ID A0A077RSI8_WHEAT Unreviewed; 749 AA.
AC A0A077RSI8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Subtilisin-like protease {ECO:0008006|Google:ProtNLM};
GN ORFNames=TRAES_3BF035300160CFD_c1 {ECO:0000313|EMBL:CDM80022.1},
GN TRAES_3BF035600020CFD_c1 {ECO:0000313|EMBL:CDM83040.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EMBL:CDM83040.1};
RN [1] {ECO:0000313|EMBL:CDM83040.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25035497; DOI=10.1126/science.1249721;
RA Choulet F., Alberti A., Theil S., Glover N., Barbe V., Daron J.,
RA Pingault L., Sourdille P., Couloux A., Paux E., Leroy P., Mangenot S.,
RA Guilhot N., Le Gouis J., Balfourier F., Alaux M., Jamilloux V., Poulain J.,
RA Durand C., Bellec A., Gaspin C., Safar J., Dolezel J., Rogers J.,
RA Vandepoele K., Aury J.M., Mayer K., Berges H., Quesneville H., Wincker P.,
RA Feuillet C.;
RT "Structural and functional partitioning of bread wheat chromosome 3B.";
RL Science 345:1249721-1249721(2014).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; HG670306; CDM80022.1; -; Genomic_DNA.
DR EMBL; HG670306; CDM83040.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077RSI8; -.
DR HOGENOM; CLU_000625_4_2_1; -.
DR ExpressionAtlas; A0A077RSI8; baseline and differential.
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:SF695; PEPTIDASE_S8 DOMAIN-CONTAINING 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};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..749
FT /note="Subtilisin-like protease"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008819319"
FT DOMAIN 36..112
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 142..571
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 643..736
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 151
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 220
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 535
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 749 AA; 79860 MW; A2554E77FDC368D0 CRC64;
MGFSSSSRRS RVASVLQLCL CMLLCRVQGG SSHGLYIVYL GEVKHGHPNH VVASHHDMLT
TLLGSKEESM ASVAYNYKHG FSGFAAMLTP EQAKQLAEVP EVISVEKNKI HTTATTRSWD
FLGLNYQMTS TSNGLLKGSK YGEDVIIGVV DTGIWPESRS FSDEGYGPIP SRWKGKCQLG
PDWGSNNCSR KIIGARFYTA GVSDVLLKMD TLSPRDNNGH GTHCASTSAG SIVEAASFNG
LAEGVARGGA PRARIAVYKS GWGSGSFSIA SVLAAIDDAI HDGVDVLSLS ITGEEQLAFG
ALHAVQKGIT VVYIAGNDGP RPQTVVNISP WVITVAASKV DRSFPTVITL GNKQQIVGQS
LYYQAKNSSG SSFAGLLVGA GCTADRLNGT DVRGIILFCL PLKDDAGTPV STFDYASQYV
RSGGGCGLIF AQYTTDLLTM TASVACQGIA CVLVDLDTGE KIRKYGGVAG SSAVAKIEPA
HIVAGKEIPG PKVAAFSSRG PSRHYPDIIK PDIAAPGANI LAAVGNSYEF KDGTSMAAPH
VSGIVALLKA EHPHWSPAAI KSAIMTTARV TDNRGMPILA EGLPRKIADP FDYGGGNINP
TGAADPGLVY DIDPRDYNKF FRCTIVRRTN ASCDATMLPA YHLNLPSIAV SELRRPITVW
RTVTNVGEAD SVYHAEVQCP AGVMMEVEPT VLVFNATDRV HSFKVKLAPM WRLQGDYTFG
SITWRKDQKT VRIPVAARMT IQDFYADVA
//
