Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8F9T2 (LFTR_LEPIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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:LA_0108
OrganismLeptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) [Reference proteome] [HAMAP]
Taxonomic identifier189518 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length219 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.

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 – 219219Leucyl/phenylalanyl-tRNA--protein transferase HAMAP-Rule MF_00688
PRO_0000207227

Sequences

Sequence LengthMass (Da)Tools
Q8F9T2 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: E461CFFE1B4FB575

FASTA21925,596
        10         20         30         40         50         60 
MKDFSDFFRN PHIWDREIVA VGGDLSPERL LYAYKNGIFP WSDQPILWYC LDPRSIFDLN 

        70         80         90        100        110        120 
KLHISKRLKR KINQKRYTIT FNRAFEQVMR CCAYRPGEDT WITDLFIKSY TEFHKLGYAH 

       130        140        150        160        170        180 
SLEVWDENGK LGGGVYGIAI GNFFAGESMF SFIPDFGKIG LFHLFETLKK DHFTLFDTQQ 

       190        200        210 
LNLVTLSLGA YQIPKKEYLK RLESAVASGK KWNPSHFVL 

« Hide

References

[1]"Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing."
Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H. expand/collapse author list , Yin H.-F., Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.
Nature 422:888-893(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 56601.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE010300 Genomic DNA. Translation: AAN47307.1.
RefSeqNP_710289.1. NC_004342.2.

3D structure databases

ProteinModelPortalQ8F9T2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING189518.LA0108.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN47307; AAN47307; LA_0108.
GeneID1149451.
KEGGlil:LA_0108.
PATRIC22381059. VBILepInt91350_0111.

Phylogenomic databases

eggNOGCOG2360.
HOGENOMHOG000102325.
KOK00684.
OMAERFRYPR.
OrthoDBEOG6WX4R3.

Enzyme and pathway databases

BioCycLINT189518:GJBB-97-MONOMER.

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_LEPIN
AccessionPrimary (citable) accession number: Q8F9T2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: March 1, 2003
Last modified: May 14, 2014
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

SIMILARITY comments

Index of protein domains and families