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Reviewed, UniProtKB/Swiss-Prot Q68XR8 (TILS_RICTY)

Last modified December 15, 2009. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    tRNA(Ile)-lysidine synthase
    EC=6.3.4.-
Alternative name(s):
    tRNA(Ile)-lysidine synthetase
    tRNA(Ile)-2-lysyl-cytidine synthase
Gene names
Name: tilS
Ordered Locus Names: RT0088
OrganismRickettsia typhi [Complete proteome] [HAMAP]
Taxonomic identifier785 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine By similarity.

Subcellular location

Cytoplasm Probable.

Domain

The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding. HAMAP MF_01161

Sequence similarities

Belongs to the tRNA(Ile)-lysidine synthase family.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processtRNA modification

Inferred from electronic annotation. Source: HAMAP

translation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ligase activity, forming carbon-nitrogen bonds

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 430430tRNA(Ile)-lysidine synthase HAMAP MF_01161
PRO_0000181758

Regions

Nucleotide binding27 – 326ATP Potential

Sequences

Sequence LengthMass (Da)Tools
Q68XR8-1 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: DCE2ADDEE3001E73

FASTA43050,397
        10         20         30         40         50         60 
MLYEKFEYNI NNLVGNFGLS KIAIAVSGGS DSVALLYLAN IWAEKNNIEL FIISVDHNLR 

        70         80         90        100        110        120 
AQSKQENYYI QSISNNLKRK YYNLSFDHQN NFSNLQARAR EGRYDLMTNL CLELDVLVLL 

       130        140        150        160        170        180 
TAHHEDDYVE NFCLRLERNS GIFGLSSSNI HWYNNIQIIR PLYNIPKSEL VKYLVTNKIK 

       190        200        210        220        230        240 
WFEDESNLSD KYRRNIIRQK LFKEENYIKA EISVQQLKTN KLIEDELKPE LISAIGEAVK 

       250        260        270        280        290        300 
IFEYGFTFLD LVKFDKFSNE VKVQIINFLL IMISGQSRSA RFYSIAPILK LISQNVNFKK 

       310        320        330        340        350        360 
TVHGCVITRI QNELLIYREF GKKLPKSKIL LDKSVIWDNR FCITKNQETP DCVITYLSLE 

       370        380        390        400        410        420 
DYKVIKKQLD LKHLKNLSCK NHNAILFTLP IIKILEKVIA IPHISYYDND MWNFEVSFAP 

       430 
NFVSRFTHFC 

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References

[1]"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae."
McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. expand/collapse author list , Hong C., Yu X.-J., Walker D.H., Weinstock G.M.
J. Bacteriol. 186:5842-5855(2004) [PubMed: 15317790] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-144 / Wilmington.

Cross-references

Sequence databases

AE017197 Genomic DNA. Translation: AAU03574.1.
RefSeqYP_067056.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2959100.
GenomeReviewsGene locus RT0088 in contig AE017197_GR.
KEGGrty:RT0088.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG586536.
OMANNIQIIR.

Enzyme and pathway databases

BioCycRTYP257363:RT0088-MON.

Family and domain databases

HAMAPMF_01161.
[Tree]
InterProIPR012094. Lysidine-tRNA-synth.
IPR012795. Lysidine-tRNA-synth_N.
IPR011063. PP_loop.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11807:SF2. ATPase_MesJ_YaeO. 1 hit.
PfamPF01171. ATP_bind_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTILS_RICTY
AccessionPrimary (citable) accession number: Q68XR8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: October 11, 2004
Last modified: December 15, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Rickettsia typhi

Rickettsia typhi (strain Wilmington): entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents