ID V7AY39_PHAVU Unreviewed; 504 AA.
AC V7AY39;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PHAVU_009G220600g {ECO:0000313|EMBL:ESW10572.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
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; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW10572.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|EMBL:ESW10572.1}
RP NUCLEOTIDE SEQUENCE.
RA Schmutz J., McClean P., Shu S., Cregan P., Rokhsar D., Jackson S.;
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; CM002296; ESW10570.1; -; Genomic_DNA.
DR EMBL; CM002296; ESW10572.1; -; Genomic_DNA.
DR RefSeq; XP_007138576.1; XM_007138514.1.
DR RefSeq; XP_007138578.1; XM_007138516.1.
DR AlphaFoldDB; V7AY39; -.
DR STRING; 3885.V7AY39; -.
DR MEROPS; A01.A03; -.
DR EnsemblPlants; ESW10570; ESW10570; PHAVU_009G220600g.
DR EnsemblPlants; ESW10572; ESW10572; PHAVU_009G220600g.
DR GeneID; 18620942; -.
DR Gramene; ESW10570; ESW10570; PHAVU_009G220600g.
DR Gramene; ESW10572; ESW10572; PHAVU_009G220600g.
DR eggNOG; KOG1339; Eukaryota.
DR OrthoDB; 1120702at2759; -.
DR Proteomes; UP000000226; Chromosome 9.
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 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; 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:SF20; EUKARYOTIC ASPARTYL PROTEASE FAMILY PROTEIN; 1.
DR Pfam; PF00026; Asp; 1.
DR Pfam; PF05184; SapB_1; 1.
DR Pfam; PF03489; SapB_2; 1.
DR PRINTS; PR00792; PEPSIN.
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:UP000000226};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..504
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010981593"
FT DOMAIN 80..501
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 310..350
FT /note="Saposin B-type"
FT /evidence="ECO:0000259|PROSITE:PS50015"
FT DOMAIN 374..415
FT /note="Saposin B-type"
FT /evidence="ECO:0000259|PROSITE:PS50015"
FT ACT_SITE 98
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 285
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 111..117
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 504 AA; 55287 MW; 7101E44C253F2830 CRC64;
MGLKCLLVVM CVWGWLGSLT SATSDDGLKR VGLKRRNLDL QSLKDARIEE SVHPSDLGGA
KKNCCDEDII YLKNYLDAQF FGEISIGSPP QYFNVVFDTG SSNLWVPSSK CIFSIACYFH
SKYRSKISST YTEIGTPCTI PYGEGSIYGF FSQDNVQVGD VIIKDQEFAE ITREGSLALS
ALPFDGILGL GFQDASIGKV TPVWYNMIEQ GHICHKIFSL WLNQDPTEEM GGQIVFGGID
YRHFRGDHTY VPLSQKGYWQ IDVGDVLLAN NSTGLCEGGC AAIVDSGTSL IAGPTSVVTQ
INHAIGAQGY VSFECKSILH NYGNSIWGSL IAGLNPDLIC SDIGLCSNNG FNTMDDVIET
VVHNESWNGS PTRESPFCSL CNMIVLWIQV QIKQSNVKEK VFKYVDELCE KLPNPPGHSF
INCNSISSMP HITFTIGNKS FPLSPDQYIL RFEDGCSTVC YGGFIAIDVP PPQGPLWVLG
NIFLGAYHTV FDYGNLRIGF AEAA
//
