CYM1_GIBZE
ID CYM1_GIBZE Reviewed; 1004 AA.
AC Q4IA56; A0A098DZE2; A0A0E0SLA3; V6RJ37;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Mitochondrial presequence protease;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=CYM1; ORFNames=FGRRES_05902, FGSG_05902;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
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; DS231665; ESU11935.1; -; Genomic_DNA.
DR EMBL; HG970334; CEF87216.1; -; Genomic_DNA.
DR RefSeq; XP_011324511.1; XM_011326209.1.
DR AlphaFoldDB; Q4IA56; -.
DR SMR; Q4IA56; -.
DR STRING; 5518.FGSG_05902P0; -.
DR PRIDE; Q4IA56; -.
DR EnsemblFungi; ESU11935; ESU11935; FGSG_05902.
DR GeneID; 23553054; -.
DR KEGG; fgr:FGSG_05902; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G19043; -.
DR eggNOG; KOG2019; Eukaryota.
DR HOGENOM; CLU_009165_0_0_1; -.
DR InParanoid; Q4IA56; -.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 35..1004
FT /note="Mitochondrial presequence protease"
FT /id="PRO_0000249947"
FT ACT_SITE 87
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1004 AA; 111979 MW; 13252944EB43FE20 CRC64;
MLRNAAAGAR KAVTELSQFP KPGEKLHGFT LVRSKHVPEL ELTALHLQHD KTGADYLHIA
RDDSNNVFSI GFKTNPPDDT GIPHILEHTT LCGSEKYPIR DPFFKMLPRT LSNFMNAFTA
SDHTFYPFAT TNAQDFKNLM SVYLDSTLHP LLKKSDFTQE GWRIGPENPL AEDEASKKLV
FKGVVYNEMK GQMSDAGYLY YIRFHDHIFP DINNSGGDPQ KITDLTYEQL QKFHAEHYHP
SNAKVFTYGD MPLIDHLKQV DTQLQAFEKI QGDKQVHEPV TLNGPKEVTL YGPLDPLVDQ
DRQYKTSVSW IMGDTTDVLE SFSLALLSTL LMDGYGSPLY RGLIEAGMGA DWSPNAGYDS
SAKKGIFSIG LTGVQEGDVP KLKEKVQQIL RDARNKGFDK TKIDGSLHQL ELSLKHKTAN
FGFSMLNRLK PKWFNGVDPF DSLAWNDTIN GFQAKMAEGN YLEGLIDKYL LNDNTLTFTM
APSTTYGEDL VKEEQERLST RIQAAIKEAG SEEKARKHFE KQEQELLVEQ NKTNTEDLGC
LPTVHVKDIP RSKEAVVVRD ENANGTKIQW HEAPTNGLTY FRAINTLENL PDELRELVPL
FTDSIMRLGT KDLNMEQLED LIKLKTGGVS VGYHCTPSPT DFHAASEGII FTGMALDHNV
PVMFDIIQKL VLGTDFDSPE AALRIRQLLQ ASADGVVNDI ASTGHRFAMG SAESGLTRSA
WLRQQVSGLS QVQLVTSLAS RPETDKLEDV ISKLKQIQNL ALVGGNLRTA ITCGSESVAA
NGASLQNFVG NLSRDPLNLK NPSPRQLPKD SKTFYPLPYQ VYYGGLSLPT TSYTSAEGAP
LQILSQLLTH KHLHHEIREK GGAYGGGAYS RALDGLFGFY SYRDPNPQNT LSIMRNAGQW
AVDKKWSDRD LEEAKISVFQ GVDAPKSVNQ EGMGRFLSGI TEEMKQKKRE QFLDVTKDQV
REAAQRYLVD GLAKGEGRVA FLGEKQAWVD GEWQIREMDV KGAE
