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Database: UniProt
Entry: Q6CGR8_YARLI
LinkDB: Q6CGR8_YARLI
Original site: Q6CGR8_YARLI 
ID   Q6CGR8_YARLI            Unreviewed;       457 AA.
AC   Q6CGR8;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 106.
DE   SubName: Full=YALI0A16819p {ECO:0000313|EMBL:CAG84076.1};
GN   ORFNames=YALI0_A16819g {ECO:0000313|EMBL:CAG84076.1};
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:CAG84076.1, ECO:0000313|Proteomes:UP000001300};
RN   [1] {ECO:0000313|EMBL:CAG84076.1, 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; CR382127; CAG84076.1; -; Genomic_DNA.
DR   RefSeq; XP_500144.1; XM_500144.1.
DR   AlphaFoldDB; Q6CGR8; -.
DR   EnsemblFungi; CAG84076; CAG84076; YALI0_A16819g.
DR   GeneID; 2906333; -.
DR   KEGG; yli:YALI0A16819g; -.
DR   VEuPathDB; FungiDB:YALI0_A16819g; -.
DR   HOGENOM; CLU_013253_9_3_1; -.
DR   InParanoid; Q6CGR8; -.
DR   OMA; CMFGISP; -.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000001300; Chromosome A.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05474; SAP_like; 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; IPR033876; SAP-like.
DR   PANTHER; PTHR47965:SF12; ASPARTIC PROTEINASE 3-RELATED; 1.
DR   PANTHER; PTHR47965; ASPARTYL PROTEASE-RELATED; 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   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
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..457
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005699344"
FT   DOMAIN          53..405
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        71
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   457 AA;  48896 MW;  FB7FE57DD8E1DEE9 CRC64;
     MKWSVLSVLG SCVLVSASLE LDIRPVEPAE ADRISLQRRT VVGVQVDRQQ AYYEAQIALG
     SPPQNLTVLL DTGSSDLWVL SKNVSCLPKG YHAADSWKGV NCSNGGMFDS AASSSFRLNA
     SANAGYQPGN KKTWPFQIAY GDSSAANGLW ASDTISIGGQ SVAEFDFGFA QNASSGLAVL
     GIGPAGNEAS TDDTPPWTYQ NLPHKLKSAG ITSSTAYSLW LNNQHSTKGS IMFGGYDRAK
     IQGGKLFTLP LVPTVDKESV TEFAVQLEAV RVDGKNYGER SNVVLDSGTT MTILPKEQID
     PIIQLTGANY SQEVSSYIFN CSDSPTSGTV DFVFMDKSAI TVQLTDLISV LSYSDGSPDT
     YVDGTLVCVV NVQVAGKKQP SILGASFLRS AYVVYDIDNE QISLGNAKFN VTDSDVVDLG
     PMGLGNTSRT REHKSEAAKV PYGSWWMAAT LLLFAFL
//
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