ID A0A074WCZ8_9PEZI Unreviewed; 400 AA.
AC A0A074WCZ8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Asp-domain-containing protein {ECO:0000313|EMBL:KEQ67787.1};
GN ORFNames=M437DRAFT_36684 {ECO:0000313|EMBL:KEQ67787.1};
OS Aureobasidium melanogenum CBS 110374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ67787.1, ECO:0000313|Proteomes:UP000030672};
RN [1] {ECO:0000313|EMBL:KEQ67787.1, ECO:0000313|Proteomes:UP000030672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ67787.1,
RC ECO:0000313|Proteomes:UP000030672};
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; KL584824; KEQ67787.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074WCZ8; -.
DR STRING; 1043003.A0A074WCZ8; -.
DR HOGENOM; CLU_013253_3_4_1; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000030672; 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 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 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|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000030672}.
FT DOMAIN 86..396
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 104
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 288
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 117..122
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 400 AA; 43423 MW; F663EAB48E9F066A CRC64;
MKGSSLMAAG ALFGSASAGV HKMKLKKVPL SEQLEGANIG QHVQALGQKY MGVRPQKHID
EMFKETSVHA EAGHPVAVSN FLNAQYFSEI AIGNPPQEFK VVLDTGSSNL WVPSSECGSI
ACYLHNKYDH SDSSTYKKNG SDFAIRYGSG AVEGYISQDT VQIGDIKIKN QLFGEATQEP
GLAFAFGRFD GILGLGYDTI SVNKIPPPFY EMVAQDLLDE PVFAFYLSDT NDKEAESEAI
FGGVNKDHYT GELTKLPLRR KAYWEVDLDA ITFGKESAEF DNMGAILDTG TSLIALPSTL
AELLNKEIGA KKGYNGQYSV ECDKRDSLPD LSFTLTGYNF TITPYDYILE VQGSCISSFM
GFDIPAPAGP LAILGDAFLR KYYSVYDLGS NSVGLAKAKA
//
