ID A0A200RDL2_9MAGN Unreviewed; 520 AA.
AC A0A200RDL2;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Leucine-rich repeat {ECO:0000313|EMBL:OVA20805.1};
GN ORFNames=BVC80_887g97 {ECO:0000313|EMBL:OVA20805.1};
OS Macleaya cordata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Macleaya.
OX NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA20805.1, ECO:0000313|Proteomes:UP000195402};
RN [1] {ECO:0000313|EMBL:OVA20805.1, 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:OVA20805.1};
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 -!- FUNCTION: Leucine-rich repeat protein that likely mediates protein
CC interactions, possibly in the context of signal transduction.
CC {ECO:0000256|ARBA:ARBA00037519}.
CC -!- SIMILARITY: Belongs to the SHOC2 family.
CC {ECO:0000256|ARBA:ARBA00023786}.
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:OVA20805.1}.
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DR EMBL; MVGT01000057; OVA20805.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200RDL2; -.
DR STRING; 56857.A0A200RDL2; -.
DR InParanoid; A0A200RDL2; -.
DR OrthoDB; 316387at2759; -.
DR Proteomes; UP000195402; Unassembled WGS sequence.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR45752:SF203; ADENYLATE CYCLASE; 1.
DR PANTHER; PTHR45752; LEUCINE-RICH REPEAT-CONTAINING; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 3.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00364; LRR_BAC; 8.
DR SMART; SM00365; LRR_SD22; 5.
DR SMART; SM00369; LRR_TYP; 8.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS51450; LRR; 3.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Reference proteome {ECO:0000313|Proteomes:UP000195402};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REGION 22..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 154..201
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 40..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 520 AA; 58257 MW; B5EA477321445DD5 CRC64;
MDPNPNKFPI LSYVMSRIPQ VGTKHPSYSD FDDIDIEQPK PRSSSSSTGS PNSNYPDGGL
MIQMPHLNDP KVMASMTSAV SDVYQTRSIL KTLGDRPDHE AVDSARSKIA EIESTLLKQL
EEIVLESKPN EIDLEKEKEI RQAAEKEKSI YKAVVQLDEM HESYEKLLRD AEERLVKIYR
SAASTEKVET AEEDVDEEVN EEVVRILQEA SVKGVERVEL SGRELRFLPE AFGKLRGLVA
LDLSSNQLQV IPDSIAGLEN LEELNLSTNL LESLPDSIGL LLNLKILNVS SNKLKALPDS
ISRCRSLVEL DASFNHLGYL PTNIGYELVN LQKLLVSLNK IRSLPTSICE MKSLRHLDVH
FNELRGLPHA IGLLTNLEIL DLSSNFSDLT ELPETFGDLT NLRELDLSNN QIHALPDTFG
RLDNLTKLNL DQNPLVIPPM EIVNQGVEAV KEFMAKRWLD ILLEEEHKSM LQANSAAQTG
WLTRSTSWLN NWVSVVSENV TGYLGGGEKS PRDPYLDQQL
//