ID A0A0C3NV94_PISTI Unreviewed; 409 AA.
AC A0A0C3NV94;
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_949586 {ECO:0000313|EMBL:KIO04795.1};
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:KIO04795.1, ECO:0000313|Proteomes:UP000054217};
RN [1] {ECO:0000313|EMBL:KIO04795.1, ECO:0000313|Proteomes:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|EMBL:KIO04795.1,
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; KN831969; KIO04795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3NV94; -.
DR STRING; 870435.A0A0C3NV94; -.
DR HOGENOM; CLU_038846_0_0_1; -.
DR InParanoid; A0A0C3NV94; -.
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..409
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002180317"
FT DOMAIN 84..399
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 102
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 281
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 409 AA; 42898 MW; 72946262E1070AD1 CRC64;
MFVIAPLLTA VLALSVSASS VEIPSPSITL PFARSLNTQG GTVNLLQHDQ ARAAALRDRG
NAIAAGRLYR RQGSIPVTNE AFSYIAAVGI GSPATTYKLI VDTGSSNTWV GSGTPYKVTS
TSVNTGEPVS VTYGSGSFSG TEYTDTVTLG SLTITKQSIG VASKSSGFSG VDGILGIGPE
DLTEGTLTNE PTTEIPTVTQ NLYTEGKIPA EIVSVSFEPT TSTSSMNGEL TFGGVDSSKY
SGTLNYTPLT TTSPASYYWG INESIAYGST TILPTTAGIV DTGTTLILIA TNAFNEYKSL
TGAVSDPTTG LLRITTSQYN ALQNLYFNIN GVTYTLTPNG QIWPRSLNAY IGGSPSYVYL
IVNDIGSKSG SGLDFINGQT FLERFYSVFD TTNSRVGFAT TPYTDATTN
//
