GenomeNet

Database: UniProt
Entry: Q6CBW5_YARLI
LinkDB: Q6CBW5_YARLI
Original site: Q6CBW5_YARLI 
ID   Q6CBW5_YARLI            Unreviewed;       447 AA.
AC   Q6CBW5;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 104.
DE   SubName: Full=YALI0C14938p {ECO:0000313|EMBL:CAG82160.1};
GN   ORFNames=YALI0_C14938g {ECO:0000313|EMBL:CAG82160.1};
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:CAG82160.1, ECO:0000313|Proteomes:UP000001300};
RN   [1] {ECO:0000313|EMBL:CAG82160.1, 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382129; CAG82160.1; -; Genomic_DNA.
DR   RefSeq; XP_501847.1; XM_501847.1.
DR   AlphaFoldDB; Q6CBW5; -.
DR   EnsemblFungi; CAG82160; CAG82160; YALI0_C14938g.
DR   GeneID; 2909342; -.
DR   KEGG; yli:YALI0C14938g; -.
DR   VEuPathDB; FungiDB:YALI0_C14938g; -.
DR   HOGENOM; CLU_013253_9_3_1; -.
DR   InParanoid; Q6CBW5; -.
DR   OMA; CPYTRFD; -.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000001300; Chromosome C.
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:InterPro.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd05474; SAP_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR033876; SAP-like.
DR   PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 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|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..447
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004271395"
FT   DOMAIN          64..393
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          418..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..432
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   447 AA;  47366 MW;  4CDF19788DD3EB5C CRC64;
     MKFSILTLAV FTALASAATD KTLKVGFNQR VNHLKNSPNP NGLSNPSKNP SNPVAILNNK
     VVEYVVDITL GTPAQKFSVQ IDTGSSDLWV KADGSDTAYN SSLSSTYEEY KPGAFFIAYG
     DQTTASGDWV KDTIDVAGAS IPDFVFAAAK KTDTDPVFGV GYPSNEASDS QDEQGPEFEY
     DNFPIRLAKA GVINTPAYSL YLDSLQATTG TLLFGAVDTS KFADELALLP FIKDSPGDPG
     PKEFQVTLNS IDFGDSNALN VARLALLDAG TTLTILPSTT FLTLFNSLGL YNTEDGPVAS
     QSQLDKWKSE GSAITYTFQG KKVNVPLTQL FIADTDGEGN QRYVTLADGS QEAAYSWLVG
     DAQSDEGQSV LGDSFLRSVY VAYDLQNNQV GLGQVKYDNS AENIVAISSG GIPSATKAPS
     AATWSTDHPI PTTAAPPSGI VGVGPKF
//
DBGET integrated database retrieval system