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
//