Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B7UJ61 (B7UJ61_ECO27) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
tRNA pseudouridine synthase B HAMAP-Rule MF_01080

EC=5.4.99.25 HAMAP-Rule MF_01080
Alternative name(s):
tRNA pseudouridine(55) synthase HAMAP-Rule MF_01080
tRNA pseudouridylate synthase HAMAP-Rule MF_01080
tRNA-uridine isomerase HAMAP-Rule MF_01080
Gene names
Name:truB HAMAP-Rule MF_01080 EMBL CAS10995.1
Ordered Locus Names:E2348C_3447 EMBL CAS10995.1
OrganismEscherichia coli O127:H6 (strain E2348/69 / EPEC) [Complete proteome] [HAMAP] EMBL CAS10995.1
Taxonomic identifier574521 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs By similarity. HAMAP-Rule MF_01080 SAAS SAAS002501

Catalytic activity

tRNA uridine55 = tRNA pseudouridine55. HAMAP-Rule MF_01080 SAAS SAAS002501

Sequence similarities

Belongs to the pseudouridine synthase TruB family. Type 1 subfamily. HAMAP-Rule MF_01080

Ontologies

Keywords
   Biological processtRNA processing HAMAP-Rule MF_01080 SAAS SAAS002501
   Molecular functionIsomerase HAMAP-Rule MF_01080 SAAS SAAS002501
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtRNA pseudouridine synthesis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: InterPro

pseudouridine synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site481Nucleophile By similarity HAMAP-Rule MF_01080
Binding site431Substrate By similarity HAMAP-Rule MF_01080
Binding site761Substrate By similarity HAMAP-Rule MF_01080
Binding site1791Substrate By similarity HAMAP-Rule MF_01080
Binding site2001Substrate By similarity HAMAP-Rule MF_01080

Sequences

Sequence LengthMass (Da)Tools
B7UJ61 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: FEA46C01E0E8E7A5

FASTA31435,087
        10         20         30         40         50         60 
MSRPRRRGRD INGVLLLDKP QGMSSNDALQ KVKRIYNANR AGHTGALDPL ATGMLPICLG 

        70         80         90        100        110        120 
EATKFSQYLL DSDKRYRVIA RLGQRTDTSD ADGQIVEERP VTFSAEQLAA ALDTFRGDIE 

       130        140        150        160        170        180 
QIPSMYSALK YQGKKLYEYA RQGIEVPREA RPITVYELLF IRHEGNELEL EIHCSKGTYI 

       190        200        210        220        230        240 
RTIIDDLGEK LGCGAHVIYL RRLAVSKYPV ERMVTLEHLR ELVEQAEQQD IPAAELLDPL 

       250        260        270        280        290        300 
LMPMDSPASD YPVVNLPLTS SVYFKNGNPV RTSGAPLEGL VRVTEGENGK FIGMGEIDDE 

       310 
GRVAPRRLVV EYPA 

« Hide

References

[1]"Complete genome sequence and comparative genome analysis of enteropathogenic Escherichia coli O127:H6 strain E2348/69."
Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.
J. Bacteriol. 191:347-354(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E2348/69 / EPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM180568 Genomic DNA. Translation: CAS10995.1.
RefSeqYP_002330915.1. NC_011601.1.

3D structure databases

ProteinModelPortalB7UJ61.
SMRB7UJ61. Positions 10-311.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING574521.E2348C_3447.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAS10995; CAS10995; E2348C_3447.
GeneID7061154.
KEGGecg:E2348C_3447.
PATRIC18346058. VBIEscCol90278_3520.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0130.
HOGENOMHOG000231223.
KOK03177.
OMAQKVKRIF.
OrthoDBEOG6358D3.
ProtClustDBPRK05033.

Enzyme and pathway databases

BioCycECOL574521:GJAO-3573-MONOMER.

Family and domain databases

Gene3D2.30.130.10. 1 hit.
HAMAPMF_01080. TruB_bact.
InterProIPR002501. PsdUridine_synth.
IPR020103. PsdUridine_synth_cat_dom.
IPR015947. PUA-like_domain.
IPR014780. tRNA_psdUridine_synth_TruB.
IPR015240. tRNA_sdUridine_synth_fam1_C.
[Graphical view]
PANTHERPTHR13767. PTHR13767. 1 hit.
PfamPF09157. TruB-C_2. 1 hit.
PF01509. TruB_N. 1 hit.
[Graphical view]
SUPFAMSSF55120. SSF55120. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsTIGR00431. TruB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB7UJ61_ECO27
AccessionPrimary (citable) accession number: B7UJ61
Entry history
Integrated into UniProtKB/TrEMBL: February 10, 2009
Last sequence update: February 10, 2009
Last modified: February 19, 2014
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)