ID A0A074Y5U2_AURPU Unreviewed; 404 AA.
AC A0A074Y5U2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 22-FEB-2023, entry version 35.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:KEQ89562.1};
GN ORFNames=M438DRAFT_9139 {ECO:0000313|EMBL:KEQ89562.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ89562.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ89562.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ89562.1,
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; KEQ89562.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074Y5U2; -.
DR STRING; 1043002.A0A074Y5U2; -.
DR HOGENOM; CLU_013253_9_3_1; -.
DR OrthoDB; 1767283at2759; -.
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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; NAPSIN-A; 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:KEQ89562.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030706};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..404
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001703005"
FT DOMAIN 47..373
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 404 AA; 42858 MW; F88BF276D8B9D17F CRC64;
MQFFTAFVLC VSVLLLHIEV AAVAATGTQV IEIALTDTLG GEVGWAYYAN ISVGTPGQVQ
SALVDTGSSD TIFPDSTATA CRTKGGCATT FVIEESPDYK VVIPGGLSVG YTDHSKMEGD
YSLDRVHIGD ISITNARIGV AKVVEDPTGI KTAILGLGYP SNEGQNTSDQ PYCSTLLQAL
VESGEIESRL YGIYLSQRDH VQDGSITFGG IDTEKFKGPL TTLNCPRDNG ITTKLELKLD
NVKAYLQDGS SQELIRSASD ESHSVDMDAG ASAWRVSEPV YRKILMLAGG NDQRPCKEVV
RGATYFQLTF SGYGSTNTAT LNVDMADLFS PYAGTCQLAV TVDSSGETLG VGHHVMRAGY
WVFDLDNGQI SVAQANLEAS SSNVVKVQKG AGGLSKAIGR KTEV
//