TRM9_YEAST
ID TRM9_YEAST Reviewed; 279 AA.
AC P49957; D6VZG0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=tRNA (carboxymethyluridine(34)-5-O)-methyltransferase;
DE EC=2.1.1.229;
DE AltName: Full=tRNA (uracil-5-)-methyltransferase TRM9;
DE AltName: Full=tRNA [Um34] methyltransferase;
DE AltName: Full=tRNA methylase 9;
GN Name=TRM9; OrderedLocusNames=YML014W; ORFNames=YM9571.04;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=14645538; DOI=10.1128/mcb.23.24.9283-9292.2003;
RA Kalhor H.R., Clarke S.;
RT "Novel methyltransferase for modified uridine residues at the wobble
RT position of tRNA.";
RL Mol. Cell. Biol. 23:9283-9292(2003).
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 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).
CC -!- FUNCTION: Required for the methylation of the wobble bases at position
CC 34 in tRNA. Appears to have a role in stress-response.
CC {ECO:0000269|PubMed:14645538}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carboxymethyluridine(34) in tRNA + S-adenosyl-L-methionine =
CC 5-(2-methoxy-2-oxoethyl)uridine(34) in tRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:43208, Rhea:RHEA-COMP:10407, Rhea:RHEA-
CC COMP:10408, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74851,
CC ChEBI:CHEBI:74882; EC=2.1.1.229;
CC Evidence={ECO:0000269|PubMed:14645538};
CC -!- SUBUNIT: Interacts with TRM112. {ECO:0000269|PubMed:15899842}.
CC -!- INTERACTION:
CC P49957; P53738: TRM112; NbExp=2; IntAct=EBI-27735, EBI-28520;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2360 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z49810; CAA89938.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09884.1; -; Genomic_DNA.
DR PIR; S55105; S55105.
DR RefSeq; NP_013698.1; NM_001182372.1.
DR AlphaFoldDB; P49957; -.
DR SMR; P49957; -.
DR BioGRID; 35155; 115.
DR ComplexPortal; CPX-1052; TRM9-TRM112 methyltransferase complex.
DR DIP; DIP-4549N; -.
DR IntAct; P49957; 2.
DR MINT; P49957; -.
DR STRING; 4932.YML014W; -.
DR iPTMnet; P49957; -.
DR MaxQB; P49957; -.
DR PaxDb; P49957; -.
DR PRIDE; P49957; -.
DR EnsemblFungi; YML014W_mRNA; YML014W; YML014W.
DR GeneID; 854994; -.
DR KEGG; sce:YML014W; -.
DR SGD; S000004476; TRM9.
DR VEuPathDB; FungiDB:YML014W; -.
DR eggNOG; KOG1331; Eukaryota.
DR GeneTree; ENSGT00940000158563; -.
DR HOGENOM; CLU_029501_2_0_1; -.
DR InParanoid; P49957; -.
DR OMA; TREYAWP; -.
DR BioCyc; MetaCyc:G3O-32618-MON; -.
DR BioCyc; YEAST:G3O-32618-MON; -.
DR BRENDA; 2.1.1.229; 984.
DR PRO; PR:P49957; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P49957; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0043527; C:tRNA methyltransferase complex; IPI:ComplexPortal.
DR GO; GO:0106335; F:tRNA (carboxymethyluridine(34)-5-O)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016300; F:tRNA (uracil) methyltransferase activity; IDA:SGD.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0008175; F:tRNA methyltransferase activity; EXP:Reactome.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IMP:SGD.
DR GO; GO:0006448; P:regulation of translational elongation; IMP:SGD.
DR GO; GO:0030488; P:tRNA methylation; IDA:SGD.
DR GO; GO:0006400; P:tRNA modification; TAS:Reactome.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IDA:ComplexPortal.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR032873; Trm9.
DR PANTHER; PTHR13069:SF21; PTHR13069:SF21; 1.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..279
FT /note="tRNA (carboxymethyluridine(34)-5-O)-
FT methyltransferase"
FT /id="PRO_0000203262"
FT REGION 172..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 279 AA; 32439 MW; 2F8795BB3C640D3B CRC64;
MEINQAAEKE QEYVHKVYNE IAPHFSQTRY KPWPIVTQFL KTRPMGSIGI DVGCGNGKYL
GVNPDIYIIG SDRSDGLIEC ARGINPSYNL LVADGLNLPH KNETFDFAIS IAVVHHWSTR
ERRVEVIRHV LSKLRQGGQA LIYCWALEQG SSRRGYHEGM EQDVFVPWVL PKSKSKPKTK
STPPAKVKTR PKPNLMNIPP KERSEYLQRW KEEQQRSKSL DDNDEKQQQD QEQEREEVKY
RYYHLYREGE LAEDCRQAGA AVHSEGFERD NWWVVAQKR
