ID I1M0I4_SOYBN Unreviewed; 778 AA.
AC I1M0I4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Subtilisin-like protease {ECO:0008006|Google:ProtNLM};
GN Name=100809885 {ECO:0000313|EnsemblPlants:KRH20579};
GN ORFNames=GLYMA_13G187000 {ECO:0000313|EMBL:KRH20579.1};
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:KRH20579.1};
RN [1] {ECO:0000313|EMBL:KRH20579.1, ECO:0000313|EnsemblPlants:KRH20579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH20579};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH20579.1};
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:KRH20579}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH20579};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH20579.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH20579.1};
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; CM000846; KRH20579.1; -; Genomic_DNA.
DR RefSeq; XP_003541562.1; XM_003541514.3.
DR AlphaFoldDB; I1M0I4; -.
DR SMR; I1M0I4; -.
DR MEROPS; S08.104; -.
DR PaxDb; 3847-GLYMA13G25650-1; -.
DR EnsemblPlants; KRH20579; KRH20579; GLYMA_13G187000.
DR GeneID; 100809885; -.
DR Gramene; KRH20579; KRH20579; GLYMA_13G187000.
DR KEGG; gmx:100809885; -.
DR eggNOG; ENOG502QU9V; Eukaryota.
DR HOGENOM; CLU_000625_4_4_1; -.
DR InParanoid; I1M0I4; -.
DR OMA; PDHTTTR; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000008827; Chromosome 13.
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:SF549; OS01G0278950 PROTEIN; 1.
DR PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 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: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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..778
FT /note="Subtilisin-like protease"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014578651"
FT DOMAIN 31..113
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 145..600
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 679..775
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 225
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 563
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 778 AA; 83928 MW; CCE837B86292EA88 CRC64;
MEGLQKFLHF FFVASLLIST TAISDHTPKP YVVYMGNSSP NKIGVESQIA ESSHLQLLSL
IIPSEESERI ALTHHFSHAF SGFSAMLTES EASALSGHDG VVSVFPDPVL ELHTTRSWDF
LESELGMKPY YSHGTPTLHK HPSTDIIIGV IDTGIWPESP SFRDEGIGEI PSKWKGVCME
GRDFKKSNCN RKLIGARYYK IQATSGDNQT HIEAAKGSPR DTVGHGTHTA SIAAGVHVNN
ASYFGLAKGT ARGGSPSTRI AAYKTCSDEG CSGATILKAI DDAVKDGVDI ISISIGLSSL
FQSDFLSDPI AIGAFHAEQK GVLVVCSAGN DGPDPFTVVN SAPWIFTIAA SNIDRNFQST
IVLGNGKYLQ GTGINFSNLT HSKMHRLVFG EQVAAKFVPA SEARNCFPGS LDFNKTAGNI
VVCVNDDPSV SRRIKKLVVQ DARAVGIILI NENNKDAPFD AGVFPFTQVG NLEGHQILKY
INSTKNPTAT ILPTTEVARS KPSPIVASFS SRGPSSLTEN ILKPDVMAPG VGILAAVIPK
SKEPGSVPIG KKPSLYAIKS GTSMACPHVT GAAAFIKSVH KKWSSSMIKS ALMTTATNYN
NMRKPLTNSS NSIAGPHEMG VGEINPLRAL NPGLVFETDV EDYLRFLCYF GYSQKIIRSI
SETNFNCPKN SSEDLISSVN YPSISISTLK RQQKAKVITR TVTNVGYLNA TYTAKVRAPQ
GLVVEVIPNK LVFSEGVQRM TYKVSFYGKE AHGGYNFGSL TWLDGHHYVH TVFAVKVE
//
