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P57166 (TSAD_BUCAI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 82. 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:BU058
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) [Reference proteome] [HAMAP]
Taxonomic identifier107806 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length336 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
Reference 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 – 336336tRNA N6-adenosine threonylcarbamoyltransferase HAMAP-Rule MF_01445
PRO_0000096959

Regions

Region133 – 1375Substrate binding By similarity

Sites

Metal binding1101Iron By similarity
Metal binding1141Iron By similarity
Metal binding3001Iron By similarity
Binding site1661Substrate By similarity
Binding site1791Substrate; via amide nitrogen By similarity
Binding site2711Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P57166 [UniParc].

Last modified December 1, 2000. Version 1.
Checksum: 11FE9A328D885971

FASTA33637,438
        10         20         30         40         50         60 
MRILGIETSC DDTGIAIYDT NKGLLINEIY NQRKLNNIYG GIIPELASRE HMEAMIVLLN 

        70         80         90        100        110        120 
KIFKKKNIYK YVDMIAYTAG PGLIGSLLVG ATFACSLGLS LNIPVLPVHH MEAHLLSPML 

       130        140        150        160        170        180 
DYKTIQFPFI GLLVSGKHTQ IIGAHKFGEY EILGNCLDDA AGEAFDKTAK LLGLKYPGGL 

       190        200        210        220        230        240 
ELSKLASKGI KDYFYFPRPM IHHSDLNFSF SGLKTFAAQT IKKSSKSMQE KANIAKAFED 

       250        260        270        280        290        300 
AVIDILLIKT KKALKKQKWK RLVIAGGVSA NQKLRKKSEI MVKKNFNGTV FYSSLEFCTD 

       310        320        330 
NAAMIAYLGS LRQKEARNSQ LEILVKPKWS IDDLCF 

« Hide

References

[1]"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS."
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.
Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: APS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000003 Genomic DNA. Translation: BAB12781.1.
RefSeqNP_239895.1. NC_002528.1.

3D structure databases

ProteinModelPortalP57166.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB12781; BAB12781; BAB12781.
GeneID1109465.
KEGGbuc:BU058.
PATRIC21243622. VBIBucAph127364_0067.

Phylogenomic databases

eggNOGCOG0533.
HOGENOMHOG000109568.
KOK01409.
OMAQLMRVDG.
OrthoDBEOG6K402S.
ProtClustDBPRK09604.

Enzyme and pathway databases

BioCycBAPH107806:GBZJ-58-MONOMER.

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_BUCAI
AccessionPrimary (citable) accession number: P57166
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: March 19, 2014
This is version 82 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

Buchnera aphidicola (subsp. Acyrthosiphon pisum)

Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names