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Q7NDF6 (SYR_GLOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 71. 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:glr4279
OrganismGloeobacter violaceus (strain PCC 7421) [Reference proteome] [HAMAP]
Taxonomic identifier251221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaGloeobacteriaGloeobacteralesGloeobacter

Protein attributes

Sequence length601 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
Reference 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 – 601601Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000151562

Regions

Motif135 – 14511"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q7NDF6 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: C48DDEBD5F9B419A

FASTA60166,957
        10         20         30         40         50         60 
MTALSLQQQL AESIYTALGT AFEAGQLGQL TQLPPRQSVV VEKPKVPEHG DYATPVAMSL 

        70         80         90        100        110        120 
AKPCRLAPLA IAEAIASYLA SDEIGVEVAK PGFINLRLGH RFVAVELQNI LELKGDYGRT 

       130        140        150        160        170        180 
VPQQPERILL EFVSANPTGP LHLGHGRWAA LGSSLERILQ FAGYTVDSEF YINDAGNQMQ 

       190        200        210        220        230        240 
LLGLSLKQRY LQVLGEAVEL PDGGYKGSYL KELAEQLVAD KGDSLGGEPV EWFSAYAEGR 

       250        260        270        280        290        300 
LLEQQKITLQ QFRTEFDRWY SERSLHCAGA IEAALADLEA RGMLYRAARS RQEQSGEITG 

       310        320        330        340        350        360 
RSKKVQAPAA FEEEDGGGEA LFFKAADFGD EMDRVVKRAD GNTTYLAADI AYHWDKYQRG 

       370        380        390        400        410        420 
YGRLINIWGA DHHGYVPRMK AVAQALGHPA DSLEILIGQM VRLFKTNPET GQKEEMRMSK 

       430        440        450        460        470        480 
RRGELVSVDD LIEEVGVDAG RWFLLSQSLN TTVNFDLDLA QSEKFDNPVF YVQYNHARCC 

       490        500        510        520        530        540 
SILRKAPERG MPILERFEFL KPDGGLWLET PQERTLALRL LAAPDEYRFA AVDRTPQRLT 

       550        560        570        580        590        600 
QYAYDLASDV SQFYEHCPIL PPLAENLEPA LRYARLGLVV ATRQVLATTL TLLGIEPRES 


M 

« Hide

References

[1]"Complete genome structure of Gloeobacter violaceus PCC 7421, a cyanobacterium that lacks thylakoids."
Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T., Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M., Tabata S.
DNA Res. 10:137-145(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7421.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000045 Genomic DNA. Translation: BAC92220.1.
RefSeqNP_927225.1. NC_005125.1.

3D structure databases

ProteinModelPortalQ7NDF6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING251221.gvip558.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC92220; BAC92220; BAC92220.
GeneID2602682.
KEGGgvi:gvip558.
PATRIC22048051. VBIGloVio86258_4307.

Phylogenomic databases

eggNOGCOG0018.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBCLSK423190.

Enzyme and pathway databases

BioCycGVIO251221:GH9A-4331-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. 2 hits.
[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.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYR_GLOVI
AccessionPrimary (citable) accession number: Q7NDF6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: April 16, 2014
This is version 71 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