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Database: UniProt
Entry: A0A0A0ANU9_CHAVO
LinkDB: A0A0A0ANU9_CHAVO
Original site: A0A0A0ANU9_CHAVO 
ID   A0A0A0ANU9_CHAVO        Unreviewed;       381 AA.
AC   A0A0A0ANU9;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   22-FEB-2023, entry version 30.
DE   SubName: Full=Cathepsin E-A {ECO:0000313|EMBL:KGL95557.1};
DE   Flags: Fragment;
GN   ORFNames=N301_01479 {ECO:0000313|EMBL:KGL95557.1};
OS   Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX   NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL95557.1, ECO:0000313|Proteomes:UP000053858};
RN   [1] {ECO:0000313|EMBL:KGL95557.1, ECO:0000313|Proteomes:UP000053858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL95557.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
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; KL872441; KGL95557.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A0ANU9; -.
DR   STRING; 50402.A0A0A0ANU9; -.
DR   MEROPS; A01.045; -.
DR   Proteomes; UP000053858; 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; 6.10.140.60; -; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR012848; Aspartic_peptidase_N.
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:SF37; CATHEPSINE-A-LIKE PROTEIN-RELATED; 1.
DR   Pfam; PF07966; A1_Propeptide; 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|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053858}.
FT   DOMAIN          63..378
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        94..99
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        257..261
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        300..337
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KGL95557.1"
FT   NON_TER         381
FT                   /evidence="ECO:0000313|EMBL:KGL95557.1"
SQ   SEQUENCE   381 AA;  42523 MW;  D717081E511D7700 CRC64;
     RIPLVRFKSI KKQLKEKGEL EEFWRNHHPD VFARRYLHCF PADIALSVGT ASERLYDYMN
     AQYYGVVSVG TPPQRFTVVF DTGSSNFWVP SAYCISEACR VHQKFKSFLS DSYEHGGEAF
     SLQYGTGQLL GIAAKDTLQI SNISIKGQDF GESVFEPGTT FALAHFDGVL GLGYPSLAVG
     NALPVFDSIM NQQLVEEPVF SFYLKRGDDT ENGGELILGG IDHSLYKGSI HWVPVTEKSY
     WQIHMNNIKI QGRVAFCSHG CEAIVDSGTS LITGPSSQIR RLQEYIGASP SHTGEFLVDC
     RRLSSLPHIS FTIGHHEYKL TAEQYVVKES IEDQTFCMSG FQSLDITTHS GPLWILGDVF
     MSAFYCIFDR GNDRVGFAKA V
//
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