ID A0A0L9V6C4_PHAAN Unreviewed; 473 AA.
AC A0A0L9V6C4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=LR48_Vigan08g144200 {ECO:0000313|EMBL:KOM50615.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM50615.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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; CM003378; KOM50615.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L9V6C4; -.
DR STRING; 3914.A0A0L9V6C4; -.
DR EnsemblPlants; KOM50615; KOM50615; LR48_Vigan08g144200.
DR Gramene; KOM50615; KOM50615; LR48_Vigan08g144200.
DR OMA; FRAWVVI; -.
DR Proteomes; UP000053144; Chromosome 8.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd05476; pepsin_A_like_plant; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034161; Pepsin-like_plant.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR032799; TAXi_C.
DR InterPro; IPR032861; TAXi_N.
DR PANTHER; PTHR13683; ASPARTYL PROTEASES; 1.
DR PANTHER; PTHR13683:SF880; EUKARYOTIC ASPARTYL PROTEASE FAMILY PROTEIN; 1.
DR Pfam; PF14541; TAXi_C; 1.
DR Pfam; PF14543; TAXi_N; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022750};
KW Protease {ECO:0000256|ARBA:ARBA00022750};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..473
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005596629"
FT DOMAIN 77..417
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 95
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 297
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 473 AA; 51143 MW; 600899132E91FEC9 CRC64;
MEAVAAVFLF AAALLSVVEG SPVTLTLERA FPSNHGVELS QLRARDSLRH RRMLQSTNYV
VDFPVKGTFD PSQVGLYYTK VKMGTPPREF YVQIDTGSDV LWIQLNYFDP RSSSTSSLIS
CSDRRCRSGV QSSDASCSSQ NNQCIYTFQY GDGSGTSGYY VSDLMHFASI FEGTLTTNAS
ASVVFGCSIQ QTGDLTKSDR AVDGIFGFGQ QGMSVISQLS SQGIAPRVFS HCLRGDNTGG
GVLVLGEIVE PNIVYTPLVP SQPHYNLYLQ SISVNGQFLQ INPAVFATSS NRGTIVDSGT
TLSYLAEEAY TTFVNAITAA IPQSVRSVLS RGNQCYLITT SSNVDMFPQV SLNFAGGASL
VLRPLDYLIQ QNYIGEGSVW CIGFQKIPGQ SVTILGDLVL KDKIFVYDVA GQRIGWTNYD
CSLPVNVSAS AGRGRSEFVD SGELGGSTSL CEGPHTLIRM LLLALFMHIT LIL
//
