ID A0A074Y0X8_AURPU Unreviewed; 407 AA.
AC A0A074Y0X8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 22-FEB-2023, entry version 34.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:KEQ89559.1};
GN ORFNames=M438DRAFT_263701 {ECO:0000313|EMBL:KEQ89559.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ89559.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ89559.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ89559.1,
RC ECO:0000313|Proteomes:UP000030706};
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; KL584974; KEQ89559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074Y0X8; -.
DR STRING; 1043002.A0A074Y0X8; -.
DR HOGENOM; CLU_013253_9_3_1; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000030706; 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:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 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};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:KEQ89559.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030706}.
FT DOMAIN 3..364
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 21
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 227
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 266..321
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 407 AA; 43573 MW; DB0D207AF6425117 CRC64;
MAYFLDILVG TPGQMQSVMI DTGSSDLIVT ASNASACITI WGCAGGTFDP VKSSTFGTVT
PDGLSITYGD YSRKVGDYVN DVTQIGDVPM NDAQLGLAYY TKDFTGVNFG IMGLGYSSNL
AGNEAVEPDE QSYPPTFIET LVHTGVIASR LFSLHLNELG KRGSIIFGGI DVDKFRGPLT
TLNCLADNDT VKDFYLNLEE VTVQSSKGGS QSLMRPTGQK PYPVLLDTGS LNWNVPTDVY
EKITEAAGAF EANDTKTERE WLEKPCDDLD RGGIDAPHIQ LTLSGNGPNT VTLDLEMADL
FIPRLNQDGS AKTNDVGQAL CELIVRDYGS PEGLDQEGGI AIGNVVTRTG YFVFDLDNGQ
ISIAQADFAA NSSNVVQVEA GPDGLKNAFD GLKAEHQTNH VEGQFGR
//