ID A0A1S3V0I5_VIGRR Unreviewed; 759 AA.
AC A0A1S3V0I5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Subtilisin-like protease SBT1.9 {ECO:0000313|RefSeq:XP_014511851.1};
GN Name=LOC106770564 {ECO:0000313|RefSeq:XP_014511851.1};
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_014511851.1};
RN [1] {ECO:0000313|RefSeq:XP_014511851.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014511851.1};
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_014511851.1; XM_014656365.2.
DR AlphaFoldDB; A0A1S3V0I5; -.
DR GeneID; 106770564; -.
DR KEGG; vra:106770564; -.
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 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; 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:SF514; SUBTILISIN-LIKE PROTEASE; 1.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF05922; Inhibitor_I9; 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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..759
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010377093"
FT DOMAIN 27..109
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 135..575
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 652..753
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 144
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 538
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 759 AA; 81663 MW; EBD27133AB1231F1 CRC64;
METPFPLMFL ITLWLLLPHH AKAETSTYVV HMDKSLMPQL FASHHDWYES IIHSIDLAIA
DDPSKQQELK LVYTYDDAMH GFSAVLSSEE LESLKKVDGF VTAYPDRSAT IDTTHTFEFL
SLDTPGGIWN ASNFGEGVIV GLIDTGIWPE SDSFKDDGMS RNIPSKWKGT CEPGQDFDAS
ICNFKLIGAR YFNKGVKAAN PNVTISMNSA RDTQGHGSHT SSTVAGNYVS GASFFGYAKG
VARGVAPRAR LAMYKVLWDE GRQASDVLAG MDQAIADGVD VISISLGFDS VPLYEDPVAI
AAFAAMEKGV LVSSSAGNEG PDVGTLHNGI PWVLTVAAGT IDRTFGSLAL GNGQTIVGWT
LFAANSIVDN FPLIYKKNLS ACNSVKLLSE AATRGIIICD AFDSISVLDQ IDLVTTASVV
GAVFISEDPR LLETGRLYSP SIVISPSDAP SVIKYAKSVE NPFASINFQQ TFVGIKPAPA
AAYYTSRGPS PSYPGILKPD VMAPGSNVLA AFVPNKPSAR IGTNVFLSSD YNFLSGTSMA
CPHASGVAAL LKAAHPDWSA AAIRSALVTT ANPFDNTQSP IRDNGNPLQY ASPLAMGAGE
IDPNKALDPG FIYDATPQDY VNLLCALGYT QNQILTITRS NFYICADNPS SDLNYPSFIV
LYSNKTRSTV QKFRRTVTNV GDGAATYRVK VKQPKGTVVK VSPETLSFGY KNEKQNYSVT
IKYRRNKTEN IPFGDIVWVE DGGARKVRSP IVVAPSEIA
//