MTQ2_YEAST
ID MTQ2_YEAST Reviewed; 221 AA.
AC Q03920; D6VSC3;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=eRF1 methyltransferase catalytic subunit MTQ2;
DE Short=eRF1 MTase catalytic subunit MTQ2;
DE EC=2.1.1.297 {ECO:0000269|PubMed:15509572};
DE AltName: Full=N(5)-glutamine methyltransferase MTQ2;
GN Name=MTQ2; Synonyms=MTC6; OrderedLocusNames=YDR140W;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 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 [5]
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 [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15509572; DOI=10.1074/jbc.m407252200;
RA Heurgue-Hamard V., Champ S., Mora L., Merkulova-Rainon T., Kisselev L.L.,
RA Buckingham R.H.;
RT "The glutamine residue of the conserved GGQ motif in Saccharomyces
RT cerevisiae release factor eRF1 is methylated by the product of the YDR140w
RT gene.";
RL J. Biol. Chem. 280:2439-2445(2005).
RN [7]
RP INTERACTION WITH TRM112.
RX PubMed=15899842; DOI=10.1128/mcb.25.11.4359-4370.2005;
RA Purushothaman S.K., Bujnicki J.M., Grosjean H., Lapeyre B.;
RT "Trm11p and Trm112p are both required for the formation of 2-
RT methylguanosine at position 10 in yeast tRNA.";
RL Mol. Cell. Biol. 25:4359-4370(2005).
RN [8]
RP FUNCTION.
RX PubMed=16321977; DOI=10.1074/jbc.m507651200;
RA Polevoda B., Span L., Sherman F.;
RT "The yeast translation release factors Mrf1p and Sup45p (eRF1) are
RT methylated, respectively, by the methyltransferases Mtq1p and Mtq2p.";
RL J. Biol. Chem. 281:2562-2571(2006).
RN [9]
RP FUNCTION, AND INTERACTION WITH TRM112.
RX PubMed=17008308; DOI=10.1074/jbc.m608571200;
RA Heurgue-Hamard V., Graille M., Scrima N., Ulryck N., Champ S.,
RA van Tilbeurgh H., Buckingham R.H.;
RT "The zinc finger protein Ynr046w is plurifunctional and a component of the
RT eRF1 methyltransferase in yeast.";
RL J. Biol. Chem. 281:36140-36148(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:0000269|PubMed:15509572,
CC ECO:0000269|PubMed:16321977, ECO:0000269|PubMed:17008308}.
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:0000269|PubMed:15509572};
CC -!- SUBUNIT: Heterodimer of MTQ2-TRM112. MTQ2 is the catalytic subunit
CC carrying the catalytic and the S-adenosyl L-methionine binding sites.
CC -!- INTERACTION:
CC Q03920; P53738: TRM112; NbExp=3; IntAct=EBI-31378, EBI-28520;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3390 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal PrmC-related family.
CC {ECO:0000305}.
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DR EMBL; Z48179; CAA88222.1; -; Genomic_DNA.
DR EMBL; AY557676; AAS56002.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11983.1; -; Genomic_DNA.
DR PIR; S51868; S51868.
DR RefSeq; NP_010424.3; NM_001180447.3.
DR AlphaFoldDB; Q03920; -.
DR SMR; Q03920; -.
DR BioGRID; 32194; 187.
DR ComplexPortal; CPX-418; MTQ2-TRM112 eRF1 methyltransferase complex.
DR DIP; DIP-1755N; -.
DR IntAct; Q03920; 5.
DR MINT; Q03920; -.
DR STRING; 4932.YDR140W; -.
DR MaxQB; Q03920; -.
DR PaxDb; Q03920; -.
DR PRIDE; Q03920; -.
DR EnsemblFungi; YDR140W_mRNA; YDR140W; YDR140W.
DR GeneID; 851718; -.
DR KEGG; sce:YDR140W; -.
DR SGD; S000002547; MTQ2.
DR VEuPathDB; FungiDB:YDR140W; -.
DR eggNOG; KOG3191; Eukaryota.
DR GeneTree; ENSGT00390000013073; -.
DR HOGENOM; CLU_018398_6_0_1; -.
DR InParanoid; Q03920; -.
DR OMA; EWDDWME; -.
DR BioCyc; MetaCyc:G3O-29737-MON; -.
DR BioCyc; YEAST:G3O-29737-MON; -.
DR Reactome; R-SCE-156581; Methylation.
DR Reactome; R-SCE-72764; Eukaryotic Translation Termination.
DR PRO; PR:Q03920; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03920; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0035657; C:eRF1 methyltransferase complex; IPI:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005840; C:ribosome; IC:ComplexPortal.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008276; F:protein methyltransferase activity; IDA:SGD.
DR GO; GO:0102559; F:protein-(glutamine-N5) methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:SGD.
DR GO; GO:0018364; P:peptidyl-glutamine methylation; IDA:SGD.
DR GO; GO:0060566; P:positive regulation of DNA-templated transcription, termination; IC:ComplexPortal.
DR GO; GO:0006417; P:regulation of translation; IDA:SGD.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR004557; PrmC-related.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR Pfam; PF05175; MTS; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00537; hemK_rel_arch; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..221
FT /note="eRF1 methyltransferase catalytic subunit MTQ2"
FT /id="PRO_0000245840"
FT BINDING 50..54
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 122..125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 221 AA; 24973 MW; C3CF6BF6A05E862D CRC64;
MLPTPYVKCD YDKVYEPAED SFLILDCLEK EHDFLKQKFG NRLAIVCEIG SGSGIVTTFL
MQNKIIPQEN SIHLAVDINP WALEATLDTA KLNSCKSSFL EVIQADLNSS IRNNQVDVLI
FNPPYVPAEC VPDVPGSREE ADQWLDLALL GGKDGMAITD KLLRQLEQIL SPDGVAYILF
CARNKPKEVI KRFVDTYKWN VKLIETRKAG WEVLSVYSFT R
