Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

tRNA (guanine-N(7)-)-methyltransferase

Gene

trmB

Organism
Histophilus somni (strain 2336) (Haemophilus somnus)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.UniRule annotation

Catalytic activityi

S-adenosyl-L-methionine + guanine(46) in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine(46) in tRNA.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei80 – 801S-adenosyl-L-methionineUniRule annotation
Binding sitei105 – 1051S-adenosyl-L-methionineUniRule annotation
Binding sitei132 – 1321S-adenosyl-L-methionineUniRule annotation
Active sitei155 – 1551By similarity
Binding sitei155 – 1551S-adenosyl-L-methionineUniRule annotation
Binding sitei159 – 1591SubstrateUniRule annotation
Binding sitei191 – 1911SubstrateUniRule annotation

GO - Molecular functioni

  1. tRNA (guanine-N7-)-methyltransferase activity Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciHSOM228400:GHWT-1868-MONOMER.
UniPathwayiUPA00989.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA (guanine-N(7)-)-methyltransferaseUniRule annotation (EC:2.1.1.33UniRule annotation)
Alternative name(s):
tRNA (guanine(46)-N(7))-methyltransferaseUniRule annotation
tRNA(m7G46)-methyltransferaseUniRule annotation
Gene namesi
Name:trmBUniRule annotation
Ordered Locus Names:HSM_1828
OrganismiHistophilus somni (strain 2336) (Haemophilus somnus)
Taxonomic identifieri228400 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus
ProteomesiUP000008543: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 251251tRNA (guanine-N(7)-)-methyltransferasePRO_1000084443Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi228400.HSM_1828.

Structurei

3D structure databases

ProteinModelPortaliB0UWE3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni228 – 2314Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0220.
HOGENOMiHOG000073968.
KOiK03439.
OMAiHYKRRFV.
OrthoDBiEOG6K6VBC.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01057. tRNA_methyltr_TrmB.
InterProiIPR029063. SAM-dependent_MTases.
IPR003358. tRNA_(Gua-N-7)_MeTrfase_Trmb.
[Graphical view]
PfamiPF02390. Methyltransf_4. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00091. TIGR00091. 1 hit.
PROSITEiPS51625. SAM_MT_TRMB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B0UWE3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEQKITFAD QKRKTVEIAE FTEDGRYKRK VRSFVLRTGR LSEFQRNMMN
60 70 80 90 100
NNWATLGLEY QTTAFDFTQI YGNTNPVILE IGFGMGKSLV EMALQNPDKN
110 120 130 140 150
YLGIEVHTPG VGACIAYAVE KQVKNLRVIC HDATEILQDC IADNSLAGLQ
160 170 180 190 200
LFFPDPWHKT KHHKRRIVQP HFVEKIQQKL VPNGFVHMAT DWENYAEYML
210 220 230 240 250
EVLTSAVGLH NTSATNDYIP RPDFRPLTKF EQRGHKLGHG VWDLFFIKNI

T
Length:251
Mass (Da):28,948
Last modified:April 8, 2008 - v1
Checksum:iFBE73D447F17A7C4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000947 Genomic DNA. Translation: ACA31614.1.
RefSeqiWP_012340923.1. NC_010519.1.
YP_001785146.1. NC_010519.1.

Genome annotation databases

EnsemblBacteriaiACA31614; ACA31614; HSM_1828.
GeneIDi6107752.
KEGGihsm:HSM_1828.
PATRICi20200924. VBIHaeSom93646_1925.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000947 Genomic DNA. Translation: ACA31614.1.
RefSeqiWP_012340923.1. NC_010519.1.
YP_001785146.1. NC_010519.1.

3D structure databases

ProteinModelPortaliB0UWE3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi228400.HSM_1828.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACA31614; ACA31614; HSM_1828.
GeneIDi6107752.
KEGGihsm:HSM_1828.
PATRICi20200924. VBIHaeSom93646_1925.

Phylogenomic databases

eggNOGiCOG0220.
HOGENOMiHOG000073968.
KOiK03439.
OMAiHYKRRFV.
OrthoDBiEOG6K6VBC.

Enzyme and pathway databases

UniPathwayiUPA00989.
BioCyciHSOM228400:GHWT-1868-MONOMER.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01057. tRNA_methyltr_TrmB.
InterProiIPR029063. SAM-dependent_MTases.
IPR003358. tRNA_(Gua-N-7)_MeTrfase_Trmb.
[Graphical view]
PfamiPF02390. Methyltransf_4. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00091. TIGR00091. 1 hit.
PROSITEiPS51625. SAM_MT_TRMB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 2336.

Entry informationi

Entry nameiTRMB_HISS2
AccessioniPrimary (citable) accession number: B0UWE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 8, 2008
Last modified: February 4, 2015
This is version 48 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.