CYM1_CANAL
ID CYM1_CANAL Reviewed; 1034 AA.
AC Q5A301; A0A1D8PKI2;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Mitochondrial presequence protease;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=CYM1; OrderedLocusNames=CAALFM_C306230WA; ORFNames=CaO19.7410;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017625; AOW28630.1; -; Genomic_DNA.
DR RefSeq; XP_716075.1; XM_710982.1.
DR AlphaFoldDB; Q5A301; -.
DR SMR; Q5A301; -.
DR BioGRID; 1225338; 1.
DR STRING; 237561.Q5A301; -.
DR MEROPS; M16.013; -.
DR GeneID; 3642244; -.
DR KEGG; cal:CAALFM_C306230WA; -.
DR CGD; CAL0000201699; CYM1.
DR VEuPathDB; FungiDB:C3_06230W_A; -.
DR eggNOG; KOG2019; Eukaryota.
DR HOGENOM; CLU_009165_0_0_1; -.
DR InParanoid; Q5A301; -.
DR OMA; MTYPDKT; -.
DR OrthoDB; 107079at2759; -.
DR Proteomes; UP000000559; Chromosome 3.
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 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..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..1034
FT /note="Mitochondrial presequence protease"
FT /id="PRO_0000249943"
FT ACT_SITE 100
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1034 AA; 117525 MW; 1FAF39E8F061F121 CRC64;
MLKTRLKQSR AISRVVRRYA CSHPISPNLD KYPVGLKLHG YEVTQTSPIP EFSLTAVSLK
HTESGATHLH LDSPNDSNNV FSIAFKTNPP DNTGVPHILE HTTLCGSKKF PVRDPFFKMT
NRSLSNFMNA MTGHDYTFYP FATTNSKDFE NLMDVYLSSV FEPQLNHTDF LQEGWRIENQ
NVHDISSKLE FKGVVYNEMK GQYSNSAYYF YIKFLESIYP SLNNSGGDPK KIVDLSYEGL
LEFHSKNYHP SNAKTFTYGK LPLEDSLSKI SKYYESFEKK VSSVDVKQPI FSTDKSEIFD
VTIPGPVDTM NGKETSEQYC TSITWNLGNP LDPNMQYDIF KWKILSSLLF DGHNSPFYQE
LIESGYGDDF SANTGLDSTT ALLSFTVGLN YLTKQKVDNF NEKVMEIINN KIIPELSNEE
SSSYHGRIDA ILHQIEIGFK RHKPDFGFGL LSSIVPSWVN GVDPIDTLQV EKILSHFKED
YKQNGLRIFK ELLEKTLCNP HSQKFKFTME PREDFTKQLV KDENLMIEKR VSELTEDNKK
AIYEQNLELA KLQLEDQNTE VLPTLTIDDI PKRGDFYAID LGQVNKKVVH ERVVDTNGLV
YANALKDISY LPTKLYKYLP LFNNCLTNLA GTENTPITEL ETKIQMLTGG ITFSSKISTD
PYNIEQLKLQ YVLSGMALKE KSSSVYDLWL EILTTTKFDT SDEVLEKLSV LIKNMGQNQI
NNIADRGHSY AAAVSSSKLT PSKYISDIVS GLSQVQFVME LNSKLESEGK EYLAKEIIPI
LQEIQKYVLQ GEFRYRLVGN QEIIVENEKL IEKFDKDISS NRPTLSLTVT DGLSALLNSF
NYNHTSENVL VNLPFQVGYS SLGKIGSSYS SKDGASLQIL SQLYSFKNLH SKIRESNGAY
GGGLTYDGLN GTLNFYSYRD PNPVKSIQTF RDSLSYGLDA NWNDKDLQEA KLRVFQSVDA
PINISSQGAS AFFENIDDYL RQERRENFLG TTLKDLRDVT EKYLVDNQNN LVTVIGDNEI
LNVDNKWQIR NFQV
