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A6Q543 (SYR_NITSB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Arginine--tRNA ligase

EC=6.1.1.19
Alternative name(s):
Arginyl-tRNA synthetase
Short name=ArgRS
Gene names
Name:argS
Ordered Locus Names:NIS_1495
OrganismNitratiruptor sp. (strain SB155-2) [Complete proteome] [HAMAP]
Taxonomic identifier387092 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaNitratiruptor

Protein attributes

Sequence length527 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). HAMAP-Rule MF_00123

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00123

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00123.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processarginyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

arginine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 527527Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000018078

Regions

Motif112 – 12211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
A6Q543 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: C98C8EA8FE957810

FASTA52760,290
        10         20         30         40         50         60 
MKKRVQSELS KLSDKSIILE KPRDRQFGHY ATPIAFSLAK ELRRSPMQIA DELAKSFESS 

        70         80         90        100        110        120 
SIFEKVEPIK GYVNFKLSES FLDEYATWAL KNESEFGKDE QGETILLEFV SANPTGPLHI 

       130        140        150        160        170        180 
GHARGAVLGE ALSRLGKHLG NEIVKEYYIN DAGNQIYLLG LSIYLAAKEE LGQEVQWPQE 

       190        200        210        220        230        240 
YYRGDYIKDL AKEAIEEFGK EAFSDESLID KLSEWGKEKM MELIVSNLAA VDIKFDHFVS 

       250        260        270        280        290        300 
EKALYEKWDE VFAILKEHDA VYEKDSKVWL KSSEYGDEKD RVVVREDGRP TYLAGDIIYH 

       310        320        330        340        350        360 
YDKFKRGFDR YINIWGADHH GYIARVKAAI KFLGFDPDKL EVLLAQMVSL LKGGEPYKMS 

       370        380        390        400        410        420 
KRAGNFILMS EVVEEIGADA LKFMFLSKKA DTHLEFDVDM LKKEDASNPV YYINYAHARI 

       430        440        450        460        470        480 
NSVLEKAGKS AGEVIDTPLK DLNEDAKDLL FEALILPEII EDAFAKRELQ RLTDYLKALA 

       490        500        510        520 
AQFHSFYNKH KVIGSEYEDR YLKLFLVVAL SIRVGLRLLG IEAKKRM 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009178 Genomic DNA. Translation: BAF70602.1.
RefSeqYP_001356959.1. NC_009662.1.

3D structure databases

ProteinModelPortalA6Q543.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING387092.NIS_1495.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF70602; BAF70602; NIS_1495.
GeneID5361001.
KEGGnis:NIS_1495.
PATRIC22685144. VBINitSp82229_1569.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMAMEHMGFG.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycNSP387092:GHA5-1540-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPMF_00123. Arg_tRNA_synth.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-ligase.
IPR005148. Arg-tRNA-synth_N.
IPR008909. DALR_anticod-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERPTHR11956. PTHR11956. 1 hit.
PfamPF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSPR01038. TRNASYNTHARG.
SMARTSM01016. Arg_tRNA_synt_N. 1 hit.
SM00836. DALR_1. 1 hit.
[Graphical view]
SUPFAMSSF47323. SSF47323. 1 hit.
SSF55190. SSF55190. 1 hit.
TIGRFAMsTIGR00456. argS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYR_NITSB
AccessionPrimary (citable) accession number: A6Q543
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: May 14, 2014
This is version 47 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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries