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Protein

tRNA (guanine-N(1)-)-methyltransferase

Gene

trmD

Organism
Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1) (Rochalimaea henselae)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Specifically methylates guanosine-37 in various tRNAs.UniRule annotation

Catalytic activityi

S-adenosyl-L-methionine + guanine(37) in tRNA = S-adenosyl-L-homocysteine + N(1)-methylguanine(37) in tRNA.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei111 – 1111S-adenosyl-L-methionine; via amide nitrogenUniRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciBHEN283166:GIVZ-1577-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA (guanine-N(1)-)-methyltransferaseUniRule annotation (EC:2.1.1.228UniRule annotation)
Alternative name(s):
M1G-methyltransferaseUniRule annotation
tRNA [GM37] methyltransferaseUniRule annotation
Gene namesi
Name:trmDUniRule annotation
Ordered Locus Names:BH15820
OrganismiBartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1) (Rochalimaea henselae)
Taxonomic identifieri283166 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella
Proteomesi
  • UP000000421 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 232232tRNA (guanine-N(1)-)-methyltransferasePRO_0000060331Add
BLAST

Proteomic databases

PaxDbiQ6G1R9.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi283166.BH15820.

Structurei

Secondary structure

1
232
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108Combined sources
Helixi12 – 143Combined sources
Helixi17 – 204Combined sources
Helixi22 – 298Combined sources
Beta strandi32 – 398Combined sources
Helixi40 – 434Combined sources
Helixi66 – 738Combined sources
Beta strandi82 – 854Combined sources
Beta strandi89 – 913Combined sources
Helixi94 – 1007Combined sources
Beta strandi103 – 1108Combined sources
Helixi118 – 1236Combined sources
Beta strandi127 – 1348Combined sources
Helixi139 – 15113Combined sources
Beta strandi157 – 1593Combined sources
Helixi160 – 1623Combined sources
Helixi168 – 1714Combined sources
Beta strandi181 – 1855Combined sources
Helixi192 – 1954Combined sources
Helixi199 – 21719Combined sources
Helixi219 – 22810Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IEFX-ray2.50A/B1-232[»]
ProteinModelPortaliQ6G1R9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6G1R9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni131 – 1366S-adenosyl-L-methionine bindingUniRule annotation

Sequence similaritiesi

Belongs to the RNA methyltransferase TrmD family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105D6X. Bacteria.
COG0336. LUCA.
HOGENOMiHOG000016242.
KOiK00554.
OMAiYKGVDQR.
OrthoDBiEOG6J48RZ.

Family and domain databases

Gene3Di1.10.1270.20. 1 hit.
3.40.1280.10. 1 hit.
HAMAPiMF_00605. TrmD.
InterProiIPR029028. Alpha/beta_knot_MTases.
IPR002649. tRNA_m1G_MeTrfase_bac.
IPR023148. tRNA_m1G_MeTrfase_C.
IPR029026. tRNA_m1G_MTases_N.
IPR016009. tRNA_MeTrfase_TRMD/TRM10.
[Graphical view]
PfamiPF01746. tRNA_m1G_MT. 1 hit.
[Graphical view]
PIRSFiPIRSF000386. tRNA_mtase. 1 hit.
SUPFAMiSSF75217. SSF75217. 1 hit.
TIGRFAMsiTIGR00088. trmD. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6G1R9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFQARVLTL YPEMFPGFLG CSLAGQALKQ GIWSLETVQI RDFALDKHHS
60 70 80 90 100
VDDTPAGGGA GMVMRADVLA AALDSCPNDS PRLLMSPRGR LLNQAYARSL
110 120 130 140 150
ARSSGVTLVC GRFEGVDERI IEARELEEVS IGDYILSGGE TAALVLLDAI
160 170 180 190 200
VRLLPGVMGN EISAKCESFE NGLLEHPQYT RPAVFEGRGI PPVLTSGHHK
210 220 230
AIANWRQQQA ESLTRQRRPD LYALYNKNRQ KT
Length:232
Mass (Da):25,463
Last modified:July 19, 2004 - v1
Checksum:i4C89D122DB57C9BB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX897699 Genomic DNA. Translation: CAF28345.1.
RefSeqiWP_011181348.1. NZ_LRIJ01000002.1.

Genome annotation databases

EnsemblBacteriaiCAF28345; CAF28345; BH15820.
KEGGibhe:BH15820.
PATRICi20547460. VBIBarHen29080_1838.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX897699 Genomic DNA. Translation: CAF28345.1.
RefSeqiWP_011181348.1. NZ_LRIJ01000002.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IEFX-ray2.50A/B1-232[»]
ProteinModelPortaliQ6G1R9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi283166.BH15820.

Proteomic databases

PaxDbiQ6G1R9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAF28345; CAF28345; BH15820.
KEGGibhe:BH15820.
PATRICi20547460. VBIBarHen29080_1838.

Phylogenomic databases

eggNOGiENOG4105D6X. Bacteria.
COG0336. LUCA.
HOGENOMiHOG000016242.
KOiK00554.
OMAiYKGVDQR.
OrthoDBiEOG6J48RZ.

Enzyme and pathway databases

BioCyciBHEN283166:GIVZ-1577-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ6G1R9.

Family and domain databases

Gene3Di1.10.1270.20. 1 hit.
3.40.1280.10. 1 hit.
HAMAPiMF_00605. TrmD.
InterProiIPR029028. Alpha/beta_knot_MTases.
IPR002649. tRNA_m1G_MeTrfase_bac.
IPR023148. tRNA_m1G_MeTrfase_C.
IPR029026. tRNA_m1G_MTases_N.
IPR016009. tRNA_MeTrfase_TRMD/TRM10.
[Graphical view]
PfamiPF01746. tRNA_m1G_MT. 1 hit.
[Graphical view]
PIRSFiPIRSF000386. tRNA_mtase. 1 hit.
SUPFAMiSSF75217. SSF75217. 1 hit.
TIGRFAMsiTIGR00088. trmD. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49882 / DSM 28221 / Houston 1.

Entry informationi

Entry nameiTRMD_BARHE
AccessioniPrimary (citable) accession number: Q6G1R9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: July 19, 2004
Last modified: May 11, 2016
This is version 78 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

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.