ID   V5NCU0_LEUGO            Unreviewed;       412 AA.
AC   V5NCU0;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Aspartic protease 2 {ECO:0000313|EMBL:AHA86292.1};
DE            EC=3.4.23.29 {ECO:0000313|EMBL:AHA86292.1};
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:AHA86292.1};
RN   [1] {ECO:0000313|EMBL:AHA86292.1}
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; KF571928; AHA86292.1; -; mRNA.
DR   AlphaFoldDB; V5NCU0; -.
DR   MEROPS; A01.019; -.
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:SF87; SACCHAROPEPSIN; 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   2: Evidence at transcript level;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:AHA86292.1};
KW   Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:AHA86292.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..412
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004740306"
FT   DOMAIN          87..402
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
SQ   SEQUENCE   412 AA;  43130 MW;  4EA0407CF40404FF CRC64;
     MFPTTLLTAL LLALFVAAKP IVQVRDSPVT LPLSRRVNIT SAQNLYQHDL NRVKAMKARA
     KVVLGDELTL EEAAIVNEPV DNQAVTYIAS VGVGSPATTY QLLSGTGSSN TWVGAGRAYV
     RTSTSQQTGN SVAVSYGSGS FSGNEFTDTV TLASLSIPGQ SIGVATRSSG FEGTDGILGI
     GPVDLTRGTL SPAVNSLIPT VTDNLFSSGR ITSNEIGISF EPTNTIEVEN GELTWGGTDS
     SKFTGAINFT PRTSTSPSSL FWGINQSVRY GSTNILGTTA GIVDTGTTLL LLASNAITLY
     QRATGAVLDN NTGLLRLTPA QFANLQSLFF TTNGVTYELT ANAQIWPRAL NSAIGGNANS
     VYLIVGDIGT PSGEGFDFVN GYAFLERFYS VFDSANGSVG FATTPFTTAT TN
//