ID Q6C080_YARLI Unreviewed; 396 AA.
AC Q6C080;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 24-JAN-2024, entry version 118.
DE SubName: Full=YALI0F27071p {ECO:0000313|EMBL:CAG78744.1};
GN ORFNames=YALI0_F27071g {ECO:0000313|EMBL:CAG78744.1};
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:CAG78744.1, ECO:0000313|Proteomes:UP000001300};
RN [1] {ECO:0000313|EMBL:CAG78744.1, 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, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; CR382132; CAG78744.1; -; Genomic_DNA.
DR RefSeq; XP_505932.1; XM_505932.1.
DR AlphaFoldDB; Q6C080; -.
DR SMR; Q6C080; -.
DR STRING; 284591.Q6C080; -.
DR MEROPS; A01.018; -.
DR EnsemblFungi; CAG78744; CAG78744; YALI0_F27071g.
DR GeneID; 2907949; -.
DR KEGG; yli:YALI0F27071g; -.
DR VEuPathDB; FungiDB:YALI0_F27071g; -.
DR HOGENOM; CLU_013253_3_4_1; -.
DR InParanoid; Q6C080; -.
DR OMA; KYDHDAS; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000001300; Chromosome F.
DR GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IEA:EnsemblFungi.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0097718; F:disordered domain specific binding; IEA:EnsemblFungi.
DR GO; GO:0070492; F:oligosaccharide binding; IEA:EnsemblFungi.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
DR GO; GO:0016237; P:lysosomal microautophagy; IEA:EnsemblFungi.
DR GO; GO:0000425; P:pexophagy; IEA:EnsemblFungi.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR CDD; cd05488; Proteinase_A_fungi; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033819; Saccharopepsin.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000001300};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..396
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004271213"
FT DOMAIN 83..393
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 101
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 285
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 114..119
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 396 AA; 42603 MW; D18E2EC5E4F9DB64 CRC64;
MKFTAAVSVL AAAGSVSAAV SKVSINKMST AELLGKENGF EDHLRMMGQK YMGKFQKLGE
FNELASIQDV SNSPLTNYLN AQYYTEIEIG TPPQKFNVIL DTGSSNLWVP SVQCNSIACY
LHQKYDSAAS SSYKANGTAF EIQYGSGSME GFVSQDTLKL GSLVLPEQDF AEATSEPGLA
FAFGKFDGIL GLAYDTISVN KIVPPVYNAV NRGLLDKNQF SFFLGDTNKG TDGGVATFGG
VDEDYFEGKI TWLPVRRKAY WEVEFNSITL GDQTAELVNT GAAIDTGTSL LALPSGLAEV
LNSEIGATKG WSGQYTVECD KVDSLPDLTF NFAGYNFTIG PRDYTLELSG SCVSAFTGFD
IPAPVGPIAI IGDAFLRRYY SVYDLDHDAV GLAKAK
//