TRM44_YEAST
ID TRM44_YEAST Reviewed; 567 AA.
AC Q02648; D6W3Y3; Q03090; Q2XN15;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=tRNA (uracil-O(2)-)-methyltransferase;
DE EC=2.1.1.211;
DE AltName: Full=tRNA(Ser) (uridine(44)-2'-O)-methyltransferase;
DE Short=tRNA Um(44) 2'-O-methyltransferase;
GN Name=TRM44; OrderedLocusNames=YPL030W;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP FUNCTION.
RX PubMed=18025252; DOI=10.1261/rna.811008;
RA Kotelawala L., Grayhack E.J., Phizicky E.M.;
RT "Identification of yeast tRNA Um(44) 2'-O-methyltransferase (Trm44) and
RT demonstration of a Trm44 role in sustaining levels of specific tRNA(Ser)
RT species.";
RL RNA 14:158-169(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: tRNA (uracil-O(2)-)-methyltransferase, which catalyzes the
CC formation of O(2)-methyluracil at position 44 (Um44) in tRNA(Ser).
CC {ECO:0000269|PubMed:18025252}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(44) in tRNA(Ser) = 2'-O-
CC methyluridine(44) in tRNA(Ser) + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43100, Rhea:RHEA-COMP:10339, Rhea:RHEA-COMP:10340,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74478; EC=2.1.1.211;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 7720 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRM44 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U36624; AAB68157.1; -; Genomic_DNA.
DR EMBL; U44030; AAB68189.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11399.1; -; Genomic_DNA.
DR PIR; S63452; S63452.
DR RefSeq; NP_015295.1; NM_001183844.1.
DR AlphaFoldDB; Q02648; -.
DR BioGRID; 36148; 122.
DR IntAct; Q02648; 4.
DR STRING; 4932.YPL030W; -.
DR iPTMnet; Q02648; -.
DR MaxQB; Q02648; -.
DR PaxDb; Q02648; -.
DR PRIDE; Q02648; -.
DR EnsemblFungi; YPL030W_mRNA; YPL030W; YPL030W.
DR GeneID; 856077; -.
DR KEGG; sce:YPL030W; -.
DR SGD; S000005951; TRM44.
DR VEuPathDB; FungiDB:YPL030W; -.
DR eggNOG; KOG3790; Eukaryota.
DR GeneTree; ENSGT00390000000645; -.
DR HOGENOM; CLU_018580_2_0_1; -.
DR InParanoid; Q02648; -.
DR OMA; WIPLLGY; -.
DR BioCyc; MetaCyc:G3O-33945-MON; -.
DR BioCyc; YEAST:G3O-33945-MON; -.
DR BRENDA; 2.1.1.211; 984.
DR PRO; PR:Q02648; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02648; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016300; F:tRNA (uracil) methyltransferase activity; IDA:SGD.
DR GO; GO:0052665; F:tRNA (uracil-2'-O-)-methyltransferase activity; TAS:Reactome.
DR GO; GO:0030488; P:tRNA methylation; IDA:SGD.
DR GO; GO:0002128; P:tRNA nucleoside ribose methylation; IMP:SGD.
DR InterPro; IPR011671; tRNA_uracil_MeTrfase.
DR PANTHER; PTHR21210; PTHR21210; 1.
DR Pfam; PF07757; AdoMet_MTase; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..567
FT /note="tRNA (uracil-O(2)-)-methyltransferase"
FT /id="PRO_0000249911"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 567 AA; 64855 MW; 5374D45014C047C0 CRC64;
MTGDGSAHIS KNNQNQHKDR FKFIVNDKSI LGPQWLSLYQ TDGKVTFAKS HFEQAMMNVI
REPNINSTVI LRADILKEIN HAAEAGSEPK FDESVLKKFE IDNGNESGEE DVKKINIEDL
NIRSCETSES LKLSPVHEFV RRIIPRNFYK DAIINQTCLI LNSKDPNFQE TSLIVYTPHI
NSEKDCPFYI PRTQSVGILL HQSVLSVHYI PFPEDKTAFT DESERVVRTA YRLLQTANKH
SKGVMQGYEK RVNHDQVVNK VNFQNTYIVL KKKYSKFLVE NWAESTDPKK HVFEDIAIAA
FLIELWIKVY GPDFRSKMQF RDLGCGNGAL CYILLSESIK GLGIDARKRK SWSIYPPEVQ
SSLKEQVIIP SILLRPHPAL KRQVPHLEHN GRFFPVKVTH EVIAPATVVY SSEDLLKSPQ
VNTAEFPPDT FIIGNHSDEL TCWIPLLGHP YMVIPCCSHN FSGQRVRFNV RKRSPRSNEI
KNQNNSKSTY SGLVDHVEYI SSRVGWKVEK EMLRIPSTRN AAIIGVENAT LKHFPTQAVY
DMIWEDGGAE GWIQNTMSLL KRNPRNH
