ID A0A1U8EHF8_CAPAN Unreviewed; 761 AA.
AC A0A1U8EHF8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Subtilisin-like protease SBT1.6 {ECO:0000313|EMBL:PHT83271.1};
GN ORFNames=T459_11714 {ECO:0000313|EMBL:PHT83271.1};
OS Capsicum annuum (Capsicum pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4072 {ECO:0000313|EMBL:PHT83271.1, ECO:0000313|Proteomes:UP000222542};
RN [1] {ECO:0000313|EMBL:PHT83271.1, ECO:0000313|Proteomes:UP000222542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CM334 {ECO:0000313|Proteomes:UP000222542};
RX PubMed=29089032; DOI=10.1186/s13059-017-1341-9;
RA Kim S., Park J., Yeom S.I., Kim Y.M., Seo E., Kim K.T., Kim M.S., Lee J.M.,
RA Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M., Lee H.A.,
RA Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E., Jeon J.,
RA Kim H., Choi G., Song H., Lee J., Lee S.C., Kwon J.K., Lee H.Y., Koo N.,
RA Hong Y., Kim R.W., Kang W.H., Huh J.H., Kang B.C., Yang T.J., Lee Y.H.,
RA Bennetzen J.L., Choi D.;
RT "New reference genome sequences of hot pepper reveal the massive evolution
RT of plant disease-resistance genes by retroduplication.";
RL Genome Biol. 18:R210.1-R210.11(2017).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PHT83271.1}.
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DR EMBL; AYRZ02000004; PHT83271.1; -; Genomic_DNA.
DR RefSeq; XP_016543329.1; XM_016687843.1.
DR AlphaFoldDB; A0A1U8EHF8; -.
DR EnsemblPlants; PHT83271; PHT83271; T459_11714.
DR GeneID; 107843528; -.
DR Gramene; PHT83271; PHT83271; T459_11714.
DR KEGG; cann:107843528; -.
DR OMA; PESNAMG; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000222542; Chromosome 4.
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; 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:SF657; SUBTILISIN-LIKE PROTEASE; 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; 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:UP000222542};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..761
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030035266"
FT DOMAIN 28..103
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 128..579
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 380..453
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 653..758
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 135
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 208
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 538
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 761 AA; 80458 MW; 9E3F8DDE5212B66A CRC64;
MSSSIVFQVI ALLALCHVTL QSTSEESTFI IHMAKSQMPD SFDDHTHWYS SSLKSVSESA
EMLYVYNNAV HGYAARLTKK EAESIQKQRG ILSVMPEMKY ELHTTRTPLF LGLDRSADFF
PESNAMGDVI VGVLDTGVWP ESKSFDDSGF GPIPASWKGE CESGTNFSSK NCNRKLIGAR
YFAKGYESTM GLIDETKESK SPRDDDGHGT HTSTTAAGSV VQGASLFGFA SGSARGMATH
ARVAVYKVCW IGGCFSSDIL AALDKAIDDN VNVLSLSLGG GNSDYYRDSV AIGAFAAMEK
GILVSCSAGN SGPSPYSLSN VAPWITTVGA GTLDRDFPAY LSLGNGKNFS GVSLYKGPMS
LSKMLPFVYA GNASNSTNGN LCMMGTLIPE QVKGKIVLCD RGLNPRVQKG SVVKAAGGVG
MVLANTAANG DELVADAHLL PATTVGQTTG EAIKKYLTSD PNPTATILFE GTKVGIKPSP
VVAAFSSRGP NSITQEILKP DIIAPGVNII AGWTGAVGPT GLAEDNRRVG FNIISGTSMS
CPHVSGLAAL LKGAHPDWSP AAIRSALMTT AYTVYKNGGA LQDVATGKPS TPFDHGAGHV
DPVAALNPGL VYDLKAEDYL NFLCALNYTS TQINSIARRP FSCDTSKKFS VTDLNYPSFA
VVFSEQMIAD SGSGSSSIKH IRTVTNVGPA GLYKVNVISP SNLVKVTVEP ETLAFTRTNE
QKSYTVTFTA PSMPSTKNVN GRIEWSDGKH VVSSPVAISW T
//
