ID A0A137QLG8_9AGAR Unreviewed; 483 AA.
AC A0A137QLG8;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Vacuolar protease A {ECO:0000313|EMBL:KXN88094.1};
GN ORFNames=AN958_07553 {ECO:0000313|EMBL:KXN88094.1};
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:KXN88094.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN88094.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN88094.1,
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, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KQ962167; KXN88094.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137QLG8; -.
DR STRING; 1714833.A0A137QLG8; -.
DR OrthoDB; 1697158at2759; -.
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:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
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; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:KXN88094.1};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..483
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007295419"
FT TRANSMEM 444..465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 56..389
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 483 AA; 52559 MW; 19801C053FDA955E CRC64;
MFRSLPAGLL AYLLLLLDFP YAHQLDIRGS RQHSHPVDHL RRGGPISLSN LADISYHADI
LLGGQHFQVL VDTGSSDLWV AGSVQQSSDT ALNASVFYAI GKVEGPIRTA HLQLGDDRVE
NQAFIQVSPS LRNREGTGIL GLGPSSGSFI LSQLSGPTGA PPLDRLFIQD ATAPDYFTIL
LGRHGDPTSF FSGTITIGSV LPDYTDILSS PKLPISLVSD GNSHNQHFQV ELDPDGIIGP
DGKPISLGPH IANKDDGKAT VVMDCGFTLP QIPQDAAEAI YSRFKDSVFT TVEGLGGVWV
VPCATEVNVT FVFGGQRYPM HPLDMTLPPE IFNLRNVTNS RGVPVCIGSF QPFTFDRGHK
ATYDLVLGMA FMRNVYTLFD YADFVLGANT TNENKGPYIQ MYSITNMSQA HLDFVKVRLG
GIDTTGDQKL LDGPRKKGDS KNPAIYYVIA VIVVIVLMVI AMIYIPWKKR NRRSLGEGGK
VVQ
//