ID A0A3S3RCQ0_9MAGN Unreviewed; 894 AA.
AC A0A3S3RCQ0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000313|EMBL:RWR97944.1};
GN ORFNames=CKAN_02741700 {ECO:0000313|EMBL:RWR97944.1};
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:RWR97944.1, ECO:0000313|Proteomes:UP000283530};
RN [1] {ECO:0000313|EMBL:RWR97944.1, 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:RWR97944.1};
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:RWR97944.1}.
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DR EMBL; QPKB01000254; RWR97944.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S3RCQ0; -.
DR STRING; 337451.A0A3S3RCQ0; -.
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; 2.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
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; 2.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 2.
DR PROSITE; PS51892; SUBTILASE; 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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..894
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018705015"
FT DOMAIN 25..108
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 131..573
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 374..449
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 644..743
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT DOMAIN 750..820
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT ACT_SITE 140
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 530
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 894 AA; 95119 MW; 25A5C4F5AEE37DE2 CRC64;
MVLLFLFAIL SFFYSSTAVP NGLQTYIVHV REPHTTVSSN SLDRESWYRS FLTTTSITGS
EDGHDRMVYS YQHVITGFAA LLSEDEVKAM EKKDGFISAY PDELLPLHTT HTPDFLGLKQ
DMGVWKNSNF GKGVIIGVLD TGAMPNHPSF SDVGMPSPPP KWKGKCEFSA CNKKIIGARS
FVEGAKAMLG ISMPATPSDE DGHGTHTAST AAGAFVEGAN VLGNANGHAV GMAPFAHLAI
YKVCGQSGCA NTDLLAGIES AIQDGVDVMS ISIGSPALPN FYTRVIDIGT FKAMQKGIFI
SCSAGNNGPS FSTVSNSAPW CLTVGASTMD RSIRTTVMLG NGEFCNGESL FQPKDFQSNK
PLPIIFPGAN GDANTTACIN GSLDGIDVKG KAVLCERGRI GDIAKGLVVK NAGGSAMIVM
NREYEGFSII AAAHVLPASH VSFSDGSKIK TYINSTLSPT AMILFRGTIL GTSPSPMVIS
FSSRGPNLPS PGILKPDVLG PGVNVLAGWP QNVGSFPILG STFNIISGTS MSCPHLSGIA
ALIKSSHPDW SPAAIKSAIM TTADVLDNRG KQIVDESLTP ADLFATGAGH VNPSRANDPG
LIYGLTPDDY LAYLCGLGYT DNQVRMLAGS NASCSIITSI REGELNYPSF SVTLGPSQTF
NRTVTNVGNA MSAYTVEIIK PQGVDVSVKP DALHFSSMNE KLTYSVTFSP LESGSGGSIG
FAEGSLKWVS SSSSTKYEVR SPISPHTTVS SNSLDRESWY RSFLTTTSIT GSEDGHDRMV
YSYQHVITGF AALLSEDEVK AMEKKDGFIS AYPDELLPLH TTHTPDFLGL KQDMGVWKNS
NFGKGVIIGV LDTGAMPNHP SFSDVGMPSP PPKWKGKCEF SACNKKNHWR EIFC
//
