TRM3_YEAST
ID TRM3_YEAST Reviewed; 1436 AA.
AC Q07527; D6VRN8; P89896; Q05336; Q7LGS3;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=tRNA (guanosine(18)-2'-O)-methyltransferase {ECO:0000305|PubMed:9917067};
DE EC=2.1.1.34 {ECO:0000269|PubMed:9917067};
DE AltName: Full=tRNA [Gm18] ribose methylase {ECO:0000303|PubMed:9917067};
DE AltName: Full=tRNA methyltransferase 3 {ECO:0000303|PubMed:9917067};
GN Name=TRM3 {ECO:0000303|PubMed:9917067};
GN OrderedLocusNames=YDL112W {ECO:0000312|SGD:S000002270};
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] OF 955-1436.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8923743;
RX DOI=10.1002/(sici)1097-0061(199610)12:13%3c1377::aid-yea35%3e3.0.co;2-r;
RA Boskovic J., Soler-Mira A., Garcia-Cantalejo J.M., Ballesta J.P.G.,
RA Jimenez A., Remacha M.A.;
RT "The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome
RT IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open
RT reading frames.";
RL Yeast 12:1377-1384(1996).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9917067; DOI=10.1017/s1355838299981475;
RA Cavaille J., Chetouani F., Bachellerie J.-P.;
RT "The yeast Saccharomyces cerevisiae YDL112w ORF encodes the putative 2'-O-
RT ribose methyltransferase catalyzing the formation of Gm18 in tRNAs.";
RL RNA 5:66-81(1999).
RN [5]
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 [6]
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).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent 2'-O-ribose
CC methyltransferase that catalyzes the formation of 2'-O-methylguanosine
CC at position 18 (Gm18) in various tRNAs. {ECO:0000269|PubMed:9917067}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(18) in tRNA + S-adenosyl-L-methionine = 2'-O-
CC methylguanosine(18) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:20077, Rhea:RHEA-COMP:10190, Rhea:RHEA-COMP:10192,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74445; EC=2.1.1.34;
CC Evidence={ECO:0000269|PubMed:9917067};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 861 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. {ECO:0000305}.
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DR EMBL; Z74160; CAA98680.1; -; Genomic_DNA.
DR EMBL; X95644; CAA64900.1; -; Genomic_DNA.
DR EMBL; Z74159; CAA98679.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11748.1; -; Genomic_DNA.
DR PIR; S67655; S67655.
DR RefSeq; NP_010171.1; NM_001180171.1.
DR AlphaFoldDB; Q07527; -.
DR SMR; Q07527; -.
DR BioGRID; 31950; 101.
DR DIP; DIP-2598N; -.
DR IntAct; Q07527; 7.
DR STRING; 4932.YDL112W; -.
DR iPTMnet; Q07527; -.
DR MaxQB; Q07527; -.
DR PaxDb; Q07527; -.
DR PRIDE; Q07527; -.
DR EnsemblFungi; YDL112W_mRNA; YDL112W; YDL112W.
DR GeneID; 851446; -.
DR KEGG; sce:YDL112W; -.
DR SGD; S000002270; TRM3.
DR VEuPathDB; FungiDB:YDL112W; -.
DR eggNOG; KOG0839; Eukaryota.
DR GeneTree; ENSGT00390000003939; -.
DR HOGENOM; CLU_005519_0_0_1; -.
DR OMA; AVIVHAY; -.
DR BioCyc; YEAST:YDL112W-MON; -.
DR PRO; PR:Q07527; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07527; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0016423; F:tRNA (guanine) methyltransferase activity; IDA:SGD.
DR GO; GO:0009020; F:tRNA (guanosine-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0052665; F:tRNA (uracil-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030488; P:tRNA methylation; IDA:SGD.
DR GO; GO:0002128; P:tRNA nucleoside ribose methylation; IMP:SGD.
DR CDD; cd18091; SpoU-like_TRM3-like; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR025759; Trm3.
DR InterPro; IPR045330; Trm3/TARBP1.
DR InterPro; IPR044748; Trm3/TARBP1_C.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR12029; PTHR12029; 1.
DR Pfam; PF00588; SpoU_methylase; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
DR PROSITE; PS51623; SAM_MT_TRMH_1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..1436
FT /note="tRNA (guanosine(18)-2'-O)-methyltransferase"
FT /id="PRO_0000270921"
FT BINDING 1365..1367
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q13395"
FT BINDING 1389
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q13395"
FT BINDING 1409..1418
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q13395"
SQ SEQUENCE 1436 AA; 165048 MW; 4B14823AF6E858F1 CRC64;
MVGGALICKY LPREEQLKLI SDLIQNDSLE EVLELIETSP LDITTDSNIE TPIFEKITEQ
VIAYASIDGE AREMFRSSRA EMNKALRTSA QLLCCLPSVW HKFQVWMSYR LNDIISENYK
HLFNDNFGKK IVQPFFDSFA EEQNANIKHE NLHLDILSLL HYLEVVYLFD ECKNGISSKC
LDFIIVPLLG CNSEEIADSC SKLMRWHIKY LSKCCNTDSN FDKLIWTFIK QLYAEGSQQA
WKQKNSLSFL LRFLLAAELS PELITYIKTD AYWRHIQTEL DNDVHEHRKL ALSILKLTIQ
KLSSHGITLQ TTFYKCNDLA NIEMLGSWKK FTTLYEMIAL DTSLNQIQAA KQDIIKIFDN
EHLHHSWGLI LLSTGLKSSM ESVRKYMMTL MFSITNMSAF SSNLPLLTKT LLPAAMSAHY
FDVKGVSCPH GEKLSLFVNN LLSQTTEGIS DILFEILKLL VEKGTSFDPS RIYLSYGILV
FFQNNKQKTI NSDHLSLIRK LYDFAAEEEV LETTIQTIYL KFLLYIDPSV SASELLFTLV
SHIKLKGGTY KYVEPLFEDY RDLAVSHFDD LQAKENLTTN IGKDTIFDLL ASIIFDFKDI
DITPDFLIEV AKSKQDIPVY TSKAVTFLTQ LLSGEPSNGY TYENATALLS YPNFTISTWK
SINVNNLFKS VMEKFSLDKF KFFAEIYQKT YECRFDTIEL NFNDLLSLYE MVKKSANQCS
RESFKVKDSA YSSYFELLNT FLKTYALNRD SSEGNDDELH ILLRLVDENI NKDNGNYLGN
LAVCKLLYFI IDSYIHCSTS VSDDDIFIVK FIFEKFSFIW ECINSERLVL KERDLHLMLI
KGLFHPVILY FGSNQYIDTL TSKLEEHAQT IISLSYSRRS LLPLLGSQLR VFMKFYGKLL
REDVNYWWLI NIIVGVFKQP QMDVNLYKLK PVISSLFDHK LNNYYIKGDE LYEKVYGPDE
ILARVSIIDS ILYANDQLKI RLIEKVTEKT NALYAIKRTD GAEALQRLLQ WQLLLLSLLT
TNEKKLSETS MIRILKSIED ESSPLVRVYK EWFISSKVVD YYKTGNPKFA EDYLFSLLED
HSKPVFVVSA EKICFMVLKD LRNDEKKYGF TQLLDRFICT LVPNAASNKP LVRHFSNSLI
ISLWPTFKAY LSDHTLRNII ENLYSNAKKT QIFGQYRAGD ANIWDLKGDR KLTNMFGGVL
KKVTDHDCPY ISESVFEKYL QEKDIVPIGT DERSLWLDKR DTNTESVNNA NISCDTSPLQ
TKSGAWETVL DLDNKKSNDV VTRSELIVVS SLVDKPPNLG GICRLCDVLG VGLLTVQDIK
VKNHPQFKNV AVTADRWMPM EEVALDEIAS FMKEKKKEGY TLIGLEQTDK SVKLDNNFQF
PKKSLILLGT EAFGIPGTLL SELDLCLEIQ QFGVIRSMNI QTATAVIVHS YTVQHM
