ID A0A0D0CKL0_9AGAR Unreviewed; 399 AA.
AC A0A0D0CKL0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 08-NOV-2023, entry version 37.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=GYMLUDRAFT_175217 {ECO:0000313|EMBL:KIK55663.1};
OS Collybiopsis luxurians FD-317 M1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC Collybiopsis luxurians.
OX NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK55663.1, ECO:0000313|Proteomes:UP000053593};
RN [1] {ECO:0000313|EMBL:KIK55663.1, ECO:0000313|Proteomes:UP000053593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK55663.1,
RC ECO:0000313|Proteomes:UP000053593};
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 (APR-2014) 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; KN834804; KIK55663.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0CKL0; -.
DR HOGENOM; CLU_038846_0_0_1; -.
DR OrthoDB; 656651at2759; -.
DR Proteomes; UP000053593; 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:SF51; NAPSIN-A; 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 Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000053593};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..399
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002208005"
FT DOMAIN 77..389
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 95
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 271
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 399 AA; 42033 MW; 67A808DA564456E2 CRC64;
MFPVISLLTF VTLALGVATS PVVVVDRSPI LSLPLKRVNN FTSGHDILAH DLARARATGQ
PVKRQSSEPV TNQVVSYTAV VGVGAPSAEY DLIVDTGSSN TWVGAGKAYV RTSTSINTGN
RVSVSYGSGD FSGTEFFDTV NLLSGINGQS IGVASESEGF EGVDGILGIG PVDLTEGTVE
NTTTVPTVTD NLFAQGTIPQ NLVAVSFRPT TISSDTNGEL TFGGTDSSKF TGEITFVYVS
CLPRVGDHWG ISQTVTYGST SILDNTDGIV DTGTTLILFE ETAFESYVTA TGGVMDENTG
LLRVTTAQFS ALQNLNFNIG STTFSLTPNA QIFPRSLNRF IGGSADNIYL IVANLGPSGG
EPFNFVNGYA FLERFYSVYD TGNNRVGIAT TPFTNATTN
//