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Q92JK6 (TSAD_RICCN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 73. 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 N6-adenosine threonylcarbamoyltransferase

EC=2.3.1.-
Alternative name(s):
t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
Gene names
Name:tsaD
Synonyms:gcp
Ordered Locus Names:RC0061
OrganismRickettsia conorii (strain ATCC VR-613 / Malish 7) [Complete proteome] [HAMAP]
Taxonomic identifier272944 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction By similarity. HAMAP-Rule MF_01445

Cofactor

Binds 1 Fe2+ ion per subunit By similarity. HAMAP-Rule MF_01445

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01445.

Sequence similarities

Belongs to the KAE1 / TsaD family.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
   LigandIron
Metal-binding
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processthreonylcarbamoyladenosine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioniron ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

transferase activity, transferring acyl groups other than amino-acyl groups

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 344344tRNA N6-adenosine threonylcarbamoyltransferase HAMAP-Rule MF_01445
PRO_0000303523

Regions

Region134 – 1385Substrate binding By similarity

Sites

Metal binding1121Iron By similarity
Metal binding1161Iron By similarity
Metal binding3081Iron By similarity
Binding site1671Substrate By similarity
Binding site1801Substrate; via amide nitrogen By similarity
Binding site2801Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92JK6 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 72B082999B0B7408

FASTA34437,302
        10         20         30         40         50         60 
MIKILGIESS CDDTAVSIIT ENREILSNII ISQNTEHAVF GGVVPEIAAR SHLSHLDKAL 

        70         80         90        100        110        120 
KNVLKESNTK LTDISTIAAT SGPGLIGGVI VGSMFARSLS SALKKPFIAI NHLEGHALTA 

       130        140        150        160        170        180 
RLTDNIPYPY LLLLASGGHC QFVAVLGLGK YKILGSTIDD AVGEAFDKVA KMLNLAFPGG 

       190        200        210        220        230        240 
PEIEKRAKLG DPHKYKFPKP IINSGNCNMS FSGLKTAVRT LIMTLKEIND TVINDIAASF 

       250        260        270        280        290        300 
QFTIGEILSS KVQDAIRAYE QITNNFDKKN IVIAGGVAAN KYLQKILSSC AKTYGYRLIY 

       310        320        330        340 
PPIHLCTDNA AMIAYAGLER YNNKLFTPLN FCPKARWSLE DISN 

« 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] [Europe PMC] [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: AAL02599.1.
PIRE97707.
RefSeqNP_359698.1. NC_003103.1.

3D structure databases

ProteinModelPortalQ92JK6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272944.RC0061.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL02599; AAL02599; RC0061.
GeneID928604.
KEGGrco:RC0061.
PATRIC17887216. VBIRicCon45613_0072.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0533.
HOGENOMHOG000109568.
KOK01409.
OMARDHVKRM.
OrthoDBEOG6K402S.
ProtClustDBPRK09604.

Family and domain databases

HAMAPMF_01445. TsaD.
InterProIPR000905. Gcp-like_dom.
IPR017861. KAE1/YgjD.
IPR017860. Peptidase_M22_CS.
IPR022450. TsaD.
[Graphical view]
PfamPF00814. Peptidase_M22. 1 hit.
[Graphical view]
PRINTSPR00789. OSIALOPTASE.
TIGRFAMsTIGR00329. gcp_kae1. 1 hit.
TIGR03723. T6A_YgjD. 1 hit.
PROSITEPS01016. GLYCOPROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTSAD_RICCN
AccessionPrimary (citable) accession number: Q92JK6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: December 1, 2001
Last modified: March 19, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Rickettsia conorii

(strain Malish 7): entries and gene names