ID Q96259_ARATH Unreviewed; 317 AA.
AC Q96259;
DT 01-FEB-1997, integrated into UniProtKB/TrEMBL.
DT 01-FEB-1997, sequence version 1.
DT 27-MAR-2024, entry version 103.
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 Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000313|EMBL:BAA13688.1};
RN [1] {ECO:0000313|EMBL:BAA13688.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9287109; DOI=10.1016/S0014-5793(97)00871-5;
RA Hirayama T., Ishida C., Kuromori T., Obata S., Shimoda C., Yamamoto M.,
RA Shinozaki K., Ohto C.;
RT "Functional cloning of a cDNA encoding Mei2-like protein from Arabidopsis
RT thaliana using a fission yeast pheromone receptor deficient mutant.";
RL FEBS Lett. 413:16-20(1997).
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 EMBL; D88747; BAA13688.1; -; mRNA.
DR AlphaFoldDB; Q96259; -.
DR TAIR; AT1G66680; -.
DR ExpressionAtlas; Q96259; baseline and differential.
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 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 2: Evidence at transcript level;
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 172..293
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 317 AA; 34808 MW; C9243C3380371586 CRC64;
MAGIRLLPEE PETTPQQQAR AAAAVTTTTT DSLASDDDRS IAADSWSIKS EYGSTLDDDQ
RHADAAEALS SANFRVSSDY SSDKEEPDAD GGGQSMLGLQ SYWDAAYSDE LTNFREHGHA
GEVWFGDDVM EIVTSWTKDL CVEISQRNMS VSENDVTTEV NDQADKYLSS WNVLDLGTGN
GLLLHQLAKE GFSDLTGTDY SDGAVELAQH LSQRDGFPNI RFMVDDILDT KLEQQFKLVM
DKGTLDAIGL HPDGPVKRVM YWDSVSKLVA PGGILVITSC NHTKDELVEE VENFNIRKSN
LCRGDGNDAN NVLSLWL
//
