ID   A0A1X7R717_9SACH        Unreviewed;       247 AA.
AC   A0A1X7R717;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Protein N-terminal and lysine N-methyltransferase EFM7 {ECO:0000256|HAMAP-Rule:MF_03223};
DE            EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03223};
DE   AltName: Full=Elongation factor methyltransferase 7 {ECO:0000256|HAMAP-Rule:MF_03223};
GN   Name=EFM7 {ECO:0000256|HAMAP-Rule:MF_03223};
GN   ORFNames=KASA_0L03113G {ECO:0000313|EMBL:SMN21259.1};
OS   Kazachstania saulgeensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX   NCBI_TaxID=1789683 {ECO:0000313|EMBL:SMN21259.1, ECO:0000313|Proteomes:UP000196158};
RN   [1] {ECO:0000313|EMBL:SMN21259.1, ECO:0000313|Proteomes:UP000196158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent protein methyltransferase
CC       that trimethylates the N-terminal glycine 'Gly-2' of elongation factor
CC       1-alpha, before also catalyzing the mono- and dimethylation of 'Lys-3'.
CC       {ECO:0000256|HAMAP-Rule:MF_03223}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03223}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. EFM7 family. {ECO:0000256|HAMAP-Rule:MF_03223}.
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DR   EMBL; FXLY01000007; SMN21259.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7R717; -.
DR   STRING; 1789683.A0A1X7R717; -.
DR   OrthoDB; 5470823at2759; -.
DR   Proteomes; UP000196158; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0071885; F:N-terminal protein N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_03223; Methyltr_EFM7; 1.
DR   InterPro; IPR025784; EFM7.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR14614; HEPATOCELLULAR CARCINOMA-ASSOCIATED ANTIGEN; 1.
DR   PANTHER; PTHR14614:SF10; PROTEIN N-TERMINAL AND LYSINE N-METHYLTRANSFERASE EFM7; 1.
DR   Pfam; PF10294; Methyltransf_16; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51560; SAM_MT_NNT1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03223};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03223,
KW   ECO:0000313|EMBL:SMN21259.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196158};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03223};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03223, ECO:0000313|EMBL:SMN21259.1}.
FT   BINDING         62
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03223"
FT   BINDING         88..90
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03223"
FT   BINDING         110
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03223"
FT   BINDING         137
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03223"
FT   BINDING         159
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03223"
SQ   SEQUENCE   247 AA;  28208 MW;  537AD4A6B0CED2AD CRC64;
     MSDIESLNGA LFEEPEDFRP PAPKEHFVTY TRDYIAPESK SQKKDIELKL VGNSPLWGHL
     LWNAGKYTAQ HIDKHPEQIV GKSVLELGAA SALPSIVAGL VGAKNVVSTD YPDADLISNI
     EHNCNGLDNV NVQGYIWGNS YNEILKLNNN EKFDFIILSD LVFNHTEHHK LLKTTRDLLK
     EDGRALVVFS PHRPKLLGDD LKFFDTAKDD YNFKVTKIEM VNWKPMFEED DETIEIRSRV
     YAYYLQL
//