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Database: UniProt
Entry: A0A093C8M4_TAUER
LinkDB: A0A093C8M4_TAUER
Original site: A0A093C8M4_TAUER 
ID   A0A093C8M4_TAUER        Unreviewed;       368 AA.
AC   A0A093C8M4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 31.
DE   SubName: Full=Gastricsin {ECO:0000313|EMBL:KFV12300.1};
GN   ORFNames=N340_08918 {ECO:0000313|EMBL:KFV12300.1};
OS   Tauraco erythrolophus (Red-crested turaco).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Musophagiformes; Musophagidae; Tauraco.
OX   NCBI_TaxID=121530 {ECO:0000313|EMBL:KFV12300.1, ECO:0000313|Proteomes:UP000053661};
RN   [1] {ECO:0000313|EMBL:KFV12300.1, ECO:0000313|Proteomes:UP000053661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N340 {ECO:0000313|EMBL:KFV12300.1};
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; KL460348; KFV12300.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093C8M4; -.
DR   Proteomes; UP000053661; 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; 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:SF70; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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; 1.
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:UP000053661};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..368
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001883087"
FT   DOMAIN          73..365
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        91
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        267
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        104..110
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   368 AA;  41205 MW;  FA16E61EAB4E165F CRC64;
     MKWLVLVLVC LQLSEGLVRI KLKKAKSIRE KMKEAGVLED YLKKIKYDPV KKYRFSKDHV
     VYEPMTNHLD SSYFGEISIG TPPQNFLVLF DTGSSNLWVP STLCRTLACC EYRNRVAQST
     PSTRAYGSLA VVLGYDTLTI QSIKVTNQEF GLSEYEPTEP FYYAEFDGIL GMAYPSLAVG
     GTPTALQGML QQNQLAEPIF SFYFSRRPTY SYGGELILGG VDTQLFQGDI VWAPVSRELY
     WQVTLDEFVI GQSATGWCSE GCQAVVDTGT GCCSSHNLLF TLSPQYAVDC NKIKNMPTLT
     FIINGAELPL HPSSYVSNVY GYCTLGVEAT YLYSLNDQPL WILGDVFLKE YYTIFDMANN
     RLGFAVSV
//
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