EFM7_YEAST
ID EFM7_YEAST Reviewed; 261 AA.
AC Q05874; D6VYS9;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein N-terminal and lysine N-methyltransferase EFM7 {ECO:0000255|HAMAP-Rule:MF_03223, ECO:0000305|PubMed:26545399};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03223, ECO:0000269|PubMed:21858014, ECO:0000269|PubMed:26545399};
DE AltName: Full=Elongation factor methyltransferase 7 {ECO:0000255|HAMAP-Rule:MF_03223, ECO:0000303|PubMed:26545399};
DE AltName: Full=Nicotinamide N-methyltransferase-like protein 1 {ECO:0000303|PubMed:12736687};
GN Name=NNT1 {ECO:0000303|PubMed:12736687};
GN Synonyms=EFM7 {ECO:0000255|HAMAP-Rule:MF_03223,
GN ECO:0000303|PubMed:26545399};
GN OrderedLocusNames=YLR285W {ECO:0000312|SGD:S000004275};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION.
RX PubMed=12736687; DOI=10.1038/nature01578;
RA Anderson R.M., Bitterman K.J., Wood J.G., Medvedik O., Sinclair D.A.;
RT "Nicotinamide and PNC1 govern lifespan extension by calorie restriction in
RT Saccharomyces cerevisiae.";
RL Nature 423:181-185(2003).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=21858014; DOI=10.1371/journal.pone.0023168;
RA Wlodarski T., Kutner J., Towpik J., Knizewski L., Rychlewski L.,
RA Kudlicki A., Rowicka M., Dziembowski A., Ginalski K.;
RT "Comprehensive structural and substrate specificity classification of the
RT Saccharomyces cerevisiae methyltransferome.";
RL PLoS ONE 6:E23168-E23168(2011).
RN [8]
RP FUNCTION.
RX PubMed=26545399; DOI=10.1074/mcp.m115.052449;
RA Hamey J.J., Winter D.L., Yagoub D., Overall C.M., Hart-Smith G.,
RA Wilkins M.R.;
RT "Novel N-terminal and lysine methyltransferases that target translation
RT elongation factor 1A in yeast and human.";
RL Mol. Cell. Proteomics 15:164-176(2016).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein methyltransferase
CC that trimethylates the N-terminal glycine 'Gly-2' of elongation factor
CC 1-alpha (TEF1 and TEF2), before also catalyzing the mono- and
CC dimethylation of 'Lys-3' (PubMed:21858014, PubMed:26545399). May be
CC involved in rDNA silencing and in lifespan determination
CC (PubMed:12736687). {ECO:0000255|HAMAP-Rule:MF_03223,
CC ECO:0000269|PubMed:12736687, ECO:0000269|PubMed:21858014,
CC ECO:0000269|PubMed:26545399}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03223,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 7280 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. EFM7 family. {ECO:0000255|HAMAP-Rule:MF_03223}.
CC -!- CAUTION: Was originally thought to be a nicotinamide N-
CC methyltransferase. {ECO:0000305|PubMed:12736687}.
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DR EMBL; U17243; AAB67330.1; -; Genomic_DNA.
DR EMBL; AY693038; AAT93057.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09595.1; -; Genomic_DNA.
DR PIR; S50370; S50370.
DR RefSeq; NP_013387.1; NM_001182172.1.
DR AlphaFoldDB; Q05874; -.
DR SMR; Q05874; -.
DR BioGRID; 31550; 72.
DR DIP; DIP-2117N; -.
DR STRING; 4932.YLR285W; -.
DR MaxQB; Q05874; -.
DR PaxDb; Q05874; -.
DR PRIDE; Q05874; -.
DR EnsemblFungi; YLR285W_mRNA; YLR285W; YLR285W.
DR GeneID; 850991; -.
DR KEGG; sce:YLR285W; -.
DR SGD; S000004275; NNT1.
DR VEuPathDB; FungiDB:YLR285W; -.
DR eggNOG; KOG2920; Eukaryota.
DR HOGENOM; CLU_032409_0_0_1; -.
DR InParanoid; Q05874; -.
DR OMA; YQPWLLP; -.
DR BioCyc; YEAST:G3O-32380-MON; -.
DR BRENDA; 2.1.1.244; 984.
DR PRO; PR:Q05874; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q05874; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0071885; F:N-terminal protein N-methyltransferase activity; IDA:SGD.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:SGD.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:SGD.
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 GO; GO:0000183; P:rDNA heterochromatin assembly; IMP:SGD.
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 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..261
FT /note="Protein N-terminal and lysine N-methyltransferase
FT EFM7"
FT /id="PRO_0000096901"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 64
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q5VZV1, ECO:0000255|HAMAP-
FT Rule:MF_03223"
FT BINDING 90..92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q5VZV1, ECO:0000255|HAMAP-
FT Rule:MF_03223"
FT BINDING 112
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q5VZV1, ECO:0000255|HAMAP-
FT Rule:MF_03223"
FT BINDING 144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q5VZV1, ECO:0000255|HAMAP-
FT Rule:MF_03223"
FT BINDING 171
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q5VZV1, ECO:0000255|HAMAP-
FT Rule:MF_03223"
SQ SEQUENCE 261 AA; 29633 MW; 74AC77E39ED55387 CRC64;
MSDIESLGEA AGLFEEPEDF LPPPPKPHFA EYQRSHITKE SKSDVKDIKL RLVGTSPLWG
HLLWNAGIYT ANHLDSHPEL IKGKTVLELG AAAALPSVIC ALNGAQMVVS TDYPDPDLMQ
NIDYNIKSNV PEDFNNVSTE GYIWGNDYSP LLAHIEKIGN NNGKFDLIIL SDLVFNHTEH
HKLLQTTKDL LAEKGQALVV FSPHRPKLLE KDLEFFELAK NEFHLVPQLI EMVNWKPMFD
EDEETIEVRS RVYAYYLTHE K
