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Database: UniProt
Entry: A0A091KUK6_9GRUI
LinkDB: A0A091KUK6_9GRUI
Original site: A0A091KUK6_9GRUI 
ID   A0A091KUK6_9GRUI        Unreviewed;       365 AA.
AC   A0A091KUK6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 33.
DE   SubName: Full=Embryonic pepsinogen {ECO:0000313|EMBL:KFP44309.1};
DE   Flags: Fragment;
GN   ORFNames=N324_09198 {ECO:0000313|EMBL:KFP44309.1};
OS   Chlamydotis macqueenii (Macqueen's bustard).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gruiformes; Otididae; Chlamydotis.
OX   NCBI_TaxID=187382 {ECO:0000313|EMBL:KFP44309.1, ECO:0000313|Proteomes:UP000053330};
RN   [1] {ECO:0000313|EMBL:KFP44309.1, ECO:0000313|Proteomes:UP000053330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N324 {ECO:0000313|EMBL:KFP44309.1};
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; KK759098; KFP44309.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091KUK6; -.
DR   Proteomes; UP000053330; 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:SF13; CHYMOSIN; 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:UP000053330}.
FT   DOMAIN          58..362
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        76
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        258
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        89..94
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        249..253
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        292..326
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP44309.1"
FT   NON_TER         365
FT                   /evidence="ECO:0000313|EMBL:KFP44309.1"
SQ   SEQUENCE   365 AA;  39877 MW;  6C46D172804FE881 CRC64;
     RLPLERGRKL RDALREKGLL QAFLQQHRYD VGTKFPHAFP NRTEVATEPL LNTLDMEYYG
     IISIGTPPQD FTVVFDTGSS NLWVPSVFCT SLACQNHQTF NPSQSSTYKS TGRNLSIFYG
     TGNMEGIVGS DTVTVASLVD TDQLFGLSTT ELGQFFVYVT FDGVLGLGYP NLAADGITLV
     FDKMVNESLL EENLFSVYLS RETTGSVVIF EGIDESYFTG SINWVSISHQ GYWQISMDSI
     IVNCQEITCI GGCQAVIDTG TSLVAGPPSS IGGIQSAVGA RQDVHGEYNV NCSSISAMPD
     VIFVINGVQY PVPASAYTEQ NDLGPCRSNF QDTAGDLWIL GDVFIRVYYS IFDRANNRVG
     LAKAI
//
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