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Q3SH93 (LFTR_THIDA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. 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:Tbd_2043
OrganismThiobacillus denitrificans (strain ATCC 25259) [Complete proteome] [HAMAP]
Taxonomic identifier292415 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaHydrogenophilalesHydrogenophilaceaeThiobacillus

Protein attributes

Sequence length228 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
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 – 228228Leucyl/phenylalanyl-tRNA--protein transferase HAMAP-Rule MF_00688
PRO_0000258106

Sequences

Sequence LengthMass (Da)Tools
Q3SH93 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: DF5F323088BCA553

FASTA22825,573
        10         20         30         40         50         60 
MKEPFTNASY FPPVETALVD PNGLLAIGGD LSQERLLDAY RHGIFPWFNP REPIQWWSPD 

        70         80         90        100        110        120 
PRMVLPPAEI RVTRSLAKRL RNAGFELRVD SAFIEVMRAC GAPREGAWGT WISAPMIAAY 

       130        140        150        160        170        180 
GRLFDAGYAH SIETWRDGRL VGGLYGVAIG RMFYGESMFS REPDASKVAL VRLARQLERW 

       190        200        210        220 
GFGLIDCQME TPHLASMGAR PIPRADFTAR LAELVNLPHL PGPWTFDS 

« Hide

References

[1]"The genome sequence of the obligately chemolithoautotrophic, facultatively anaerobic bacterium Thiobacillus denitrificans."
Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W., Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.
J. Bacteriol. 188:1473-1488(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25259.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000116 Genomic DNA. Translation: AAZ97996.1.
RefSeqYP_315801.1. NC_007404.1.

3D structure databases

ProteinModelPortalQ3SH93.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292415.Tbd_2043.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ97996; AAZ97996; Tbd_2043.
GeneID3672214.
KEGGtbd:Tbd_2043.
PATRIC23970261. VBIThiDen82923_2021.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2360.
HOGENOMHOG000102325.
KOK00684.
OMAIGHAHSV.
OrthoDBEOG6WX4R3.

Enzyme and pathway databases

BioCycTDEN292415:GHWG-2089-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_THIDA
AccessionPrimary (citable) accession number: Q3SH93
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 11, 2005
Last modified: May 14, 2014
This is version 57 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