ID A0A0D3AVM8_BRAOL Unreviewed; 729 AA.
AC A0A0D3AVM8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Subtilisin-like protease {ECO:0008006|Google:ProtNLM};
GN Name=106322888 {ECO:0000313|EnsemblPlants:Bo2g136770.1};
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:Bo2g136770.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo2g136770.1, 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:Bo2g136770.1}
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}.
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 RefSeq; XP_013616490.1; XM_013761036.1.
DR AlphaFoldDB; A0A0D3AVM8; -.
DR STRING; 109376.A0A0D3AVM8; -.
DR EnsemblPlants; Bo2g136770.1; Bo2g136770.1; Bo2g136770.
DR GeneID; 106322888; -.
DR Gramene; Bo2g136770.1; Bo2g136770.1; Bo2g136770.
DR KEGG; boe:106322888; -.
DR eggNOG; ENOG502QT5U; Eukaryota.
DR HOGENOM; CLU_000625_3_1_1; -.
DR OMA; INFLCHE; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000032141; Chromosome C2.
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; 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:SF402; SUBTILISIN-LIKE PROTEASE SBT1.9; 1.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
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 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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..729
FT /note="Subtilisin-like protease"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002257283"
FT DOMAIN 25..101
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 124..557
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 622..721
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 133
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 205
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 522
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 729 AA; 78748 MW; 8B52AFE616A640BA CRC64;
MAFTVMILFL IPFSITTATT ETSIYIIHMD LSAKPTPFTD HQSWFSTTLT SVTTGRKPKI
LYAYTDSVHG FSAVLTNSEL KRLQHKPGYV SFTKDLPVKL HTTFSPQFIG LASNSGTWPV
SSYGAGTVIG IVDTGIWPDH PSFHDDGLGS LPSTWKGKCE FNYSSLCNKK LIGARVFNKG
LFANNPDLRG TKKDQYSSPY DTIGHGTHVA AIAAGNRVKN ASYFSYAQGT ASGIAPYAHI
AMYKAAWEEG VYSSDVIAAI DQAVRDGVDV ISLSLGLSID DDDGDDVGLE NDPIAVAAFA
AIQKGVFVVA SGGNDGPYYW SLINGAPWVM TVGAGTIGRE FQGILTLGNG VSFSFPSLFP
GEFPSVQFPV TYVESCDAGN KTLVSRIIVC NGNIQQARST GATAVVIITD RLLAEQDTVK
FQFPVAFISS KHGEAIKSYA SSYSNNATAK LEFRKTVIGT KPAPEVDSYS SRGPFASFPQ
ILKPDILAPG SLVLSAWPPS KPVAGTRARP LFSGFNLLTG TSMASPHVAG VAALIKHVHQ
DWSPSAIKSA IMTTALTLNN PLAVGAGHVR ADRVLSPGLI YDTSPQDFIN FLCHEVKQSR
KLINIITRSN ASDACRHPSP YLNYPSIIAY FTSDQNGPKI VRRTLTNVRE AKRSYSVRVR
GLKGINVVIE PTRVMFSKKN EKQSYTVRLE SQRALRGDVV YGVVSWVDDE DAKFEVSCPV
VATSLVQES
//
