EFM7_ASHGO
ID EFM7_ASHGO Reviewed; 265 AA.
AC Q74ZB5;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=AGR284W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein methyltransferase
CC that trimethylates the N-terminal glycine 'Gly-2' of elongation factor
CC 1-alpha, before also catalyzing the mono- and dimethylation of 'Lys-3'.
CC {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 methyltransferase
CC superfamily. EFM7 family. {ECO:0000255|HAMAP-Rule:MF_03223}.
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DR EMBL; AE016820; AAS54774.1; -; Genomic_DNA.
DR RefSeq; NP_986950.1; NM_212012.1.
DR AlphaFoldDB; Q74ZB5; -.
DR SMR; Q74ZB5; -.
DR STRING; 33169.AAS54774; -.
DR EnsemblFungi; AAS54774; AAS54774; AGOS_AGR284W.
DR GeneID; 4623252; -.
DR KEGG; ago:AGOS_AGR284W; -.
DR eggNOG; KOG2920; Eukaryota.
DR HOGENOM; CLU_032409_0_0_1; -.
DR InParanoid; Q74ZB5; -.
DR OMA; YQPWLLP; -.
DR Proteomes; UP000000591; Chromosome VII.
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; IBA:GO_Central.
DR GO; GO:0018013; P:N-terminal peptidyl-glycine methylation; IEA:UniProtKB-UniRule.
DR GO; GO:0018027; P:peptidyl-lysine dimethylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_03223; Methyltr_EFM7; 1.
DR InterPro; IPR025784; EFM7.
DR InterPro; IPR019410; Methyltransf_16.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR14614; PTHR14614; 1.
DR Pfam; PF10294; Methyltransf_16; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51560; SAM_MT_NNT1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..265
FT /note="Protein N-terminal and lysine N-methyltransferase
FT EFM7"
FT /id="PRO_0000096889"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 67
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
FT BINDING 93..95
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
FT BINDING 115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
FT BINDING 152
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
FT BINDING 176
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
SQ SEQUENCE 265 AA; 29379 MW; 606D6F1F87AFED1A CRC64;
MSSDHEEDSL YGATELFGEP DGFYEKPAES HFAEYERSAV PAQSARRDTQ VRIRLVGSSP
LWGHLLWNSA IYTARHLDAH PEQVVGRCVL ELGAAGALPS LVAGLLGARQ VVATDYPDAD
LVGNIQYNVD HVIYGGKPPT EAPHVAVEGY IWGNDYGPLR RHLPPGQTGF DLVLLSDLVF
NHTEHHKLLQ TTRDLLAPAG RALVVFSPHR PWLLEKDLQF FETAAEYGLR AELIEQVTWA
PMFADDPGPA EVRARVYAYY LTHCA
