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
//