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Database: UniProt
Entry: A0A200PZF4_9MAGN
LinkDB: A0A200PZF4_9MAGN
Original site: A0A200PZF4_9MAGN 
ID   A0A200PZF4_9MAGN        Unreviewed;       720 AA.
AC   A0A200PZF4;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Peptidase S8/S53 domain {ECO:0000313|EMBL:OVA03587.1};
GN   ORFNames=BVC80_1651g94 {ECO:0000313|EMBL:OVA03587.1};
OS   Macleaya cordata.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC   Macleaya.
OX   NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA03587.1, ECO:0000313|Proteomes:UP000195402};
RN   [1] {ECO:0000313|EMBL:OVA03587.1, 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:OVA03587.1};
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:OVA03587.1}.
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DR   EMBL; MVGT01003660; OVA03587.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A200PZF4; -.
DR   STRING; 56857.A0A200PZF4; -.
DR   InParanoid; A0A200PZF4; -.
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; 3.30.70.80; 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; 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:SF592; LOW QUALITY PROTEIN: SUBTILISIN-LIKE PROTEASE SBT5.3; 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; 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..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..720
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012397097"
FT   DOMAIN          28..99
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          128..555
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          363..423
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          620..713
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        136
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        211
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        506
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   720 AA;  77084 MW;  67501E4C709ED511 CRC64;
     MKLAVVLTLL CFLRCALTNE AISTKKHYIV YMGEHSHPDP HRVSHEMLTS VTGSVHGAEE
     AVVHLYSKSF KGFSAMLTSE QAQQLAKKES VISVFESKTN LVHTTHSWEF LGVDGILEYN
     QLTVESKSDV IVGVIDTGVW PESESFSDKG LGPVPKRFKG ECVVGDHFTV KNCNRKIIGA
     RFYSKGFEAE MGPLESLNET FFRSARDADG HGTHTASTVA GSVVSNVSLF GMARGTARGG
     MPSARLAIYK ACWFGYCSDA DLLSAFDDAT NDGVDIISIS AGPDPPQGSF FSDANSIGSF
     HAFRKGVLVS ASAGNSGLPN TATNVAPWIL TVAASSIDRE FNSNVYLGNS KIFCKNNTLD
     HNLIKGKIVV CTIETVTDIR REKSLVVREG GGVGMILIDP IAKDVGFQFV IPATLIGQEE
     AEVLQEYLTT AKNPTAKIIP TVTIHNTSPA PKMAVFSSVG PNVITPDILK PDITAPGVNI
     LAAWSPLAIE AAAERSVDFN IISGTSMSCP HVSAVAAIIK SCHPSWSPSA IKSAIMTTAT
     LMDNTGRPIL KDPYGSPTTP FDYGSGHINP VAALDPGLIY DFGSNDIINF LCSNSDSPAE
     IRNVTGEPVT CKNPPIPSYD LNYPSIGVAS MNGSVSVLRT VTYYGKGPTV FKASVENPPG
     VKVAVTPYSL KFKEAREKMS FKVDFMPYKS SNGSFVFGSI TWSNGIYKVR SPIGLNVVSV
//
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