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Database: UniProt
Entry: V7CF40_PHAVU
LinkDB: V7CF40_PHAVU
Original site: V7CF40_PHAVU 
ID   V7CF40_PHAVU            Unreviewed;       644 AA.
AC   V7CF40;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=PHAVU_002G014200g {ECO:0000313|EMBL:ESW28744.1};
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:ESW28744.1, 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; CM002289; ESW28744.1; -; Genomic_DNA.
DR   RefSeq; XP_007156750.1; XM_007156688.1.
DR   AlphaFoldDB; V7CF40; -.
DR   STRING; 3885.V7CF40; -.
DR   MEROPS; A01.A59; -.
DR   EnsemblPlants; ESW28744; ESW28744; PHAVU_002G014200g.
DR   GeneID; 18636616; -.
DR   Gramene; ESW28744; ESW28744; PHAVU_002G014200g.
DR   KEGG; pvu:PHAVU_002G014200g; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   OMA; YQLVEWN; -.
DR   OrthoDB; 335768at2759; -.
DR   Proteomes; UP000000226; Chromosome 2.
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; PTHR13683; ASPARTYL PROTEASES; 1.
DR   PANTHER; PTHR13683:SF817; OS07G0592200 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; 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:UP000000226};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..644
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004755641"
FT   TRANSMEM        594..619
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          91..429
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          53..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        109
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        305
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   644 AA;  71499 MW;  AC2DE47EB51675F0 CRC64;
     MALQRTQLIS VVSLILSLAQ WVVATGDSGE VLLLPNEGSR PAMILPLHHS VPDDSSVSDF
     SPRRQLQRSQ SQRHPDARMR LYDDLLRNGY YTTRLWIGTP PQRFALIVDT GSTVTYVPCS
     TCQHCGKHQD PKFQPEDSET YQPVKCTWQC NCDTDRKQCT YERRYAEMST SSGVLGEDVI
     SFGNQSELSP QRATFGCEND ETGDLYTQHA DGIMGLGRGD LSIMDQLVEK KVISDAFSLC
     YGGMGVGGGA MVLGGISPPA DMVFTHSDPG RSPYYNINLK EVHVAGKRLN LNPKVFDGKH
     GTVLDSGTTY AYLPESAFLA FKDAIMKDTH SLKRISGPDP RYNDICFSGA GSDVSQLSKS
     FPVVDMVFEN GHKLSLSPEN YLFRHLKVRG AYCLGVFSNG NDPTTLLGGI VVRNTLVMYD
     REHTKIGFWK TNCSELWERL HVSDAPPPLS PKSEGTNLTK AFEPSVAPSP SPSQYNLPLG
     ELQIAQIIVV ISFNISYMEM KPYITQLTGL IANELDVNTS QVHLLNVSSL GNGSLSKWLI
     TPRPYADFFS NATAMSMIAR LSEHRMQLPD SLGSYKFLGW NAKPPLKRTW WQQYYLTVAL
     AVLLTLLLGI SALGVFLIWR NRQQAEQSYE PVNVAVQEQE LQPL
//
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