ID A0A074XGA9_9PEZI Unreviewed; 415 AA.
AC A0A074XGA9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 22-FEB-2023, entry version 36.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:KEQ73606.1};
GN ORFNames=M436DRAFT_46043 {ECO:0000313|EMBL:KEQ73606.1};
OS Aureobasidium namibiae CBS 147.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ73606.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ73606.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ73606.1,
RC ECO:0000313|Proteomes:UP000027730};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KL584709; KEQ73606.1; -; Genomic_DNA.
DR RefSeq; XP_013427423.1; XM_013571969.1.
DR AlphaFoldDB; A0A074XGA9; -.
DR STRING; 1043004.A0A074XGA9; -.
DR GeneID; 25410439; -.
DR HOGENOM; CLU_013253_0_0_1; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000027730; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06097; Aspergillopepsin_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; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF23; ASPARTIC ENDOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G15950)-RELATED; 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}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:KEQ73606.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027730}.
FT DOMAIN 104..411
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 120
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 305
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 415 AA; 43059 MW; 2CF35A11EE74A2B7 CRC64;
MTTPDGSPWV AVSKTPTTIN LHANTSAPSN TTSSDQSIAT NDRHLSDLRS WLYATFSWGY
ETPAASSAVA APSTQATYAA ASSAAHSSAT GEVLATPADN GAEYLSPVTI GGQKLDLNFD
TGSSDLWVFS TALTSAQIGE HSAYDPSKSS SYQQLDGSTF SLSYGDGSGA AGVVGFDTVD
IGGATVTRQA IELATSVSSA FVSDADSDGL VGLAFSTLNS VSPRPQKTFF DNIMSELAQP
VFTAALDLDG SGTYEFGTID SSKFTGDLQF TPVNASSGFW QVDSNRYSIG GKDCDRTNAS
PAIIDTGTSL LLLDPEVVQA YYADIPSASY DSTVGGYTYD CSESLPEFAV AVGDYMANIP
GSGITFAPVS TKTCFGGVQS NSGSDLQIFG DVLLKHHFVV FNGQSEVIGM AAKAE
//