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Database: UniProt
Entry: A0A093BQP7_9AVES
LinkDB: A0A093BQP7_9AVES
Original site: A0A093BQP7_9AVES 
ID   A0A093BQP7_9AVES        Unreviewed;       309 AA.
AC   A0A093BQP7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 35.
DE   SubName: Full=Embryonic pepsinogen {ECO:0000313|EMBL:KFV02923.1};
DE   Flags: Fragment;
GN   ORFNames=N339_05208 {ECO:0000313|EMBL:KFV02923.1};
OS   Pterocles gutturalis (yellow-throated sandgrouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Ciconiiformes; Pteroclidae; Pterocles.
OX   NCBI_TaxID=240206 {ECO:0000313|EMBL:KFV02923.1, ECO:0000313|Proteomes:UP000053149};
RN   [1] {ECO:0000313|EMBL:KFV02923.1, ECO:0000313|Proteomes:UP000053149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N339 {ECO:0000313|EMBL:KFV02923.1};
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; KL226462; KFV02923.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093BQP7; -.
DR   MEROPS; A01.028; -.
DR   Proteomes; UP000053149; 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; 2.60.40.1960; -; 1.
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:UP000053149}.
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:KFV02923.1"
FT   NON_TER         309
FT                   /evidence="ECO:0000313|EMBL:KFV02923.1"
SQ   SEQUENCE   309 AA;  33105 MW;  ABAF97624E6BDB2A CRC64;
     EYYGSISIGT PPQNFTVVFD TGSSNLWVPS ASCISLACQN HQMFNPSQSS TYKNMGQNLS
     IQYGTGDMEG IVGSDTVTVA SLVDTNQLFG LSTTEPGEFF VNVKFDGILG LGYPELAADG
     LTPVFDNLMN ESLLEENLFS VYLSRDTAGS VVIFGGIDES YFTGSINWIP VSYQGYWQIS
     MDSIIVNSQE IACSGGCQAI IDTGTSLVAG PPSGISNIQS AVGAMEDMYG EYNVNCSSIA
     AMPDVIFVID GVQYPVSALA YTEPNSEGPC LSSFQNTSGD LWILGDVFIR VYYSIFDRAN
     NRVGLAKAI
//
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