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Database: UniProt
Entry: G8JR47_ERECY
LinkDB: G8JR47_ERECY
Original site: G8JR47_ERECY 
ID   G8JR47_ERECY            Unreviewed;       274 AA.
AC   G8JR47;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
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   OrderedLocusNames=Ecym_3108 {ECO:0000313|EMBL:AET38616.1};
OS   Eremothecium cymbalariae (strain CBS 270.75 / DBVPG 7215 / KCTC 17166 /
OS   NRRL Y-17582) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=931890 {ECO:0000313|EMBL:AET38616.1, ECO:0000313|Proteomes:UP000006790};
RN   [1] {ECO:0000313|Proteomes:UP000006790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582
RC   {ECO:0000313|Proteomes:UP000006790};
RX   DOI=10.1534/g3.111.000745;
RA   Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA   Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA   Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA   Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA   Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA   Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA   Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA   Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT   "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT   genome resolution following polyploidization.";
RL   G3 (Bethesda) 2:299-311(2012).
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; CP002499; AET38616.1; -; Genomic_DNA.
DR   RefSeq; XP_003645433.1; XM_003645385.1.
DR   AlphaFoldDB; G8JR47; -.
DR   STRING; 931890.G8JR47; -.
DR   GeneID; 11468680; -.
DR   KEGG; erc:Ecym_3108; -.
DR   eggNOG; KOG2920; Eukaryota.
DR   HOGENOM; CLU_032409_0_0_1; -.
DR   InParanoid; G8JR47; -.
DR   OMA; VGHNPLW; -.
DR   OrthoDB; 5470823at2759; -.
DR   Proteomes; UP000006790; Chromosome 3.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000006790};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03223};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03223}.
FT   BINDING         66
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03223"
FT   BINDING         92..94
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03223"
FT   BINDING         114
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03223"
FT   BINDING         161
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03223"
FT   BINDING         185
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03223"
SQ   SEQUENCE   274 AA;  30986 MW;  CDFDCD50C5F21C06 CRC64;
     MDVEEKDIIG DSGGLFAEPE DFYGSQPECH FTKYVREEIS ESSKSKVKEV AVRLVGSSPL
     WGHILWNSGI YTAKHLDKHV EECKNKCVLE LGAAGALPSL ISGLIGANKV VCTDYPDADL
     ISNMQYNVDH ALYSGESLSR DSMLLKKQLG ERNVIVEGYI WGNDYSNLVK HLPGGQNKFD
     LIILSDLVFN HTEHHKLLRT TKDLLADDGK ALVVFSPHRP WLLEKDLGFF ETAKEYSLKS
     ELIEIAHWRP MFEQDPGSEE IRSRVYAYYL IHDT
//
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