GenomeNet

Database: UniProt
Entry: A0A078B4K2_STYLE
LinkDB: A0A078B4K2_STYLE
Original site: A0A078B4K2_STYLE 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system