ID   EFM3_CHATD              Reviewed;         336 AA.
AC   P0CU27; G0SAE3;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=Protein-lysine N-methyltransferase EFM3 {ECO:0000250|UniProtKB:P47163};
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:P47163};
DE   AltName: Full=Elongation factor methyltransferase 3 {ECO:0000250|UniProtKB:P47163};
GN   ORFNames=CTHT_0041970.1;
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=759272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA   Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC       methyltransferase that methylates elongation factor 2.
CC       {ECO:0000250|UniProtKB:P47163}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P47163}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. EEF2KMT family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EGS19715.1; Type=Erroneous gene model prediction; Note=The predicted gene CTHT_0041970 has been split into 2 genes: CTHT_0041970.1 and CTHT_0041970.2.; Evidence={ECO:0000305};
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DR   EMBL; GL988043; EGS19715.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; P0CU27; -.
DR   SMR; P0CU27; -.
DR   STRING; 759272.P0CU27; -.
DR   EnsemblFungi; EGS19715; EGS19715; CTHT_0041970.
DR   eggNOG; KOG2497; Eukaryota.
DR   eggNOG; KOG3424; Eukaryota.
DR   OrthoDB; 958308at2759; -.
DR   Proteomes; UP000008066; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006479; P:protein methylation; IEA:UniProt.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR14614; PTHR14614; 1.
DR   Pfam; PF10294; Methyltransf_16; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00529; RIBOSOMAL_S24E; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..336
FT                   /note="Protein-lysine N-methyltransferase EFM3"
FT                   /id="PRO_0000437792"
FT   BINDING         147
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   BINDING         173..175
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   BINDING         196
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   BINDING         232
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
FT   BINDING         251
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H867"
SQ   SEQUENCE   336 AA;  37265 MW;  811F0352628B4FBE CRC64;
     MVASRNPQTA RFCWQYLQLE QSLDFPDGEL LRDEAVQETI YQQLFAPNAP TPLPPARYRL
     RVLKELTSRI ESAIEDWETH GISDNLMDAM AELVAQPLPS EAEAAQERCY VTYYLSLLEG
     GLEKPHITLL ESRSLISASG TTGLRTWEAA LHLGQFLSVN SGLVKDKRVL ELGTGTGYLA
     VLCAKYLGTS HVIASDGSEE VVEKLSDNLF VNGLQDSDKV QPMELKWGHA LLGTEEEHWN
     GGRKIDVVLG ADITYDVSVI PALIATLEEL VDLYPGISII IAATERNRET YETFLAACGR
     RGFSVTPESF PVPSRAEQKG PFYKDGTPIH ICQLRR