MTQ2_SCHPO
ID MTQ2_SCHPO Reviewed; 231 AA.
AC Q9UT94;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=eRF1 methyltransferase catalytic subunit mtq2;
DE Short=eRF1 MTase catalytic subunit mtq2;
DE EC=2.1.1.297 {ECO:0000250|UniProtKB:Q03920};
DE AltName: Full=N(5)-glutamine methyltransferase catalytic subunit mtq2;
GN Name=mtq2; ORFNames=SPAC323.05c;
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: Methylates eRF1 on 'Gln-182' using S-adenosyl L-methionine as
CC methyl donor. eRF1 needs to be complexed to eRF3 in its GTP-bound form
CC to be efficiently methylated. {ECO:0000250|UniProtKB:Q03920}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-
CC methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release
CC factor] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42896, Rhea:RHEA-
CC COMP:10271, Rhea:RHEA-COMP:10272, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30011, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61891; EC=2.1.1.297;
CC Evidence={ECO:0000250|UniProtKB:Q03920};
CC -!- SUBUNIT: Heterodimer of mtq2-trm112. mtq2 is the catalytic subunit
CC carrying the catalytic and the S-adenosyl L-methionine binding sites
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal PrmC-related family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB53408.1; -; Genomic_DNA.
DR PIR; T38642; T38642.
DR RefSeq; NP_594375.1; NM_001019796.2.
DR AlphaFoldDB; Q9UT94; -.
DR SMR; Q9UT94; -.
DR BioGRID; 278936; 1.
DR STRING; 4896.SPAC323.05c.1; -.
DR MaxQB; Q9UT94; -.
DR PaxDb; Q9UT94; -.
DR EnsemblFungi; SPAC323.05c.1; SPAC323.05c.1:pep; SPAC323.05c.
DR GeneID; 2542476; -.
DR KEGG; spo:SPAC323.05c; -.
DR PomBase; SPAC323.05c; mtq2.
DR VEuPathDB; FungiDB:SPAC323.05c; -.
DR eggNOG; KOG3191; Eukaryota.
DR HOGENOM; CLU_018398_6_0_1; -.
DR InParanoid; Q9UT94; -.
DR OMA; EWDDWME; -.
DR PhylomeDB; Q9UT94; -.
DR Reactome; R-SPO-156581; Methylation.
DR Reactome; R-SPO-72764; Eukaryotic Translation Termination.
DR PRO; PR:Q9UT94; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0035657; C:eRF1 methyltransferase complex; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008276; F:protein methyltransferase activity; IBA:GO_Central.
DR GO; GO:0102559; F:protein-(glutamine-N5) methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; ISO:PomBase.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0002184; P:cytoplasmic translational termination; ISO:PomBase.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..231
FT /note="eRF1 methyltransferase catalytic subunit mtq2"
FT /id="PRO_0000362148"
FT BINDING 54..58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 130..133
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 231 AA; 25560 MW; FE6FBF6BF3AE81F0 CRC64;
MLSTPVTSQL RLKEFQDVYE PAEDTFALLD ALEKDAKKLR QMAEMKNLLT AEIGCGSGCA
SSFLKSGILK NKPIVHFMSD ISNSACRASK ITALNNRELY KDDNGLFITV QTSFLDGIRL
GNGVDILIFN PPYVPTEFEE IPSEAATIAS AWAGGTDGMD VTSTLLNQLK DILSQDGVFY
MVAVARNKLH SICEILQKDG FIVNETLKRK AGRETLSILR IYRIGNTIWD E
