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Q9JTM7 (SYR_NEIMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 87. 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:NMA1707
OrganismNeisseria meningitidis serogroup A / serotype 4A (strain Z2491) [Complete proteome] [HAMAP]
Taxonomic identifier122587 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length572 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 – 572572Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000151582

Regions

Motif122 – 13211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q9JTM7 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: A2666E45EEE90173

FASTA57262,705
        10         20         30         40         50         60 
MNLHQTVERE AAAAFAAAGI ADSPVVLQPT KNAEHGDFQI NGVMGAAKKA KQNPRELAQK 

        70         80         90        100        110        120 
VAEALADNAV IESAEVAGPG FINLRLRPEF LAQNIQTALN DARFGIAKTD KPQTVVIDYS 

       130        140        150        160        170        180 
SPNLAKEMHV GHLRSSIIGD SISRVLAFMG NTVVRQNHVG DWGTQFGMLV AYLVEQQKDN 

       190        200        210        220        230        240 
AAFELADLEQ FYRAAKVRFD EDPAFADTAR EYVVKLQGGD ETVLALWKQF VDISLSHAQA 

       250        260        270        280        290        300 
VYDTLGLKLR PEDVAGESKY NDDLQPVVDD LVQKGLAVED DGAKVVFLDE FKNKEGEPAA 

       310        320        330        340        350        360 
FIVQKQGGGF LYASTDLACL RYRVGTLHAD RLLYVVDHRQ ALHFEQLFTT SRKAGYLPEN 

       370        380        390        400        410        420 
VGAAFVGFGT MMGKDGKPFK TRSGDTVKLV DLLTEAVERA AALVKEKNPE LGADEAAKIG 

       430        440        450        460        470        480 
KTVGIGAVKY ADLSKNRTSN YVFDWDAMLS FEGNTAPYLQ YAYTRVQSVF RKAGEWDATA 

       490        500        510        520        530        540 
PTVLSEPLEK QLAAELLKFE DVLQSVADTA YPHYLAAYLY QIATLFSRFY EACPILKAES 

       550        560        570 
ASRNSRLQLA KLTGDTLKQG LDLLGIDVLD VM 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL157959 Genomic DNA. Translation: CAM08836.1.
PIRF81866.
RefSeqYP_002343001.1. NC_003116.1.

3D structure databases

ProteinModelPortalQ9JTM7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING122587.NMA1707.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM08836; CAM08836; NMA1707.
GeneID908096.
KEGGnma:NMA1707.
PATRIC20364634. VBINeiMen132687_2018.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMAAGEWDAT.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycNMEN122587:GI3Q-1552-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_NEIMA
AccessionPrimary (citable) accession number: Q9JTM7
Secondary accession number(s): A1ISS4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 87 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