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Protein

tRNA (guanosine(18)-2'-O)-methyltransferase

Gene

trmH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the 2'-O methylation of guanosine at position 18 in tRNA. Type II methylase, which methylates only a subset of tRNA species.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + guanosine(18) in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylguanosine(18) in tRNA.UniRule annotation1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei96 – 961S-adenosyl-L-methionineUniRule annotation
Binding sitei139 – 1391S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygenUniRule annotation
Binding sitei148 – 1481S-adenosyl-L-methionine; via amide nitrogenUniRule annotation

GO - Molecular functioni

  • RNA binding Source: GO_Central
  • tRNA (guanosine-2'-O-)-methyltransferase activity Source: EcoCyc
  • tRNA binding Source: UniProtKB-KW

GO - Biological processi

  • tRNA guanine ribose methylation Source: EcoCyc
  • tRNA methylation Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

RNA-binding, S-adenosyl-L-methionine, tRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10967-MONOMER.
ECOL316407:JW3626-MONOMER.
MetaCyc:EG10967-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA (guanosine(18)-2'-O)-methyltransferaseUniRule annotationCurated (EC:2.1.1.34UniRule annotation1 Publication)
Alternative name(s):
tRNA [Gm18] methyltransferaseUniRule annotationCurated
Gene namesi
Name:trmH1 PublicationUniRule annotation
Synonyms:spoU1 Publication
Ordered Locus Names:b3651, JW3626
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10967. trmH.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 229229tRNA (guanosine(18)-2'-O)-methyltransferasePRO_0000159772Add
BLAST

Proteomic databases

PaxDbiP0AGJ2.
PRIDEiP0AGJ2.

Interactioni

Protein-protein interaction databases

BioGridi4262569. 160 interactions.
DIPiDIP-35977N.
IntActiP0AGJ2. 11 interactions.
STRINGi511145.b3651.

Structurei

3D structure databases

ProteinModelPortaliP0AGJ2.
SMRiP0AGJ2. Positions 12-186.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105FE8. Bacteria.
COG0566. LUCA.
HOGENOMiHOG000285175.
InParanoidiP0AGJ2.
KOiK00556.
OMAiVHAVWPT.
OrthoDBiEOG6GBMDM.
PhylomeDBiP0AGJ2.

Family and domain databases

Gene3Di3.40.1280.10. 1 hit.
HAMAPiMF_02060. tRNA_methyltr_TrmH.
InterProiIPR029028. Alpha/beta_knot_MTases.
IPR022724. rRNA_MeTrfase_SpoU_C.
IPR001537. SpoU_MeTrfase.
IPR029026. tRNA_m1G_MTases_N.
[Graphical view]
PfamiPF12105. SpoU_methylas_C. 1 hit.
PF00588. SpoU_methylase. 1 hit.
[Graphical view]
SUPFAMiSSF75217. SSF75217. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AGJ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPTRYARIC EMLARRQPDL TVCMEQVHKP HNVSAIIRTA DAVGVHEVHA
60 70 80 90 100
VWPGSRMRTM ASAAAGSNSW VQVKTHRTIG DAVAHLKGQG MQILATHLSD
110 120 130 140 150
NAVDFREIDY TRPTCILMGQ EKTGITQEAL ALADQDIIIP MIGMVQSLNV
160 170 180 190 200
SVASALILYE AQRQRQNAGM YLRENSMLPE AEQQRLLFEG GYPVLAKVAK
210 220
RKGLPYPHVN QQGEIEADAD WWATMQAAG
Length:229
Mass (Da):25,343
Last modified:December 20, 2005 - v1
Checksum:iBC5AB6B804BDEE2E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24503 Genomic DNA. Translation: AAB00161.1.
L10328 Genomic DNA. Translation: AAA62004.1.
U00096 Genomic DNA. Translation: AAC76675.1.
AP009048 Genomic DNA. Translation: BAE77642.1.
PIRiJV0043.
RefSeqiNP_418108.1. NC_000913.3.
WP_001070177.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76675; AAC76675; b3651.
BAE77642; BAE77642; BAE77642.
GeneIDi948161.
KEGGiecj:JW3626.
eco:b3651.
PATRICi32122789. VBIEscCol129921_3771.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24503 Genomic DNA. Translation: AAB00161.1.
L10328 Genomic DNA. Translation: AAA62004.1.
U00096 Genomic DNA. Translation: AAC76675.1.
AP009048 Genomic DNA. Translation: BAE77642.1.
PIRiJV0043.
RefSeqiNP_418108.1. NC_000913.3.
WP_001070177.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0AGJ2.
SMRiP0AGJ2. Positions 12-186.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262569. 160 interactions.
DIPiDIP-35977N.
IntActiP0AGJ2. 11 interactions.
STRINGi511145.b3651.

Proteomic databases

PaxDbiP0AGJ2.
PRIDEiP0AGJ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76675; AAC76675; b3651.
BAE77642; BAE77642; BAE77642.
GeneIDi948161.
KEGGiecj:JW3626.
eco:b3651.
PATRICi32122789. VBIEscCol129921_3771.

Organism-specific databases

EchoBASEiEB0960.
EcoGeneiEG10967. trmH.

Phylogenomic databases

eggNOGiENOG4105FE8. Bacteria.
COG0566. LUCA.
HOGENOMiHOG000285175.
InParanoidiP0AGJ2.
KOiK00556.
OMAiVHAVWPT.
OrthoDBiEOG6GBMDM.
PhylomeDBiP0AGJ2.

Enzyme and pathway databases

BioCyciEcoCyc:EG10967-MONOMER.
ECOL316407:JW3626-MONOMER.
MetaCyc:EG10967-MONOMER.

Miscellaneous databases

PROiP0AGJ2.

Family and domain databases

Gene3Di3.40.1280.10. 1 hit.
HAMAPiMF_02060. tRNA_methyltr_TrmH.
InterProiIPR029028. Alpha/beta_knot_MTases.
IPR022724. rRNA_MeTrfase_SpoU_C.
IPR001537. SpoU_MeTrfase.
IPR029026. tRNA_m1G_MTases_N.
[Graphical view]
PfamiPF12105. SpoU_methylas_C. 1 hit.
PF00588. SpoU_methylase. 1 hit.
[Graphical view]
SUPFAMiSSF75217. SSF75217. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the spoT gene of Escherichia coli."
    Sarubbi E., Rudd K.E., Xiao H., Ikehara K., Kalman M., Cashel M.
    J. Biol. Chem. 264:15074-15082(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / JM109 / ATCC 53323.
  2. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
    Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
    Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Residual guanosine 3',5'-bispyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutations."
    Xiao H., Kalman M., Ikehara K., Zemel S., Glaser G., Cashel M.
    J. Biol. Chem. 266:5980-5990(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE NAME.
  6. "SpoU protein of Escherichia coli belongs to a new family of putative rRNA methylases."
    Koonin E.V., Rudd K.E.
    Nucleic Acids Res. 21:5519-5519(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE FUNCTION.
  7. "The spoU gene of Escherichia coli, the fourth gene of the spoT operon, is essential for tRNA (Gm18) 2'-O-methyltransferase activity."
    Persson B.C., Jaeger G., Gustafsson C.
    Nucleic Acids Res. 25:4093-4097(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiTRMH_ECOLI
AccessioniPrimary (citable) accession number: P0AGJ2
Secondary accession number(s): P19396, Q2M7W4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: June 8, 2016
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

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.