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
//