ID A0A091NRG3_APAVI Unreviewed; 380 AA.
AC A0A091NRG3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 32.
DE SubName: Full=Cathepsin E-A {ECO:0000313|EMBL:KFP91951.1};
DE Flags: Fragment;
GN ORFNames=N311_01407 {ECO:0000313|EMBL:KFP91951.1};
OS Apaloderma vittatum (Bar-tailed trogon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Trogoniformes; Trogonidae; Apaloderma.
OX NCBI_TaxID=57397 {ECO:0000313|EMBL:KFP91951.1, ECO:0000313|Proteomes:UP000054244};
RN [1] {ECO:0000313|EMBL:KFP91951.1, ECO:0000313|Proteomes:UP000054244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N311 {ECO:0000313|EMBL:KFP91951.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-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; KL392078; KFP91951.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091NRG3; -.
DR MEROPS; A01.045; -.
DR Proteomes; UP000054244; 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:UP000054244}.
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:KFP91951.1"
FT NON_TER 380
FT /evidence="ECO:0000313|EMBL:KFP91951.1"
SQ SEQUENCE 380 AA; 42550 MW; 59A8644311DA8259 CRC64;
RIPLTQFKSI RRQLKEKGQL EEFWRNHYPD IFARRYLHCF PADIALSVGT ASERLYDYMN
AQYYGVVNVG TPPQRFTVVF DTGSSNFWVP SAYCISEACR LHQKFKSFLS DSYEHGGEAF
SLQYGTGQLL GVAGKDTLQI SNISIKGQDF GESVLEPGMT FAFAHFDGVL GLGYPSLAVG
NALPVFDSIM NQQLVEEPVF SFYLRRGDDT ENGGELILGG IDHSLYKGSI HWVPVTEKSY
WQIHLNNIKI QGRVAFCSHG CEAIVDSGTS LITGPSSQIR RLQEYIGASP SRTGEFLVDC
RRLSSLPHIS FTIGHHEYKL SAEQYVVKES IEDQTFCMSG FQSLDIPTRA GPLWILGDVF
MSAFYCIFDR GNDRVGFAKA
//