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Database: UniProt
Entry: A0A093I7F8_EURHL
LinkDB: A0A093I7F8_EURHL
Original site: A0A093I7F8_EURHL 
ID   A0A093I7F8_EURHL        Unreviewed;       309 AA.
AC   A0A093I7F8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Embryonic pepsinogen {ECO:0000313|EMBL:KFV98629.1};
DE   Flags: Fragment;
GN   ORFNames=N326_03202 {ECO:0000313|EMBL:KFV98629.1};
OS   Eurypyga helias (Sunbittern) (Ardea helias).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Eurypygimorphae; Eurypygiformes;
OC   Eurypygidae; Eurypyga.
OX   NCBI_TaxID=54383 {ECO:0000313|EMBL:KFV98629.1, ECO:0000313|Proteomes:UP000054232};
RN   [1] {ECO:0000313|EMBL:KFV98629.1, ECO:0000313|Proteomes:UP000054232}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N326 {ECO:0000313|EMBL:KFV98629.1};
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; KK556745; KFV98629.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093I7F8; -.
DR   MEROPS; A01.028; -.
DR   Proteomes; UP000054232; 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; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
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:SF13; CHYMOSIN; 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|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054232}.
FT   DOMAIN          2..306
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        20
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        202
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        33..38
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        193..197
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        236..270
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV98629.1"
FT   NON_TER         309
FT                   /evidence="ECO:0000313|EMBL:KFV98629.1"
SQ   SEQUENCE   309 AA;  33259 MW;  5525221BA7558842 CRC64;
     EYYGTISIGT PPQDFSVVFD TGSSNLWVPS ISCTSLACQN HQMFNPSQSS TYRSTGQNLS
     IQYGTGNMEG IVGSDTVTVA SLVDTNQLFG LSTTEPGQFF VHVKFDGILG LGYPNLAADG
     ITPVFDNLVN ESLLEEDLFS VYLSCETTGS VVIFGGIDES YFTGSINWIS VSYQGYWQIS
     MDSIVVNNQE IACNGGCQAI IDTGTSLVAG PPSGISNIQS TVGAWLDMYG EYIVDCSSIS
     AMPDVIFVIN GLQYPVSASA YIEQNDQGPC ISSFQNTSGD LWILGDVFIR VYYSIFDRAN
     NRIGLAKAI
//
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