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Database: UniProt
Entry: A0A091PMS8_HALAL
LinkDB: A0A091PMS8_HALAL
Original site: A0A091PMS8_HALAL 
ID   A0A091PMS8_HALAL        Unreviewed;       309 AA.
AC   A0A091PMS8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 38.
DE   SubName: Full=Embryonic pepsinogen {ECO:0000313|EMBL:KFP95951.1};
DE   Flags: Fragment;
GN   ORFNames=N329_03625 {ECO:0000313|EMBL:KFP95951.1};
OS   Haliaeetus albicilla (White-tailed sea-eagle) (Falco albicilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC   Accipitrinae; Haliaeetus.
OX   NCBI_TaxID=8969 {ECO:0000313|EMBL:KFP95951.1, ECO:0000313|Proteomes:UP000054379};
RN   [1] {ECO:0000313|EMBL:KFP95951.1, ECO:0000313|Proteomes:UP000054379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N329 {ECO:0000313|EMBL:KFP95951.1};
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; KK640821; KFP95951.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091PMS8; -.
DR   MEROPS; A01.028; -.
DR   Proteomes; UP000054379; 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:UP000054379}.
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:KFP95951.1"
FT   NON_TER         309
FT                   /evidence="ECO:0000313|EMBL:KFP95951.1"
SQ   SEQUENCE   309 AA;  33242 MW;  980284A590E186C9 CRC64;
     EYYGTISIGT PPQDFTVVFD TGSSNLWVPS ISCTSLACQN HQMFNPSQSS TYKSTGQNLS
     IQYGTGNMEG IVGSDTVTVA SLVDTNQLFG LSTTEPGQFF VHVKFDGVLG LGYPNLAADG
     ITPVFDNLVN ESLLEENLFS VYLSRETTGS VVIFGGIDES YFTGSINWIF VSYQGYWQIS
     MDSIIVNSQE IACSGGCQAI VDTGTSLVAG PPSGISNIQS AVGARQDTYG EYIVNCSSIS
     TMPDVIFVID GVQYPVSALA YIEQNDQGPC ISSFQNTSGD LWILGDVFIR VYYSIFDRAN
     NRVGLAKAI
//
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