TR112_YEAST
ID TR112_YEAST Reviewed; 135 AA.
AC P53738; D6W1M1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Multifunctional methyltransferase subunit TRM112;
DE AltName: Full=eRF1 methyltransferase subunit TRM112;
DE Short=eRF1 MTase subunit TRM112;
DE AltName: Full=tRNA methyltransferase 112;
GN Name=TRM112; OrderedLocusNames=YNR046W; ORFNames=N3445;
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=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 [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 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 [4]
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 [5]
RP FUNCTION, AND INTERACTION WITH TRM9; TRM11; LYS9 AND MTQ2.
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 [6]
RP FUNCTION, AND INTERACTION WITH BUD23; NOP2 AND RCM1.
RX PubMed=22956767; DOI=10.1091/mbc.e12-05-0370;
RA Sardana R., Johnson A.W.;
RT "The methyltransferase adaptor protein Trm112 is involved in biogenesis of
RT both ribosomal subunits.";
RL Mol. Biol. Cell 23:4313-4322(2012).
RN [7]
RP FUNCTION, AND INTERACTION WITH BUD23.
RX PubMed=22493060; DOI=10.1128/mcb.06623-11;
RA Figaro S., Wacheul L., Schillewaert S., Graille M., Huvelle E.,
RA Mongeard R., Zorbas C., Lafontaine D.L., Heurgue-Hamard V.;
RT "Trm112 is required for Bud23-mediated methylation of the 18S rRNA at
RT position G1575.";
RL Mol. Cell. Biol. 32:2254-2267(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), FUNCTION, AND INTERACTION WITH MTQ2.
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: Acts as an activator of both rRNA/tRNA and protein
CC methyltransferases. Together with methyltransferase MTQ2, required for
CC the methylation of eRF1 on 'Gln-182'. Together with methyltransferase
CC TRM11, required for the formation of 2-methylguanosine at position 10
CC (m2G10) in tRNA. Together with methyltransferase BUD23, required for
CC the formation of 7-methylguanine at position 1575 (m7G1575) in 18S
CC rRNA. Involved in biogenesis of both 40S and 60S ribosomal subunits.
CC {ECO:0000269|PubMed:15899842, ECO:0000269|PubMed:17008308,
CC ECO:0000269|PubMed:22493060, ECO:0000269|PubMed:22956767}.
CC -!- SUBUNIT: Heterodimer of MTQ2-TRM112, forming the eRF1
CC methyltransferase. TRM112 is necessary for the solubility and activity
CC of the catalytic subunit MTQ2. Interacts with TRM11; required for full
CC tRNA methyltransferase activity. Interacts with BUD23; required for
CC full rRNA methyltransferase activity. Interacts with RCM1, NOP2, TRM9
CC and LYS9. {ECO:0000269|PubMed:15899842, ECO:0000269|PubMed:17008308,
CC ECO:0000269|PubMed:22493060, ECO:0000269|PubMed:22956767}.
CC -!- INTERACTION:
CC P53738; P25627: BUD23; NbExp=5; IntAct=EBI-28520, EBI-21924;
CC P53738; Q03920: MTQ2; NbExp=3; IntAct=EBI-28520, EBI-31378;
CC P53738; Q12463: TRM11; NbExp=4; IntAct=EBI-28520, EBI-30471;
CC P53738; P49957: TRM9; NbExp=2; IntAct=EBI-28520, EBI-27735;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 4800 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRM112 family. {ECO:0000305}.
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DR EMBL; Z71661; CAA96327.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10587.1; -; Genomic_DNA.
DR PIR; S63377; S63377.
DR RefSeq; NP_014444.1; NM_001183223.1.
DR PDB; 2J6A; X-ray; 1.70 A; A=1-135.
DR PDB; 4QTT; X-ray; 2.00 A; A/C=1-135.
DR PDB; 4QTU; X-ray; 2.12 A; A/C=1-135.
DR PDBsum; 2J6A; -.
DR PDBsum; 4QTT; -.
DR PDBsum; 4QTU; -.
DR AlphaFoldDB; P53738; -.
DR SMR; P53738; -.
DR BioGRID; 35871; 82.
DR ComplexPortal; CPX-1047; BUD23-TRM112 methyltransferase complex.
DR ComplexPortal; CPX-1052; TRM9-TRM112 methyltransferase complex.
DR ComplexPortal; CPX-418; MTQ2-TRM112 eRF1 methyltransferase complex.
DR ComplexPortal; CPX-778; TRM11-TRM112 tRNA (m2G10) methyltransferase complex.
DR DIP; DIP-2052N; -.
DR IntAct; P53738; 8.
DR MINT; P53738; -.
DR STRING; 4932.YNR046W; -.
DR iPTMnet; P53738; -.
DR MaxQB; P53738; -.
DR PaxDb; P53738; -.
DR PRIDE; P53738; -.
DR EnsemblFungi; YNR046W_mRNA; YNR046W; YNR046W.
DR GeneID; 855782; -.
DR KEGG; sce:YNR046W; -.
DR SGD; S000005329; TRM112.
DR VEuPathDB; FungiDB:YNR046W; -.
DR eggNOG; KOG1088; Eukaryota.
DR GeneTree; ENSGT00940000164608; -.
DR HOGENOM; CLU_086140_0_0_1; -.
DR InParanoid; P53738; -.
DR OMA; NMLTSKC; -.
DR BioCyc; MetaCyc:G3O-33353-MON; -.
DR BioCyc; YEAST:G3O-33353-MON; -.
DR Reactome; R-SCE-156581; Methylation.
DR Reactome; R-SCE-72764; Eukaryotic Translation Termination.
DR EvolutionaryTrace; P53738; -.
DR PRO; PR:P53738; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53738; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0035657; C:eRF1 methyltransferase complex; IPI:SGD.
DR GO; GO:0005730; C:nucleolus; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005840; C:ribosome; IC:ComplexPortal.
DR GO; GO:0043528; C:tRNA (m2G10) methyltransferase complex; IPI:SGD.
DR GO; GO:0043527; C:tRNA methyltransferase complex; IPI:ComplexPortal.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IMP:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IMP: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:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:SGD.
DR GO; GO:0070476; P:rRNA (guanine-N7)-methylation; IMP:SGD.
DR GO; GO:0030488; P:tRNA methylation; IDA:ComplexPortal.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IDA:ComplexPortal.
DR InterPro; IPR039127; Trm112.
DR InterPro; IPR005651; Trm112-like.
DR PANTHER; PTHR12773; PTHR12773; 1.
DR Pfam; PF03966; Trm112p; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..135
FT /note="Multifunctional methyltransferase subunit TRM112"
FT /id="PRO_0000215805"
FT DOMAIN 2..131
FT /note="TRM112"
FT HELIX 3..7
FT /evidence="ECO:0007829|PDB:2J6A"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:2J6A"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:2J6A"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:2J6A"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:2J6A"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:2J6A"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:2J6A"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:2J6A"
FT HELIX 87..100
FT /evidence="ECO:0007829|PDB:2J6A"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:2J6A"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2J6A"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:2J6A"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:2J6A"
SQ SEQUENCE 135 AA; 15066 MW; 3CFB2ABDDFB0E38A CRC64;
MKFLTTNFLK CSVKACDTSN DNFPLQYDGS KCQLVQDESI EFNPEFLLNI VDRVDWPAVL
TVAAELGNNA LPPTKPSFPS SIQELTDDDM AILNDLHTLL LQTSIAEGEM KCRNCGHIYY
IKNGIPNLLL PPHLV
