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Database: UniProt
Entry: A0A1E4TD88_9ASCO
LinkDB: A0A1E4TD88_9ASCO
Original site: A0A1E4TD88_9ASCO 
ID   A0A1E4TD88_9ASCO        Unreviewed;       236 AA.
AC   A0A1E4TD88;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
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=CANCADRAFT_28924 {ECO:0000313|EMBL:ODV89725.1};
OS   Tortispora caseinolytica NRRL Y-17796.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Trigonopsidaceae; Tortispora.
OX   NCBI_TaxID=767744 {ECO:0000313|EMBL:ODV89725.1, ECO:0000313|Proteomes:UP000095023};
RN   [1] {ECO:0000313|Proteomes:UP000095023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-17796 {ECO:0000313|Proteomes:UP000095023};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Jeffries T.W., Grigoriev I.V.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (FEB-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; KV453843; ODV89725.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E4TD88; -.
DR   OrthoDB; 2787189at2759; -.
DR   Proteomes; UP000095023; Unassembled WGS sequence.
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   CDD; cd02440; AdoMet_MTases; 1.
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:UP000095023};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03198};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03198}.
FT   BINDING         47
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT   BINDING         81..83
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT   BINDING         103
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT   BINDING         131
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT   BINDING         150
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
SQ   SEQUENCE   236 AA;  26068 MW;  ECC1F68B529ED918 CRC64;
     MLDNGLVPAS EETTSGVVDL DLSDIKPGLT ISIATDGGAS GCGGKIWPAG ELLVKYILFK
     EQQIRSVLSA SGTRPLVLEL GSGTGISGLA VGKLGCADVW ITDQAQMVDL MHQNIVLNNL
     EDIVHAKELN WGEPLPNEIV KRPPAIVLAA DCVYLEPAFP LLEKTLEDLA ALNEECLILM
     AYKKRRKADA KYFKLARKHF ILEEISDFPE YEQYKKDSVR LYRFHLKKRS GTLKTE
//
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