ID W9QMR3_9ROSA Unreviewed; 527 AA.
AC W9QMR3;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase {ECO:0000313|EMBL:EXB34472.1};
GN ORFNames=L484_004862 {ECO:0000313|EMBL:EXB34472.1};
OS Morus notabilis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX NCBI_TaxID=981085 {ECO:0000313|EMBL:EXB34472.1, ECO:0000313|Proteomes:UP000030645};
RN [1] {ECO:0000313|Proteomes:UP000030645}
RP NUCLEOTIDE SEQUENCE.
RA He N., Zhao S.;
RT "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KE343542; EXB34472.1; -; Genomic_DNA.
DR RefSeq; XP_010088354.1; XM_010090052.1.
DR AlphaFoldDB; W9QMR3; -.
DR STRING; 981085.W9QMR3; -.
DR eggNOG; KOG1337; Eukaryota.
DR Proteomes; UP000030645; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:InterPro.
DR GO; GO:0030785; F:[ribulose-bisphosphate carboxylase]-lysine N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd19179; SET_RBCMT; 1.
DR Gene3D; 3.90.1420.10; Rubisco LSMT, substrate-binding domain; 1.
DR Gene3D; 3.90.1410.10; set domain protein methyltransferase, domain 1; 1.
DR InterPro; IPR011192; Rubisco_LSMT_MeTrfase_plant.
DR InterPro; IPR015353; Rubisco_LSMT_subst-bd.
DR InterPro; IPR036464; Rubisco_LSMT_subst-bd_sf.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044431; SET_RBCMT.
DR PANTHER; PTHR13271:SF123; RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE_OXYGENASE SMALL SUBUNIT N-METHYLTRANSFERASE I-RELATED; 1.
DR PANTHER; PTHR13271; UNCHARACTERIZED PUTATIVE METHYLTRANSFERASE; 1.
DR Pfam; PF09273; Rubis-subs-bind; 1.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF009328; RMT_SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF81822; RuBisCo LSMT C-terminal, substrate-binding domain; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EXB34472.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030645};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR009328-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EXB34472.1}.
FT DOMAIN 87..303
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT BINDING 245
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 266..267
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
SQ SEQUENCE 527 AA; 60121 MW; F6C35AA55FE5B92F CRC64;
MAEASGILQT SLISNFHPFH KTHLPQLHPV LSFRRNPTIP IQCSVSTSET TKTTTTQNAI
PWGCDIDSLE NASALQKWLS QSGLPPQKMA IERVDVGERG LVALKNIRKG EKLLFVPPSL
VISADSEWSC EEAGEVMKKN SVPDWPLLAT YLISEASLME SSRWSNYISA LPRQPYSLLY
WTRDELDRYL EASQIRERAI ERVTNVIGTY KDLRLRIFSK YPHLFPEEVY NLETFSWSFG
ILFSRLVRLP SMDGKFALVP WADMLNHNCE VETFLDYDKS SQGVLFTTDR PYQPGEQVFI
SYGKKSNGEL LLSYGFVPKE GTNPSDSVEL SLSLSKSDKC YKQKLAALRK HGLQVSQRYP
IRITGWPLEL MAYAYLAVSP PSMSSQFDEM AAAASNKTDI KKDLRYPEIE EEALQFILDS
CESSISKYNK FLQQSGTLDL DVTSPKQLNR RLFLKQLAVD LCTSERRILF RTQYSFKFFS
RRTLVELPST LQIVFSRRLQ ILLPKNVKNK DSQNELTLCN SETPKAH
//