UniProtKB - P0AE01 (TRMJ_ECOLI)
Protein
tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ
Gene
trmJ
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA (PubMed:16848900, PubMed:24951554, PubMed:26202969). Can also methylate adenosine or guanosine, even though these nucleosides are rare or absent at position 32 in the anticodon loop of tRNA (PubMed:24951554).3 Publications
Catalytic activityi
- cytidine32 in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine32 in tRNA + H+ + S-adenosyl-L-homocysteine3 PublicationsEC:2.1.1.2003 Publications
- S-adenosyl-L-methionine + uridine32 in tRNA = 2'-O-methyluridine32 in tRNA + H+ + S-adenosyl-L-homocysteine3 PublicationsEC:2.1.1.2003 Publications
Kineticsi
kcat is 1.52 min(-1) with tRNA(fMet1) as substrate. kcat is 1.42 min(-1) with tRNA(fMet2) as substrate. kcat is 1.31 min(-1) with tRNA(Trp1) as substrate. kcat is 1.20 min(-1) with tRNA(Gln1) as substrate. kcat is 1.41 min(-1) with tRNA(Gln2) as substrate. kcat is 2.30 min(-1) with tRNA(Ser1) as substrate.1 Publication
- KM=0.67 µM for tRNA(fMet1)1 Publication
- KM=0.81 µM for tRNA(fMet2)1 Publication
- KM=0.94 µM for tRNA(Trp1)1 Publication
- KM=9.88 µM for tRNA(Gln1)1 Publication
- KM=5.79 µM for tRNA(Gln2)1 Publication
- KM=11.82 µM for tRNA(Ser1)1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 114 | S-adenosyl-L-methionine; via amide nitrogen2 Publications | 1 | |
Binding sitei | 134 | S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen2 Publications | 1 |
GO - Molecular functioni
- RNA binding Source: InterPro
- tRNA (cytosine-2'-O-)-methyltransferase activity Source: EcoCyc
- tRNA (uracil-2'-O-)-methyltransferase activity Source: EcoCyc
GO - Biological processi
- tRNA nucleoside ribose methylation Source: EcoCyc
Keywordsi
Molecular function | Methyltransferase, Transferase |
Biological process | tRNA processing |
Ligand | S-adenosyl-L-methionine |
Enzyme and pathway databases
BioCyci | EcoCyc:G7327-MONOMER MetaCyc:G7327-MONOMER |
BRENDAi | 2.1.1.200, 2026 |
Names & Taxonomyi
Protein namesi | Recommended name: tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJCurated (EC:2.1.1.2003 Publications)Alternative name(s): TrMet(Xm32)1 Publication tRNA (cytidine(32)/uridine(32)-2'-O)-methyltransferaseCurated tRNA Cm32/Um32 methyltransferaseCurated |
Gene namesi | Name:trmJ1 Publication Synonyms:yfhQ Ordered Locus Names:b2532, JW2516 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm Curated
Cytosol
- cytosol Source: EcoCyc
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 23 | R → A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 82 | R → A: Loss of tRNA binding affinity. Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 84 | R → A: Loss of tRNA binding affinity. Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 115 | R → A: No change in tRNA binding affinity. No change in activity. 1 Publication | 1 | |
Mutagenesisi | 140 | Y → F: Strong decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 172 | H → A: No change in activity. 1 Publication | 1 | |
Mutagenesisi | 175 | T → A: No change in activity. 1 Publication | 1 | |
Mutagenesisi | 177 | Y → A: No change in activity. 1 Publication | 1 | |
Mutagenesisi | 199 | F → A: Strong decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 211 | K → A: Strong decrease in tRNA binding affinity. Strong decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 213 | R → A: Strong decrease in tRNA binding affinity. Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 214 | R → A: Strong decrease in tRNA binding affinity. Strong decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 218 | R → A: Strong decrease in tRNA binding affinity. Strong decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 225 | E → A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 228 | I → A: Strong decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 229 | L → A: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 231 | G → A: Loss of activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000159824 | 1 – 246 | tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJAdd BLAST | 246 |
Proteomic databases
jPOSTi | P0AE01 |
PaxDbi | P0AE01 |
PRIDEi | P0AE01 |
Interactioni
Subunit structurei
Homodimer.
3 PublicationsProtein-protein interaction databases
BioGRIDi | 4263050, 19 interactors 852903, 1 interactor |
IntActi | P0AE01, 3 interactors |
STRINGi | 511145.b2532 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0AE01 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 79 – 81 | S-adenosyl-L-methionine binding2 Publications | 3 | |
Regioni | 141 – 143 | S-adenosyl-L-methionine binding2 Publications | 3 |
Domaini
Both the catalytic N-terminal domain and the extensional C-terminal domain play key roles in tRNA binding and methylation.1 Publication
Sequence similaritiesi
Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.Curated
Phylogenomic databases
eggNOGi | COG0565, Bacteria |
HOGENOMi | CLU_056931_0_1_6 |
InParanoidi | P0AE01 |
PhylomeDBi | P0AE01 |
Family and domain databases
Gene3Di | 3.40.1280.10, 1 hit |
InterProi | View protein in InterPro IPR029028, Alpha/beta_knot_MTases IPR004384, RNA_MeTrfase_TrmJ/LasT IPR001537, SpoU_MeTrfase IPR029026, tRNA_m1G_MTases_N |
PANTHERi | PTHR42786, PTHR42786, 1 hit |
Pfami | View protein in Pfam PF00588, SpoU_methylase, 1 hit |
PIRSFi | PIRSF004808, LasT, 1 hit |
SUPFAMi | SSF75217, SSF75217, 1 hit |
TIGRFAMsi | TIGR00050, rRNA_methyl_1, 1 hit |
i Sequence
Sequence statusi: Complete.
P0AE01-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MLQNIRIVLV ETSHTGNMGS VARAMKTMGL TNLWLVNPLV KPDSQAIALA
60 70 80 90 100
AGASDVIGNA HIVDTLDEAL AGCSLVVGTS ARSRTLPWPM LDPRECGLKS
110 120 130 140 150
VAEAANTPVA LVFGRERVGL TNEELQKCHY HVAIAANPEY SSLNLAMAVQ
160 170 180 190 200
VIAYEVRMAW LATQENGEQV EHEETPYPLV DDLERFYGHL EQTLLATGFI
210 220 230 240
RENHPGQVMN KLRRLFTRAR PESQELNILR GILASIEQQN KGNKAE
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U00096 Genomic DNA Translation: AAC75585.1 AP009048 Genomic DNA Translation: BAA16426.1 |
PIRi | C65030 |
RefSeqi | NP_417027.1, NC_000913.3 WP_000940019.1, NZ_SSZK01000005.1 |
Genome annotation databases
EnsemblBacteriai | AAC75585; AAC75585; b2532 BAA16426; BAA16426; BAA16426 |
GeneIDi | 58390231 948610 |
KEGGi | ecj:JW2516 eco:b2532 |
PATRICi | fig|511145.12.peg.2633 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U00096 Genomic DNA Translation: AAC75585.1 AP009048 Genomic DNA Translation: BAA16426.1 |
PIRi | C65030 |
RefSeqi | NP_417027.1, NC_000913.3 WP_000940019.1, NZ_SSZK01000005.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4CND | X-ray | 1.50 | A/B | 1-246 | [»] | |
4CNE | X-ray | 1.90 | A/B | 1-246 | [»] | |
4XBO | X-ray | 2.60 | A/B | 1-246 | [»] | |
SMRi | P0AE01 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4263050, 19 interactors 852903, 1 interactor |
IntActi | P0AE01, 3 interactors |
STRINGi | 511145.b2532 |
Proteomic databases
jPOSTi | P0AE01 |
PaxDbi | P0AE01 |
PRIDEi | P0AE01 |
Genome annotation databases
EnsemblBacteriai | AAC75585; AAC75585; b2532 BAA16426; BAA16426; BAA16426 |
GeneIDi | 58390231 948610 |
KEGGi | ecj:JW2516 eco:b2532 |
PATRICi | fig|511145.12.peg.2633 |
Organism-specific databases
EchoBASEi | EB3225 |
Phylogenomic databases
eggNOGi | COG0565, Bacteria |
HOGENOMi | CLU_056931_0_1_6 |
InParanoidi | P0AE01 |
PhylomeDBi | P0AE01 |
Enzyme and pathway databases
BioCyci | EcoCyc:G7327-MONOMER MetaCyc:G7327-MONOMER |
BRENDAi | 2.1.1.200, 2026 |
Miscellaneous databases
PROi | PR:P0AE01 |
Family and domain databases
Gene3Di | 3.40.1280.10, 1 hit |
InterProi | View protein in InterPro IPR029028, Alpha/beta_knot_MTases IPR004384, RNA_MeTrfase_TrmJ/LasT IPR001537, SpoU_MeTrfase IPR029026, tRNA_m1G_MTases_N |
PANTHERi | PTHR42786, PTHR42786, 1 hit |
Pfami | View protein in Pfam PF00588, SpoU_methylase, 1 hit |
PIRSFi | PIRSF004808, LasT, 1 hit |
SUPFAMi | SSF75217, SSF75217, 1 hit |
TIGRFAMsi | TIGR00050, rRNA_methyl_1, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | TRMJ_ECOLI | |
Accessioni | P0AE01Primary (citable) accession number: P0AE01 Secondary accession number(s): P76993, P77438 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 6, 2005 |
Last sequence update: | December 6, 2005 | |
Last modified: | April 7, 2021 | |
This is version 113 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families