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Database: UniProt
Entry: V7BGQ6_PHAVU
LinkDB: V7BGQ6_PHAVU
Original site: V7BGQ6_PHAVU 
ID   V7BGQ6_PHAVU            Unreviewed;       508 AA.
AC   V7BGQ6;
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=Aspartic proteinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PHAVU_007G205100g {ECO:0000313|EMBL:ESW17037.1};
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:ESW17037.1, ECO:0000313|Proteomes:UP000000226};
RN   [1] {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; CM002294; ESW17037.1; -; Genomic_DNA.
DR   RefSeq; XP_007145043.1; XM_007144981.1.
DR   AlphaFoldDB; V7BGQ6; -.
DR   STRING; 3885.V7BGQ6; -.
DR   MEROPS; A01.020; -.
DR   EnsemblPlants; ESW17037; ESW17037; PHAVU_007G205100g.
DR   GeneID; 18626516; -.
DR   Gramene; ESW17037; ESW17037; PHAVU_007G205100g.
DR   KEGG; pvu:PHAVU_007G205100g; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   OMA; EYLVICR; -.
DR   OrthoDB; 1120702at2759; -.
DR   Proteomes; UP000000226; Chromosome 7.
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:SF28; PLASMEPSIN X; 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..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..508
FT                   /note="Aspartic proteinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004754529"
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   ACT_SITE        103
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        116..122
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        281..285
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   508 AA;  55697 MW;  105044826042A0A6 CRC64;
     MGNTYLLLTF CLWALTCSLL PSFSCGLMKI GLKKRDVDLD SIRTARMVRE KLRIGRPVLG
     AYDQYLGKPT DEGIVPLKNY LDAQYYGEIG IGTPPQKFNV IFDTGSSNLW VPSSKCYFSL
     ACYTHKWYKP KKSKTYIKNG TSCKISYGSG SISGFFSEDS VKVGDIVVKK QDFIEATREG
     SLSFLLAKFD GLLGLGFQEI SVENAVPVWY NMVQQNLVSD QVFSFWLNGD PSAKEGGELV
     FGGVDPKHFK GNHTYVPVTK KGYWQIEMGD FFVGGLSTGV CEGGCAAIVD SGTSLLAGPT
     TVVTEINHAI GAEGVLSVEC KEVVSEYGEL LWDLLISGVR PGDVCSQVGL CVAKRGQSES
     NGIEMVTEKE HRELSAKDTV LCTPCQMLVI WIQNQLKQQK TKETVFNYVN QLCENLPSPN
     GESVVNCNGI SGLPNITFTV GDKPFTLTPE QYILKTGEGI AEVCISGFIA FDIPPPRGPL
     WILGDVFMRV YHTVFDYGNL RVGFAKAA
//
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