ID A0A445K4N1_GLYSO Unreviewed; 769 AA.
AC A0A445K4N1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Subtilisin-like protease SBT1.7 {ECO:0000313|EMBL:RZC05773.1};
GN ORFNames=D0Y65_013730 {ECO:0000313|EMBL:RZC05773.1};
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:RZC05773.1, ECO:0000313|Proteomes:UP000289340};
RN [1] {ECO:0000313|EMBL:RZC05773.1, 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:RZC05773.1};
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:RZC05773.1}.
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DR EMBL; QZWG01000006; RZC05773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A445K4N1; -.
DR SMR; A0A445K4N1; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000289340; Chromosome 6.
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; 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:SF388; XYLEM SERINE PROTEINASE 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; 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: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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..769
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018977635"
FT DOMAIN 38..113
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 137..591
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 376..462
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 662..765
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT REGION 203..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 218
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 547
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 769 AA; 82511 MW; 9E92866DEA4CD0F3 CRC64;
MVDKMNMLIF KSLVISWLLV FSSRHTTAEK KTHHTKNTYI IHMDKFNMPE SFNDHLHWYD
SSLKSVSDSA ERLYTYKKVA HGFSTRLTTQ EAELLSKQPG VLSVIPEVRY ELHTTRTPEF
LGLAKYTTLS LASGKQSDVI VGVLDTGVWP ELKSFDDTGL EPVPSSWKGE CERGKNFKPS
NCNKKLVGAR FFSRGYEAAF GPIDEKTESK SPRDDDGHGS HTSTTAAGSA VFGASLFGFA
NGTARGMATQ ARVATYKVCW LGGCFTSDIA AGIDKAIEDG VNILSMSIGG GLTDYYKDTI
AIGTFAATAH GILVSNSAGN GGPSQATLSN VAPWLTTVGA GTIDRDFPAY ITLGNGKIYT
GVSLYNGKLP LNSPLPIVYA GNASEESQNL CTRGSLIAKK VAGKIVICDR GGNARVEKGL
VVKSAGGIGM ILSNNEDYGE ELVADSYLLP AAALGQKSSN ELKKYVFSFP NPTAKLGFGG
TQLGVQPSPV VAAFSSRGPN VLTPKILKPD LIAPGVNILA GWTGAVGPTG LAEDTRHVDF
NIISGTSMSC PHVTGLAALL KGIHPEWSPA AIRSALMTTA YRTYKNGQTI KDVATGLPAT
PFDYGAGHVD PVAAFDPGLV YDTTVDDYLS FFCALNYSPY QIKLVARRDF TCSKRKKYRV
EDLNYPSFAV PFNTAYGVKG GSSKPATVQY TRTLTNVGAA GTYKVSVSQS PVKIVVQPQT
LSFRGLNEKK NYTVTFMSSS KPSGTTSFAY LEWSDGKHKV TSPIAFSWT
//
