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Database: UniProt
Entry: Q6FVI0_CANGA
LinkDB: Q6FVI0_CANGA
Original site: Q6FVI0_CANGA 
ID   Q6FVI0_CANGA            Unreviewed;       539 AA.
AC   Q6FVI0;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 107.
DE   SubName: Full=Candida glabrata strain CBS138 chromosome E complete sequence {ECO:0000313|EMBL:CAG58683.1};
GN   Name=YPS3 {ECO:0000313|CGD:CAL0129038};
GN   OrderedLocusNames=CAGL0E01727g {ECO:0000313|CGD:CAL0129038,
GN   ECO:0000313|EMBL:CAG58683.1};
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG58683.1, ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG58683.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
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}.
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DR   EMBL; CR380951; CAG58683.1; -; Genomic_DNA.
DR   RefSeq; XP_445764.1; XM_445764.1.
DR   AlphaFoldDB; Q6FVI0; -.
DR   EnsemblFungi; CAGL0E01727g-T; CAGL0E01727g-T-p1; CAGL0E01727g.
DR   GeneID; 2887369; -.
DR   KEGG; cgr:CAGL0E01727g; -.
DR   CGD; CAL0129038; YPS3.
DR   VEuPathDB; FungiDB:CAGL0E01727g; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_9_1_1; -.
DR   InParanoid; Q6FVI0; -.
DR   OMA; IRYHEEL; -.
DR   PHI-base; PHI:7927; -.
DR   Proteomes; UP000002428; Chromosome E.
DR   GO; GO:0005576; C:extracellular region; IDA:CGD.
DR   GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
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   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          53..416
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          475..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..513
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        71
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        308
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        344..377
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   539 AA;  58907 MW;  F768EBC65AFF327A CRC64;
     MKFLLFAAVA QAYLQLDFER QTAQDVALAK RHTSNGVANA MDVPIEQIGD LMYTVQLHVG
     TPPQNVTVQL DTGSSDLWFP VASNPYCKRN AKLAPKKVKA LPATGFATEN DQVAKKLRTF
     DCDAFGLFNS SMSSSFKSND SSEFFVKYED GTYASGMWGT DTFKLNHHNV SNITFALANI
     ANASMGVLGV GFPAEETTDD PSPGSLIDKE HYQYDNFPIA LKRTRTIKKV SYSIFLNDTN
     SKKGVILFGG VDHSKYQGTL WTVPMVNNLL TLNQTTTSRP EITLNGLGFR DDKKNVTLWG
     EKIPVLLDTG TTLAYAPKQV VDVIAKRVNG TIDSKTGGIK LKKCPNAKDN SELIFNFAGA
     EIPVSLLNMV EKRKGKCYLE IRYHEELSKT GMLLGDIFMR HVYSVFNMED MEVSFAVANG
     NDSAPLQIEA IISDVPSAVK APQYYNTFAS SNLPSTVTND IFASTATASM EPPSSVLESL
     KSKSSSTSSI DTSVPSDDKK IIDDDHSGHD HAKRDAYSNT AGILQISTTL VLVAMTLLL
//
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