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Database: UniProt
Entry: A5DNR0_PICGU
LinkDB: A5DNR0_PICGU
Original site: A5DNR0_PICGU 
ID   A5DNR0_PICGU            Unreviewed;       240 AA.
AC   A5DNR0;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 2.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Peptidase M16 N-terminal domain-containing protein {ECO:0000259|Pfam:PF00675};
GN   ORFNames=PGUG_04911 {ECO:0000313|EMBL:EDK40813.2};
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK40813.2, ECO:0000313|Proteomes:UP000001997};
RN   [1] {ECO:0000313|EMBL:EDK40813.2, ECO:0000313|Proteomes:UP000001997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC   Y-324 {ECO:0000313|Proteomes:UP000001997};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
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DR   EMBL; CH408160; EDK40813.2; -; Genomic_DNA.
DR   RefSeq; XP_001482956.1; XM_001482906.1.
DR   AlphaFoldDB; A5DNR0; -.
DR   STRING; 294746.A5DNR0; -.
DR   MEROPS; M16.013; -.
DR   GeneID; 5124530; -.
DR   KEGG; pgu:PGUG_04911; -.
DR   VEuPathDB; FungiDB:PGUG_04911; -.
DR   eggNOG; KOG2019; Eukaryota.
DR   HOGENOM; CLU_1156767_0_0_1; -.
DR   InParanoid; A5DNR0; -.
DR   OrthoDB; 5477696at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 1.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR   PANTHER; PTHR43016:SF13; PRESEQUENCE PROTEASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001997}.
FT   DOMAIN          98..192
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
SQ   SEQUENCE   240 AA;  27300 MW;  1B01E9CA8ACA54FF CRC64;
     MPEYGSSRSH LLISATMLRA QLRHYARRNL HANALKDIQS KYVLGADISG YKVEQVEPIS
     EFSLVAVKLK HGKTGSEHLH LDASHDNNNV FSIAFKTNPP DNTGVPHILE HTTLCGSEKY
     PVRDPFFKML NRSLSNFMNA MTGHDYTYYP FATTNSKDFD NLMDVYLSSV LEPKLAIQDF
     MQEGWRLENE VTTDSKSPII FKGVVFNEMK GPVLQLGLLL LDQISGSYLC FAQQFWRRSF
//
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