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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//