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Q92JK0 (TILS_RICCN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
tRNA(Ile)-lysidine synthase

EC=6.3.4.19
Alternative name(s):
tRNA(Ile)-2-lysyl-cytidine synthase
tRNA(Ile)-lysidine synthetase
Gene names
Name:tilS
Ordered Locus Names:RC0067
OrganismRickettsia conorii (strain ATCC VR-613 / Malish 7) [Complete proteome] [HAMAP]
Taxonomic identifier272944 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length478 AA.
Sequence statusComplete.
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. HAMAP MF_01161

Catalytic activity

(tRNA(Ile2))-cytidine(34) + L-lysine + ATP = (tRNA(Ile2))-lysidine(34) + AMP + diphosphate + H2O. HAMAP MF_01161

Subcellular location

Cytoplasm Probable HAMAP MF_01161.

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 processing

Inferred from electronic annotation. Source: UniProtKB-KW

   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: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 478478tRNA(Ile)-lysidine synthase HAMAP MF_01161
PRO_0000181756

Regions

Nucleotide binding27 – 326ATP Potential

Sequences

Sequence LengthMass (Da)Tools
Q92JK0 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: A169B1D28E9EE7CE

FASTA47855,546
        10         20         30         40         50         60 
MLYEKFEYNI NNLIGNFGLS KISIAVSGGS DSVALLYLAN IWAEKNNIEL FVISVDHNLR 

        70         80         90        100        110        120 
EQSKQETHYI QNISNSLNRK HYSLSFDHQN NFSNLQERAR EGRYDLMTNL CLELDILVLL 

       130        140        150        160        170        180 
TAHHEDDYVE NFCLRLERNS GIFGLSSSNI NWYNNIQIIR PLYNIPKSEL VEYLVRHNIK 

       190        200        210        220        230        240 
WFEDESNSSD KYRRNVIRQK LAKGADYIRH FSKPVYREEF KGDTERSTAA YTLVREDAST 

       250        260        270        280        290        300 
GTASKLSLEA KCGKMSKAAI ISQQLKTNKL IENEFKPELI SAIAEAVKIF EYGFAFLDLV 

       310        320        330        340        350        360 
KFDKFSNEVK VQIINFLLII ISGQSRAARF YSVEPILKLI TQDVNFKNTL HGCIIKRIQN 

       370        380        390        400        410        420 
ELLIYREFGK KLPESKILLD KSVIWDNRFC ITKNQETPNC FVTHLSLKDY KIIKKQLDLE 

       430        440        450        460        470 
PLKNLSCKNH NAVLLTLPII KILEKVIAIP HISYYDNDMW NFEVSFSPNF VSRFTHFC 

« Hide

References

[1]"Mechanisms of evolution in Rickettsia conorii and R. prowazekii."
Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.
Science 293:2093-2098(2001) [PubMed: 11557893] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006914 Genomic DNA. Translation: AAL02605.1.
PIRC97708.
RefSeqNP_359704.1. NC_003103.1.

3D structure databases

ProteinModelPortalQ92JK0.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID928597.
GenomeReviewsGene locus RC0067 in contig AE006914_GR.
KEGGrco:RC0067.
NMPDRfig|272944.1.peg.67.
PATRIC17887228. VBIRicCon45613_0078.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMANIQIIRP.
ProtClustDBCLSK870716.

Enzyme and pathway databases

BioCycRCON272944:RC0067-MONOMER.

Family and domain databases

HAMAPMF_01161. tRNA(Ile)-lys_synt.
[Tree]
InterProIPR012094. Lysidine-tRNA-synth.
IPR012795. Lysidine-tRNA-synth_N.
IPR005728. Rickett_RPE.
IPR014729. Rossmann-like_a/b/a_fold.
IPR011063. tRNA-lysidine/thiocyt_synth.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KOK04075.
PANTHERPTHR11807:SF2. ATPase_MesJ_YaeO. 1 hit.
PfamPF01171. ATP_bind_3. 1 hit.
[Graphical view]
TIGRFAMsTIGR02432. Lysidine_TilS_N. 1 hit.
TIGR01045. RPE1. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTILS_RICCN
AccessionPrimary (citable) accession number: Q92JK0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: December 1, 2001
Last modified: January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Rickettsia conorii

(strain Malish 7): entries and gene names

SIMILARITY comments

Index of protein domains and families