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Entry: I1KMF9_SOYBN
LinkDB: I1KMF9_SOYBN
Original site: I1KMF9_SOYBN 
ID   I1KMF9_SOYBN            Unreviewed;       487 AA.
AC   I1KMF9;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=SET domain-containing protein {ECO:0000259|PROSITE:PS50280};
GN   Name=100818113 {ECO:0000313|EnsemblPlants:KRH50559};
GN   ORFNames=GLYMA_07G228300 {ECO:0000313|EMBL:KRH50559.1};
OS   Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH50559.1};
RN   [1] {ECO:0000313|EMBL:KRH50559.1, ECO:0000313|EnsemblPlants:KRH50559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH50559};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH50559.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH50559}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH50559};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH50559.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH50559.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) 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}.
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DR   EMBL; CM000840; KRH50559.1; -; Genomic_DNA.
DR   RefSeq; XP_003529470.1; XM_003529422.3.
DR   AlphaFoldDB; I1KMF9; -.
DR   SMR; I1KMF9; -.
DR   STRING; 3847.I1KMF9; -.
DR   PaxDb; 3847-GLYMA07G35510-1; -.
DR   EnsemblPlants; KRH50559; KRH50559; GLYMA_07G228300.
DR   GeneID; 100818113; -.
DR   Gramene; KRH50559; KRH50559; GLYMA_07G228300.
DR   KEGG; gmx:100818113; -.
DR   eggNOG; KOG1337; Eukaryota.
DR   HOGENOM; CLU_028149_1_0_1; -.
DR   InParanoid; I1KMF9; -.
DR   OMA; DFWMKIP; -.
DR   OrthoDB; 51002at2759; -.
DR   Proteomes; UP000008827; Chromosome 7.
DR   ExpressionAtlas; I1KMF9; baseline and differential.
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; IBA:GO_Central.
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:UP000008827};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRSR:PIRSR009328-1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          62..286
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   BINDING         78..80
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         220
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         240..241
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         298
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
SQ   SEQUENCE   487 AA;  54862 MW;  F34AE04E0618BD72 CRC64;
     MASVFSACSG SAVLFHSRNS FSSKGSFLHL KRPLSANCVA SLGTEVSVSP AVDTFWQWLK
     EEGVVSGKTP VKPGVVPEGL GLVALKDISR NEVVLQVPKR LWINPDAVAA SEIGKVCSGL
     KPWLAVALFL IRERSRSDSL WKHYFSILPK ETDSTIYWSE EELSELQGTQ LLNTTRSVKQ
     YVQNEFRRLE EEIIIPNKKL FPSSITLDDF FWAFGILRSR AFSRLRNENL VVIPLADLIN
     HSARVTTDDH AYEIKGAAGL FSWDYLFSLR SPLSLKAGDQ VYIQYDLNKS NAELALDYGF
     IEPNTDRNAY TLTLQISESD PFFGDKLDIA ESNGFGETAY FDIFYNRPLP PGLLPYLRLV
     ALGGTDAFLL ESIFRNSIWG HLELPVSRDN EELICRVVRE TCKTALAGYH TTIEEDQKLK
     EAKLDSRHAI AVGIREGEKN LLQQIDEIFK EKELELAQLE YYQERRLKDL GLCGENGDIL
     GDLGKFF
//
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