ID A0A0D3ADS4_BRAOL Unreviewed; 775 AA.
AC A0A0D3ADS4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Subtilisin-like protease {ECO:0008006|Google:ProtNLM};
GN Name=106317378 {ECO:0000313|EnsemblPlants:Bo1g134630.1};
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:Bo1g134630.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo1g134630.1, 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:Bo1g134630.1}
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_013610663.1; XM_013755209.1.
DR AlphaFoldDB; A0A0D3ADS4; -.
DR STRING; 109376.A0A0D3ADS4; -.
DR MEROPS; S08.A28; -.
DR EnsemblPlants; Bo1g134630.1; Bo1g134630.1; Bo1g134630.
DR GeneID; 106317378; -.
DR Gramene; Bo1g134630.1; Bo1g134630.1; Bo1g134630.
DR KEGG; boe:106317378; -.
DR eggNOG; ENOG502QZDA; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR OMA; TGIWSER; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000032141; Chromosome C1.
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; 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:SF780; SUBTILISIN-LIKE PROTEASE SBT1.4; 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; 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 Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..775
FT /note="Subtilisin-like protease"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002256892"
FT DOMAIN 32..110
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 133..588
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 375..458
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 662..765
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT REGION 200..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 215
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 544
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 775 AA; 81668 MW; 16F76B4792D7E8A9 CRC64;
MAAKLSLSSV LIVLSLFLCF SSSSSSWDGL ESYIVHVQGS HKPSLFFSHK HWHNSLLRSL
PSSPQPATLL YSYSRAVHGF SARLSPSQTS ALRRHPSVIS VIPDQAREIH TTHTPAFLGF
SDNSGLWSNS NYGEDVIVGV LDTGIWPEHP SFSDSGLDPV PSTWKGACEI GPDFPASSCN
RKLIGARAFY KGYLTHRNGS KHAEESKSPR DTAGHGTHTA STAAGSVVVN ASLYQYAQGV
ARGMASKARI AAYKICWTGG CYDSDILAAM DQAVADGVHV ISLSVGANGF APEYHKDSIA
IGAFGAMRHG IVVSCSAGNS GPGPQTATNI APWILTVGAS TVDREFTANA ITGNGKVFTG
TSLYAGEPLP DSQISLVYSG DCGSRLCYPG KLNSSLVEGK IVLCDRGGNA RVEKGSAVKI
AGGAGMILAN TAESGEELTA DSHLVPATMV GAKAGDQIRD YIQKSNSPTA TISFLGTLIG
PSPPSPRVAA FSSRGPNHIT PVILKPDVIA PGVNILAGWT GMVGPTDLDI DPRRVKFNII
SGTSMSCPHV SGLAALLRKA HPDWSPAAIK SALVTTAYDT ENSGEPIEDL ATGESSNSFI
HGAGHVDPNK ALNPGLVYDV DAKEYVAFLC AVGYEFPGIL VFLQDPSLYD ACETSKLRTA
GDLNYPSFSV VFGSNDGVVK YRRVIKNVGS NVDAVYEVGV KAPANVEIDV SPSKLTFSKE
TREMEYEVTF KSVVLGGGVG SVPGHEFGSI EWTDGEHVVK SPVAVQWSQG SVQSF
//
