ID A0A078B4K2_STYLE Unreviewed; 369 AA.
AC A0A078B4K2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 28-JUN-2023, entry version 37.
DE SubName: Full=Cathepsin d {ECO:0000313|EMBL:CDW88152.1};
GN Name=Contig17806.g18934 {ECO:0000313|EMBL:CDW88152.1};
GN ORFNames=STYLEM_17269 {ECO:0000313|EMBL:CDW88152.1};
OS Stylonychia lemnae (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW88152.1, ECO:0000313|Proteomes:UP000039865};
RN [1] {ECO:0000313|EMBL:CDW88152.1, ECO:0000313|Proteomes:UP000039865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=130c {ECO:0000313|EMBL:CDW88152.1,
RC ECO:0000313|Proteomes:UP000039865};
RA Swart Estienne;
RL Submitted (JUN-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; CCKQ01016276; CDW88152.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078B4K2; -.
DR EnsemblProtists; CDW88152; CDW88152; STYLEM_17269.
DR InParanoid; A0A078B4K2; -.
DR OMA; KMPSIRD; -.
DR OrthoDB; 1120702at2759; -.
DR Proteomes; UP000039865; 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 Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
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|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:UP000039865};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..369
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001729813"
FT DOMAIN 64..362
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 82
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 259
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 95..100
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 285..322
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 369 AA; 40563 MW; 8CEA99BA829DED1C CRC64;
MQKLAVLLLL ASSALTAKIP LRKVQITKQK FLSAKERLNS EVPKFLDNGL GESIPVKDYM
NTQYFVDVEI GTPAQTFTVV PDTGSSNLWV YSSKCYAIVC YYHSLYNAAK SSTYKKNGEK
FDITYGSGSI SGTVSEDVSN LGGTHSHIGF GEITSVSGAS FYASQMSGIL GLAYDTISVD
KIPTFIDQSD LTDKSFAFYL HSNPDASYMT IPGYDTDAVG NNEFTFHNVV EQRYYSLNLT
GLKQGDTSIP SNNFKAVIDS GTSVLVGPNS LVNPLIKGIT VNDDCSGLDK LPTITFQIDN
LDYTLTPNDY VLQVTQGSDT ECVLAVMGQD FPAGFDYFIL GDTFMRKFYS YFDKKNNRVG
FINAEKLHH
//