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Protein

tRNA (uracil-O(2)-)-methyltransferase

Gene

TRM44

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

tRNA (uracil-O(2)-)-methyltransferase, which catalyzes the formation of O(2)-methyluracil at position 44 (Um44) in tRNA(Ser).1 Publication

Catalytic activityi

S-adenosyl-L-methionine + uridine(44) in tRNA(Ser) = S-adenosyl-L-homocysteine + 2'-O-methyluridine(44) in tRNA(Ser).

GO - Molecular functioni

GO - Biological processi

  • tRNA methylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16614.
YEAST:G3O-33945-MONOMER.
BRENDAi2.1.1.211. 984.
ReactomeiR-SCE-6782315. tRNA modification in the nucleus and cytosol.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA (uracil-O(2)-)-methyltransferase (EC:2.1.1.211)
Alternative name(s):
tRNA(Ser) (uridine(44)-2'-O)-methyltransferase
Short name:
tRNA Um(44) 2'-O-methyltransferase
Gene namesi
Name:TRM44
Ordered Locus Names:YPL030W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL030W.
SGDiS000005951. TRM44.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 567567tRNA (uracil-O(2)-)-methyltransferasePRO_0000249911Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei107 – 1071PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ02648.

PTM databases

iPTMnetiQ02648.

Interactioni

Protein-protein interaction databases

BioGridi36148. 23 interactions.
IntActiQ02648. 4 interactions.
MINTiMINT-4504434.

Structurei

3D structure databases

ProteinModelPortaliQ02648.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TRM44 family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000000645.
HOGENOMiHOG000248551.
InParanoidiQ02648.
KOiK15447.
OMAiEPIQNRL.
OrthoDBiEOG7XDBQN.

Family and domain databases

InterProiIPR011671. tRNA_uracil_MeTrfase.
[Graphical view]
PfamiPF07757. AdoMet_MTase. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02648-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGDGSAHIS KNNQNQHKDR FKFIVNDKSI LGPQWLSLYQ TDGKVTFAKS
60 70 80 90 100
HFEQAMMNVI REPNINSTVI LRADILKEIN HAAEAGSEPK FDESVLKKFE
110 120 130 140 150
IDNGNESGEE DVKKINIEDL NIRSCETSES LKLSPVHEFV RRIIPRNFYK
160 170 180 190 200
DAIINQTCLI LNSKDPNFQE TSLIVYTPHI NSEKDCPFYI PRTQSVGILL
210 220 230 240 250
HQSVLSVHYI PFPEDKTAFT DESERVVRTA YRLLQTANKH SKGVMQGYEK
260 270 280 290 300
RVNHDQVVNK VNFQNTYIVL KKKYSKFLVE NWAESTDPKK HVFEDIAIAA
310 320 330 340 350
FLIELWIKVY GPDFRSKMQF RDLGCGNGAL CYILLSESIK GLGIDARKRK
360 370 380 390 400
SWSIYPPEVQ SSLKEQVIIP SILLRPHPAL KRQVPHLEHN GRFFPVKVTH
410 420 430 440 450
EVIAPATVVY SSEDLLKSPQ VNTAEFPPDT FIIGNHSDEL TCWIPLLGHP
460 470 480 490 500
YMVIPCCSHN FSGQRVRFNV RKRSPRSNEI KNQNNSKSTY SGLVDHVEYI
510 520 530 540 550
SSRVGWKVEK EMLRIPSTRN AAIIGVENAT LKHFPTQAVY DMIWEDGGAE
560
GWIQNTMSLL KRNPRNH
Length:567
Mass (Da):64,855
Last modified:November 1, 1996 - v1
Checksum:i5374D45014C047C0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U36624 Genomic DNA. Translation: AAB68157.1.
U44030 Genomic DNA. Translation: AAB68189.1.
BK006949 Genomic DNA. Translation: DAA11399.1.
PIRiS63452.
RefSeqiNP_015295.1. NM_001183844.1.

Genome annotation databases

EnsemblFungiiYPL030W; YPL030W; YPL030W.
GeneIDi856077.
KEGGisce:YPL030W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U36624 Genomic DNA. Translation: AAB68157.1.
U44030 Genomic DNA. Translation: AAB68189.1.
BK006949 Genomic DNA. Translation: DAA11399.1.
PIRiS63452.
RefSeqiNP_015295.1. NM_001183844.1.

3D structure databases

ProteinModelPortaliQ02648.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36148. 23 interactions.
IntActiQ02648. 4 interactions.
MINTiMINT-4504434.

PTM databases

iPTMnetiQ02648.

Proteomic databases

MaxQBiQ02648.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL030W; YPL030W; YPL030W.
GeneIDi856077.
KEGGisce:YPL030W.

Organism-specific databases

EuPathDBiFungiDB:YPL030W.
SGDiS000005951. TRM44.

Phylogenomic databases

GeneTreeiENSGT00390000000645.
HOGENOMiHOG000248551.
InParanoidiQ02648.
KOiK15447.
OMAiEPIQNRL.
OrthoDBiEOG7XDBQN.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16614.
YEAST:G3O-33945-MONOMER.
BRENDAi2.1.1.211. 984.
ReactomeiR-SCE-6782315. tRNA modification in the nucleus and cytosol.

Miscellaneous databases

PROiQ02648.

Family and domain databases

InterProiIPR011671. tRNA_uracil_MeTrfase.
[Graphical view]
PfamiPF07757. AdoMet_MTase. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  6. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Identification of yeast tRNA Um(44) 2'-O-methyltransferase (Trm44) and demonstration of a Trm44 role in sustaining levels of specific tRNA(Ser) species."
    Kotelawala L., Grayhack E.J., Phizicky E.M.
    RNA 14:158-169(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTRM44_YEAST
AccessioniPrimary (citable) accession number: Q02648
Secondary accession number(s): D6W3Y3, Q03090, Q2XN15
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 7720 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.