EFM4_SCHPO
ID EFM4_SCHPO Reviewed; 238 AA.
AC Q9P7Z3; P78819;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Protein-lysine N-methyltransferase efm4 {ECO:0000255|HAMAP-Rule:MF_03188};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03188};
DE AltName: Full=Elongation factor methyltransferase 4 {ECO:0000255|HAMAP-Rule:MF_03188};
DE AltName: Full=Secretion and early endocytosis protein 1 homolog {ECO:0000250|UniProtKB:P40516};
GN Name=see1 {ECO:0000312|PomBase:SPBC839.14c};
GN Synonyms=efm4 {ECO:0000255|HAMAP-Rule:MF_03188};
GN ORFNames=SPBC839.14c {ECO:0000312|PomBase:SPBC839.14c};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 25-238.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
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-lysine N-
CC methyltransferase that mono- and dimethylates elongation factor 1-alpha
CC at 'Lys-316'. May play a role in intracellular transport.
CC {ECO:0000255|HAMAP-Rule:MF_03188}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03188,
CC ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. EFM4 family. {ECO:0000255|HAMAP-Rule:MF_03188}.
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DR EMBL; CU329671; CAB46707.1; -; Genomic_DNA.
DR EMBL; D89168; BAA13830.1; -; mRNA.
DR PIR; T40721; T40721.
DR PIR; T42530; T42530.
DR RefSeq; NP_595254.1; NM_001021160.1.
DR AlphaFoldDB; Q9P7Z3; -.
DR SMR; Q9P7Z3; -.
DR STRING; 4896.SPBC839.14c.1; -.
DR MaxQB; Q9P7Z3; -.
DR PaxDb; Q9P7Z3; -.
DR PRIDE; Q9P7Z3; -.
DR EnsemblFungi; SPBC839.14c.1; SPBC839.14c.1:pep; SPBC839.14c.
DR GeneID; 2541223; -.
DR KEGG; spo:SPBC839.14c; -.
DR PomBase; SPBC839.14c; see1.
DR VEuPathDB; FungiDB:SPBC839.14c; -.
DR eggNOG; KOG1271; Eukaryota.
DR HOGENOM; CLU_044783_1_0_1; -.
DR InParanoid; Q9P7Z3; -.
DR OMA; LGTKQYW; -.
DR PhylomeDB; Q9P7Z3; -.
DR Reactome; R-SPO-8876725; Protein methylation.
DR PRO; PR:Q9P7Z3; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISO:PomBase.
DR GO; GO:0018027; P:peptidyl-lysine dimethylation; IBA:GO_Central.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; IBA:GO_Central.
DR GO; GO:2000765; P:regulation of cytoplasmic translation; NAS:PomBase.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_03188; Methyltr_EFM4; 1.
DR InterPro; IPR026635; Efm4/METTL10.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Transport.
FT CHAIN 1..238
FT /note="Protein-lysine N-methyltransferase efm4"
FT /id="PRO_0000116780"
SQ SEQUENCE 238 AA; 27011 MW; 01AE9FC16DEF2616 CRC64;
MSGLPESKLG TKQYWDNVYE REVSNFTEFN DEGEVWFGEE AEERIVQWLE DHISTSFREV
SEAAPFRVLD LGTGNGHLLF RLLEEEDTLL PSPCQLVGVD YSEAAIVLAK NIARHRQFSD
KVKFQQLDII KDSKFCSKDW DLILDKGTFD AISLSGELLD GRPLNSVYVD RVRGMLSPNG
IFLITSCNWT IQELEERFTK NGFIVHSTVP VPVFEFQGST GSSTSVIAFQ IDPSFNRK
