ID A0A1I8GDJ3_9PLAT Unreviewed; 362 AA.
AC A0A1I8GDJ3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Protein-lysine N-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03188};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03188};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0001576-snap-gene-0.2-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0001576-snap-gene-0.2-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC methyltransferase that methylates elongation factor 1-alpha.
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 AlphaFoldDB; A0A1I8GDJ3; -.
DR WBParaSite; maker-uti_cns_0001576-snap-gene-0.2-mRNA-1; maker-uti_cns_0001576-snap-gene-0.2-mRNA-1; maker-uti_cns_0001576-snap-gene-0.2.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; 1.10.1530.10; -; 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; IPR043144; Mal/L-sulf/L-lact_DH-like_ah.
DR InterPro; IPR036111; Mal/L-sulfo/L-lacto_DH-like_sf.
DR InterPro; IPR003767; Malate/L-lactate_DH-like.
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; PF02615; Ldh_2; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF89733; L-sulfolactate dehydrogenase-like; 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};
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}.
FT DOMAIN 103..158
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 362 AA; 39248 MW; BA06B281C680AADA CRC64;
QTFQSRAASE APAGDNDPAS SSLSLDSDCI DPEPSQLGRR DYWQRFYGQE LANYLDEAAA
NDEEGGSGDD RGEVWFGAAA EQRLVSYVER RLNAIRDACP TQQLAVVDIG CGNGHLALRL
AANSHLLTGL SRLLCLDYSE PAIELTNRLA SKAGVSDLVI ARLLDVTEPG AAASALEFLR
APDSNIHYPN LLLLDKGTYD AISLCPDNSQ GKRFAYRQFA VKLLDSVANS NNQLVVASCN
WTETELIAQF SDQFKHVETL PGRAFKFGGA VGADVTTVKS RMSAMTTEKL VPESEVTRLV
IECMRWAGAD STHAARLAEI LLSADRRGHY SHGINRLDVY VRDVRAGVTQ GSGEPAILKE
TA
//
