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A4VRK4

- TRMB_PSEU5

UniProt

A4VRK4 - TRMB_PSEU5

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Protein

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

Gene

trmB

Organism
Pseudomonas stutzeri (strain A1501)
Status
Reviewed - 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 sitei68 – 681S-adenosyl-L-methionineUniRule annotation
Binding sitei93 – 931S-adenosyl-L-methionineUniRule annotation
Binding sitei120 – 1201S-adenosyl-L-methionineUniRule annotation
Active sitei143 – 1431By similarity
Binding sitei143 – 1431S-adenosyl-L-methionineUniRule annotation
Binding sitei147 – 1471SubstrateUniRule annotation
Binding sitei179 – 1791SubstrateUniRule 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

BioCyciPSTU379731:GJER-3977-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:PST_3982
OrganismiPseudomonas stutzeri (strain A1501)
Taxonomic identifieri379731 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000000233: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 238238tRNA (guanine-N(7)-)-methyltransferasePRO_1000064406Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi379731.PST_3982.

Structurei

3D structure databases

ProteinModelPortaliA4VRK4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni216 – 2194Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0220.
HOGENOMiHOG000073968.
KOiK03439.
OMAiHSTLEMA.
OrthoDBiEOG6K6VBC.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01057. tRNA_methyltr_TrmB.
InterProiIPR029063. SAM-dependent_MTases-like.
IPR003358. tRNA_(Gua-N-7)_MeTrfase.
[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.

A4VRK4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTEQNPAAEE QQSAPRRTIK SFVMRAGRMT EGQQRGLEQG WPKYGLELAD
60 70 80 90 100
GLRDFDEVFG RSAPRTFEIG FGMGHSTLEM AAAAPEQDFI GVEVHKPGVG
110 120 130 140 150
ALLSGLVSQK LTNVRVYSCD ALEVLRDCVA DASLDRVLLF FPDPWHKSRH
160 170 180 190 200
HKRRIVQPAF AELVRRKLKV GGVLHMATDW EPYAEHMLEV MNVAPGYRNL
210 220 230
AQDGRCVPRP TERPVTKFER RGERLGHGVW DLKFQRID
Length:238
Mass (Da):26,934
Last modified:May 29, 2007 - v1
Checksum:i9094E37DD6474AA1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000304 Genomic DNA. Translation: ABP81605.1.
RefSeqiYP_001174447.1. NC_009434.1.

Genome annotation databases

EnsemblBacteriaiABP81605; ABP81605; PST_3982.
GeneIDi5096943.
KEGGipsa:PST_3982.
PATRICi19968468. VBIPseStu31643_3963.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000304 Genomic DNA. Translation: ABP81605.1 .
RefSeqi YP_001174447.1. NC_009434.1.

3D structure databases

ProteinModelPortali A4VRK4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 379731.PST_3982.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABP81605 ; ABP81605 ; PST_3982 .
GeneIDi 5096943.
KEGGi psa:PST_3982.
PATRICi 19968468. VBIPseStu31643_3963.

Phylogenomic databases

eggNOGi COG0220.
HOGENOMi HOG000073968.
KOi K03439.
OMAi HSTLEMA.
OrthoDBi EOG6K6VBC.

Enzyme and pathway databases

UniPathwayi UPA00989 .
BioCyci PSTU379731:GJER-3977-MONOMER.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
HAMAPi MF_01057. tRNA_methyltr_TrmB.
InterProi IPR029063. SAM-dependent_MTases-like.
IPR003358. tRNA_(Gua-N-7)_MeTrfase.
[Graphical view ]
Pfami PF02390. Methyltransf_4. 1 hit.
[Graphical view ]
SUPFAMi SSF53335. SSF53335. 1 hit.
TIGRFAMsi TIGR00091. TIGR00091. 1 hit.
PROSITEi PS51625. SAM_MT_TRMB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete genome sequence of the metabolically versatile and root-associated nitrogen-fixing bacterium Pseudomonas stutzeri A1501."
    Yan Y., Yang J., Dou Y., Ping S., Chen M., Yao Z., Li H., Lu W., Zhang W., Peng J., Liu W., He S., Geng L., Zhang X., Yang F., Li D., Lin Z., Wang Y.
    , Elmerich C., Lin M., Jin Q.
    Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: A1501.

Entry informationi

Entry nameiTRMB_PSEU5
AccessioniPrimary (citable) accession number: A4VRK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 29, 2007
Last modified: October 29, 2014
This is version 52 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