MTQ1_YEAST
ID MTQ1_YEAST Reviewed; 314 AA.
AC P53944; D6W1B7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Mitochondrial MRF1 N(5)-glutamine methyltransferase MTQ1;
DE EC=2.1.1.297 {ECO:0000269|PubMed:16321977};
GN Name=MTQ1; OrderedLocusNames=YNL063W; ORFNames=N2420, YNL2420W;
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 [GENOMIC DNA].
RC STRAIN=S288c / FY1676;
RX PubMed=8533472; DOI=10.1002/yea.320111008;
RA Bergez P., Doignon F., Crouzet M.;
RT "The sequence of a 44 420 bp fragment located on the left arm of chromosome
RT XIV from Saccharomyces cerevisiae.";
RL Yeast 11:967-974(1995).
RN [2]
RP ERRATUM OF PUBMED:8533472.
RX PubMed=8904343;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<297::aid-yea940>3.0.co;2-d;
RA Bergez P., Doignon F., Crouzet M.;
RL Yeast 12:297-297(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Methylates MRF1 on 'Gln-287' using S-adenosyl L-methionine as
CC methyl donor. {ECO:0000269|PubMed:16321977}.
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:16321977};
CC -!- INTERACTION:
CC P53944; P30775: MRF1; NbExp=2; IntAct=EBI-28737, EBI-14964;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16321977}.
CC -!- MISCELLANEOUS: Present with 13200 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC family. {ECO:0000305}.
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DR EMBL; U12141; AAA99648.1; -; Genomic_DNA.
DR EMBL; Z71339; CAA95936.1; -; Genomic_DNA.
DR EMBL; AY692585; AAT92604.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10483.1; -; Genomic_DNA.
DR PIR; S58715; S58715.
DR RefSeq; NP_014336.1; NM_001182901.1.
DR AlphaFoldDB; P53944; -.
DR SMR; P53944; -.
DR BioGRID; 35760; 30.
DR DIP; DIP-6545N; -.
DR IntAct; P53944; 4.
DR STRING; 4932.YNL063W; -.
DR MaxQB; P53944; -.
DR PaxDb; P53944; -.
DR PRIDE; P53944; -.
DR EnsemblFungi; YNL063W_mRNA; YNL063W; YNL063W.
DR GeneID; 855662; -.
DR KEGG; sce:YNL063W; -.
DR SGD; S000005007; MTQ1.
DR VEuPathDB; FungiDB:YNL063W; -.
DR eggNOG; KOG2904; Eukaryota.
DR GeneTree; ENSGT00390000014125; -.
DR HOGENOM; CLU_018398_0_2_1; -.
DR InParanoid; P53944; -.
DR OMA; FWKTTTR; -.
DR BioCyc; YEAST:G3O-33093-MON; -.
DR PRO; PR:P53944; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53944; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro.
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:0006451; P:translational readthrough; IGI:SGD.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR004556; HemK-like.
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; TIGR00536; hemK_fam; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Mitochondrion; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..314
FT /note="Mitochondrial MRF1 N(5)-glutamine methyltransferase
FT MTQ1"
FT /id="PRO_0000203448"
FT BINDING 118..122
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 188..191
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 314 AA; 35871 MW; 2281F44B511EAA65 CRC64;
MPRISTSLIR KASRIRPGLH LLLPECRTLE QAKLEYKWLT EELPPDKSIR WACLQRYKHV
PLQYILRSQP FGALDIVCKP GVLIPRWETE EWVMAIIRAL NNSMLSRHTI PLHICDTFTG
TGCIALALSH GIANCTFTAI DVSTRAIKLV KENMLKNKVS GGKLVQHNIL SSKASDEYPS
HIDILTGNPP YIRKRDFNRD VKTSVKLFEP RLALVGELEC YINLVNYWLP KTDSFFYEIG
DVEQFNYVER RIKEDSYLSR IWSIGLKYDS NGKARVVYGF KATPKGRILH QIFASFGTIR
HLATALSGHK ANCN
