ID A0A1G4JK46_9SACH Unreviewed; 252 AA.
AC A0A1G4JK46;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Protein-lysine N-methyltransferase EFM6 {ECO:0000256|HAMAP-Rule:MF_03198};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03198};
DE AltName: Full=Elongation factor methyltransferase 6 {ECO:0000256|HAMAP-Rule:MF_03198};
GN Name=EFM6 {ECO:0000256|HAMAP-Rule:MF_03198};
GN ORFNames=LAMI_0E03862G {ECO:0000313|EMBL:SCU90857.1};
OS Lachancea mirantina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1230905 {ECO:0000313|EMBL:SCU90857.1, ECO:0000313|Proteomes:UP000191024};
RN [1] {ECO:0000313|EMBL:SCU90857.1, ECO:0000313|Proteomes:UP000191024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 11717 {ECO:0000313|EMBL:SCU90857.1};
RA Devillers H.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC methyltransferase that methylates elongation factor 1-alpha.
CC {ECO:0000256|HAMAP-Rule:MF_03198}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03198}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. METTL21 family. EFM6 subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_03198}.
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DR EMBL; LT598465; SCU90857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4JK46; -.
DR STRING; 1230905.A0A1G4JK46; -.
DR OrthoDB; 2787189at2759; -.
DR Proteomes; UP000191024; Chromosome e.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_03198; Methyltr_EFM6; 1.
DR InterPro; IPR033684; EFM6.
DR InterPro; IPR019410; Methyltransf_16.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR14614; HEPATOCELLULAR CARCINOMA-ASSOCIATED ANTIGEN; 1.
DR PANTHER; PTHR14614:SF98; PROTEIN-LYSINE N-METHYLTRANSFERASE EFM6; 1.
DR Pfam; PF10294; Methyltransf_16; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03198};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03198};
KW Reference proteome {ECO:0000313|Proteomes:UP000191024};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03198};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03198}.
FT BINDING 50
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT BINDING 90..92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT BINDING 115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT BINDING 143
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT BINDING 166
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
SQ SEQUENCE 252 AA; 28277 MW; 2640186363CB316C CRC64;
MEDVFGFEGI VAPRPIEHLG DSDFSFGGQL TPPLKIHEDG GESGCGGKVW IAGELLCEYL
IEKSTSDAVL SRMERGLGQT GEFEKILELG SGTGLVGICL ALLCETRDLE VYVTDIGGLI
GLMQRNIDLN GVCAKVHAKE LKWGDPLEPK FQPEAGKRKV DLVLAADCVY LEKAFPLLEK
TLLDLTSCDD PPMILMSCKK RRKADKHFFQ QIKKNFQVIE IQDFAKFERY LAQRTRLFQL
KRVHKKPLMF SR
//
