ID B6Q2Q4_TALMQ Unreviewed; 267 AA.
AC B6Q2Q4;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=PMAA_028300 {ECO:0000313|EMBL:EEA28003.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA28003.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; DS995899; EEA28003.1; -; Genomic_DNA.
DR RefSeq; XP_002144518.1; XM_002144482.1.
DR AlphaFoldDB; B6Q2Q4; -.
DR STRING; 441960.B6Q2Q4; -.
DR VEuPathDB; FungiDB:PMAA_028300; -.
DR HOGENOM; CLU_055721_2_1_1; -.
DR OrthoDB; 2787189at2759; -.
DR PhylomeDB; B6Q2Q4; -.
DR Proteomes; UP000001294; 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 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:UP000001294};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03198};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03198}.
FT BINDING 90
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT BINDING 117..119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT BINDING 141
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT BINDING 169
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT BINDING 187
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
SQ SEQUENCE 267 AA; 29703 MW; 5C4A169A46DCC202 CRC64;
MEETNVASPA QQRIPNTIED AEITNTYFSF TEPSSPADDP DNSQLLIGES LIPVRERRHA
GTTVVSIDGL LKEPLQLKED LKEGCGGQLW PAGLLLSRYM LEEHATDLVG KTIVELGAGG
GLVGLAVARG CQTDKPIYVT DQKPMMQLMA DNISLNGLST KVKPVLLDWA ESPPAEIPEH
PEIVLAADCV YFEPAFPLLI STLQRLLGPD TICYFCFKRR RRADLRCIKM VKKLFNVTEV
NSFSTCDGYN RENLFLYKIQ SRQKSKD
//
