ID A0A0L9V2T7_PHAAN Unreviewed; 492 AA.
AC A0A0L9V2T7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=LR48_Vigan08g008800 {ECO:0000313|EMBL:KOM49261.1};
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:KOM49261.1, 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, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; CM003378; KOM49261.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L9V2T7; -.
DR EnsemblPlants; KOM49261; KOM49261; LR48_Vigan08g008800.
DR Gramene; KOM49261; KOM49261; LR48_Vigan08g008800.
DR OMA; CEECYLQ; -.
DR Proteomes; UP000053144; Chromosome 8.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR001969; Aspartic_peptidase_AS.
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; PTHR47967:SF66; ASPARTIC PROTEINASE CDR1-RELATED; 1.
DR PANTHER; PTHR47967; OS07G0603500 PROTEIN-RELATED; 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; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 47..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 145..484
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 163
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 371
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 492 AA; 54962 MW; 0EF9E050C3E2654E CRC64;
MYSKKKGVGA NQEYIRYKVL NIVTIIADNF TVLIRRQQEL QIHLKRLFVY ELILCMYMMT
MVVRYSSFLI VLVFLQNISF SKALKSSFSV EMIHRDSPKS PFYRPTETHF QRVQNAILRS
IHRAKYFKLD SNDVEGTVTP VSGEFLVNYS VGTPPVQMLG IVDTGSDMVW IQCQPCKNCY
KEKRPIFDPS TSRTYSSMAC VSAYCLSAPH SFCNFNHGNH CAYKVTYDDG TTSEGDFSWD
TITLTSSTKN VPVAFPETVI GCGHNNVGVL GEQTSGIVGL GNGPFSLAGQ LKPKTGGTFY
YCLTPMYEGE AKPSYLHFGD LGEVVEEAVS TPLIRNLEQP FLYYVVMEAI SVGSKRIEFP
RKGDDGNIII DSGTTLTFLP DEVYSSLEEE MVNAVNLPRI NRPQEGVKLC YEITPGQQYQ
IPTVYAHFKG GGTVKLHSIN TFFQASESVI CLAFHSGSEA ILGNLAQQDI LVTYDTDHDT
VTFLNTDCTS EL
//
