ID A0A443P7D2_9MAGN Unreviewed; 736 AA.
AC A0A443P7D2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Subtilisin-like protein protease SBT1.2 {ECO:0000313|EMBL:RWR86636.1};
GN ORFNames=CKAN_01554500 {ECO:0000313|EMBL:RWR86636.1};
OS Cinnamomum micranthum f. kanehirae.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Cinnamomum.
OX NCBI_TaxID=337451 {ECO:0000313|EMBL:RWR86636.1, ECO:0000313|Proteomes:UP000283530};
RN [1] {ECO:0000313|EMBL:RWR86636.1, ECO:0000313|Proteomes:UP000283530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chaw 1501 {ECO:0000313|Proteomes:UP000283530};
RC TISSUE=Young leaves {ECO:0000313|EMBL:RWR86636.1};
RX PubMed=30626928; DOI=10.1038/s41477-018-0337-0;
RA Chaw S.M., Liu Y.C., Wu Y.W., Wang H.Y., Lin C.I., Wu C.S., Ke H.M.,
RA Chang L.Y., Hsu C.Y., Yang H.T., Sudianto E., Hsu M.H., Wu K.P., Wang L.N.,
RA Leebens-Mack J.H., Tsai I.J.;
RT "Stout camphor tree genome fills gaps in understanding of flowering plant
RT genome evolution.";
RL Nat. Plants 5:63-73(2019).
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:RWR86636.1}.
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DR EMBL; QPKB01000006; RWR86636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443P7D2; -.
DR STRING; 337451.A0A443P7D2; -.
DR Proteomes; UP000283530; Unassembled WGS sequence.
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; IPR023827; Peptidase_S8_Asp-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:SF463; OS12G0427600 PROTEIN; 1.
DR PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 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; PS00136; SUBTILASE_ASP; 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:UP000283530};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 21..100
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 124..560
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 356..441
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 637..733
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 198
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 523
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 736 AA; 78131 MW; 7E5A722B42F0984C CRC64;
MGRTQHALLT HKTTKSPHLQ TYIVHVRQLE KEVFTSSEDR ESWYRSFLPS SVASSEENRM
VYSYTHAITG FAAQLSEEEV EAMKGKEGFV SAFPDRLLPL QTTHSPSFMG LQPDAGFWKD
SNFGKGVIIG VLDTGIFPDH PSFGGEGMPP PPAKWKGRCD FNATSCNNKL IGARTFDSGA
KAMLGRPTAE APVDDEGHGT HTSSTAAGAF VENVSIFGNA NGTAAGMAPL AHLAMYKVCF
SGGCADSDLL AGLDAAVEDN VDVLSLSIGG FSIPFYADSI AIGAFGAIQK NIFVSCAAGN
SGPYNQSLSN EAPWILTVGA STMDRRIVAT VKLGNGEEYD GESVYQPKNF SSDLLPLVFP
GASGKPGAAT CDEGSLNGTD LSGQVVLCLR GGASGRVEKG AIVQAAGGAA MILLNREEDG
YTTIADTHVL PASDVSFMDA LKIVSYWNSS ESPMATIIFK GTVLGYRPSP TVASFSSRGP
SLASPGILKP DIIGPGVSVL AAWPFQVDPA NPLLTFNIIS GTSMATPHLS GIAALLKSSH
PDWSPAAIKS AIMTTANTTT KTFGAIVDQT MRPADVFTMG SGHVNPSQAN DPGLIYDLEP
MDYIPYLCGL NYSDAEVQSI TRYIVSCSNY TSISEGELNY PSFSVKLGPT QTFSRTVTNV
GEANSSYTME FWWPDGVDVI VEPMVLVFGE VMEKKTYNVT FSESPSSGKS GTFAEGYLTW
VSPKYSVRSP ISVAFE
//
