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Database: UniProt
Entry: Q6FVH4_CANGA
LinkDB: Q6FVH4_CANGA
Original site: Q6FVH4_CANGA 
ID   Q6FVH4_CANGA            Unreviewed;       505 AA.
AC   Q6FVH4;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 113.
DE   SubName: Full=Candida glabrata strain CBS138 chromosome E complete sequence {ECO:0000313|EMBL:CAG58689.1};
GN   Name=YPS10 {ECO:0000313|CGD:CAL0128986};
GN   OrderedLocusNames=CAGL0E01859g {ECO:0000313|CGD:CAL0128986,
GN   ECO:0000313|EMBL:CAG58689.1};
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:CAG58689.1, ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG58689.1, 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, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; CR380951; CAG58689.1; -; Genomic_DNA.
DR   RefSeq; XP_445770.1; XM_445770.1.
DR   AlphaFoldDB; Q6FVH4; -.
DR   STRING; 284593.Q6FVH4; -.
DR   MEROPS; A01.030; -.
DR   EnsemblFungi; CAGL0E01859g-T; CAGL0E01859g-T-p1; CAGL0E01859g.
DR   GeneID; 2887387; -.
DR   KEGG; cgr:CAGL0E01859g; -.
DR   CGD; CAL0128986; YPS10.
DR   VEuPathDB; FungiDB:CAGL0E01859g; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_9_1_1; -.
DR   InParanoid; Q6FVH4; -.
DR   OMA; GIGYKTN; -.
DR   PHI-base; PHI:7934; -.
DR   Proteomes; UP000002428; Chromosome E.
DR   GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR   GO; GO:0005576; C:extracellular region; IDA:CGD.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
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; 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; PS00141; ASP_PROTEASE; 1.
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:UP000002428};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          46..409
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        64
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        301
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        337..370
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   505 AA;  55332 MW;  1DCB9592D847924E CRC64;
     MLFLVPFLSV AQAYVALDFE KSHGDDLVKR DVQDVKLINS QKAMLYNIQL SVGTPPQNIT
     AQLDTGSSDL WFPDSTNPYC KANKKQAPKS IASLDAGTRP TSPAQVPKSL RNLDCAEFGL
     FNSSASTTFN SNKTEFFISY LDSSYAEGVW ATDNLYLNGL NISGLNFGLA YFSNSSNSVL
     GVGLTPLEAS YDTDIKQDDS PRFQYPNFPQ ILKQKGAISK VTYSLYLNDT KSKYGQILFG
     GVDHSKYVGQ LYTIPLVNSK YQKSPGVIAD LEVTLNGLGI RDNTTNTNTT LYTQKLPALF
     DSGTSYSYVP YTMAQVIASQ VNGTIDNKTE AIRLPKCPSK KDTREVVFNF NGVEIAIPLK
     QFYQKKSGKC YLDLMVAPPN NGPGLLLGDT FLRQVYTVFD LEAQELSIAR ANFNSSLPAD
     VEEIKSTVPS AIKAPQYYNT FSAYDNATQV VGNIFDATAT ASMAPKNQSN SSNLSRRALN
     YENNSARSST LSIVLVLAAI TTLFM
//
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