trmJ

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
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
S-adenosyl-L-methionine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
2'-O-methylcytidine³² in tRNA
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
S-adenosyl-L-homocysteine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.4
  "The yfhQ gene of Escherichia coli encodes a tRNA:Cm32/Um32 methyltransferase."
  Purta E., van Vliet F., Tkaczuk K.L., Dunin-Horkawicz S., Mori H., Droogmans L., Bujnicki J.M.
  BMC Mol. Biol. 7:23-23(2006) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
- Ref.5
  "Characterization of two homologous 2'-O-methyltransferases showing different specificities for their tRNA substrates."
  Somme J., Van Laer B., Roovers M., Steyaert J., Versees W., Droogmans L.
  RNA 20:1257-1271(2014) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF ARG-23 AND TYR-140.
- Ref.6
  "tRNA recognition by a bacterial tRNA Xm32 modification enzyme from the SPOUT methyltransferase superfamily."
  Liu R.J., Long T., Zhou M., Zhou X.L., Wang E.D.
  Nucleic Acids Res. 43:7489-7503(2015) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN, MUTAGENESIS OF ARG-82; ARG-84; ARG-115; HIS-172; THR-175; TYR-177; PHE-199; LYS-211; ARG-213; ARG-214; ARG-218; GLU-225; ILE-228; LEU-229 AND GLY-231.
EC:
2.1.1.200
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.4
  "The yfhQ gene of Escherichia coli encodes a tRNA:Cm32/Um32 methyltransferase."
  Purta E., van Vliet F., Tkaczuk K.L., Dunin-Horkawicz S., Mori H., Droogmans L., Bujnicki J.M.
  BMC Mol. Biol. 7:23-23(2006) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
- Ref.5
  "Characterization of two homologous 2'-O-methyltransferases showing different specificities for their tRNA substrates."
  Somme J., Van Laer B., Roovers M., Steyaert J., Versees W., Droogmans L.
  RNA 20:1257-1271(2014) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF ARG-23 AND TYR-140.
- Ref.6
  "tRNA recognition by a bacterial tRNA Xm32 modification enzyme from the SPOUT methyltransferase superfamily."
  Liu R.J., Long T., Zhou M., Zhou X.L., Wang E.D.
  Nucleic Acids Res. 43:7489-7503(2015) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN, MUTAGENESIS OF ARG-82; ARG-84; ARG-115; HIS-172; THR-175; TYR-177; PHE-199; LYS-211; ARG-213; ARG-214; ARG-218; GLU-225; ILE-228; LEU-229 AND GLY-231.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
cytidine³² in tRNA
CMP residue
zoom
+
S-adenosyl-L-methionine
zoom
=
2'-O-methylcytidine³² in tRNA
2'-O-methylcytidine 5'-phosphate residue
zoom
+
H⁺
+
S-adenosyl-L-homocysteine
zoom
S-adenosyl-L-methionine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
uridine³² in tRNA
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
=
2'-O-methyluridine³² in tRNA
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
S-adenosyl-L-homocysteine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.4
  "The yfhQ gene of Escherichia coli encodes a tRNA:Cm32/Um32 methyltransferase."
  Purta E., van Vliet F., Tkaczuk K.L., Dunin-Horkawicz S., Mori H., Droogmans L., Bujnicki J.M.
  BMC Mol. Biol. 7:23-23(2006) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
- Ref.5
  "Characterization of two homologous 2'-O-methyltransferases showing different specificities for their tRNA substrates."
  Somme J., Van Laer B., Roovers M., Steyaert J., Versees W., Droogmans L.
  RNA 20:1257-1271(2014) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF ARG-23 AND TYR-140.
- Ref.6
  "tRNA recognition by a bacterial tRNA Xm32 modification enzyme from the SPOUT methyltransferase superfamily."
  Liu R.J., Long T., Zhou M., Zhou X.L., Wang E.D.
  Nucleic Acids Res. 43:7489-7503(2015) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN, MUTAGENESIS OF ARG-82; ARG-84; ARG-115; HIS-172; THR-175; TYR-177; PHE-199; LYS-211; ARG-213; ARG-214; ARG-218; GLU-225; ILE-228; LEU-229 AND GLY-231.
EC:
2.1.1.200
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.4
  "The yfhQ gene of Escherichia coli encodes a tRNA:Cm32/Um32 methyltransferase."
  Purta E., van Vliet F., Tkaczuk K.L., Dunin-Horkawicz S., Mori H., Droogmans L., Bujnicki J.M.
  BMC Mol. Biol. 7:23-23(2006) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
- Ref.5
  "Characterization of two homologous 2'-O-methyltransferases showing different specificities for their tRNA substrates."
  Somme J., Van Laer B., Roovers M., Steyaert J., Versees W., Droogmans L.
  RNA 20:1257-1271(2014) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF ARG-23 AND TYR-140.
- Ref.6
  "tRNA recognition by a bacterial tRNA Xm32 modification enzyme from the SPOUT methyltransferase superfamily."
  Liu R.J., Long T., Zhou M., Zhou X.L., Wang E.D.
  Nucleic Acids Res. 43:7489-7503(2015) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN, MUTAGENESIS OF ARG-82; ARG-84; ARG-115; HIS-172; THR-175; TYR-177; PHE-199; LYS-211; ARG-213; ARG-214; ARG-218; GLU-225; ILE-228; LEU-229 AND GLY-231.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
S-adenosyl-L-methionine
zoom
+
uridine³² in tRNA
UMP residue
zoom
=
2'-O-methyluridine³² in tRNA
2'-O-methyluridine 5'-phosphate residue
zoom
+
H⁺
+
S-adenosyl-L-homocysteine
zoom

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

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

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

tRNA nucleoside ribose methylation
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- Ref.4
  "The yfhQ gene of Escherichia coli encodes a tRNA:Cm32/Um32 methyltransferase."
  Purta E., van Vliet F., Tkaczuk K.L., Dunin-Horkawicz S., Mori H., Droogmans L., Bujnicki J.M.
  BMC Mol. Biol. 7:23-23(2006) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Methyltransferase, Transferase
Biological process	tRNA processing
Ligand	S-adenosyl-L-methionine

Enzyme and pathway databases

BioCycⁱ	EcoCyc:G7327-MONOMER ECOL316407:JW2516-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	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Subcellular locationⁱ

Cytoplasm Curated

GO - Cellular componentⁱ

cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth."
  Lopez-Campistrous A., Semchuk P., Burke L., Palmer-Stone T., Brokx S.J., Broderick G., Bottorff D., Bolch S., Weiner J.H., Ellison M.J.
  Mol. Cell. Proteomics 4:1205-1209(2005) [PubMed] [Europe PMC] [Abstract]
- "Protein abundance profiling of the Escherichia coli cytosol."
  Ishihama Y., Schmidt T., Rappsilber J., Mann M., Hartl F.U., Kerner M.J., Frishman D.
  BMC Genomics 9:102-102(2008) [PubMed] [Europe PMC] [Abstract]

Complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	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 Publications

Protein-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

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	2 – 4	Combined sources	3
Beta strandⁱ	5 – 11	Combined sources	7
Helixⁱ	15 – 27	Combined sources	13
Beta strandⁱ	32 – 37	Combined sources	6
Helixⁱ	44 – 50	Combined sources	7
Helixⁱ	51 – 53	Combined sources	3
Helixⁱ	54 – 58	Combined sources	5
Beta strandⁱ	61 – 64	Combined sources	4
Helixⁱ	66 – 70	Combined sources	5
Beta strandⁱ	74 – 79	Combined sources	6
Beta strandⁱ	84 – 86	Combined sources	3
Helixⁱ	93 – 104	Combined sources	12
Beta strandⁱ	109 – 113	Combined sources	5
Turnⁱ	116 – 118	Combined sources	3
Helixⁱ	122 – 125	Combined sources	4
Beta strandⁱ	129 – 132	Combined sources	4
Helixⁱ	145 – 162	Combined sources	18
Helixⁱ	180 – 196	Combined sources	17
Helixⁱ	207 – 218	Combined sources	12
Helixⁱ	223 – 237	Combined sources	15

Show more details

3D 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	ENOG4105CVS Bacteria COG0565 LUCA
HOGENOMⁱ	HOG000229628
InParanoidⁱ	P0AE01
KEGG Orthology (KO) More...KOⁱ	K15396
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
Pfam protein domain database More...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

Sequenceⁱ

Sequence statusⁱ: Complete.

P0AE01-1 [UniParc]FASTA Add to basket

« Hide

        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

Length:246

Mass (Da):27,048

Last modified:December 6, 2005 - v1

Checksum:ⁱ83C1AE4507E097D2

GO

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
NCBI Reference Sequences More...RefSeqⁱ	NP_417027.1, NC_000913.3 WP_000940019.1, NZ_SSZK01000005.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC75585; AAC75585; b2532 BAA16426; BAA16426; BAA16426
GeneIDⁱ	948610
KEGGⁱ	ecj:JW2516 eco:b2532
PATRICⁱ	fig\|511145.12.peg.2633

Protein	Similar proteins		Species	Score	Length	Source
P0AE01	tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ		ECOK1		246	UniRef100_A1AE69
tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ		ECOL6		246
tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ		ECOUT		246
tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ		SHIBS		246
tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ		SHIF8		246
+200

Protein	Similar proteins		Species	Score	Length	Source
P0AE01	tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ		CITK8		243	UniRef90_A8AD50
tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ		ECOL5		246
tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ		ECOK1		246
tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ		ECOL6		246
tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ		ECOUT		246
+968

Protein	Similar proteins		Species	Score	Length	Source
P0AE01	tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ		PHOLL		241	UniRef50_Q7N222
tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ		CROS8		245
tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ		ECOK1		246
tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ		ECOL6		246
tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ		ECOUT		246
+2328

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: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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	948610
KEGGⁱ	ecj:JW2516 eco:b2532
PATRICⁱ	fig\|511145.12.peg.2633

Organism-specific databases

EchoBASEⁱ	EB3225

EchoBASEⁱ

EB3225

Phylogenomic databases

eggNOGⁱ	ENOG4105CVS Bacteria COG0565 LUCA
HOGENOMⁱ	HOG000229628
InParanoidⁱ	P0AE01
KOⁱ	K15396
PhylomeDBⁱ	P0AE01

Enzyme and pathway databases

BioCycⁱ	EcoCyc:G7327-MONOMER ECOL316407:JW2516-MONOMER MetaCyc:G7327-MONOMER
BRENDAⁱ	2.1.1.200 2026

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P0AE01

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:	November 13, 2019
	This is version 105 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, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P0AE01 (TRMJ_ECOLI)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

Catalytic activityⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ