ID A0A1J6KAC2_NICAT Unreviewed; 491 AA.
AC A0A1J6KAC2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Ribulose-1,5 bisphosphate carboxylaseoxygenase large subunit n-methyltransferase, chloroplastic {ECO:0000313|EMBL:OIT26997.1};
GN Name=RBCMT_0 {ECO:0000313|EMBL:OIT26997.1};
GN ORFNames=A4A49_23157 {ECO:0000313|EMBL:OIT26997.1};
OS Nicotiana attenuata (Coyote tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=49451 {ECO:0000313|EMBL:OIT26997.1, ECO:0000313|Proteomes:UP000187609};
RN [1] {ECO:0000313|EMBL:OIT26997.1, ECO:0000313|Proteomes:UP000187609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UT {ECO:0000313|Proteomes:UP000187609};
RC TISSUE=Leaves {ECO:0000313|EMBL:OIT26997.1};
RA Xu S., Brockmoeller T., Gaquerel E., Navarro A., Kuhl H., Gase K., Ling Z.,
RA Zhou W., Kreitzer C., Stanke M., Tang H., Lyons E., Pandey P., Pandey S.P.,
RA Timmermann B., Baldwin I.T.;
RT "The genome of Nicotiana attenuata.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Plant protein-lysine LSMT methyltransferase family.
CC {ECO:0000256|PROSITE-ProRule:PRU00916}.
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:OIT26997.1}.
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DR EMBL; MJEQ01002571; OIT26997.1; -; Genomic_DNA.
DR RefSeq; XP_019234056.1; XM_019378511.1.
DR AlphaFoldDB; A0A1J6KAC2; -.
DR STRING; 49451.A0A1J6KAC2; -.
DR EnsemblPlants; OIT26997; OIT26997; A4A49_23157.
DR GeneID; 109214572; -.
DR Gramene; OIT26997; OIT26997; A4A49_23157.
DR KEGG; nau:109214572; -.
DR OMA; DFWMKIP; -.
DR OrthoDB; 51002at2759; -.
DR Proteomes; UP000187609; 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:SF113; [FRUCTOSE-BISPHOSPHATE ALDOLASE]-LYSINE N-METHYLTRANSFERASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR13271; UNCHARACTERIZED PUTATIVE METHYLTRANSFERASE; 1.
DR Pfam; PF09273; Rubis-subs-bind; 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; PS51583; SAM_MT127; 1.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU00916}; Reference proteome {ECO:0000313|Proteomes:UP000187609};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR009328-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OIT26997.1}.
FT DOMAIN 67..291
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT BINDING 83..85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 225
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 245..246
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
SQ SEQUENCE 491 AA; 55935 MW; 5B60305A4D85DAC2 CRC64;
MASVFSVHPL PSSSFLCPLK TTKSRTKQYQ TCYTYQKPIL INSLQLKQLD PKIPEPVQTF
WQWLCKEGVV TAKTPVKPGI VPEGLGLVAN RDIAKGETVL EVPRRFWINP DAVAESEIGN
VCSGLKPWIS VALFLLREKW RDDSKWKYYM DVLPKSTDST IYWSEEELSE IQGTQLLSTT
LSVKDYVQNE FQKVEEEVIL RNKQLFPFPI TLDDFFWAFG ILRSRAFSRL RNQNLILVPF
ADLTNHNARV TTEDHAHEVR GPAGLFSWDL LFSLRSPLKL KAGDQLFIQY DLNKSNADMA
LDYGFIEPSS ARDAFTLTLE ISESDEFYGD KLDIAETNGI GETAYFDIKI GQSLPPTMIP
YLRLVALGGT DAFLLESIFR NSVWGHLGLP VSRANEELIC KVVRDACKSA LSGYHTTIEE
DEKLMEEGNL STRLQIAVGI RLGEKKVLKQ IDDIFREREL ELDELEYYGE RRLKDLGLVG
EQGDIIFWEP K
//
