ID A0A200QF15_9MAGN Unreviewed; 459 AA.
AC A0A200QF15;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 28-JUN-2023, entry version 15.
DE SubName: Full=PDZ domain {ECO:0000313|EMBL:OVA09015.1};
GN ORFNames=BVC80_9097g80 {ECO:0000313|EMBL:OVA09015.1};
OS Macleaya cordata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Macleaya.
OX NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA09015.1, ECO:0000313|Proteomes:UP000195402};
RN [1] {ECO:0000313|EMBL:OVA09015.1, 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:OVA09015.1};
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 S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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:OVA09015.1}.
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DR EMBL; MVGT01002224; OVA09015.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200QF15; -.
DR STRING; 56857.A0A200QF15; -.
DR InParanoid; A0A200QF15; -.
DR OrthoDB; 313901at2759; -.
DR Proteomes; UP000195402; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000195402}.
FT DOMAIN 349..447
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 459 AA; 48957 MW; A2C6B2F69024D506 CRC64;
MQVLLCNSLP QSQSFVIPRS LGRRKVCFDG VSSFCSQKDI QSNSSVNNVV SSQSTSVQRP
VEDCAEDLRE VICNKIPFTT RRMLFASPLI YFCSYTSRYF SALALGDSSV TIEQVTPPVL
PSGALFPSEE RIVKLFENNT YSVVNIFDVT LRPQLKMTGV VEVPEGNGSG VIWDEQGHIV
TNYHVVGNAL SRNPTPGQVV ARVNILASDG VQKNFEGKLI GADRDKDLAV LKVEASEDLL
KPIKVGQSSA LRVGQQCLAI GNPFGFDHTL TVGVISGLNR EIFSQAGVTI SGGIQTDAAI
NPGNSGGPLL DSKGNLIGIN TAIFTQTGTS AGVGFAIASS TVLKIVPQLI QFGKVVRAGL
NLDIAPDLLA NQLNVRNGAL ILQVPGNSPA AKAGLLPTSR GFAGNIVLGD IIVAVDNKPV
RNKAELSKVL DDYNVGEKVL LKIQRGSENL EVFLVLEEI
//
