ID A0A074XDN5_AURPU Unreviewed; 223 AA.
AC A0A074XDN5;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=M438DRAFT_399101 {ECO:0000313|EMBL:KEQ81849.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ81849.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ81849.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ81849.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584990; KEQ81849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074XDN5; -.
DR STRING; 1043002.A0A074XDN5; -.
DR HOGENOM; CLU_055721_2_1_1; -.
DR OrthoDB; 2787189at2759; -.
DR Proteomes; UP000030706; 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:UP000030706};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03198};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03198}.
FT BINDING 57
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT BINDING 84..86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT BINDING 108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT BINDING 136
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
FT BINDING 154
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03198"
SQ SEQUENCE 223 AA; 25220 MW; CBD89769C4AB961E CRC64;
MSLSDDERNG VFGIGEELVP VRELKQAGVM ELDFDGLLST PLRLEEDLKK GCGGMLWPAG
MVMGKYLMRQ DRNTFMDKSI VELGAGGGLV GLAVALKFQP DQPLQITDQI PMFALMERNI
ALNDLQDRVK PSIYDWGEAV PEGIPQHPDI ILAAECVYFE PAFPLLQQTM KDLIGPNTVC
YFCFKKRRRA DMNFVKVMKK MFVVEPIEDD PDKPKWSREN LHL
//
