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Database: UniProt
Entry: A0A091NRG3_APAVI
LinkDB: A0A091NRG3_APAVI
Original site: A0A091NRG3_APAVI 
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
//
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