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Database: UniProt
Entry: A0A445HYW0_GLYSO
LinkDB: A0A445HYW0_GLYSO
Original site: A0A445HYW0_GLYSO 
ID   A0A445HYW0_GLYSO        Unreviewed;       762 AA.
AC   A0A445HYW0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Subtilisin-like protease SBT5.3 {ECO:0000313|EMBL:RZB79010.1};
GN   ORFNames=D0Y65_029395 {ECO:0000313|EMBL:RZB79010.1};
OS   Glycine soja (Wild soybean).
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=3848 {ECO:0000313|EMBL:RZB79010.1, ECO:0000313|Proteomes:UP000289340};
RN   [1] {ECO:0000313|EMBL:RZB79010.1, ECO:0000313|Proteomes:UP000289340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC   TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZB79010.1};
RA   Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT   "A high-quality reference genome of wild soybean provides a powerful tool
RT   to mine soybean genomes.";
RL   Submitted (SEP-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RZB79010.1}.
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DR   EMBL; QZWG01000011; RZB79010.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445HYW0; -.
DR   SMR; A0A445HYW0; -.
DR   OrthoDB; 11910at2759; -.
DR   Proteomes; UP000289340; 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; 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:SF382; OS06G0624100 PROTEIN; 1.
DR   PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 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; 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:UP000289340};
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..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..762
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019190944"
FT   DOMAIN          32..112
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          139..579
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          402..467
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          657..751
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        219
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        543
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   762 AA;  81876 MW;  BD434CE52BD4BA2F CRC64;
     MSCSNYARSC TFFYLFLAVL LAKTSSCFSA KVYVVYMGSK TGEDPDDILK HNHQMLASVH
     SGSIEQAQAS HVYSYKHAFR GFAAKLTNEQ AYQISKMPGV VSVFPNAKRK LHTTHSWDFI
     GLLGNESMEI HGHSTKNQEN IIIGFIDTGI WPESSSFSDT DMPPVPRGWK GHCQLGEAFN
     ASSCNRKVIG ARYYISGHEA EEESDREVSF ISARDSSGHG SHTASTAAGR YVANMNYKGL
     AAGGARGGAP KARIAVYKVC WDSGCYDVDL LAAFDDAIRD GVHIISLSLG PESPQGDYFS
     DAVSVASFHA AKHRVLVVAS VGNQGNPGSA TNVAPWIITV AASSIDRNFT SDITLGNGVN
     ITGESLSLLG MDASRRLIDA SEAFSGYFTP YQSSYCVDSS LNKTKAKGKV LVCRHAEYSG
     ESKLEKSKIV KKAGGVGMIL IDEANQGVST PFVIPSAVVG TKTGERILSY INSTRMPMSR
     ISKAKTVLGV QPAPRVAAFS SKGPNALTPE ILKPDVTAPG LNILAAWSPA SAGMKFNIIS
     GTSMSCPHIT GIATLVKAVH PSWSPSAIKS AIMTTATILD KHHQPIRADP DRRRANAFDY
     GSGFVNPSRV LDPGLVYDSH PEDFVAFLCS LGYDERSLHL VTGDNSTCDR AFKTPSDLNY
     PSIAVPNLED NFSVTRVVTN VGKARSIYKA VVVSPAGVNV TVVPNRLVFT RIGEKIKFTV
     NFKVVAPSKD YAFGFLSWKN GRTQVTSPLV IKVAPASHGL VR
//
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