ID A0A0L9UXH3_PHAAN Unreviewed; 769 AA.
AC A0A0L9UXH3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Subtilisin-like protease SBT1.1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=LR48_Vigan07g095800 {ECO:0000313|EMBL:KOM47254.1};
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:KOM47254.1, 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; CM003377; KOM47254.1; -; Genomic_DNA.
DR RefSeq; XP_017429689.1; XM_017574200.1.
DR AlphaFoldDB; A0A0L9UXH3; -.
DR EnsemblPlants; KOM47254; KOM47254; LR48_Vigan07g095800.
DR GeneID; 108337634; -.
DR Gramene; KOM47254; KOM47254; LR48_Vigan07g095800.
DR OMA; CWSSGCT; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000053144; Chromosome 7.
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..769
FT /note="Subtilisin-like protease SBT1.1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005596037"
FT DOMAIN 25..115
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 139..586
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 375..460
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 665..766
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 147
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 221
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 769 AA; 82619 MW; 8AB4082AB5EDE1EF CRC64;
MIFRTLVLVL AFMVANSTAL ADQQTYIVHI DKTKIRASIH SQDSSKPWFE SIIDSISEAS
MQEDGEEDIL APQLLYAYET SMFGFAAHLS KKHLKYLNQV EGFLSAIPDE LSTLHTTYSP
QFLGLRSRRE LWTASNLAND VIIGVLDSGI WPEHTSFRDS GLSPVPSHWK GVCEKGTKFS
SSNCNKKLIG ARAYFKGYEK FFGKKINETV DYLSPRDSQG HGTHTASTAA GDMVKNANFL
GQARGTATGM RYTSRIAVYK VCWSSGCTNS DVLAAMDQAV SDGVDVLSLS LGSIPKPFYS
DSIAIASFGA TQKGVLVACS AGNSGPFPST VGNGAPWIMT VAASSTDRTF PTKVKLGNGQ
IFKGSSLYQG KKTTQLPLVY GKSAGATKEA QYCTGGSLDP KLVHGKIVAC ERGINGRTEK
GEEVKMAGGS GMILLNNEYQ GEELFADPHI LPATSLGASA SKIVRSYSES VKKPTASISF
MGTKFRDPAP VMAAFSSRGP SLVGSDVIKP DVTAPGVNIL AAWPPKISPS FLKSDKRKVS
FNILSGTSMS CPHVSGIAAL LKSLHKDWSP AAIKSALMTT AYTLNNKGAP ISDMAYNDSP
LATPFVFGSG HVNPVSASDP GLVYDISTKD YFNYLCNINY TSSQIALLSR SNFVCSRKAF
LQAGDLNYPS FAVLFGRSAF NASVTYRRVV TNVGKSRSSY AVKVEQPNGV SVSVEPRKLK
FEKLGQKLSY NVTFLATGGG KVGGSSSFGS LIWVSDRYKV RSPIAITWQ
//
