ID I1IEK3_BRADI Unreviewed; 780 AA.
AC I1IEK3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Subtilisin-like protease {ECO:0008006|Google:ProtNLM};
GN Name=100838394 {ECO:0000313|EnsemblPlants:KQK01622};
GN ORFNames=BRADI_3g57130v3 {ECO:0000313|EMBL:KQK01622.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EnsemblPlants:KQK01622};
RN [1] {ECO:0000313|EMBL:KQK01622.1, ECO:0000313|EnsemblPlants:KQK01622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK01622.1,
RC ECO:0000313|EnsemblPlants:KQK01622};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQK01622.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK01622.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQK01622}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK01622};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM000882; KQK01622.1; -; Genomic_DNA.
DR RefSeq; XP_003570499.1; XM_003570451.3.
DR AlphaFoldDB; I1IEK3; -.
DR MEROPS; S08.A28; -.
DR EnsemblPlants; KQK01622; KQK01622; BRADI_3g57130v3.
DR GeneID; 100838394; -.
DR Gramene; KQK01622; KQK01622; BRADI_3g57130v3.
DR KEGG; bdi:100838394; -.
DR eggNOG; ENOG502QZDA; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR InParanoid; I1IEK3; -.
DR OMA; WTPAMIM; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000008810; Chromosome 3.
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; 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:SF406; OS02G0779900 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:UP000008810};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..780
FT /note="Subtilisin-like protease"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014095218"
FT DOMAIN 36..120
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 145..587
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 379..464
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 666..768
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 153
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 221
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 550
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 780 AA; 81102 MW; 2E036E28255A79A7 CRC64;
MEPRPLAALC VVLALVVAAA AAVPAEELET AEAMSSYIVH VAPGHAPKLP RRGLHTTRAY
ASFLRAHIPV EMMSSAKPKV LYSYSHAAAG FAARLTSRQA EHLASVSSVL AVVPDTMHER
HTTLTPSFLG LSESSGLLQA SNGATNVVIG VIDTGIYPID RASFAADPSL PPPPSKFNGS
CVSTPSFNGS AYCNNKLVGA KFFSKGQRFP PDDSPLDTNG HGTHTASTAA GSAVAGAAFF
DYARGKAVGV APGARIAAYK ACWEAGCASI DILAAFDEAI ADGVDVISVS LGAVGQAPEF
YDDLTAVGAF SAVRKGIVVS ASAGNAGPGE KTAVNIAPWI LTVGASTINR VFPADAVLGN
GETFTGTSLY AGKPLGSAKL PLVYGGDVGS NVCEAQKLNA TKVAGKIVLC DPGVNGRAEK
GEAVKLAGGA GAILASTEAF GEQAISSPHI IAATAVPFAA AKKIKKYISM QKSPVATIIF
RGTVVGGSPP SPRMASFSSR GPNIHAPEIL KPDVTAPGVD ILAAWTGANS PTELESDKRR
VKFNIISGTS MSCPHVSGIA ALLRQARPKW SPAMIKSALM TTAYNMDNSG SIIGDMSTGK
ASTPFARGAG HVDPNRAVDP GLVYDADTDD YVTFLCALGY TDEQVAIMTR DATSCSTRNM
GAAVGDHNYP AFAATFTINK FAVIKQRRTV RNVGSNARAT YSAKVTSPAG TRVTVKPETL
RFSETKEMLE YEVTFAQRMF DIVTDKHTFG SIEWSDGGEH KVTSPIAITW PALATQLSEM
//
