ID G3AL17_SPAPN Unreviewed; 244 AA.
AC G3AL17;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=SPAPADRAFT_55010 {ECO:0000313|EMBL:EGW33060.1};
OS Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN [1] {ECO:0000313|EMBL:EGW33060.1, ECO:0000313|Proteomes:UP000000709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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; GL996501; EGW33060.1; -; Genomic_DNA.
DR RefSeq; XP_007374575.1; XM_007374513.1.
DR AlphaFoldDB; G3AL17; -.
DR STRING; 619300.G3AL17; -.
DR GeneID; 18871904; -.
DR KEGG; spaa:SPAPADRAFT_55010; -.
DR eggNOG; KOG1271; Eukaryota.
DR HOGENOM; CLU_044783_1_0_1; -.
DR InParanoid; G3AL17; -.
DR OMA; YWEDAYQ; -.
DR OrthoDB; 609682at2759; -.
DR Proteomes; UP000000709; 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:UP000000709};
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 69..215
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
SQ SEQUENCE 244 AA; 27747 MW; FCE8AE17BDD9F939 CRC64;
MTEDIRLNSS KLGTQEYWNN FYKKEQSNFQ DNDEDTGECW FDDSDAESKM IQFLIDKLND
GELPVTETPH IRMLDLGTGN GHLLFQLSQD LSEEYEGDSE FQFIGIDYSP DSVEFAKDIA
GKKYGDVNFE FEQVDLLQKE APFLKNKFDI LLDKGTLDAI ALNQDPLQEF DGEIGMDVYA
RQVEQLMNKG SILLITSCNF TETELVKIIT TGTNLQVWDK INYPSFQFGG VKGSTVCSIA
FIKD
//
