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Database: UniProt
Entry: A0A3B6EMZ2_WHEAT
LinkDB: A0A3B6EMZ2_WHEAT
Original site: A0A3B6EMZ2_WHEAT 
ID   A0A3B6EMZ2_WHEAT        Unreviewed;       777 AA.
AC   A0A3B6EMZ2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Subtilisin-like protease {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CFC21_037527 {ECO:0000313|EMBL:KAF7025331.1};
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|EnsemblPlants:TraesCS3A02G420500.1.cds1};
RN   [1] {ECO:0000313|EMBL:KAF7025331.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7025331.1};
RX   PubMed=29069494;
RA   Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT   "The first near-complete assembly of the hexaploid bread wheat genome,
RT   Triticum aestivum.";
RL   Gigascience 6:1-7(2017).
RN   [2] {ECO:0000313|EnsemblPlants:TraesCS3A02G420500.1.cds1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS3A02G420500.1.cds1};
RX   PubMed=30115783; DOI=10.1126/science.aar7191;
RG   International wheat genome sequencing consortium (IWGSC);
RT   "Shifting the limits in wheat research and breeding using a fully annotated
RT   reference genome.";
RL   Science 361:EAAR7191-EAAR7191(2018).
RN   [3] {ECO:0000313|EnsemblPlants:TraesCS3A02G420500.1.cds1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) to UniProtKB.
RN   [4] {ECO:0000313|EMBL:KAF7025331.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7025331.1};
RA   Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT   "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT   aestivum) genome.";
RL   Submitted (MAR-2020) 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       ECO:0000256|RuleBase:RU003355}.
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DR   EMBL; CM022217; KAF7025331.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B6EMZ2; -.
DR   SMR; A0A3B6EMZ2; -.
DR   STRING; 4565.A0A3B6EMZ2; -.
DR   EnsemblPlants; TraesCS3A02G420500.1; TraesCS3A02G420500.1.cds1; TraesCS3A02G420500.
DR   Gramene; TraesCAD_scaffold_052207_01G000100.1; TraesCAD_scaffold_052207_01G000100.1; TraesCAD_scaffold_052207_01G000100.
DR   Gramene; TraesCLE_scaffold_040444_01G000400.1; TraesCLE_scaffold_040444_01G000400.1; TraesCLE_scaffold_040444_01G000400.
DR   Gramene; TraesCS3A02G420500.1; TraesCS3A02G420500.1.cds1; TraesCS3A02G420500.
DR   Gramene; TraesCS3A03G0975800.1; TraesCS3A03G0975800.1.CDS1; TraesCS3A03G0975800.
DR   Gramene; TraesKAR3A01G0407710.1; cds.TraesKAR3A01G0407710.1; TraesKAR3A01G0407710.
DR   Gramene; TraesPAR_scaffold_113168_01G000100.1; TraesPAR_scaffold_113168_01G000100.1; TraesPAR_scaffold_113168_01G000100.
DR   Gramene; TraesROB_scaffold_069948_01G000100.1; TraesROB_scaffold_069948_01G000100.1; TraesROB_scaffold_069948_01G000100.
DR   Gramene; TraesWEE_scaffold_028704_01G000100.1; TraesWEE_scaffold_028704_01G000100.1; TraesWEE_scaffold_028704_01G000100.
DR   OMA; DFPETAC; -.
DR   OrthoDB; 11910at2759; -.
DR   Proteomes; UP000019116; Chromosome 3A.
DR   Proteomes; UP000815260; Chromosome 3A.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0016485; P:protein processing; IBA:GO_Central.
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; IPR023827; Peptidase_S8_Asp-AS.
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:SF542; SUBTILISIN-LIKE PROTEASE SBT1.5; 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; PS00136; SUBTILASE_ASP; 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:UP000019116};
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..777
FT                   /note="Subtilisin-like protease"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039990624"
FT   DOMAIN          27..106
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          134..597
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          374..460
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          664..770
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        143
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        216
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        548
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   777 AA;  79705 MW;  9BE42D1F6D56C930 CRC64;
     MPRHLLLPLL LVAAVGASGG DAGGERTYIV RVDADAKPSA FPTHAHWYES AVLAASGGGG
     GWPEGGPLIH TYSSALHGFS ARMSPSAAAA LAGARGVAAV LPERVRCLDT TRSPRFLGML
     SSPPSAILAD SDFGSDLVIA VIDTGISPAH RSFRDRGLGP VPPRWRGACA SGPGFPPGSC
     NRKLVGARFF SAGYEATSGR MNETAEVRSP LDNDGHGTHT ASIAAGRYVF PASTLGYARG
     VASGMAPKAR LAAYKVCWAG GCFDSDILAA FDAAVADGVD VVSLSVGGAV VPYYLDAIAI
     GAFGATEAGI VVSASAGNGG PGGLSVTNVA PWMTTVGAGS MDRAFPANVR LGNGQVLDGV
     SVYGGPVLQS GKMYELVYAG ATSYSASTCL DGSLDQAAVR GKIVVCDRGV NSRAAKGDVV
     HRAGAAGMVL ANGAFDGEGL VADCHVLPAT AVGAAAGEKL RKYIASSTPQ KPATGTIVFE
     GTHLGVHPAP VVAAFSARGP NPQSPETLKP DLIAPGLNIL AAWPSGVGPA GIPSDGRRTE
     FNILSGTSMA CPHVSGLAAL LKAAHPTWSP AAIKSALMTT AYTRDNSNGT MLDESTGKVA
     DVFDFGAGHV DPMRAMDPGL VYDIAPADYV SFLCNLNYTG QNIRAITRRQ ADCRGARRAG
     HAGNLNYPSL SVTFVADGAR AKMRTHFIRT VTNVGGGRSA YRATVRSPEG CNVTVRPDRL
     AFRRDGQKLS FTVHVEAAAR ARMEPGSSLV RSGALTWGDG RHAVVSPIVV TLQAPVQ
//
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