ID A0A0L9U9A8_PHAAN Unreviewed; 508 AA.
AC A0A0L9U9A8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=LR48_Vigan03g268800 {ECO:0000313|EMBL:KOM39306.1};
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:KOM39306.1, 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; CM003373; KOM39306.1; -; Genomic_DNA.
DR RefSeq; XP_017419343.1; XM_017563854.1.
DR AlphaFoldDB; A0A0L9U9A8; -.
DR EnsemblPlants; KOM39306; KOM39306; LR48_Vigan03g268800.
DR GeneID; 108329584; -.
DR Gramene; KOM39306; KOM39306; LR48_Vigan03g268800.
DR OMA; KYDHDAS; -.
DR OrthoDB; 1120702at2759; -.
DR Proteomes; UP000053144; Chromosome 3.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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:SF78; FUNGAL PROTEINASE A, ASPARTIC PROTEINASE SUPERFAMILY 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; 1.
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; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..508
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005595491"
FT DOMAIN 85..505
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 315..355
FT /note="Saposin B-type"
FT /evidence="ECO:0000259|PROSITE:PS50015"
FT DOMAIN 378..419
FT /note="Saposin B-type"
FT /evidence="ECO:0000259|PROSITE:PS50015"
FT DISULFID 116..122
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 508 AA; 55644 MW; 8441A33551B865B9 CRC64;
MGQKHLVVAF CLWALTCSSL PSFSYGILKI GLRKRPLDLN SIHAARKARE GLRYGRPIMG
EHDQFIGKAK GEDSVPLKNY LDAQYFGEIG IGTPPQTFTV VFDTGSSNLW VPSSKCYFSL
ACYTHNWYKP KKSRTYVKNG TSCKINYGSG SISGYFSQDS VKVGNAVVKQ LDFIEATREG
SLSFLSAKFD GILGLGFQEI SVANSVPLWY KMVDQNLISE KVFSFWLNGD PNAKKGGEIV
FGGVNPKHFK GDHTYVPVTE KGYWQIEIGD FFIGGASTGV CEGGCAAIVD SGTSLLAGPT
PVVAEINHAI GAEGVLSVEC KEVVSQYGEM IWDLLVSGVK PDDICSQVGL CSAKRIQSKS
PGIEMVTEKE QSELTARDTP LCSSCQMLVL WIQNQLKQKQ TKDRVFNYVN QLCESLPSPS
GESVISCNSL SKMPNITFTI GDKPFVLTPE QYILRTGEGI TEVCLSGFMA FDVPPPRGPL
WILGDVFMRA YHTIFDYGNL RVGFAEAV
//
