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Q8DKJ8 (LFTR_THEEB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Leucyl/phenylalanyl-tRNA--protein transferase

EC=2.3.2.6
Alternative name(s):
L/F-transferase
Leucyltransferase
Phenyalanyltransferase
Gene names
Name:aat
Ordered Locus Names:tlr0861
OrganismThermosynechococcus elongatus (strain BP-1) [Reference proteome] [HAMAP]
Taxonomic identifier197221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus

Protein attributes

Sequence length196 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine By similarity. HAMAP-Rule MF_00688

Catalytic activity

L-leucyl-tRNA(Leu) + [protein] = tRNA(Leu) + L-leucyl-[protein]. HAMAP-Rule MF_00688

L-phenylalanyl-tRNA(Phe) + [protein] = tRNA + L-phenylalanyl-[protein]. HAMAP-Rule MF_00688

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00688.

Sequence similarities

Belongs to the L/F-transferase family.

Sequence caution

The sequence BAC08413.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionleucyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 196196Leucyl/phenylalanyl-tRNA--protein transferase HAMAP-Rule MF_00688
PRO_0000207245

Sequences

Sequence LengthMass (Da)Tools
Q8DKJ8 [UniParc].

Last modified July 25, 2003. Version 2.
Checksum: 21D1C1479603EB7E

FASTA19622,749
        10         20         30         40         50         60 
MEISQAEWVR DTFIDHRYAQ GYFLMGAGDR LEWYTSRQRA LIPLDERFRY PASLRRVLNQ 

        70         80         90        100        110        120 
NRFQVAINRD FSAVVEGCAD RPMTWITPRL KEVYHLLYAT GWAVSFETWQ GDELAGGILG 

       130        140        150        160        170        180 
IVIGGAFIGE SMFYRIPNGS KVAMVKLVEH LRQRGFLLFD AQLQNPHLER FGAYVVSPRK 

       190 
YRQLLAQAIR KPCQFL 

« Hide

References

[1]"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1."
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takeuchi C., Yamada M., Tabata S.
DNA Res. 9:123-130(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BP-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000039 Genomic DNA. Translation: BAC08413.1. Different initiation.
RefSeqNP_681651.1. NC_004113.1.

3D structure databases

ProteinModelPortalQ8DKJ8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING197221.tlr0861.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC08413; BAC08413; BAC08413.
GeneID1011482.
KEGGtel:tlr0861.
PATRIC23927012. VBITheElo119873_0906.

Phylogenomic databases

eggNOGCOG2360.
HOGENOMHOG000102326.
KOK00684.
OMAYFLMADE.
OrthoDBEOG6WX4R3.
ProtClustDBPRK00301.

Family and domain databases

HAMAPMF_00688. Leu_Phe_trans.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR004616. Leu/Phe-tRNA_Trfase.
[Graphical view]
PfamPF03588. Leu_Phe_trans. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
TIGRFAMsTIGR00667. aat. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLFTR_THEEB
AccessionPrimary (citable) accession number: Q8DKJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: July 25, 2003
Last modified: February 19, 2014
This is version 60 of the entry and version 2 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