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Database: UniProt
Entry: I1NDM7_SOYBN
LinkDB: I1NDM7_SOYBN
Original site: I1NDM7_SOYBN 
ID   I1NDM7_SOYBN            Unreviewed;       487 AA.
AC   I1NDM7;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=SET domain-containing protein {ECO:0000259|PROSITE:PS50280};
GN   Name=100801721 {ECO:0000313|EnsemblPlants:KRG89557};
GN   ORFNames=GLYMA_20G031600 {ECO:0000313|EMBL:KRG89557.1};
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|EnsemblPlants:KRG89557};
RN   [1] {ECO:0000313|EMBL:KRG89557.1, ECO:0000313|EnsemblPlants:KRG89557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRG89557};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRG89557.1};
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:KRG89557}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRG89557};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRG89557.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRG89557.1};
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; CM000853; KRG89557.1; -; Genomic_DNA.
DR   RefSeq; XP_003556768.1; XM_003556720.3.
DR   AlphaFoldDB; I1NDM7; -.
DR   SMR; I1NDM7; -.
DR   STRING; 3847.I1NDM7; -.
DR   PaxDb; 3847-GLYMA20G03950-1; -.
DR   EnsemblPlants; KRG89557; KRG89557; GLYMA_20G031600.
DR   GeneID; 100801721; -.
DR   Gramene; KRG89557; KRG89557; GLYMA_20G031600.
DR   KEGG; gmx:100801721; -.
DR   eggNOG; KOG1337; Eukaryota.
DR   HOGENOM; CLU_028149_1_0_1; -.
DR   InParanoid; I1NDM7; -.
DR   OMA; STIWSRF; -.
DR   OrthoDB; 51002at2759; -.
DR   Proteomes; UP000008827; Chromosome 20.
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;  55052 MW;  06DA4485C71EB355 CRC64;
     MASVFSACSG SAVLFYSRNS FPSKGSFIHL KRPLSANCVA SLGTEVSVSP AVDTFWQWLK
     EEGVVSAKTP VKPSVVPEGL GLVALKDISR NEVVLQVPKR LWINPDAVAA SEIGKVCIGL
     KPWLAVALFL IRERSRSNSL WKHYFSVLPK ETDSTIYWSE EELSELQGTQ LLNTTRSVKQ
     YVENEYRRLE EEIILPNKKL FPSPLTLDDF FWAFGILRSR AFSRLRNENL VVIPFADFIN
     HSARVTTEDH AYEIKGAAGL FSWDYLFSLR SPLSLKAGDQ VYIQYDLNKS NAELALDYGF
     IEPNADRNAY TLTLQISESD PFFGDKLDIA ESNGFGETAY FDIFYSRPLP PGLLPYLRLV
     ALGGTDAFLL ESIFRNSIWG HLELPVSRDN EELICRVVRE TCKTALAGYH TTIEEDQKLK
     EAKLDSRHAI AVGIREGEKQ LLQQIDETFK EKELELDQLE YYQERRLKDL GLCGENGDIL
     GDLGKFF
//
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