ID A0A0C3KNP3_PISTI Unreviewed; 411 AA.
AC A0A0C3KNP3;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=M404DRAFT_837805 {ECO:0000313|EMBL:KIO11232.1};
OS Pisolithus tinctorius Marx 270.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX NCBI_TaxID=870435 {ECO:0000313|EMBL:KIO11232.1, ECO:0000313|Proteomes:UP000054217};
RN [1] {ECO:0000313|EMBL:KIO11232.1, ECO:0000313|Proteomes:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|EMBL:KIO11232.1,
RC ECO:0000313|Proteomes:UP000054217};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|Proteomes:UP000054217};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) 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; KN831950; KIO11232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3KNP3; -.
DR STRING; 870435.A0A0C3KNP3; -.
DR HOGENOM; CLU_038846_0_0_1; -.
DR InParanoid; A0A0C3KNP3; -.
DR OrthoDB; 656651at2759; -.
DR Proteomes; UP000054217; Unassembled WGS sequence.
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; 2.
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 Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000054217};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..411
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002175621"
FT DOMAIN 86..401
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 104
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 283
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 411 AA; 43330 MW; E524D644CF6AEFAF CRC64;
MFPVASLLTT VLLALSTAAS PVEIRSPLIT LPFARSLSTR DGTVNLLQHD QVRATALRDR
GNAIAAGRLD RRQSNMPITT FEAAGYIAAV GVGSPATTYN LIVDTGSSNT WVGAGTPYKV
TNTSVDTGEP VYVPYGSGSF SGTEYTDTVT LGSLTITKQS IGVASTSTDF SGVDGVLGIG
PEDLTLGSLT NEPSTEIPTV TQNLSTEGKI PAEIVGVSFE PSTTTSSMNG ELTFGGIDTS
KYNGVLNYTP LTTTSPASYY WGINESITYG WTTILSTTAG IVDTGTTLIL IATDAFNQYQ
SLTGAVSDSA IGMLRITTSQ YNALQNLYFS INGVTYTLTP NGQIWPRSLN TYIGGSSSYV
YLIVNDIGSN SGSGLDFVNG KGFLERFYSV FDTTNSRVGL ATTSYTYAII N
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