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Database: UniProt
Entry: J5JZK4_BEAB2
LinkDB: J5JZK4_BEAB2
Original site: J5JZK4_BEAB2 
ID   J5JZK4_BEAB2            Unreviewed;       883 AA.
AC   J5JZK4;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:EJP69763.1};
GN   ORFNames=BBA_01728 {ECO:0000313|EMBL:EJP69763.1};
OS   Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS   (Tritirachium shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP69763.1, ECO:0000313|Proteomes:UP000002762};
RN   [1] {ECO:0000313|EMBL:EJP69763.1, ECO:0000313|Proteomes:UP000002762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP69763.1,
RC   ECO:0000313|Proteomes:UP000002762};
RX   PubMed=22761991; DOI=10.1038/srep00483;
RA   Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA   St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT   "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT   Beauveria bassiana.";
RL   Sci. Rep. 2:483-483(2012).
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DR   EMBL; JH725152; EJP69763.1; -; Genomic_DNA.
DR   RefSeq; XP_008595047.1; XM_008596825.1.
DR   AlphaFoldDB; J5JZK4; -.
DR   STRING; 655819.J5JZK4; -.
DR   EnsemblFungi; BB8028_0002g04780.1; BB8028_0002g04780.1; BB8028_0002g04780.
DR   GeneID; 19884740; -.
DR   HOGENOM; CLU_009988_1_0_1; -.
DR   InParanoid; J5JZK4; -.
DR   OrthoDB; 1831139at2759; -.
DR   Proteomes; UP000002762; 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   CDD; cd12087; TM_EGFR-like; 1.
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:EJP69763.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:EJP69763.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002762};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..883
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003784121"
FT   TRANSMEM        446..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          42..404
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          420..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          616..734
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          763..883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..501
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        635..734
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        763..793
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        804..821
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   883 AA;  95886 MW;  6ECCAE69BF465C9D CRC64;
     MRSSRMAAAA SVAATAVFVN AYDPAAVSIP YGDWLGIDGN WSTVRFLLGT ESDLVNIIPS
     TSLSELWAVG PGGCQSKEQH CMTARGGIYT PGDSKRWTSW GQYFLGLEYL GYGGNGAYGI
     DNINTWSPFT NIAFGMSSVL VAAYNTTDYF NGLFGLGISQ GRFKGNIGES ALTQAVKTFG
     WIPSYSYGYT AGASYKNMPG SLTLGGFDSA RLVDHDTLFT ITQSDNSPRV NVRSINVFND
     RKPHGWDSSI NKLSSYNDTF MALVDSTTPY LWLPESICES FASALNLTYN DTYKLYTLTN
     TQYQDYSTSN AYSFTFSLAS IDNNDNFGLP LSAPGVVNIT VPIKAFVGSL QYPFAKEAIK
     YGQPAVPYFM LRKATNSSSI IIGRSFLQEA YIRTKFDSGV FSLHQAAFPR DPDTDIKLNL
     IKQPSNSPYP RPPPTKDHHG LTTPQMIGIA VGVVAFCTLL LAALCFWNRR RKQKKHGETA
     AKEAESQDSS STISPESPMT PVSRILSKIV RRKRSRRTTT TTRTSAPTEA PASEIYELPA
     PLPPAELAAH NEDDDSVLGG TVAGTDDSQN LSAYELARRK LARQLAGPVP AYAPPENGIV
     PAEKDMHIDT NVVRTTTIPH PQPTYHFHNV SPVRSHEGLG TNSLPGTLPS PVSPRTDWNT
     NDLPSPITAS LHPNSASSQS GSTGRRRAGS NTMNGTSSEY GSARRSDSNS SSNSNGQEQS
     RERKVSFPLP QASFQRTPIE PSKVVCLGPL PENVSLFKQQ MLPSASATRE QSWTGPAHHS
     HHRPSTGSLG SNYTDEEDAM VEELTRQSTS VSRSLGSQNV NRPPALVDPL IRTVLPERTE
     EENVSPTSDK SGAGSHSSGG RIGGGDLIHV PQMAEKRYSW EEE
//
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