ID A0A137QWP2_9AGAR Unreviewed; 543 AA.
AC A0A137QWP2;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Putative aspartic-type endopeptidase CTSD {ECO:0000313|EMBL:KXN91695.1};
GN ORFNames=AN958_12547 {ECO:0000313|EMBL:KXN91695.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN91695.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN91695.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN91695.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-2016) 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; KQ961965; KXN91695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137QWP2; -.
DR STRING; 1714833.A0A137QWP2; -.
DR OrthoDB; 4946at2759; -.
DR Proteomes; UP000070249; 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:SF75; ENDOPEPTIDASE (CTSD), PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07040)-RELATED; 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};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000070249};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..543
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007295686"
FT DOMAIN 222..540
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 65..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 240
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 430
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 465..501
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 543 AA; 55468 MW; FFCA8E978E7763C9 CRC64;
MQLRVSFMTL LAGIFVVLSS TNNPVNALPL SKKETPGIVT LPLKRVPLPR DVHPQILLQQ
HINRSRRRLA RMTGRNEPSA EELEQHMKRR VVSVEGPEGL QKRYNRQGVP KTQGGATGKT
NNQKATGGRN GQQGNGATGQ SGNNNGGNQT TGNKGGKGAG NSKGGKGAGA ATGAAAGAAG
GAAGATAGAT SGGAATQAVT NANTPTAGNS LGLDIEANDV GYLATVQMGT PPQDFLILMD
SGSADLWVGA ENCQSANGGD CGNHRFLGSQ SSSSFVDTNQ PFSVTYGTGS VSGDIITDNI
AIAGLQLNQH TFGVATTESA DFSDNTTPFD GLMGLAQSTL SEQKTLTPIE ALAKQGVVNQ
AVIGYKISRL ADNKNDGEIT FGGTDSAKFD SATVVDLPNV SQQGFWESAM DAVSVDGKSL
GLNGRTAILD TGTTLIVAPD ADAQAVHAAI TGAQPDGQGG FTIPCNTQAS VALTFGGTSF
AIDPRDIAFQ PVDPNNPNGD CVSGISSGNV GGANEWLVGD VFLKNAYFST DVGKNSMSLA
KLA
//