ID   V5ND85_LEUGO            Unreviewed;       413 AA.
AC   V5ND85;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Aspartic protease 1 {ECO:0000313|EMBL:AHA86291.1};
DE            EC=3.4.23.25 {ECO:0000313|EMBL:AHA86291.1};
OS   Leucoagaricus gongylophorus (Leaf-cutting ant fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX   NCBI_TaxID=79220 {ECO:0000313|EMBL:AHA86291.1};
RN   [1] {ECO:0000313|EMBL:AHA86291.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24401858; DOI=10.1038/ismej.2013.231;
RA   Kooij P.W., Rogowska-Wrzesinska A., Hoffmann D., Roepstorff P.,
RA   Boomsma J.J., Schiott M.;
RT   "Leucoagaricus gongylophorus uses leaf-cutting ants to vector proteolytic
RT   enzymes towards new plant substrate.";
RL   ISME J. 8:1032-1040(2014).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; KF571927; AHA86291.1; -; mRNA.
DR   AlphaFoldDB; V5ND85; -.
DR   MEROPS; A01.018; -.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
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:SF87; SACCHAROPEPSIN; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   2: Evidence at transcript level;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:AHA86291.1};
KW   Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:AHA86291.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..413
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004739489"
FT   DOMAIN          102..410
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        120
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        302
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        133..138
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   413 AA;  44788 MW;  7FA4CC9AF5488DEB CRC64;
     MLFSLVPFVV GLLPFTTYAK THTLRLHKLA PVTKNPDLEG AWLAKKYGSP STVQTPLIGA
     GGSGRHVRPP TSKNGEPLFW TQEEHVDGGH SVPLNNFMNA QYYTEISLGT PPQTFKVILD
     TGSSNLWIPS AKCISIACFL HSKYDSSSSS TYKANGSEFA IQYGSGAMEG FVSSDKLVIG
     DLAVHNQDFA EATKEPGLAF AFGKFDGILG LAYDTISVNG IVPPFYNMIQ QNLLDEPIVS
     FRLGSDENDG GEATFGGINP SSYRGDITYV PVRKNAYWEV ALDKISFGSD ELELESTGAA
     IDTGTSLIAL PTDMAEMLNA QIGAKKDWSG QYTVDCAKLP SLPELTFWFG GKPFPLKGTD
     YVLQVQGSCI SAFTGLDINL PWGSLWIIGD VFLRRYFTVY DLGRNAVGFA EST
//