ID Q7RWU0_NEUCR Unreviewed; 311 AA.
AC Q7RWU0;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 24-JAN-2024, entry version 99.
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=NCU00487 {ECO:0000313|EMBL:EAA26936.1};
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110 {ECO:0000313|EMBL:EAA26936.1, ECO:0000313|Proteomes:UP000001805};
RN [1] {ECO:0000313|EMBL:EAA26936.1, ECO:0000313|Proteomes:UP000001805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
RC {ECO:0000313|Proteomes:UP000001805};
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.,
RA FitzHugh W., Ma L.J., Smirnov S., Purcell S., Rehman B., Elkins T.,
RA Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.,
RA Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R., Yarden O.,
RA Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R., Natvig D.O.,
RA Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S.,
RA Lander E.S., Nusbaum C., Birren B.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM002238; EAA26936.1; -; Genomic_DNA.
DR RefSeq; XP_956172.1; XM_951079.2.
DR AlphaFoldDB; Q7RWU0; -.
DR STRING; 367110.Q7RWU0; -.
DR PaxDb; 5141-EFNCRP00000000111; -.
DR EnsemblFungi; EAA26936; EAA26936; NCU00487.
DR GeneID; 3872319; -.
DR KEGG; ncr:NCU00487; -.
DR VEuPathDB; FungiDB:NCU00487; -.
DR HOGENOM; CLU_044783_1_1_1; -.
DR InParanoid; Q7RWU0; -.
DR OrthoDB; 609682at2759; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-UniRule.
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:UP000001805};
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 83..128
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13847"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 311 AA; 34580 MW; 7852B9884739FEB3 CRC64;
MSADNTTPVT TTAGGEKPAH LEPSKLGTKE YWDALYTREI SNHASNPSDE GTVWFDDSDA
ENKIVQFLDE QEHELFSGIL SRDDAAIMDL GCGNGSLLFA LHDDGWEGRL CGVDYSEQSV
ELARRVLRTR VLGEDVPAVE EEGEGEEEQS AAAKEEEGTR QEQDEDVGIE FKVWDVLNGD
FSTVQARPPS SQQPLEGDKN AGWDLVLDKG TFDAVSLSDS RDARGRRICE NYGARVLQLL
RPGGFFLVTS CNWTEEELKG WFETDFAEVY EGTEKKKLGL RQVGRIEYPS FSFGGVKGQT
ISTLCFQKRD I
//
