argS

Functionⁱ

Catalytic activityⁱ

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

GO - Molecular functionⁱ

arginine-tRNA ligase activity Source: UniProtKB-EC
ATP binding Source: UniProtKB-KW

Complete GO annotation...

GO - Biological processⁱ

arginyl-tRNA aminoacylation Source: InterPro

Complete GO annotation...

Keywordsⁱ

Molecular function	Aminoacyl-tRNA synthetase, Ligase
Biological process	Protein biosynthesis
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCycⁱ	SENT216597:GJB7-1834-MONOMER.

BioCycⁱ

SENT216597:GJB7-1834-MONOMER.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Arginine--tRNA ligase (EC:6.1.1.19) Alternative name(s): Arginyl-tRNA synthetase Short name: ArgRS
Gene namesⁱ	Name:argS Ordered Locus Names:SL1344_1844
Organismⁱ	Salmonella typhimurium (strain SL1344)
Taxonomic identifierⁱ	216597 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I › Salmonella typhimurium
Proteomesⁱ	UP000008962 Componentⁱ: Chromosome

Subcellular locationⁱ

Cytoplasm By similarity

GO - Cellular componentⁱ

cytoplasm Source: UniProtKB-SubCell

Complete GO annotation...

Keywords - Cellular componentⁱ

Cytoplasm

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000406087	1 – 577	Arginine--tRNA ligaseAdd BLAST		577

Interactionⁱ

Subunit structureⁱ

Monomer.By similarity

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	E1WGF0.
SMRⁱ	E1WGF0.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	122 – 132	"HIGH" regionAdd BLAST		11

Sequence similaritiesⁱ

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

Phylogenomic databases

KEGG Orthology (KO) More...KOⁱ	K01887.
OMAⁱ	NKPLHLG.

Family and domain databases

Gene3Dⁱ	1.10.730.10. 1 hit. 3.30.1360.70. 1 hit. 3.40.50.620. 1 hit.
HAMAPⁱ	MF_00123. Arg_tRNA_synth. 1 hit.
InterProⁱ	View protein in InterPro IPR001412. 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_Ia_anticodon-bd.
PANTHERⁱ	PTHR11956. PTHR11956. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF03485. Arg_tRNA_synt_N. 1 hit. PF05746. DALR_1. 1 hit. PF00750. tRNA-synt_1d. 1 hit.
PRINTSⁱ	PR01038. TRNASYNTHARG.
SMARTⁱ	View protein in SMART SM01016. Arg_tRNA_synt_N. 1 hit. SM00836. DALR_1. 1 hit.
SUPFAMⁱ	SSF47323. SSF47323. 1 hit. SSF55190. SSF55190. 1 hit.
TIGRFAMsⁱ	TIGR00456. argS. 1 hit.
PROSITEⁱ	View protein in PROSITE PS00178. AA_TRNA_LIGASE_I. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

E1WGF0-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MNIQALLSEK VSQAMIAAGA PADCEPQVRQ SAKVQFGDYQ ANGMMAVAKK 
        60         70         80         90        100
LGMAPRQLAE QVLTHLDLSG IASKVEIAGP GFINIFLEPA FLAEQVQQAL 
       110        120        130        140        150
ASDRLGVSQP TRQTIVVDYS APNVAKEMHV GHLRSTIIGD AAVRTLEFLG 
       160        170        180        190        200
HHVIRANHVG DWGTQFGMLI AWLEKQQQEN AGDMALADLE GFYRDAKKHY 
       210        220        230        240        250
DEDEAFAERA RNYVVKLQSG DTYFREMWRK LVDITMTQNQ ITYDRLNVTL 
       260        270        280        290        300
TRDDVMGESL YNPMLPGIVA DLKAKGLAVE SEGATVVFLD EFKNKEGDPM 
       310        320        330        340        350
GVIIQKKDGG YLYTTTDIAC AKYRYETLHA DRVLYYIDSR QHQHLMQAWT 
       360        370        380        390        400
IVRKAGYVPD SVPLEHHMFG MMLGKDGKPF KTRAGGTVKL ADLLDEALER 
       410        420        430        440        450
ARRLVAEKNP DMPADELEKL ANAVGIGAVK YADLSKNRTT DYIFDWDNML 
       460        470        480        490        500
AFEGNTAPYM QYAYTRVLSV FRKANIDEQA LASAPVIISE DREAQLAARL 
       510        520        530        540        550
LQFEETLTVV AREGTPHVMC AYLYDVAGLF SGFYEHCPIL SAENDAVRNS 
       560        570 
RLKLAQLTAK TLKLGLDTLG IETVERM

Length:577

Mass (Da):64,275

Last modified:November 30, 2010 - v1

Checksum:ⁱ842D46DD38EB44B7

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	491	D → H in AAC44610 (PubMed:8930920).Curated	1
Sequence conflictⁱ	498	A → D in AAC44610 (PubMed:8930920).Curated	1
Sequence conflictⁱ	555	A → V in AAC44610 (PubMed:8930920).Curated	1
Sequence conflictⁱ	569	L → S in AAC44610 (PubMed:8930920).Curated	1
Sequence conflictⁱ	574	V → A in AAC44610 (PubMed:8930920).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	FQ312003 Genomic DNA. Translation: CBW17938.1. U62714 Genomic DNA. Translation: AAC44610.1.
NCBI Reference Sequences More...RefSeqⁱ	WP_001025361.1. NC_016810.1.

Genome annotation databases

EnsemblBacteriaⁱ	CBW17938; CBW17938; SL1344_1844.
KEGGⁱ	sey:SL1344_1844.
PATRICⁱ	fig\|216597.6.peg.2047.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	FQ312003 Genomic DNA. Translation: CBW17938.1. U62714 Genomic DNA. Translation: AAC44610.1.
NCBI Reference Sequences More...RefSeqⁱ	WP_001025361.1. NC_016810.1.

3D structure databases

ProteinModelPortalⁱ	E1WGF0.
SMRⁱ	E1WGF0.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	CBW17938; CBW17938; SL1344_1844.
KEGGⁱ	sey:SL1344_1844.
PATRICⁱ	fig\|216597.6.peg.2047.

Phylogenomic databases

KEGG Orthology (KO) More...KOⁱ	K01887.
OMAⁱ	NKPLHLG.

Enzyme and pathway databases

BioCycⁱ	SENT216597:GJB7-1834-MONOMER.

BioCycⁱ

SENT216597:GJB7-1834-MONOMER.

Family and domain databases

Gene3Dⁱ	1.10.730.10. 1 hit. 3.30.1360.70. 1 hit. 3.40.50.620. 1 hit.
HAMAPⁱ	MF_00123. Arg_tRNA_synth. 1 hit.
InterProⁱ	View protein in InterPro IPR001412. 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_Ia_anticodon-bd.
PANTHERⁱ	PTHR11956. PTHR11956. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF03485. Arg_tRNA_synt_N. 1 hit. PF05746. DALR_1. 1 hit. PF00750. tRNA-synt_1d. 1 hit.
PRINTSⁱ	PR01038. TRNASYNTHARG.
SMARTⁱ	View protein in SMART SM01016. Arg_tRNA_synt_N. 1 hit. SM00836. DALR_1. 1 hit.
SUPFAMⁱ	SSF47323. SSF47323. 1 hit. SSF55190. SSF55190. 1 hit.
TIGRFAMsⁱ	TIGR00456. argS. 1 hit.
PROSITEⁱ	View protein in PROSITE PS00178. AA_TRNA_LIGASE_I. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	SYR_SALTS
Accessionⁱ	E1WGF0Primary (citable) accession number: E1WGF0 Secondary accession number(s): P74871
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	March 8, 2011
	Last sequence update:	November 30, 2010
	Last modified:	June 7, 2017
	This is version 41 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome

Documents

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

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 one 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.

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - E1WGF0 (SYR_SALTS)

Your basket is currently empty.

Arginine--tRNA ligase

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ