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Database: UniProt
Entry: A0A074XEL5_AURPU
LinkDB: A0A074XEL5_AURPU
Original site: A0A074XEL5_AURPU 
ID   A0A074XEL5_AURPU        Unreviewed;       504 AA.
AC   A0A074XEL5;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Acid protease {ECO:0000313|EMBL:KEQ83863.1};
GN   ORFNames=M438DRAFT_405987 {ECO:0000313|EMBL:KEQ83863.1};
OS   Aureobasidium pullulans EXF-150.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ83863.1, ECO:0000313|Proteomes:UP000030706};
RN   [1] {ECO:0000313|EMBL:KEQ83863.1, ECO:0000313|Proteomes:UP000030706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ83863.1,
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).
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DR   EMBL; KL584983; KEQ83863.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074XEL5; -.
DR   STRING; 1043002.A0A074XEL5; -.
DR   HOGENOM; CLU_009988_3_1_1; -.
DR   OrthoDB; 1831139at2759; -.
DR   Proteomes; UP000030706; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   Pfam; PF00026; Asp; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KEQ83863.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:KEQ83863.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030706};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        396..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          21..360
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          426..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..445
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..476
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   504 AA;  55092 MW;  0FAAD252548712B8 CRC64;
     MDGPDGRWST FHVEVGGQTV RLLPSTSASA GSSTWVVIDE GCTVANPNLT NCNNERGYLF
     HRNESSSWST RRLFGEGLYS LNIFVEGYLG LTGNAYYGFD TINLGLTGSG LPTVQGQVIA
     GFGTNDFWLG TLGLSPYPFN FTDLDDPQPS LLSTLRNQSL IPSLSWAYTA GAQYKNPPVL
     GSLTLGGYDT TRFTPNNVSF PFGADFSRDL LVKLRSISYD TFGSPPLLTS EIDIFLDSAV
     TQMWLPVNVC QQFEKAFNLT WNATAELYLL DEDTHSALLS RNPIFTFTIA NGSNSADGTV
     DIVLPYSAFD LNITQPYVNT ETRYFPLKQA QNSSQFALGR VFLQEAYVVA DYGHRNFSVS
     QALFPQTNVE QNIVAIHTPN YKAGDDRPDG LSGGSIAGIV GAAVVVLVSI IAATIWFKRR
     STRKVKISTE QTRHDTDEKD NTAAQGISEL DHGDTAVQEA DGWHGYKPEL EVNDGSSGRH
     ELPTPVKMHE VAGHLPVELE APLR
//
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