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Database: UniProt
Entry: A8QCW0_MALGO
LinkDB: A8QCW0_MALGO
Original site: A8QCW0_MALGO 
ID   A8QCW0_MALGO            Unreviewed;       394 AA.
AC   A8QCW0;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   08-NOV-2023, entry version 75.
DE   SubName: Full=Hypothetical aspartyl protease {ECO:0000313|EMBL:EDP41672.1};
GN   ORFNames=MGL_4053 {ECO:0000313|EMBL:EDP41672.1};
OS   Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP41672.1, ECO:0000313|Proteomes:UP000008837};
RN   [1] {ECO:0000313|EMBL:EDP41672.1, ECO:0000313|Proteomes:UP000008837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX   PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA   Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA   Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA   Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA   Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT   "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT   virulence traits shared with plant and human fungal pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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:EDP41672.1}.
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DR   EMBL; AAYY01000018; EDP41672.1; -; Genomic_DNA.
DR   RefSeq; XP_001728886.1; XM_001728834.1.
DR   AlphaFoldDB; A8QCW0; -.
DR   GeneID; 5853192; -.
DR   KEGG; mgl:MGL_4053; -.
DR   VEuPathDB; FungiDB:MGL_4053; -.
DR   InParanoid; A8QCW0; -.
DR   OMA; ATRCAGN; -.
DR   OrthoDB; 4946at2759; -.
DR   Proteomes; UP000008837; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF57; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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   Hydrolase {ECO:0000313|EMBL:EDP41672.1};
KW   Protease {ECO:0000313|EMBL:EDP41672.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008837};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..394
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002728081"
FT   DOMAIN          98..391
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        116
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        280
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   394 AA;  43220 MW;  5BF501E19C92AC07 CRC64;
     MLLLPKLFAG VAAIASLVAA QKHEGISIPM SRRGISKGET NFHELAAGIK KVFNKYEFGM
     NNFKLKMGKD HPLLGSKLEK RDSTSSIKMF DIAGETQWIG EISIGTPPQR MLVQFDTGSA
     NVIIAPDAYK PSQSNSSFKA KDQFKTGYGD GTKVEGNVYV DNFELGGIKA RNLSFGLTNE
     NFLQDFERES SGIGGLSFPS ISNFDSKYLT LIEALMQQKS LKQNVFQFTL KPGEGSTLIF
     GDIDHSKFNG DLTWVKVNPL FGFYIADAKI NGKKIRTAVD SGTTVIIGSR SQVKDLVERT
     NGVHYAEDRS TNIGYGLFDC DFSPEVIITY GGTDFKLNRD QVSRGTANGK CLLSVIGIDS
     ILPFDTWIMG DPFFQAASIV FDHDNNRLGF ASQA
//
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