(data stored in ACNUC8465 zone)

SWISSPROT: EFM7_CANGA

ID   EFM7_CANGA              Reviewed;         256 AA.
AC   Q6FJ22;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 67.
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=CAGL0M09801g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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 mono-
CC       and dimethylation of 'Lys-3'. {ECO:0000255|HAMAP-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; CR380959; CAG62750.1; -; Genomic_DNA.
DR   RefSeq; XP_449772.1; XM_449772.1.
DR   ProteinModelPortal; Q6FJ22; -.
DR   STRING; 284593.XP_449772.1; -.
DR   EnsemblFungi; CAG62750; CAG62750; CAGL0M09801g.
DR   KEGG; cgr:CAGL0M09801g; -.
DR   CGD; CAL0136847; CAGL0M09801g.
DR   EuPathDB; FungiDB:CAGL0M09801g; -.
DR   eggNOG; KOG2920; Eukaryota.
DR   eggNOG; ENOG4111NE8; LUCA.
DR   HOGENOM; HOG000199189; -.
DR   InParanoid; Q6FJ22; -.
DR   KO; K17878; -.
DR   OMA; VVFSPHR; -.
DR   OrthoDB; EOG092C4ME2; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0071885; F:N-terminal protein N-methyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0000183; P:chromatin silencing at rDNA; IEA:EnsemblFungi.
DR   GO; GO:0018013; P:N-terminal peptidyl-glycine methylation; IEA:EnsemblFungi.
DR   GO; GO:0018027; P:peptidyl-lysine dimethylation; IEA:EnsemblFungi.
DR   HAMAP; MF_03223; Methyltr_EFM7; 1.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR025784; Nicotinamide_N-MeTfrase_put.
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;
DR   PRODOM; Q6FJ22.
DR   SWISS-2DPAGE; Q6FJ22.
KW   Complete proteome; Cytoplasm; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    256       Protein N-terminal and lysine N-
FT                                methyltransferase EFM7.
FT                                /FTId=PRO_0000096892.
FT   REGION       90     92       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_03223}.
FT   BINDING      64     64       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_03223}.
FT   BINDING     112    112       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_03223}.
FT   BINDING     145    145       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_03223}.
FT   BINDING     168    168       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_03223}.
SQ   SEQUENCE   256 AA;  29176 MW;  3EA9B15469C66D21 CRC64;
     MSDTESLNDA LGLFDEPEDF RPEKPKEHYA NYERIDVPDI SKSKITNLKL QLVGSSPLWG
     HLLWNAGIYT ARHLDKYPEL VSNKNVLELG AASALPSLVA GLIGAKRAVV TDYPDADLMA
     NIQYNVNTII PDELKENVRV EGYIWGNEYD PLTIHLDGDK KFDLIILSDL VFNHNQHDKL
     LQTTKDLLAT NGKALVVFSP HRPHLLEADL QFFETCKEYG LTPEKIEMVN WKPMFEEDEE
     TAEVRSRVYA YYMTHA
//

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