ID A0A1V8SVD0_9PEZI Unreviewed; 254 AA.
AC A0A1V8SVD0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=B0A48_11368 {ECO:0000313|EMBL:OQO03113.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO03113.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQO03113.1}.
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DR EMBL; NAJO01000025; OQO03113.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8SVD0; -.
DR STRING; 1507870.A0A1V8SVD0; -.
DR InParanoid; A0A1V8SVD0; -.
DR OrthoDB; 609682at2759; -.
DR Proteomes; UP000192596; 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:UP000192596};
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 76..200
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 254 AA; 28396 MW; 682AF6188D895345 CRC64;
MSTPSPPAEG NPRLLDPSEL GTKDYWNKAY TRELSNHATA PDDEGTIWFD ESNAEDAVCR
LLDRLEEEGH FERATARVLD LGTGNGHMLF TLREEEWEGE LVGVDYSATS VELARRIEEA
RQLDDGMGVR FEEWDMLVQP PGDWCGRGGF DVVLDKGTFD AISLMPREAD EVAVSDVYRR
TAEGLVKTDG LLVVTSCNWT KVELCGWLAP EEGNLEFLQE AKYPSFKFGG RTGQSVVTIA
FRKKSATLED HELI
//
