ID A0A074X914_AURPU Unreviewed; 422 AA.
AC A0A074X914;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 22-FEB-2023, entry version 33.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:KEQ81858.1};
DE Flags: Fragment;
GN ORFNames=M438DRAFT_258888 {ECO:0000313|EMBL:KEQ81858.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ81858.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ81858.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ81858.1,
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL584990; KEQ81858.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074X914; -.
DR STRING; 1043002.A0A074X914; -.
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:KEQ81858.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030706}.
FT DOMAIN 1..350
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 19
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 228
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 261..312
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KEQ81858.1"
FT NON_TER 422
FT /evidence="ECO:0000313|EMBL:KEQ81858.1"
SQ SEQUENCE 422 AA; 43707 MW; 58BCDCD46C65C6DA CRC64;
YFVNFTVGTP GQLQTALLDT GSSDTILLAS DASICAKKSS CPGGSYNSSA SSTFSLLSAG
AIKAQYGASV VSGTMTGDLV TDVIQVGDIA VTGAHFGVAH EAQGRFLGNG AFVGIMGLAY
SATEALREGQ PLYPTFVESL VGAGAIPSRL FSLYLNEVSS FGSILFGGID TEKYEGNLTT
LNFLQVSAEE KPISAFWMHL DEVSMTRDDG TKEQIVEPDE IQQPVLPDSG SAYWDVPTDV
YNKIINATGA TISQNNALLA CSKISNGTSF AFTFSGNGTN KVNLEVPLSS FFTPAVLTDG
SGLAKIGGED ACLLMAQDAG SDAKFYLVGD PVIRAGYWVY DLDNGQVSIA QARLSATASN
IVAVEAGRHG VMNVTDQASE LAANQTERVA GTATASVSYS LSTASEAVGQ TAGPQSTDLS
SA
//