Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Leucyl/phenylalanyl-tRNA--protein transferase

Gene

aat

Organism
Cupriavidus necator (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134))
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = tRNA(Leu) + N-terminal L-leucyl-L-lysyl-[protein].UniRule annotation
L-leucyl-tRNA(Leu) + N-terminal L-arginyl-[protein] = tRNA(Leu) + N-terminal L-leucyl-L-arginyl-[protein].UniRule annotation
L-phenylalanyl-tRNA(Phe) + [protein] = tRNA + L-phenylalanyl-[protein].UniRule annotation

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Leucyl/phenylalanyl-tRNA--protein transferaseUniRule annotation (EC:2.3.2.6UniRule annotation)
Alternative name(s):
L/F-transferaseUniRule annotation
LeucyltransferaseUniRule annotation
PhenyalanyltransferaseUniRule annotation
Gene namesi
Name:aatUniRule annotation
Ordered Locus Names:Reut_A1319
OrganismiCupriavidus necator (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134))
Taxonomic identifieri264198 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
Proteomesi
  • UP000002697 Componenti: Chromosome 1

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002580831 – 250Leucyl/phenylalanyl-tRNA--protein transferaseAdd BLAST250

Interactioni

Protein-protein interaction databases

STRINGi264198.Reut_A1319

Structurei

3D structure databases

ProteinModelPortaliQ472J4
SMRiQ472J4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the L/F-transferase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108R4Z Bacteria
COG2360 LUCA
HOGENOMiHOG000102325
KOiK00684
OMAiYRQGIFP
OrthoDBiPOG091H045I

Family and domain databases

HAMAPiMF_00688 Leu_Phe_trans, 1 hit
InterProiView protein in InterPro
IPR016181 Acyl_CoA_acyltransferase
IPR004616 Leu/Phe-tRNA_Trfase
PANTHERiPTHR30098 PTHR30098, 1 hit
PfamiView protein in Pfam
PF03588 Leu_Phe_trans, 1 hit
SUPFAMiSSF55729 SSF55729, 1 hit
TIGRFAMsiTIGR00667 aat, 1 hit

Sequencei

Sequence statusi: Complete.

Q472J4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIAWLDPHDP FPPVERALGP ATEAPGLLAA SRDLSPQRLL LAYRQGIFPW
60 70 80 90 100
YSVGQPVLWW STDPRMVLAP QALKISATFR KTLRRVLRDP DWEIRVDDDF
110 120 130 140 150
LAVMRACAMT PREGQDGTWI TREIIAAYGA LHSNGMAHSV ETWYRGTRVG
160 170 180 190 200
GLYGVALGRM FYGESMFAHR TDASKIALAA LCAFLGSHGV PMIDCQQETD
210 220 230 240 250
HLASLGARPI ARAEFLAHVR NASAQPAITP WWFDKSVLER WTATPATPAV
Length:250
Mass (Da):27,751
Last modified:September 13, 2005 - v1
Checksum:i1DEE76B7D03DB727
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000090 Genomic DNA Translation: AAZ60689.1
RefSeqiWP_011297489.1, NC_007347.1

Genome annotation databases

EnsemblBacteriaiAAZ60689; AAZ60689; Reut_A1319
KEGGireu:Reut_A1319

Similar proteinsi

Entry informationi

Entry nameiLFTR_CUPNJ
AccessioniPrimary (citable) accession number: Q472J4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: September 13, 2005
Last modified: May 23, 2018
This is version 74 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health