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Database: UniProt
Entry: A0A200PPK5_9MAGN
LinkDB: A0A200PPK5_9MAGN
Original site: A0A200PPK5_9MAGN 
ID   A0A200PPK5_9MAGN        Unreviewed;       755 AA.
AC   A0A200PPK5;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   08-NOV-2023, entry version 20.
DE   SubName: Full=Peptidase S8/S53 domain {ECO:0000313|EMBL:OVA00151.1};
GN   ORFNames=BVC80_1671g14 {ECO:0000313|EMBL:OVA00151.1};
OS   Macleaya cordata.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC   Macleaya.
OX   NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA00151.1, ECO:0000313|Proteomes:UP000195402};
RN   [1] {ECO:0000313|EMBL:OVA00151.1, ECO:0000313|Proteomes:UP000195402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BLH2017 {ECO:0000313|Proteomes:UP000195402};
RC   TISSUE=Root {ECO:0000313|EMBL:OVA00151.1};
RX   PubMed=28552780; DOI=.1016/j.molp.2017.05.007;
RA   Liu X., Liu Y., Huang P., Ma Y., Qing Z., Tang Q., Cao H., Cheng P.,
RA   Zheng Y., Yuan Z., Zhou Y., Liu J., Tang Z., Zhuo Y., Zhang Y., Yu L.,
RA   Huang J., Yang P., Peng Q., Zhang J., Jiang W., Zhang Z., Lin K., Ro D.K.,
RA   Chen X., Xiong X., Shang Y., Huang S., Zeng J.;
RT   "The Genome of Medicinal Plant Macleaya cordata Provides New Insights into
RT   Benzylisoquinoline Alkaloids Metabolism.";
RL   Mol. Plant 10:975-989(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:OVA00151.1}.
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DR   EMBL; MVGT01004352; OVA00151.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A200PPK5; -.
DR   STRING; 56857.A0A200PPK5; -.
DR   InParanoid; A0A200PPK5; -.
DR   OrthoDB; 11910at2759; -.
DR   Proteomes; UP000195402; 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; 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:SF541; SUBTILISIN-LIKE PROTEASE SBT4.14; 1.
DR   Pfam; PF17766; fn3_6; 1.
DR   Pfam; PF05922; Inhibitor_I9; 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:UP000195402};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..755
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012984561"
FT   DOMAIN          39..117
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          139..591
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          649..749
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        147
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        212
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        540
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   755 AA;  80721 MW;  E09AE0E384B6F97F CRC64;
     MSIRDESTQV LFRRLLLLQV ILSGLASVNG SDDQQKNFYI VYMGDSPSSL KDSIVESHVN
     LLSSVVGSVG AAKDSIVHSY INNFNAFAAK LSPNEAKMLE RSSSVISVFP NQYRKLHTTK
     SWDFMGFNQN VKRNLKLESN IVVGLLDTGI TPGSESFSDK GLGPPPAKWK GTCGPFANFS
     GCNNKLVGAR FFKLDGNPDP TDIMSPVDVE GHGSHTSSTV VGNVVNGADL FGLAKGTARG
     AVPSARVAMY KVCWASSGCS DMDLLAGFDA AIEDGVDVIS VSIGGSSESY LRDPIAIGAF
     HAMKKGIITV ASAGNEGPGL SSVVNHAPWI LTVAASGIDR QFRSKIMLGN GKLLSGIGIN
     TFTPKQRLYP LISGADAGFN SSVDPSTSSM YCMGDSLDPK KVKGKVVLCE LQQWGADSVV
     KKAGGTGTLL ESSINPDTAQ IFMAPGTMIN YSIAKDINDY ISSTRSPSAV IYRTQEVKVS
     APFVASFSSR GPSMGSRHVL KPDITAPGID ILAAYTPLKS LTGLDGDKQY SKFTIMSGTS
     MSCPHVAGVA AYVKSFHPAW SPAAIKSAII TTAKPMSPKV NVGAEFSYGA GLLNPIQAVH
     PGLIYDMDQL PYIQFLCFEG YKDDPIRVIV GSRTVNCSEL PPAQGSDALN YPTMQLSMKT
     SDKKPGIAVF RRRVTNVGPA KSIYNATINA PKNVEITVNP TNLVFTRRFQ KRSFKVVVKA
     KTVASEQEIQ SGSLVWRSDI HTVRSPIVVF TSDYF
//
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