ID A0A197JC13_9FUNG Unreviewed; 280 AA.
AC A0A197JC13;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Protein-lysine N-methyltransferase EFM4 {ECO:0000256|HAMAP-Rule:MF_03188};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03188};
DE AltName: Full=Elongation factor methyltransferase 4 {ECO:0000256|HAMAP-Rule:MF_03188};
GN Name=EFM4 {ECO:0000256|HAMAP-Rule:MF_03188};
GN ORFNames=K457DRAFT_143270 {ECO:0000313|EMBL:OAQ22640.1};
OS Linnemannia elongata AG-77.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ22640.1, ECO:0000313|Proteomes:UP000078512};
RN [1] {ECO:0000313|EMBL:OAQ22640.1, ECO:0000313|Proteomes:UP000078512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-77 {ECO:0000313|EMBL:OAQ22640.1,
RC ECO:0000313|Proteomes:UP000078512};
RG DOE Joint Genome Institute;
RA Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA Bonito G.;
RT "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT the earliest lineages of terrestrial Fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC methyltransferase that mono- and dimethylates elongation factor 1-alpha
CC at 'Lys-316'. May play a role in intracellular transport.
CC {ECO:0000256|HAMAP-Rule:MF_03188}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03188}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. EFM4 family. {ECO:0000256|HAMAP-Rule:MF_03188}.
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DR EMBL; KV442150; OAQ22640.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A197JC13; -.
DR STRING; 1314771.A0A197JC13; -.
DR OrthoDB; 609682at2759; -.
DR Proteomes; UP000078512; 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 GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_03188; Methyltr_EFM4; 1.
DR InterPro; IPR026635; Efm4/METTL10.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12843:SF5; EEF1A LYSINE METHYLTRANSFERASE 2; 1.
DR PANTHER; PTHR12843; PROTEIN-LYSINE N-METHYLTRANSFERASE METTL10; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03188};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_03188}; Reference proteome {ECO:0000313|Proteomes:UP000078512};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_03188};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03188}; Transport {ECO:0000256|HAMAP-Rule:MF_03188}.
FT DOMAIN 65..253
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
SQ SEQUENCE 280 AA; 31365 MW; 5833C09A2470705C CRC64;
MSDEAAIPQP DFKPSKLGTK DYWDKVYNRE VINFKDHGDI GEIWFGEDSA VKMVDWVEEH
YEGEKETCAI LDLGCGNGHL LLDLAELGFE DLTGIDYSPA AIELAKAVAE DKEVDHIIKY
EAVDFLAEKE TLEWCAQQAT PGSDSHGEPK KFKVMLDKGT YDAISLHQKS KADAVAAAAA
ANADADSGER EDEESVAKDN IVLAENDDNM EELADRYPKR VASMMRDDGR LLITSCNWTQ
PELIQRFSQY FEYDCHLKYP TFTFGGVKGQ TISSVVFRKK
//
