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Database: UniProt
Entry: Q6C080_YARLI
LinkDB: Q6C080_YARLI
Original site: Q6C080_YARLI 
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
//
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