ID A0A091RMI6_NESNO Unreviewed; 380 AA.
AC A0A091RMI6;
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:KFQ43905.1};
DE Flags: Fragment;
GN ORFNames=N333_11635 {ECO:0000313|EMBL:KFQ43905.1};
OS Nestor notabilis (Kea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Nestor.
OX NCBI_TaxID=176057 {ECO:0000313|EMBL:KFQ43905.1, ECO:0000313|Proteomes:UP000053840};
RN [1] {ECO:0000313|EMBL:KFQ43905.1, ECO:0000313|Proteomes:UP000053840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N333 {ECO:0000313|EMBL:KFQ43905.1};
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; KK928074; KFQ43905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091RMI6; -.
DR MEROPS; A01.045; -.
DR Proteomes; UP000053840; 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:UP000053840}.
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:KFQ43905.1"
FT NON_TER 380
FT /evidence="ECO:0000313|EMBL:KFQ43905.1"
SQ SEQUENCE 380 AA; 42507 MW; BCF8526FA7F19C43 CRC64;
RIPLIRFKSI KKQLKEKGEL EEFWRNHHPD IFARRYLHCF PADIALSVGT ASERLYDYMN
AQYYGVVSVG TPPQKFTVVF DTGSSNFWVP SAYCISEACR VHQKFKSFLS DSYEHGGEAF
SLQYGTGQLL GIAGKDTLQI SNISIKGQDF GESVFEPGVT FALAHFDGVL GLGYPSLIVG
NALPVFDSIM NQQLVEEPVF SFYLKRGDDT ENGGELILGG IDHSLYKGSI HWVPVTEKSY
WQIHLNNIKI QGRVAFCSHG CEAIVDSGTS LITGPSSQIR RLQEYIGASP SRTGEFLVDC
RRLSSLPHIS FTIGHHEYKL TAEQYVIKES IEDQTFCMSG FQALDIPTRN GLLWILGDVF
MSAFYCIFDR GNDRVGFAKA
//