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Database: UniProt
Entry: A0A1S3V7S3_VIGRR
LinkDB: A0A1S3V7S3_VIGRR
Original site: A0A1S3V7S3_VIGRR 
ID   A0A1S3V7S3_VIGRR        Unreviewed;       769 AA.
AC   A0A1S3V7S3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Subtilisin-like protease SBT1.3 {ECO:0000313|RefSeq:XP_014514398.1};
GN   Name=LOC106772488 {ECO:0000313|RefSeq:XP_014514398.1};
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
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=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014514398.1};
RN   [1] {ECO:0000313|RefSeq:XP_014514398.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_014514398.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   RefSeq; XP_014514398.1; XM_014658912.2.
DR   AlphaFoldDB; A0A1S3V7S3; -.
DR   EnsemblPlants; Vradi08g19310.1; Vradi08g19310.1; Vradi08g19310.
DR   GeneID; 106772488; -.
DR   Gramene; Vradi08g19310.1; Vradi08g19310.1; Vradi08g19310.
DR   KEGG; vra:106772488; -.
DR   OrthoDB; 11910at2759; -.
DR   Proteomes; UP000087766; Chromosome 8.
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; IPR003137; PA_domain.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-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; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR   PANTHER; PTHR10795:SF322; SUBTILISIN-LIKE PROTEASE SBT1.3; 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; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
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:UP000087766};
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..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..769
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010383792"
FT   DOMAIN          25..109
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          135..591
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          374..465
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          665..763
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        143
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        216
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        550
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   769 AA;  82878 MW;  CC41E23A97B98CBB CRC64;
     MGLILTIYLL LCILSSANAE FSKKTYIIQM DKSAKPQTFS NHLEWYTSKV KSILSTSVEA
     EMDKEERIIY TYQTAFHGLA AKLSQEEAEK LEAEEGVVAM FPDTKYQLHT TRSPTFLGLE
     PTQSTNVWSE KLANHDVTVG VLDTGIWPES ESFNDTGMRS VPSHWKGACE TGRGFEKYHC
     NKKIVGARMF YHGYEAATGK IDEKTEYISP RDQDGHGTHT AATVAGSPVH DANLLGYAHG
     TARGMAPRAR IAAYKVCWTG GCFSSDILSA VDTAVADGVD VLSISLGGGV SSYYRDSLSV
     AAFGAMEKGV LVSCSAGNAG PDPVSLTNVS PWITTVGAST MDRDFPADVS LGNGRKITGT
     SLYKGRSVLS VKKQYPLVYM GNTNSSIPDP RSLCLEGTLD RRMVSGKIVI CDRGISPRVQ
     KGQVVKNAGG VGMILTNTAA NGEELVADCH LLPAVAIGEK EGKELKHYVL TSKKATATLA
     FLATRLGVRP SPVVAAFSSR GPNFLTLEIL KPDVVAPGVN ILAAWSGAIG PSSLPTDHRR
     VKFNILSGTS MSCPHVSGIA ALLKARHPEW SPAAIKSALM TTAYVHDNTI KPLKDASSAD
     ASTPYDHGAG HINPIRALDP GLVYDIQPQD YFEFLCTQKL TPSELGVFAK YSNRTCSHTL
     ANPGDLNYPA ISVVFPQTNS SSVLTVHRTA TNVGPAVSKY HVVVSHFKGA SVKVEPKTLS
     FTKKYQKLSY KVTFTTQSRQ TEPEFGGLVW KDGVHKVRSP IVITYLSPI
//
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