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
//