CYM1_DEBHA
ID CYM1_DEBHA Reviewed; 1063 AA.
AC Q6BTC0;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Mitochondrial presequence protease;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=CYM1; OrderedLocusNames=DEHA2D01892g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382136; CAG86682.2; -; Genomic_DNA.
DR RefSeq; XP_458550.2; XM_458550.1.
DR AlphaFoldDB; Q6BTC0; -.
DR SMR; Q6BTC0; -.
DR STRING; 4959.XP_458550.2; -.
DR MEROPS; M16.013; -.
DR EnsemblFungi; CAG86682; CAG86682; DEHA2D01892g.
DR GeneID; 2901568; -.
DR KEGG; dha:DEHA2D01892g; -.
DR VEuPathDB; FungiDB:DEHA2D01892g; -.
DR eggNOG; KOG2019; Eukaryota.
DR HOGENOM; CLU_009165_0_0_1; -.
DR InParanoid; Q6BTC0; -.
DR OMA; MTYPDKT; -.
DR OrthoDB; 107079at2759; -.
DR Proteomes; UP000000599; Chromosome D.
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; 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..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..1063
FT /note="Mitochondrial presequence protease"
FT /id="PRO_0000249945"
FT ACT_SITE 108
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1063 AA; 120013 MW; E91844C0B1FE2086 CRC64;
MLRLANRVSR KDSGNLGIAQ LKKRLLATSG VSQGEILSKY PIGLNMHGYV IEQVQPIPEF
SLVAVKLKHS RTGSEHLHLD TPNDKNNVFS VAFKTNAPDA TGVPHILEHT TLCGSFKYPV
RDPFFKMLNR SLSNFMNAMT GHDYTYYPFA TTNAKDFENL MDVYLSSVFE PLLTHESFMQ
EGWRLENSDL SDPKSPIIFK GVVYNEMKGQ YSNSAYYYWI KFQEAIYGSL NNSGGNPNEI
TDLRYEDLVD FHSSNYHPSN AKTFTYGNIE LVNHLNKLNE FFESFGSRGI RTNVRKPITE
LNPNYESDVT VKGPLDTMSS RPIEEQYKSS ITWVIGNPLD ESKLYDVFKW KVLSSLLCDG
HNSPFYQELI EKEYGEDFAV NYGLDATTAL LSFTIGLNNL SLEKAKNLED KVRGIFVEKI
IPELQKGKES GFNDRIEAIL HQIELNFKNH KPEFGIGLLS SVVSTWVNGL NPVKSLQIDH
ILNRFKEDYK LNGLKMFQDL LDESVLKDDT PKFKFTMEPD ESFGKNLTSQ ETERLNKKIE
ALTEEDKEII YKRSIELAEK QKKEEDVSAL PTLTVKDIPR EGDFYPLDFA DINSKKLQKR
IVDTNGLIYM NATKDISYLP SKYYEYLPLF DCCLTNLAGT SKTPITELEI KIQKLTGGVT
FNVSAKTDPF DISKTNMKFM LSGMALKDKS QNVYDLWFEI LTQTKFDSED EQVVDKLFTL
VKNLGQNQMN TIADSGHSYA NSYSNSQLTP TKYIHNLIGG IGQVSFISDL NRKLETEGRD
FLKKELLPVL KDIQRHLVNG FTDGNHSGFE YSLVGDSESV IKNEKMIKEF DDLLTANSNR
VAGTNELSSL ISQFNSNKLG LNNNGRSTLI DLPFQVGYAS LAKLGAAYTS KDGAALRVLS
QLLTFKHLHS VIREANGAYG GGLSFDGLGG CLNFYSYRDP NPLTSVQSFK DSTSVALGKM
INSENNGWSP KDLQEAKLTI FQGVDAPSHI SSQGSLDFLE HITDEMRQER RERFLDVTYE
DLKNVTEKYL LNGSQDIVTV IGDNETLKID SSDAQWNIKK LTA
