ID I1J2W1_BRADI Unreviewed; 747 AA.
AC I1J2W1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KQJ85083.1, ECO:0000313|EnsemblPlants:KQJ85083};
GN Name=100845041 {ECO:0000313|EnsemblPlants:KQJ85083};
GN ORFNames=BRADI_5g24780v3 {ECO:0000313|EMBL:KQJ85083.1};
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|EMBL:KQJ85083.1};
RN [1] {ECO:0000313|EMBL:KQJ85083.1, ECO:0000313|EnsemblPlants:KQJ85083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ85083.1,
RC ECO:0000313|EnsemblPlants:KQJ85083};
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:KQJ85083.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ85083.1};
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:KQJ85083}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ85083};
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}.
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DR EMBL; CM000884; KQJ85083.1; -; Genomic_DNA.
DR RefSeq; XP_003579422.1; XM_003579374.1.
DR AlphaFoldDB; I1J2W1; -.
DR MEROPS; S08.006; -.
DR EnsemblPlants; KQJ85083; KQJ85083; BRADI_5g24780v3.
DR GeneID; 100845041; -.
DR Gramene; KQJ85083; KQJ85083; BRADI_5g24780v3.
DR KEGG; bdi:100845041; -.
DR eggNOG; ENOG502QPQR; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR InParanoid; I1J2W1; -.
DR OMA; WFSHETP; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000008810; Chromosome 5.
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; 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; 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:SF845; SUBTILISIN-LIKE PROTEASE SBT1.9; 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.
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:UP000008810};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..747
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014095701"
FT DOMAIN 31..107
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 132..571
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 369..444
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 639..742
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT REGION 188..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 141
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 526
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 747 AA; 77677 MW; DF924DEDBFFB4180 CRC64;
MGSFKLSMLV SLLPFLLFAL ADAGTGEELS TYIVHVQHQD ENHVFGTADD RKTWYKSFLP
EDGHGRLLHA YHHVASGFAA RLTRRELDAI TAMPGFVAAV PNVFYKVQTT HTPRFLGLDT
PLGGRNVTVG SGDGVIIGVL DTGVFPNHPS FSGAGMPPPP AKWKGRCDFN GSACNNKLIG
AQSFISADPS PRAPPTDEVG HGTHTTSTTA GAVVPGAQVL DQGSGNASGM APRAHVAMYK
VCAGEGCASV DILAGIDAAV SDGCDVISMS LGGPPFPFFQ DSIAIGTFAA AEKGIFVSMA
AGNSGPIPTS LSNEAPWMLT VAASTMDRLI LAQVILGNGS SFDGESVFQP NSTAVVALAY
AGASSTPGAQ FCGNGSLDGF DVKGKIVLCV RGGGVGRVDK GAEVLRAGGA GMIMTNQLLD
GYSTLADAHV LPASHVSYTA GAEIMTYINS TTNPTAQIAF KGTVLGTSPA PAITSFSSRG
PSTQNPGILK PDITGPGVSV LAAWPSQVGP PRFDLRPTYN IISGTSMSTP HLAGIAALIK
SKHPDWSPAA IKSAIMTTAD VNDRSGTPIL NEQHQTADLF AVGAGHVNPE KAMDPGLIYD
IAPAEYIGYL CGMYTDKEVS VIARSPVNCS AVPNISQSQL NYPSIAVTFP ANRSELAPVV
VKRTAKLVGE SPAEYQAVIE VPAGSSVNVT VTPSVLWFSE ASPTQNFLVL VFSWATEASP
APVQASIRWV SDKHTVRSPI SISYTPR
//
