ID I1K3S7_SOYBN Unreviewed; 773 AA.
AC I1K3S7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 24-JAN-2024, entry version 81.
DE RecName: Full=Subtilisin-like protease {ECO:0008006|Google:ProtNLM};
GN Name=100794807 {ECO:0000313|EnsemblPlants:KRH58852};
GN ORFNames=GLYMA_05G152200 {ECO:0000313|EMBL:KRH58852.1};
OS Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH58852.1};
RN [1] {ECO:0000313|EMBL:KRH58852.1, ECO:0000313|EnsemblPlants:KRH58852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH58852};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH58852.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH58852}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH58852};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH58852.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH58852.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; CM000838; KRH58852.1; -; Genomic_DNA.
DR RefSeq; XP_003524185.1; XM_003524137.3.
DR AlphaFoldDB; I1K3S7; -.
DR SMR; I1K3S7; -.
DR MEROPS; S08.119; -.
DR PaxDb; 3847-GLYMA05G28500-1; -.
DR EnsemblPlants; KRH58852; KRH58852; GLYMA_05G152200.
DR GeneID; 100794807; -.
DR Gramene; KRH58852; KRH58852; GLYMA_05G152200.
DR KEGG; gmx:100794807; -.
DR eggNOG; ENOG502QT1T; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR InParanoid; I1K3S7; -.
DR OMA; VYFGAHS; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000008827; Chromosome 5.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
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; 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:SF688; SUBTILISIN-LIKE PROTEASE SBT5.3; 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; SSF52025; PA domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 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:UP000008827};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..773
FT /note="Subtilisin-like protease"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014577481"
FT DOMAIN 30..115
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 143..617
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 402..473
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 671..766
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 152
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 222
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 559
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 773 AA; 83295 MW; B9174B4E9DE2E3C0 CRC64;
MRPPSSSIHF LLQILLVFLL HRPSFALKKS YVVYLGAHSH KPELSSVDFN QVTQSHHEFL
GSFLGSSNTT KDSIFYSYTR HINGFAAILE EEVAAEISKH PKVLSVFENR GRKLHTTRSW
DFMGLEHNGV IQSNSIWKKA RFGEGVIIGN LDTGVWPESK SFSEEGLGPI PSKWRGICHN
GIDHTFHCNR KLIGARYFNK GYASVAGPLN SSFDSPRDNE GHGTHTLSTA GGNMVARVSV
FGQGHGTAKG GSPMARVAAY KVCWPPVAGD ECFDADILAA FDLAIHDGVD VLSLSLGGSA
STFFKDSVAI GSFHAAKHGI VVVCSAGNSG PADATAENLA PWHVTVAAST MDRQFPTYVF
LGNNITFKGE SLSATILAPK FYPIIKATDA KLASARAEDA VLCQNGTLDP NKVKGKIVVC
LRGINARVDK GEQAFLAGAV GMVLANDKTT GNEIIADPHV LPASHINFTD GSAVFTYINS
TKFPVAYITH PKTQLDTKPA PFMAAFSSKG PNTIVPEILK PDITAPGVSV IAAYTEAQGP
TNQVFDKRRI PFNSVSGTSM SCPHVSGIVG LLRALYPTWS PAAIKSAIMT TATTLDNEVE
PLLNATDGKA TPFSYGAGHV QPNRAMDPGL VYDTTIDDYL NFLCALGYNA TQISVFTEGP
YQCRKKFSLL NLNYPSITVP KLSGSVTVTR RLKNVGSPGT YIAHVQNPHG ITISVKPSIL
KFKNVGEEKS FKVTFKAMQG KATNNYVFGK LIWSDGKHYV TSPIVVKALL TRN
//
