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
//