ID A0A2I0VKS6_9ASPA Unreviewed; 499 AA.
AC A0A2I0VKS6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic {ECO:0000313|EMBL:PKU63973.1};
GN Name=RBCMT {ECO:0000313|EMBL:PKU63973.1};
GN ORFNames=MA16_Dca012559 {ECO:0000313|EMBL:PKU63973.1};
OS Dendrobium catenatum.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC Epidendroideae; Malaxideae; Dendrobiinae; Dendrobium.
OX NCBI_TaxID=906689 {ECO:0000313|EMBL:PKU63973.1, ECO:0000313|Proteomes:UP000233837};
RN [1] {ECO:0000313|EMBL:PKU63973.1, ECO:0000313|Proteomes:UP000233837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=The whole plant {ECO:0000313|EMBL:PKU63973.1};
RX PubMed=26754549; DOI=10.1038/srep19029;
RA Zhang G.Q., Xu Q., Bian C., Tsai W.C., Yeh C.M., Liu K.W., Yoshida K.,
RA Zhang L.S., Chang S.B., Chen F., Shi Y., Su Y.Y., Zhang Y.Q., Chen L.J.,
RA Yin Y., Lin M., Huang H., Deng H., Wang Z.W., Zhu S.L., Zhao X., Deng C.,
RA Niu S.C., Huang J., Wang M., Liu G.H., Yang H.J., Xiao X.J., Hsiao Y.Y.,
RA Wu W.L., Chen Y.Y., Mitsuda N., Ohme-Takagi M., Luo Y.B., Van de Peer Y.,
RA Liu Z.J.;
RT "The Dendrobium catenatum Lindl. genome sequence provides insights into
RT polysaccharide synthase, floral development and adaptive evolution.";
RL Sci. Rep. 6:19029-19029(2016).
RN [2] {ECO:0000313|EMBL:PKU63973.1, ECO:0000313|Proteomes:UP000233837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=The whole plant {ECO:0000313|EMBL:PKU63973.1};
RX PubMed=28902843; DOI=10.1038/nature23897;
RA Zhang G.Q., Liu K.W., Li Z., Lohaus R., Hsiao Y.Y., Niu S.C., Wang J.Y.,
RA Lin Y.C., Xu Q., Chen L.J., Yoshida K., Fujiwara S., Wang Z.W., Zhang Y.Q.,
RA Mitsuda N., Wang M., Liu G.H., Pecoraro L., Huang H.X., Xiao X.J., Lin M.,
RA Wu X.Y., Wu W.L., Chen Y.Y., Chang S.B., Sakamoto S., Ohme-Takagi M.,
RA Yagi M., Zeng S.J., Shen C.Y., Yeh C.M., Luo Y.B., Tsai W.C.,
RA Van de Peer Y., Liu Z.J.;
RT "The Apostasia genome and the evolution of orchids.";
RL Nature 549:379-383(2017).
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DR EMBL; KZ503453; PKU63973.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0VKS6; -.
DR STRING; 906689.A0A2I0VKS6; -.
DR OrthoDB; 169378at2759; -.
DR Proteomes; UP000233837; 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:PKU63973.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000233837};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR009328-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PKU63973.1}.
FT DOMAIN 84..300
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT BINDING 242
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 263..264
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
SQ SEQUENCE 499 AA; 56523 MW; EC74CA57576799E0 CRC64;
MAEVSSAFCT SFLPKFPKLP VLPNIHGFAA SGRASHRLTR CSISAEPMPS GTSSSTIPWG
CEIESLESAF ALQRWLSESG LPPQKMDIRR VDVGERGLVA LKSIRKGEKL LFVPPSLVIT
ADSEWTNTEA GYVMRNNSVP DWPLLATYLI SEASLRDSSR WSIYISALPR QPYSLLYWTR
AELDMYLVAS QIRIRAIERD SDVTGVFNDL RARIFSKHPT VFPEEVFNLD TFKWSFGILF
SRLVRLSAMD GKVALVPWAD MLNHNSEVET FLDYDKSSRG IVFSTDRVYQ SGEQVFISYG
KKSNGELLLS YGFVPKEGTN PNDSVELSLC LKKDDKCYNE KVVALRKHGL STPQQFPMQI
TGWSLEMMAY AYLVVSSSDM RQRFDEMAAC AAGKTKSRME INYPELEEQT LQFILDCCES
SISKYSKFLE GGSPPDPITT NAQEANRRLL LKQLAVALCT SERRILFRAQ YILRRRLRDI
RSGELRALTI FNGFRKLFK
//
