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Database: UniProt
Entry: A0A371GEF9_MUCPR
LinkDB: A0A371GEF9_MUCPR
Original site: A0A371GEF9_MUCPR 
ID   A0A371GEF9_MUCPR        Unreviewed;       477 AA.
AC   A0A371GEF9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic {ECO:0000313|EMBL:RDX88900.1};
DE   Flags: Fragment;
GN   Name=RBCMT {ECO:0000313|EMBL:RDX88900.1};
GN   ORFNames=CR513_29443 {ECO:0000313|EMBL:RDX88900.1};
OS   Mucuna pruriens (Velvet bean) (Dolichos pruriens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Mucuna.
OX   NCBI_TaxID=157652 {ECO:0000313|EMBL:RDX88900.1, ECO:0000313|Proteomes:UP000257109};
RN   [1] {ECO:0000313|EMBL:RDX88900.1, ECO:0000313|Proteomes:UP000257109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Jos {ECO:0000313|Proteomes:UP000257109};
RC   TISSUE=Seed {ECO:0000313|EMBL:RDX88900.1};
RA   Nnadi N.E., Vos R., Hasami M.H., Devisetty U.K., Aguiy J.C.;
RT   "Draft genome of Mucuna pruriens seed.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:RDX88900.1}.
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DR   EMBL; QJKJ01005812; RDX88900.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A371GEF9; -.
DR   STRING; 157652.A0A371GEF9; -.
DR   Proteomes; UP000257109; 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:RDX88900.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRSR:PIRSR009328-1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RDX88900.1}.
FT   DOMAIN          74..290
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   BINDING         232
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         253..254
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         264
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         289
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         301
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:RDX88900.1"
SQ   SEQUENCE   477 AA;  54320 MW;  91DC51D26F64F239 CRC64;
     MAEASRMMLY SSLVPCFSLR RHVSQRQLRS VSRKQQIECS ASAGGTVAWG CEIESLENAS
     ALQRWLSDSG LPPQKMRIER VDVGERGLVA SKNIRKGEKL LFVPPSLVIT PLSEWSCPEA
     GEVLKKNSVP DWPLLATYLI SEASLMESSR WSNYISALPR QPYSLLYWSQ AELDRYLEAS
     QIRERAIERI NNVIGTYNDL RLRIFSKYPD LFPDEVFNIE SFKWSFGILF SRLVRLPSMD
     GNVALVPWAD MLNHSCDVET FLDYDKTSKG IVFTTDRPYQ PGEQVFISYG KKSNGELLLS
     YGFVPKEGAN PSDSVELSLS LKKSDESYKE KLELLKKYGL SVSQCFPIQI TGWPLELMAY
     AYLAVSPSSM RGEFEEMAAA ASSSTTSKKD LRYPEIEEQA LQFILDSCES SISKYNNGSL
     DLDVTSPKQL NRRLFLKQLA MDLCTSERRI LFRAQYILRR KLRDMRAGEL RALKMYM
//
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