ID A0A0L9VRL6_PHAAN Unreviewed; 772 AA.
AC A0A0L9VRL6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Subtilisin-like protease SBT1.1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=LR48_Vigan11g043200 {ECO:0000313|EMBL:KOM57399.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
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=3914 {ECO:0000313|EMBL:KOM57399.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CM003381; KOM57399.1; -; Genomic_DNA.
DR RefSeq; XP_017441541.1; XM_017586052.1.
DR RefSeq; XP_017441542.1; XM_017586053.1.
DR AlphaFoldDB; A0A0L9VRL6; -.
DR EnsemblPlants; KOM57399; KOM57399; LR48_Vigan11g043200.
DR GeneID; 108346974; -.
DR Gramene; KOM57399; KOM57399; LR48_Vigan11g043200.
DR KEGG; var:108346974; -.
DR OMA; GALVWIC; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000053144; Chromosome 11.
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; IPR023827; Peptidase_S8_Asp-AS.
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:SF564; SUBTILISIN-LIKE PROTEASE SBT1.1; 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; PS00136; SUBTILASE_ASP; 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:UP000053144};
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..772
FT /note="Subtilisin-like protease SBT1.1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005597081"
FT DOMAIN 25..119
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 143..592
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 379..464
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 668..769
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 151
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 224
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 551
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 772 AA; 82036 MW; 18F72825F7125752 CRC64;
MNFRALLLFL AFMVTKSVAV VEKQTYIVHM DKTKMEASVH SQGLAKPWFK SKPWFKSVID
FISEASFEEE EGGGEPQLLY VYETSLFGFA AQLSNKQLEY LNQVDGFVAA LPDELLTLHT
TYTPHFLGLQ EGEGLWSASN LASDVIIGVL DTGIWPEHIS FQDTGLSKVP SRWKGACEAG
TNFSASSCNK KLVGARVFLQ GYEKFAGRIN ETMDYRSARD AQGHGSHTAS TAAGNMVKNA
SFFGLASGSA SGMRYTSRIA AYKVCWRLGC ANSDILAAID KAVADGVDVL SLSLGGSARP
YYSDSIAIAS FGATQNGVFV SCSAGNSGPF SSTVGNVAPW IMTVAASYTD RSFPTQVKLG
NGKLFKGSSL YKGKKTNQLP LVYVNSSKEH RTAQYCTKGS LDPKFVKGKI VACERGINSR
TAKGEEVKMA GGAGMILLNS ENQGEELFAD HHVLPGTSLG ASASKIIRSY IHSAKAPTAS
ISFQGTAYGD PAPAMAAFSS RGPSAVGGDV IKPDVTAPGV NILAAWPPIT SPSMLKSDKT
SAVFNIVSGT SMSCPHVSGI AALIKSAHNG WSPAAIKSAL MTTASVSNNK GAAIADYGSK
TSALADPFAF GSGHVNPERA SDPGLVYDIT TKDYLNYLCS LKYTPSQIAL LSKGNFTCPK
KSALQAGDLN YPSFAVLFGT RALKASVTFK RVVTNVGNPK ISYAVKVEEP NGVSVRVEPR
NISFRKTGQK MSYKVSFVSN GNTTVTGNSS FGSLTWVSGK YAVRSPIAVT WK
//
