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B8H4W0 (SYR_CAUCN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 41. 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:CCNA_03469
OrganismCaulobacter crescentus (strain NA1000 / CB15N) [Complete proteome] [HAMAP]
Taxonomic identifier565050 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter

Protein attributes

Sequence length600 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 – 600600Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000198882

Regions

Motif123 – 13311"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B8H4W0 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: AEACF49AE89F5D21

FASTA60066,335
        10         20         30         40         50         60 
MNDLKRSLSE AAAAAFQAAG LPPEFGRVTA SDRPDLADFQ CNGALAAAKS AKRNPREIAV 

        70         80         90        100        110        120 
QVVDILKGDP RLASVEIAGV GFINMRVSDE ALSARAREIA SDDRTGAQLL ETPRRVLIDY 

       130        140        150        160        170        180 
AGPNVAKPMH VGHLRASIIG ESVKRLYRFR GDDVVGDAHF GDWGFQMGLL ISAIMDEDPF 

       190        200        210        220        230        240 
INALMEKLPE APRGFSSADE AKVMAEFEKR ITLADLDRIY PAASVRQKED PAFKERARKA 

       250        260        270        280        290        300 
TAELQNGRFG YRLLWRHFVN VSRVALEREF HALGVDFDLW KGESDVNDLI EPMVLQLEAK 

       310        320        330        340        350        360 
GLLVQDQGAR IVRVAREGDK RDVPPLLVVS SEGSAMYGTT DLATILDRRK SFDPHLILYC 

       370        380        390        400        410        420 
VDQRQADHFE TVFRAAYLAG YAEEGALEHI GFGTMNGADG KPFKTRAGGV LKLHDLIEMA 

       430        440        450        460        470        480 
REKARERLRE AGLGAELSEE QFEDTAHKVG VAALKFADLQ NFRGTSYVFD LDRFTSFEGK 

       490        500        510        520        530        540 
TGPYLLYQSV RIKSVLRRAA ESGAVAGRVE IHEPAERDLA MLLDAFEGAL QEAYDKKAPN 

       550        560        570        580        590        600 
FVAEHAYKLA QSFSKFYAAC PIMSADTETL RASRLTLAET TLRQLELALD LLGIEAPERM 

« Hide

References

[1]"The genetic basis of laboratory adaptation in Caulobacter crescentus."
Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V., Walunas T.L., Crosson S.
J. Bacteriol. 192:3678-3688(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NA1000 / CB15N.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001340 Genomic DNA. Translation: ACL96934.1.
RefSeqYP_002518842.1. NC_011916.1.

3D structure databases

ProteinModelPortalB8H4W0.
SMRB8H4W0. Positions 3-599.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190650.CC_3359.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL96934; ACL96934; CCNA_03469.
GeneID7332466.
KEGGccs:CCNA_03469.
PATRIC21311427. VBICauCre52860_3383.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMAYVKFHDE.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycCAULONA1000:CCNA_03469-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_CAUCN
AccessionPrimary (citable) accession number: B8H4W0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: June 11, 2014
This is version 41 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