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Database: UniProt
Entry: A0A137QG95_9AGAR
LinkDB: A0A137QG95_9AGAR
Original site: A0A137QG95_9AGAR 
ID   A0A137QG95_9AGAR        Unreviewed;       558 AA.
AC   A0A137QG95;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   08-NOV-2023, entry version 22.
DE   SubName: Full=Gastricsin {ECO:0000313|EMBL:KXN86268.1};
GN   ORFNames=AN958_10130 {ECO:0000313|EMBL:KXN86268.1};
OS   Leucoagaricus sp. SymC.cos.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX   NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN86268.1, ECO:0000313|Proteomes:UP000070249};
RN   [1] {ECO:0000313|EMBL:KXN86268.1, ECO:0000313|Proteomes:UP000070249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SymC.cos {ECO:0000313|EMBL:KXN86268.1,
RC   ECO:0000313|Proteomes:UP000070249};
RA   Hu H.;
RT   "Leucoagaricus sp. SymC.cos WGS genome.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; KQ962369; KXN86268.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A137QG95; -.
DR   STRING; 1714833.A0A137QG95; -.
DR   OrthoDB; 1656645at2759; -.
DR   Proteomes; UP000070249; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF73; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070249};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..558
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007295296"
FT   TRANSMEM        449..476
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          66..387
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   558 AA;  60357 MW;  DCE77F623D59310C CRC64;
     MKVPLTLSLV FAAFASAHKF SLKRIPKQQP HDFLRRSPQS LSSDGQVVTS NPETDFSLGT
     IHDLIYLVNI TVGDNGYSVQ LDTGSSDLWI KGSVTPLPGA TSTDTSYNIS YVLGWASGRL
     SYAPVEFIGL KVPKQAFIDV DQANNPVLGY GLDGIVGLGF TSLSSIDYAV NETSSDAGRS
     LLYNLFAVNP SEPNFLAFSL LRSTDPDGEA EGSFSIGEYE PKYAQVANTS RISTWPVHTP
     KRWTVLLDSV IVGGNIIVPT TQVTGAPSNK AVVLMDSGAS YTYAPKSITD AIYANVTGAQ
     FDEKSNQWLV PCDYEVDMAF QIGGQIFPLH PLDVAPATAG NNSTCVGSFI PTQLGAQSQF
     DWLVGDNFLR SVYAVYDFGD YDSRGVMGDP YMQLLSITNP DEASADFHKV RGGEPKRNIT
     YVGLNGTANA PSFFISDDVS ESIEMISRFV PAMLGVVALN ALVLLGLVIG GLCYWMRKRR
     LRRHDRVRST RGTRGRMTPM QLDTIPSYVA GEQSSPSGPA IYQPVSMALT EDTFVPPSPA
     FHKFDGVVSP GDRPKSIA
//
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