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Database: UniProt
Entry: EFM7_YARLI
LinkDB: EFM7_YARLI
Original site: EFM7_YARLI 
ID   EFM7_YARLI              Reviewed;         273 AA.
AC   Q6CHE9;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   08-MAY-2019, entry version 83.
DE   RecName: Full=Protein N-terminal and lysine N-methyltransferase EFM7 {ECO:0000255|HAMAP-Rule:MF_03223};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03223};
DE   AltName: Full=Elongation factor methyltransferase 7 {ECO:0000255|HAMAP-Rule:MF_03223};
GN   Name=EFM7 {ECO:0000255|HAMAP-Rule:MF_03223}; Synonyms=NNT1;
GN   OrderedLocusNames=YALI0A09636g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida
OS   lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent protein
CC       methyltransferase that trimethylates the N-terminal glycine 'Gly-
CC       2' of elongation factor 1-alpha, before also catalyzing the
CC       mono- and dimethylation of 'Lys-3'. {ECO:0000255|HAMAP-
CC       Rule:MF_03223}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03223}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. EFM7 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03223}.
DR   EMBL; CR382127; CAG83839.1; -; Genomic_DNA.
DR   RefSeq; XP_499912.1; XM_499912.1.
DR   SMR; Q6CHE9; -.
DR   PRIDE; Q6CHE9; -.
DR   EnsemblFungi; CAG83839; CAG83839; YALI0_A09636g.
DR   GeneID; 2905822; -.
DR   KEGG; yli:YALI0A09636g; -.
DR   HOGENOM; HOG000199189; -.
DR   InParanoid; Q6CHE9; -.
DR   KO; K17878; -.
DR   OMA; FYTHHRP; -.
DR   Proteomes; UP000001300; Chromosome A.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0071885; F:N-terminal protein N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0018013; P:N-terminal peptidyl-glycine methylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0018027; P:peptidyl-lysine dimethylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03223; Methyltr_EFM7; 1.
DR   InterPro; IPR025784; EFM7.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF10294; Methyltransf_16; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51560; SAM_MT_NNT1; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    273       Protein N-terminal and lysine N-
FT                                methyltransferase EFM7.
FT                                /FTId=PRO_0000096900.
FT   REGION       92     94       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_03223}.
FT   BINDING      65     65       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_03223}.
FT   BINDING     114    114       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_03223}.
FT   BINDING     161    161       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_03223}.
FT   BINDING     183    183       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_03223}.
SQ   SEQUENCE   273 AA;  30729 MW;  53976572AA2530CF CRC64;
     MSDIEDLASG GLFDEPKDFY KPEEQPGSDS YARQEKHVAA SEYKEPTNFN LRLTAKNPLW
     GHLLWNAGKV TSDYLDEHSK ELVEGKKVIE FGAGAGLPSL LCHAVGAKQV VITDYPDADL
     LYNLKYNVDQ LKKDWDAKNA DFSGPSPCAD VSSMKVEGFI WGNDASELIE MSGGTGYDLV
     ILSDVVFNHS EHAKLVRSAK ELLAPGGKVF VVFTPHRAKL FNEDLDFFRR AKDEAGFESE
     KLFELKYYPM FEEEEETKEL RSMVFGYMLT LKE
//
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