ID F2Z5X7_CANGA Unreviewed; 541 AA.
AC F2Z5X7;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Candida glabrata strain CBS138 chromosome J complete sequence {ECO:0000313|EMBL:CAG60753.1};
GN Name=BAR1 {ECO:0000313|CGD:CAL0133208};
GN OrderedLocusNames=CAGL0J02288g {ECO:0000313|CGD:CAL0133208,
GN ECO:0000313|EMBL:CAG60753.1};
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:CAG60753.1, ECO:0000313|Proteomes:UP000002428};
RN [1] {ECO:0000313|EMBL:CAG60753.1, 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; CR380956; CAG60753.1; -; Genomic_DNA.
DR RefSeq; XP_447804.1; XM_447804.1.
DR AlphaFoldDB; F2Z5X7; -.
DR STRING; 284593.F2Z5X7; -.
DR MEROPS; A01.015; -.
DR EnsemblFungi; CAGL0J02288g-T; CAGL0J02288g-T-p1; CAGL0J02288g.
DR GeneID; 2889757; -.
DR KEGG; cgr:CAGL0J02288g; -.
DR CGD; CAL0133208; BAR1.
DR VEuPathDB; FungiDB:CAGL0J02288g; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_1_1; -.
DR InParanoid; F2Z5X7; -.
DR OMA; SIYCEND; -.
DR Proteomes; UP000002428; Chromosome J.
DR GO; GO:0071944; C:cell periphery; IEA:UniProt.
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, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..541
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003290198"
FT DOMAIN 53..391
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 71
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 282
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 317..356
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 541 AA; 59524 MW; 91CE4DC96358A3DA CRC64;
MIQFINCYFI FNLVTVVNCL RLTIEKRIVS SHASLSKRSA VDLQFRRFNN LYYESVLEFG
TPPQSIPLVL DTGSSDLWVT LIGNPLCYNK GSGKPPKCLI DCSGLVFYDM DKSQTFDYLK
NVTFKIGYAD TTYTSGIWIV DIITLPEGHL KDLQFGMAFA TNATFSGVLG IGFPAMESVN
GYEFAPGKFY PNFPLALKNA GFTNIAAYSI EYNDESKKGS ILFGSIDTSR FIGPLYTFPM
INEFPGIADE PSTLSLTLDG IGIDGSCEQW VISNTKLPAL LDTGSTLIEL PHPITQSIAS
YLNATWSDDH GLFVLACPSD DFLTTTDLAF TFGELHMKIP LRSFILLPDE ESNGLCGLGI
TSSKGRVILG DSFLTHVYTV FDLDNYMISL APMAKSSLPG KVIEIPANGL IENAVISKSE
KWTHFNDITV NEYGFRNYCD GELQDIHSYS SKLNSSSLVY SSNFSSDEEQ NSSESVSPSI
FNTDSSIKEI YPSLSQKEHL SALLTTISTS EIHKPVTATI TDSITTTIRV TKILTVLQCA
T
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