ID I1HEQ0_BRADI Unreviewed; 503 AA.
AC I1HEQ0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=Aspartic proteinase {ECO:0008006|Google:ProtNLM};
GN Name=100842338 {ECO:0000313|EnsemblPlants:KQK04010};
GN ORFNames=BRADI_2g11190v3 {ECO:0000313|EMBL:KQK04010.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:KQK04010.1};
RN [1] {ECO:0000313|EMBL:KQK04010.1, ECO:0000313|EnsemblPlants:KQK04010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK04010.1,
RC ECO:0000313|EnsemblPlants:KQK04010};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQK04010.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK04010.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQK04010}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK04010};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; CM000881; KQK04010.1; -; Genomic_DNA.
DR RefSeq; XP_003567538.1; XM_003567490.3.
DR RefSeq; XP_010230799.1; XM_010232497.2.
DR AlphaFoldDB; I1HEQ0; -.
DR STRING; 15368.I1HEQ0; -.
DR MEROPS; A01.020; -.
DR EnsemblPlants; KQK04010; KQK04010; BRADI_2g11190v3.
DR GeneID; 100842338; -.
DR Gramene; KQK04010; KQK04010; BRADI_2g11190v3.
DR KEGG; bdi:100842338; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_1_1; -.
DR InParanoid; I1HEQ0; -.
DR OMA; DYVIQIS; -.
DR OrthoDB; 1120702at2759; -.
DR Proteomes; UP000008810; Chromosome 2.
DR ExpressionAtlas; I1HEQ0; baseline.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd06098; phytepsin; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR Gene3D; 1.10.225.10; Saposin-like; 1.
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 InterPro; IPR033869; Phytepsin.
DR InterPro; IPR007856; SapB_1.
DR InterPro; IPR008138; SapB_2.
DR InterPro; IPR011001; Saposin-like.
DR InterPro; IPR008139; SaposinB_dom.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF28; OS01G0290000 PROTEIN; 1.
DR Pfam; PF00026; Asp; 1.
DR Pfam; PF05184; SapB_1; 1.
DR Pfam; PF03489; SapB_2; 1.
DR PRINTS; PR00792; PEPSIN.
DR SMART; SM00741; SapB; 2.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF47862; Saposin; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50015; SAP_B; 2.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW 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:UP000008810};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..503
FT /note="Aspartic proteinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014094545"
FT DOMAIN 84..500
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 314..354
FT /note="Saposin B-type"
FT /evidence="ECO:0000259|PROSITE:PS50015"
FT DOMAIN 373..414
FT /note="Saposin B-type"
FT /evidence="ECO:0000259|PROSITE:PS50015"
FT DISULFID 115..121
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 422..459
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 503 AA; 55094 MW; 2E505C1253CD604E CRC64;
MGPRHLLWVT CLWTLSCALL LGASSDGVLR INLSKKRLDK EALTAAKLAR QQRNVLRSGD
GSYRYLGVSD DDIVPLDNYL DTQYYGEIGV GTPPQNFTVI FDTGSSNLWV PSSKCYFSIA
CYLHHKYKST KSSTYKKNGE TCTISYGSGS IAGFFSEDSV LVGDLVVKNQ KFIETTREAS
PSFIIGKFDG ILGLGFPEIS VGSAPPVWQS MQEQKLIAKD IFSFWLNRDP DAPTGGELVF
GGVDQKHYKG KHTYVPVTRK GYWQFDMGDL LIGGQSTGFC AGGCAAIVDS GTSLLAGPTT
IVAQVNHAIG AEGIISMECK EVVREYGEMI LELLVAQTRP QKVCSQIGLC VFDGTKSVSN
QIESVVEKEN RGSDLLCTAC EMAVVWIQNQ LRQNQTKELI LQYANQLCER LPSPNGESTV
DCHQISKMPN LAFTIANKTF TLTPEQYIVK LEQSGQTICI SGFMAFDIPP PRGPLWILGD
VFMGAYHTVF DFGDSKIGFA KSA
//