QRVLQETLQR GFNDEKVQGF LHQLELALRH KTANFGLGVI QKTFTSWFNG SDPMKELAWN
     EVINAFKSRY EKGGYLEALM QKYLINDNCL TFTMVGTPSF NKELDDKEMA RKEKKFEQLT
     QQHGSVEKAV TELAKAELQL LEVQEKAQHA DLSCLPSLRV EDISRQKEHK PVRESKVEGT
     DIVWREAPTN GLTYFQAVNA FADLPDDLRL LLPLFNDAIM RLGTPTRTME QWEDLIKLKT
     GGVSTSNFHT TSPTEMGKYT EGLQFSGFAL DKNVPDMLEI LTALVTETDF TSPSAPAMIQ
     ELLRLTTNGA LDAVAGTGHR YALNAAAAGL SRSFWAQEQT SGLAQLQATA NLLRDAETSP
     ERLAELIEKL RLIQSFAISK TSGLRVRLVC EPASSTQNES VLQRWVTGLP KVPSPTSQPQ
     RFDLSTPSKK AFYDLPYKVY YSGLALPTVP FTHSSSATLS VLSQLLTHNY LHPEIREKGG
     AYGAGASNGP VKGLFAFTSY RDPNPANTLK VFKNSGVFAR DRAWSDREIN EAKLGIFQGL
     DAPVSVDEEG SRYFLNGITH EMDQRWREQV LDVTAKDVNE VAQTFLVDGT RRSVCLLGEK
     KDWAESEGWE VRKLSMNPNG SNIPSGDAA