ID   TRM3_YEAST              Reviewed;        1436 AA.
AC   Q07527; P89896; Q05336; Q7LGS3;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 51.
DE   RecName: Full=tRNA guanosine-2'-O-methyltransferase TRM3;
DE            EC=2.1.1.34;
DE   AltName: Full=tRNA [Gm18] methyltransferase;
DE   AltName: Full=tRNA methylase 3;
GN   Name=TRM3; OrderedLocusNames=YDL112W;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=97313263; 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.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 955-1436.
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   MEDLINE=97082507; PubMed=8923743;
RX   DOI=10.1002/(SICI)1097-0061(199610)12:13<1377::AID-YEA35>3.0.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
RT   chromosome IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes,
RT   and five new open reading frames.";
RL   Yeast 12:1377-1384(1996).
RN   [3]
RP   FUNCTION.
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
RT   2'-O-ribose methyltransferase catalyzing the formation of Gm18 in
RT   tRNAs.";
RL   RNA 5:66-81(1999).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923954; 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   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Specifically methylates guanosine-18 in various tRNAs.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-
CC       homocysteine + tRNA containing 2'-O-methylguanosine.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: Present with 861 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the RNA methyltransferase trmH family.
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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   PIR; S67655; S67655.
DR   RefSeq; NP_010171.1; -.
DR   DIP; DIP:2598N; -.
DR   IntAct; Q07527; 14.
DR   PeptideAtlas; Q07527; -.
DR   PRIDE; Q07527; -.
DR   Ensembl; YDL112W; Saccharomyces cerevisiae.
DR   GeneID; 851446; -.
DR   GenomeReviews; Z71256_GR; YDL112W.
DR   KEGG; sce:YDL112W; -.
DR   NMPDR; fig|4932.3.peg.909; -.
DR   CYGD; YDL112w; -.
DR   SGD; S000002270; TRM3.
DR   HOGENOM; Q07527; -.
DR   OMA; Q07527; NIQTATA.
DR   BRENDA; 2.1.1.34; 250.
DR   NextBio; 968696; -.
DR   ArrayExpress; Q07527; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0009020; F:tRNA (guanosine-2'-O-)-methyltransferase ac...; IEA:EC.
DR   GO; GO:0030488; P:tRNA methylation; IDA:SGD.
DR   InterPro; IPR001537; SpoU_MeTrfase.
DR   Pfam; PF00588; SpoU_methylase; 1.
DR   ProDom; PD001243; SpoU_mtfrase; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN         1   1436       tRNA guanosine-2'-O-methyltransferase
FT                                TRM3.
FT                                /FTId=PRO_0000270921.
FT   COMPBIAS   1013   1019       Poly-Leu.
FT   BINDING    1389   1389       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING    1409   1409       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen (By
FT                                similarity).
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
//