ID A0A0D3E3G2_BRAOL Unreviewed; 815 AA.
AC A0A0D3E3G2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:Bo9g027580.1};
GN Name=106318247 {ECO:0000313|EnsemblPlants:Bo9g027580.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo9g027580.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo9g027580.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo9g027580.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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 RefSeq; XP_013611593.1; XM_013756139.1.
DR RefSeq; XP_013611594.1; XM_013756140.1.
DR RefSeq; XP_013611595.1; XM_013756141.1.
DR RefSeq; XP_013611597.1; XM_013756143.1.
DR RefSeq; XP_013611598.1; XM_013756144.1.
DR RefSeq; XP_013611599.1; XM_013756145.1.
DR AlphaFoldDB; A0A0D3E3G2; -.
DR STRING; 109376.A0A0D3E3G2; -.
DR EnsemblPlants; Bo9g027580.1; Bo9g027580.1; Bo9g027580.
DR GeneID; 106318247; -.
DR Gramene; Bo9g027580.1; Bo9g027580.1; Bo9g027580.
DR KEGG; boe:106318247; -.
DR eggNOG; ENOG502QS8I; Eukaryota.
DR HOGENOM; CLU_000625_3_1_1; -.
DR OMA; NTPCNYD; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000032141; Chromosome C9.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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; IPR010435; Fn3_5.
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 PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR PANTHER; PTHR10795:SF722; SUBTILISIN-LIKE PROTEASE SBT2.5; 1.
DR Pfam; PF06280; fn3_5; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 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:UP000032141};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..815
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002260295"
FT DOMAIN 22..124
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 151..633
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 409..490
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 699..809
FT /note="Fn3-like"
FT /evidence="ECO:0000259|Pfam:PF06280"
FT ACT_SITE 160
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 234
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 596
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 815 AA; 87877 MW; 6520452E62097F2A CRC64;
MDMGMIFFVV SALLVTVTAD VYIVTIEGDP IISYKGGENG YEATAVESDE KIDTSSELVT
SYARHLERKH DMILGMLFEE GSYKKLYSYK HLINGFAVHV SPEQAETLRR TPGIKSVNKD
WKVRRLTTHT PEFLGLPTDV WPTGGGFERA GEDIVIGFVD SGIYPHHPSF ASHHRLPYGP
LHHYKGKCEE DPHTKKSFCN RKIVGAQHFA EAAKAAGAFN PNIDYASPMD GDGHGSHTAA
IAAGNNGIPL RMHGYEFGRA SGMAPRARIA VYKALYRLFG GFVADVVAAI DQAVHDGVDI
LSLSVGPNSP PTTTKTTFLN PFDATLLGAV KAGVFVAQAA GNGGPFPKTL VSYSPWITTV
AAAIDDRRYK NHLTLGNGKM LAGLGLSPST RPHRLYTLVS ANDVLLDSSA SKYNPSDCQR
PEVFNKKLVE GKILLCGYSF NFVVGTASIK KVVATVKHLG AAGFVLVVEN VSPGTKFDPV
PSAVPGILIT DVSKSMDLID YYNVSTTRDW TGRVKSFKAE GSIGDGLAPV YHKSAPQVAL
FSARGPNTKD FSFQDADLLK PDILAPGYLI WAAWCPNGTD EPNYVGEGFA LISGTSMAAP
HIAGIAALVK QKYPQWSPAA IKSALMTTST VIDRAGRLLQ AQQYSDTEAV TLVKATPFDY
GSGHVNPHAA LDPGLVFDAG YEDYLGFLCT TPGIDAHEIR NYTNTPCNYD MKHPSNFNAA
SIAISHLVGT QTVTRRVTNV AEVEETYTIT ARMQPSTAIE VNPPAMTLRP GASRIFSVTL
TVRSVSGVYS FGEVKLKGSR GHKVRIPVVA LGHRH
//
