ID A0A0D3E6P2_BRAOL Unreviewed; 790 AA.
AC A0A0D3E6P2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Subtilisin-like protease SBT5.6 {ECO:0008006|Google:ProtNLM};
GN Name=106318698 {ECO:0000313|EnsemblPlants:Bo9g062640.1};
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:Bo9g062640.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo9g062640.1, 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:Bo9g062640.1}
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}.
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DR RefSeq; XP_013612248.1; XM_013756794.1.
DR AlphaFoldDB; A0A0D3E6P2; -.
DR STRING; 109376.A0A0D3E6P2; -.
DR EnsemblPlants; Bo9g062640.1; Bo9g062640.1; Bo9g062640.
DR GeneID; 106318698; -.
DR Gramene; Bo9g062640.1; Bo9g062640.1; Bo9g062640.
DR KEGG; boe:106318698; -.
DR eggNOG; ENOG502QRC5; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR OMA; EEHHHSY; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000032141; Chromosome C9.
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; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR PANTHER; PTHR10795:SF562; SUBTILISIN-LIKE PROTEASE SBT5.5-RELATED; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51892; SUBTILASE; 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 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..790
FT /note="Subtilisin-like protease SBT5.6"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002260334"
FT DOMAIN 25..103
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 151..617
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 401..491
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 685..787
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
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 235
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 578
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 790 AA; 85246 MW; C867E190317B60B3 CRC64;
MKLTSLVPLL FLVPLLTSCS EQKQVYIVYF GEHKGDKALH EIEEHHHSYL QSVKESEEEA
KSSLLYSYKH SINGFAAELT PDEASKLEKM EEVISVIESH PRKYETHTTR SWEFVGLKEE
ETDGDEVQRP KNDVDDRFRV GRKFLKQAKH GNGIIVGVLD SGVWPESKSF SDKGMGPVPE
SWKGICQTGI AFNSSHCNRK IIGARYYVKG YEKYYGAFNV TANRDFLSPR DPDGHGSHTA
STAVGRRVKG ASALGGFAMG SASGGAPLAR LAVYKACWAK PNQEKVDGNV CLQEDMLAAI
DDAIGDGVHV ISVSIGTTDP LPYSQDGIAI GALHAVKRNI VVAASAGNSG PKPGTLSNPA
PWIITVGAST LDRAFVGGLV LGNGYTVKTE SITAFKMDKF APLVYAANVA VPGIALNNTS
QCLPNSLKPE LVNGKVVLCL RGAGSRIGKG MEVKRAGGVG MILGNSLANG NEIPSDSHFV
ATAAVTPTVV EKILDYIKID KNPIAFIKPG TTVYKNQPAP LMTGFSSRGP NVVDPNILKP
DITAPGLNIL AAWSGADSPS KLWVDQRVAD YNIYTGTSMS CPHVSGAIAL LKAIHPKWSS
AAIRSALMTT AWMTNDEKKP IQDISGLPAN PFALGSGHFR PTKAADPGLV YDASYRAYLL
YGCSVGFTNI DPTFKCPSKI PPGYNLNYPS ISIPNLNRTV TVKRTVTNVG NGNSTSTYIF
SARSPLGVSV KAKPSVLSFN RIGQKKRFKI MVTVRMDKMN VTEKGQYQFG WFSWTDKYHV
VRSPIAISLA
//
