ID A0A166A2C0_DAUCS Unreviewed; 775 AA.
AC A0A166A2C0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Subtilisin-like protease SBT1.3 {ECO:0008006|Google:ProtNLM};
GN ORFNames=DCAR_009413 {ECO:0000313|EMBL:KZN00659.1};
OS Daucus carota subsp. sativus (Carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZN00659.1};
RN [1] {ECO:0000313|EMBL:KZN00659.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaf {ECO:0000313|EMBL:KZN00659.1};
RX PubMed=27158781; DOI=10.1038/ng.3565;
RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT "A high-quality carrot genome assembly provides new insights into
RT carotenoid accumulation and asterid genome evolution.";
RL Nat. Genet. 48:657-666(2016).
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:KZN00659.1}.
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DR EMBL; LNRQ01000003; KZN00659.1; -; Genomic_DNA.
DR RefSeq; XP_017243387.1; XM_017387898.1.
DR AlphaFoldDB; A0A166A2C0; -.
DR EnsemblPlants; KZN00659; KZN00659; DCAR_009413.
DR GeneID; 108215397; -.
DR Gramene; KZN00659; KZN00659; DCAR_009413.
DR KEGG; dcr:108215397; -.
DR OMA; HSNRTCK; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000077755; Chromosome 3.
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:SF322; SUBTILISIN-LIKE PROTEASE SBT1.3; 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; PS51892; SUBTILASE; 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:UP000077755};
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..775
FT /note="Subtilisin-like protease SBT1.3"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007870381"
FT DOMAIN 30..116
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 142..597
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 381..471
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 670..768
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 223
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 556
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 775 AA; 83216 MW; BB1A3CE469AC4B3E CRC64;
MVVKWVFLLL LASLTITNVV SLTASPFTKT YIVQIDRLAK PETFGDHVEW YASVIQSVSA
ELNDEENDDG ENERIMYSYQ TAFHGVAARL SLEEVERLQQ HPAVMAVFPE VAYELHTTRS
PWFLGLGSEE STSVWSEKLA DHDVVVGVLD TGIWPESRSF NDTGLTAIPA RWKGTCQIGR
GFDKSHCNKK IVGARMFYHG YEAGAGKINE QEEYKSPRDQ DGHGTHTAAT VAGSPVQGAN
LLGYAKGTAR GMAPGARIAA YKVCWASGCF SSDILAAVDQ AVADGVNVLS ISLGGGSSSY
QHDSLSIATF GAMEKGVFVS CSAGNGGPTP VSLTNISPWI TTVGASTMDR DFPSTVKLGS
GQKITGSSLY KGRRKLSPAK QYPLVYTGGN SSILDPSSLC LQDTLNPKVV RGKIVICNRG
VTPRVQKGQV VKDAGGIGMI LANTEDNGEE LVADCHLLPT VAVGEKAGRS IKEYAMTNSH
PTATLSFQGT RLGVKPSPVV AAFSSRGPNY LSLEVLKPDI VAPGVNILAA WTNTLGPSSL
ATDKRIVNFN ILSGTSMSCP HVSGIAALIK ARHPDWSPAA IKSAIMTTAY IHDNNYTPLR
DASTGAPSTP YDHGAGHINP LKALNPGLVY DLKPQDYFEF LCAQLSPGDM VVFAKFSNRS
CRNTLASPGD LNYPALSVLF LEKGNNSVLT LHRTVTNVGK AVSNYHAVVS PFKSVVIKVE
PTTLHFTKKH QKLSYKVTFI GKKLQAGPEF GHLMWKDGVH KVRTPVIVTR VPVPI
//
