ID Q6CD28_YARLI Unreviewed; 382 AA.
AC Q6CD28;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=YALI0C04279p {ECO:0000313|EMBL:CAG81733.1};
GN ORFNames=YALI0_C04279g {ECO:0000313|EMBL:CAG81733.1};
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG81733.1, ECO:0000313|Proteomes:UP000001300};
RN [1] {ECO:0000313|EMBL:CAG81733.1, ECO:0000313|Proteomes:UP000001300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
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., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; CR382129; CAG81733.1; -; Genomic_DNA.
DR RefSeq; XP_501434.1; XM_501434.1.
DR AlphaFoldDB; Q6CD28; -.
DR EnsemblFungi; CAG81733; CAG81733; YALI0_C04279g.
DR GeneID; 2909397; -.
DR KEGG; yli:YALI0C04279g; -.
DR VEuPathDB; FungiDB:YALI0_C04279g; -.
DR HOGENOM; CLU_660911_0_0_1; -.
DR InParanoid; Q6CD28; -.
DR OrthoDB; 2550277at2759; -.
DR Proteomes; UP000001300; Chromosome C.
DR GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF89; SACCHAROPEPSIN; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001300};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..382
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004271422"
FT DOMAIN 55..357
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 73
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 252
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 382 AA; 41369 MW; 050390290AC1A3DC CRC64;
MIFSNILLST VAAAAVINLP LKARDLSDAP EIAAELFKRQ AGVFHSTQTK GDIFYEAEIE
IGTPPQKVSV CFDTGSPLLW VPGSNSTQCK DSCKGRTYDV SKSSSWQYQK EGKNWGGTGN
WGKDTVSYAG QTLEDFNVWV SKDKIANSQG IFGQSISDNK HGSFIQGLAD SGKISRAVYS
LNAEKPVLFA DASTKGVVTN VYYGGFDKAK YEGPLTTINC SHPGGYGMPL GGLSIQGEEI
PEEKNKRQIV LDTGGIKVQY SNNTVEALSK KFGGEGQFSE GAWEVGCDQK PEITYHFGET
KIDMPLSDYV SKGKDGKCRI NKIHLSGNDV KTLLTGPTLI SRALVIYDNE RSQITIAKAK
YTDETDVVEI TGDIPGAVPF KP
//
