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Protein

Leucine--tRNA ligase

Gene

leuS

Organism
Nitratiruptor sp. (strain SB155-2)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu).UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei586 – 5861ATPUniRule annotation

GO - Molecular functioni

  1. aminoacyl-tRNA editing activity Source: InterPro
  2. arginine-tRNA ligase activity Source: InterPro
  3. ATP binding Source: UniProtKB-HAMAP
  4. leucine-tRNA ligase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. arginyl-tRNA aminoacylation Source: InterPro
  2. leucyl-tRNA aminoacylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciNSP387092:GHA5-1509-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Leucine--tRNA ligaseUniRule annotation (EC:6.1.1.4UniRule annotation)
Alternative name(s):
Leucyl-tRNA synthetaseUniRule annotation
Short name:
LeuRSUniRule annotation
Gene namesi
Name:leuSUniRule annotation
Ordered Locus Names:NIS_1464
OrganismiNitratiruptor sp. (strain SB155-2)
Taxonomic identifieri387092 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaNitratiruptor
ProteomesiUP000001118: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 815815Leucine--tRNA ligasePRO_1000009382Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi387092.NIS_1464.

Structurei

3D structure databases

ProteinModelPortaliA6Q512.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi40 – 5011"HIGH" regionAdd
BLAST
Motifi583 – 5875"KMSKS" region

Sequence similaritiesi

Belongs to the class-I aminoacyl-tRNA synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0495.
HOGENOMiHOG000200747.
KOiK01869.
OMAiQSSWYFL.
OrthoDBiEOG63Z74X.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 2 hits.
HAMAPiMF_00049_B. Leu_tRNA_synth_B.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR001278. Arg-tRNA-ligase.
IPR002302. Leu-tRNA-ligase.
IPR025709. Leu_tRNA-synth_edit.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view]
PANTHERiPTHR11946:SF7. PTHR11946:SF7. 1 hit.
PfamiPF00133. tRNA-synt_1. 1 hit.
PF13603. tRNA-synt_1_2. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSiPR00985. TRNASYNTHLEU.
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsiTIGR00396. leuS_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A6Q512-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQYDPKAIEQ KWQNEWKEKN AFEPQENYSK EKMYVLSMFP YPSGRIHMGH
60 70 80 90 100
VRNYTIGDAI ARYYRKTGAN VLHPIGWDAF GMPAENAAIK HKVHPKKWTY
110 120 130 140 150
ENIDYMRKEL DALGLSFSHD REFATCDPLY SKWEQSFIID MWNRGLLYRK
160 170 180 190 200
KAAVNWCPHD KTVLANEQVI EGRCWRCDTE VVQKEIEQYF LKITDYAQEL
210 220 230 240 250
LEDLKKLEGN WPNQVIAMQR NWIGRSEGLE FRLHFDETSA KKAGIDGFEV
260 270 280 290 300
FTTRPDTIYG VTYTALAPEH PVVKHLIETK QLSDEAVQKI CTMQNQNART
310 320 330 340 350
RQQAEKEGLF LDLYVIHPLT KQKIPVWVAN FVLAEYGSGA VMAVPAHDER
360 370 380 390 400
DFEFAHKYNL PIKYIIKPKE GELDTTKAYT EPGILFDSGE FSGFESSEAK
410 420 430 440 450
QKIIEYFEEN GIGKRSVNYK LKDWLVSRQR YWGTPIPLIK CPKCGIVPEK
460 470 480 490 500
KENLPVTLPE DVEITGEGNP LELHPTWKKT TCPKCGGEAE RETDTLDTFV
510 520 530 540 550
ESSWYFLRYT TPRKYWEEVP FRKEDTDYWM PVDQYIGGIE HAILHLLYAR
560 570 580 590 600
FFTKVLRDLG YVNLDEPFKR LLTQGMVLKD GAKMSKSKGN TVDPDEIVAK
610 620 630 640 650
FGADTARLFI LFAAPPAKEL EWSDSAVEGA YRFIKRFFER SQNAYKTKSL
660 670 680 690 700
PKIDQKSLSK EEKEARKKVY EALQKSTDVY TKSFSFNTLI AASMEALNAL
710 720 730 740 750
NGQNNPDIWT EGYWVLTNIL EPIIPHTCWE ISHNLFERNN FTRLQLDPAA
760 770 780 790 800
LEEDSVTLAV TVNGKRRAEI EVPKDASKEE ILAKAKEIAK KWIDGKTIVK
810
EIVVPGRLVN IVVKG
Length:815
Mass (Da):94,146
Last modified:August 21, 2007 - v1
Checksum:i48FB5009F2996E89
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009178 Genomic DNA. Translation: BAF70571.1.
RefSeqiWP_012082834.1. NC_009662.1.
YP_001356928.1. NC_009662.1.

Genome annotation databases

EnsemblBacteriaiBAF70571; BAF70571; NIS_1464.
GeneIDi5360666.
KEGGinis:NIS_1464.
PATRICi22685078. VBINitSp82229_1536.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009178 Genomic DNA. Translation: BAF70571.1.
RefSeqiWP_012082834.1. NC_009662.1.
YP_001356928.1. NC_009662.1.

3D structure databases

ProteinModelPortaliA6Q512.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi387092.NIS_1464.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAF70571; BAF70571; NIS_1464.
GeneIDi5360666.
KEGGinis:NIS_1464.
PATRICi22685078. VBINitSp82229_1536.

Phylogenomic databases

eggNOGiCOG0495.
HOGENOMiHOG000200747.
KOiK01869.
OMAiQSSWYFL.
OrthoDBiEOG63Z74X.

Enzyme and pathway databases

BioCyciNSP387092:GHA5-1509-MONOMER.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 2 hits.
HAMAPiMF_00049_B. Leu_tRNA_synth_B.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR001278. Arg-tRNA-ligase.
IPR002302. Leu-tRNA-ligase.
IPR025709. Leu_tRNA-synth_edit.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view]
PANTHERiPTHR11946:SF7. PTHR11946:SF7. 1 hit.
PfamiPF00133. tRNA-synt_1. 1 hit.
PF13603. tRNA-synt_1_2. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSiPR00985. TRNASYNTHLEU.
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsiTIGR00396. leuS_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Deep-sea vent epsilon-proteobacterial genomes provide insights into emergence of pathogens."
    Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K., Horikoshi K.
    Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SB155-2.

Entry informationi

Entry nameiSYL_NITSB
AccessioniPrimary (citable) accession number: A6Q512
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: January 7, 2015
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.