EFM7_SCHPO
ID EFM7_SCHPO Reviewed; 255 AA.
AC Q9UT28;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=nnt1 {ECO:0000250|UniProtKB:Q05874};
GN Synonyms=efm7 {ECO:0000255|HAMAP-Rule:MF_03223};
GN ORFNames=SPAC8F11.09c {ECO:0000312|PomBase:SPAC8F11.09c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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; CU329670; CAB52170.1; -; Genomic_DNA.
DR PIR; T39184; T39184.
DR RefSeq; NP_593958.1; NM_001019385.2.
DR AlphaFoldDB; Q9UT28; -.
DR SMR; Q9UT28; -.
DR STRING; 4896.SPAC8F11.09c.1; -.
DR iPTMnet; Q9UT28; -.
DR MaxQB; Q9UT28; -.
DR PaxDb; Q9UT28; -.
DR EnsemblFungi; SPAC8F11.09c.1; SPAC8F11.09c.1:pep; SPAC8F11.09c.
DR GeneID; 2543599; -.
DR KEGG; spo:SPAC8F11.09c; -.
DR PomBase; SPAC8F11.09c; nnt1.
DR VEuPathDB; FungiDB:SPAC8F11.09c; -.
DR eggNOG; KOG2920; Eukaryota.
DR HOGENOM; CLU_032409_0_0_1; -.
DR InParanoid; Q9UT28; -.
DR OMA; YQPWLLP; -.
DR PhylomeDB; Q9UT28; -.
DR PRO; PR:Q9UT28; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0071885; F:N-terminal protein N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008112; F:nicotinamide N-methyltransferase activity; ISO:PomBase.
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:0006769; P:nicotinamide metabolic process; ISO:PomBase.
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..255
FT /note="Protein N-terminal and lysine N-methyltransferase
FT efm7"
FT /id="PRO_0000096899"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
FT BINDING 84..86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
FT BINDING 106
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
FT BINDING 137
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
FT BINDING 162
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03223"
SQ SEQUENCE 255 AA; 28490 MW; 8E16DB39F6173EA0 CRC64;
MADNDFEGFG IFEEPEGFRP STPPPKEVLH TRVIVPNGPE EIKLRLVGSH SLWAHYLWNS
GIELANYIDK NPDTVRAKKV LELGAGAGLP SIVSAFDGAK FVVSTDYPDP ALIDNLEHNV
KQYAEIASKI SAVGYLWGSN IKEVMSNAGF KDNEVFDILL LSDLVFNHTE HSKLIKSCKM
AIEGNPNAVV YVFFTHHRPH LAKKDMIFFD IAQSEGFQIE KILEEKRTPM FEEDPGAPEI
RATVHGYKMT IPIPV
