ID   M3JXS4_CANMX            Unreviewed;       418 AA.
AC   M3JXS4;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Vacuolar aspartic protease {ECO:0000313|EMBL:EMG47219.1};
GN   ORFNames=G210_2479 {ECO:0000313|EMBL:EMG47219.1};
OS   Candida maltosa (strain Xu316) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG47219.1, ECO:0000313|Proteomes:UP000011777};
RN   [1] {ECO:0000313|EMBL:EMG47219.1, ECO:0000313|Proteomes:UP000011777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA   Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT   "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT   for xylitol and ethanol production.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMG47219.1}.
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DR   EMBL; AOGT01001674; EMG47219.1; -; Genomic_DNA.
DR   AlphaFoldDB; M3JXS4; -.
DR   STRING; 1245528.M3JXS4; -.
DR   MEROPS; A01.018; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_3_4_1; -.
DR   OMA; KYDHDAS; -.
DR   OrthoDB; 615305at2759; -.
DR   Proteomes; UP000011777; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR   GO; GO:0000324; C:fungal-type vacuole; IEA:InterPro.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05488; Proteinase_A_fungi; 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; IPR033819; Saccharopepsin.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF89; SACCHAROPEPSIN; 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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:EMG47219.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011777};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..418
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004035485"
FT   DOMAIN          103..414
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        121
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        306
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        134..139
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        340..373
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   418 AA;  45288 MW;  4E3E6FDA0AEF639F CRC64;
     MQLSLSVLST IALALTSIVD AKPHSVKLSK LSNEETLDAS NFQEYTDSLA SKYMNLFNAA
     HGNPTSYGLQ HILANKQPEV PFVVPEKDGK YDAPLTNYLN AQYFTEIQLG TPGQTFKVIL
     DTGSSNLWVP SQDCTSLACF LHSKYDHDAS SSYKANGSEF SIQYGSGSME GYISQDVLAI
     GDLVIPKQDF AEATSEPGLA FAFGKFDGIL GLAYDTISVN HIVPPIYNAI NQGLLDKPQF
     GFYLGDTNKD ENDGGSATFG GYDASLFQGK ITWLPVRRKA YWEVSFEGIG LGDEYAQLSK
     TGAAIDTGTS LITLPSSLAE IINAKIGATK SWSGQYQIDC AKRDSLPDLT LTFAGYNFTL
     TAYDYVLEVG GSCISVFTPM DFPQPIGDLA IVGDAFLRKY YSIYDLEKNA VGLAPAKI
//