RRG1_SCHPO
ID RRG1_SCHPO Reviewed; 303 AA.
AC P40389;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protein-lysine N-methyltransferase rrg1 {ECO:0000250|UniProtKB:P38347, ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:P38347};
DE AltName: Full=Elongation factor methyltransferase 2 {ECO:0000250|UniProtKB:P38347};
DE AltName: Full=Rapid response to glucose protein 1 {ECO:0000303|PubMed:11861905};
GN Name=rrg1 {ECO:0000303|PubMed:11861905};
GN Synonyms=uvi22 {ECO:0000303|PubMed:8048925};
GN ORFNames=SPCC338.11c {ECO:0000312|PomBase:SPCC338.11c};
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 [MRNA].
RC STRAIN=JY741;
RX PubMed=8048925; DOI=10.1006/bbrc.1994.2043;
RA Lee J.K., Park E.J., Chung H.K., Hong S.H., Joe C.O., Park S.D.;
RT "Isolation of UV-inducible transcripts from Schizosaccharomyces pombe.";
RL Biochem. Biophys. Res. Commun. 202:1113-1119(1994).
RN [2]
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 [3]
RP INDUCTION.
RX PubMed=11861905; DOI=10.1093/nar/30.5.1145;
RA Kim M.J., Kim J.B., Kim D.S., Park S.D.;
RT "Glucose-inducible expression of rrg1+ in Schizosaccharomyces pombe: post-
RT transcriptional regulation of mRNA stability mediated by the downstream
RT region of the poly(A) site.";
RL Nucleic Acids Res. 30:1145-1153(2002).
RN [4]
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 methylates elongation factor 2 and elongation
CC factor 3A. {ECO:0000250|UniProtKB:P38347}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- INDUCTION: By glucose, sucrose and fructose.
CC {ECO:0000269|PubMed:11861905}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. METTL21 family. {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:8048925) thought to be induced by UV
CC light and alkylating agents. The authors from PubMed:11861905 have
CC found from further investigation that it is induced and regulated by
CC glucose. {ECO:0000305|PubMed:11861905, ECO:0000305|PubMed:8048925}.
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DR EMBL; Z34299; CAA84069.1; -; mRNA.
DR EMBL; CU329672; CAA19342.1; -; Genomic_DNA.
DR PIR; JC2442; JC2442.
DR RefSeq; NP_588157.1; NM_001023146.2.
DR AlphaFoldDB; P40389; -.
DR SMR; P40389; -.
DR BioGRID; 275617; 3.
DR STRING; 4896.SPCC338.11c.1; -.
DR MaxQB; P40389; -.
DR PaxDb; P40389; -.
DR EnsemblFungi; SPCC338.11c.1; SPCC338.11c.1:pep; SPCC338.11c.
DR GeneID; 2539044; -.
DR KEGG; spo:SPCC338.11c; -.
DR PomBase; SPCC338.11c; rrg1.
DR VEuPathDB; FungiDB:SPCC338.11c; -.
DR eggNOG; KOG2793; Eukaryota.
DR HOGENOM; CLU_049351_1_1_1; -.
DR InParanoid; P40389; -.
DR OMA; CWWSIWG; -.
DR PhylomeDB; P40389; -.
DR PRO; PR:P40389; -.
DR Proteomes; UP000002485; Chromosome III.
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:0045182; F:translation regulator activity; ISO:PomBase.
DR GO; GO:0018022; P:peptidyl-lysine methylation; IBA:GO_Central.
DR GO; GO:2000765; P:regulation of cytoplasmic translation; ISO:PomBase.
DR Gene3D; 3.40.50.150; -; 1.
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.
PE 2: Evidence at transcript level;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..303
FT /note="Protein-lysine N-methyltransferase rrg1"
FT /id="PRO_0000097443"
FT BINDING 117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 143..145
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 165
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 198
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
FT BINDING 221
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H867"
SQ SEQUENCE 303 AA; 34534 MW; E8E35F469A59F504 CRC64;
MILEDTDLPL SHEQPSYSQI KDVLDKIPTG EHLWDLPKYE EKIILNWLIK LLATNLEWIT
VEEERDYLVS TICERIAERS GRLAAPTRKR EFSLSNGVSV VLREPTMTYN TLGFKTWGSA
PLLSANLPKW EDLSNSINAL ELGAGTGLVG ISAAIQLGWQ VVCTDLPDIV ENMQYNVDYN
SELIQQYAGS VSCHVLDWMN PPDDDNRPSW LIKPFQRIIA SDCIYETHFG ELAIALFRKY
LAKDGIVITE YPLRETHLEE IGVFEKGMDA AGFERQMGEE IGEEDFGSLY PVTCRWSRWK
YHG
