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Database: UniProt
Entry: A0A0A2VK45_BEABA
LinkDB: A0A0A2VK45_BEABA
Original site: A0A0A2VK45_BEABA 
ID   A0A0A2VK45_BEABA        Unreviewed;       218 AA.
AC   A0A0A2VK45;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Mite allergen Eur m 3 {ECO:0000313|EMBL:KGQ08236.1};
GN   ORFNames=BBAD15_g6443 {ECO:0000313|EMBL:KGQ08236.1};
OS   Beauveria bassiana D1-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ08236.1, ECO:0000313|Proteomes:UP000030106};
RN   [1] {ECO:0000313|EMBL:KGQ08236.1, ECO:0000313|Proteomes:UP000030106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-5 {ECO:0000313|EMBL:KGQ08236.1,
RC   ECO:0000313|Proteomes:UP000030106};
RA   Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA   Du Q., Sun Z.;
RT   "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT   bassiana D1-5.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|ARBA:ARBA00007664}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGQ08236.1}.
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DR   EMBL; ANFO01000600; KGQ08236.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2VK45; -.
DR   STRING; 1245745.A0A0A2VK45; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   HOGENOM; CLU_006842_7_5_1; -.
DR   Proteomes; UP000030106; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001254; Trypsin_dom.
DR   PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR   PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000030106};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..218
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001995708"
FT   DOMAIN          49..192
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   REGION          197..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   218 AA;  22768 MW;  A60D1CD062637376 CRC64;
     MQSKAAISLT VALSAFSAAA VTIDRRIVGG EDAKDGEFPS VVSITGSEEF ECPIKKSDKI
     DYASLPADGS DAMVGSTGTV AGWGVQEADW TFAGDVAEEN LAKVTLPVHA REVCDKLEPS
     VKGRDTVLCI GGNGKSACRY DSGGGFFDDT TGQVVGVASW GIVDKEWLMC NNAPMIYTRV
     GSYVSFIKQH LEGADAAANP DPAAAQNTTT PDQGPRAK
//
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