ID V7CM29_PHAVU Unreviewed; 765 AA.
AC V7CM29;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESW30423.1};
GN ORFNames=PHAVU_002G152500g {ECO:0000313|EMBL:ESW30423.1};
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:ESW30423.1, 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 S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; CM002289; ESW30423.1; -; Genomic_DNA.
DR RefSeq; XP_007158429.1; XM_007158367.1.
DR AlphaFoldDB; V7CM29; -.
DR EnsemblPlants; ESW30423; ESW30423; PHAVU_002G152500g.
DR GeneID; 18638043; -.
DR Gramene; ESW30423; ESW30423; PHAVU_002G152500g.
DR KEGG; pvu:PHAVU_002G152500g; -.
DR eggNOG; ENOG502QPQR; Eukaryota.
DR OMA; VACEHTT; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000000226; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009610; P:response to symbiotic fungus; IEA:UniProt.
DR CDD; cd02120; PA_subtilisin_like; 1.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 2.60.40.2310; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034197; Peptidases_S8_3.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR045051; SBT.
DR InterPro; IPR041469; Subtilisin-like_FN3.
DR PANTHER; PTHR10795:SF463; OS12G0427600 PROTEIN; 1.
DR PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000000226};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..765
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004755486"
FT DOMAIN 49..133
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 157..584
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 383..470
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 662..762
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 166
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 548
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 765 AA; 81045 MW; 38721EC31EFA9EB5 CRC64;
MELALPLALI FMLISICQTS AHRNPEFVKA IKEHYFPTQE IDVPNSLLTY IVRVKKGDEG
GDGDSLGSMD LHSWYHSLLP SSTRSDQKQN RITFLYRNVM DGFSVELTPE EADALQEKEE
VVSVRPERTF SLHTTHTPSF LGLQQGLGGL WSNSDSGKGI IIGILDTGIT PDHPSFSDEG
MPFPPAKWKG LCEFSGRRTC NNKLIGARHF IKSSNSSLPL DHVGHGTHTA STATGRFVQG
ANVFGNAKGT AVGMAPDAHL AIYKVCDIFG CSESAILAGM DTAIEDGVDV LSLSIGGRSG
PLFDDPIALG AFSAIQKGIF VSCSAGNSGP GYTTLSNEAP WILTVGASTI DRRIVAAAKL
GNGQVFNGES VFQPNNFTST LLPLVYAGSI GNSSSSLCAP GSLENVDVKG KVVLCEVGGF
IRRVSKGQEV KNAGGVAMIL MNSLKEDFNP FADVHVLPAT HVSYPAGLAI KSYINSTSTP
TATILFGGTV IGSVSAPAVT SFSSRGPSFA SPGILKPDII GPGQNILAAW PVSLDNNVPS
FNILSGTSMS CPHLSGIAAL LKNSHPDWSP AAIKSAIMTS ANAVNLGGKS ILDERLLPAD
VFATGAGHVN PLKANDPGLV YDIEPNDYIP YLCGLNYTDE EVGLILNQNV DCSQVKSIPQ
AQLNYPSFSI RLGSTSQFYT RTLTNVGAAS VTYNVEIEAP LGVGISISPA EITFTEVKQK
VTYSVGFVPE DKKNRGNHPF SQGSIRWVSG NGKYSVSIPI AVVFL
//
