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Q5UXX8 (SYR_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. 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:rrnAC3169
OrganismHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) [Complete proteome] [HAMAP]
Taxonomic identifier272569 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula

Protein attributes

Sequence length579 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

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 – 579579Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242128

Regions

Motif123 – 13311"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q5UXX8 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: 9E99E129A6C5B57F

FASTA57964,318
        10         20         30         40         50         60 
MFLQLRAEVE DALADALTTL DLPAEDLGIE EPPEDVDAVL ASSVAFRLAG EVGTAPPNVA 

        70         80         90        100        110        120 
SDIADAIAAD DLTYVSDVTT QGPYVNFLPS EAYFAETLQS VTESGFGRLP DRDTSVVVEH 

       130        140        150        160        170        180 
TSANPTGPVH VGRARNPIIG DAVARVLDYA GYDVDRHYYV NDAGRQIAVF TWAYETFDED 

       190        200        210        220        230        240 
DLPEPERESP EYEMVRYYRK GNTILEDGDP DEVEAAEAEV QSILQGLEDG DEETYERVAE 

       250        260        270        280        290        300 
VVDTVLGGMQ NTLGRLPAEF DEFVKETKFM RNGDTDDLVD RLKGLDCAVY EEDAWQLDLP 

       310        320        330        340        350        360 
DFEKNLVFLR SDGTSLYTTR DLAHHEWKFD TYDRAVTVLG EDHKLQADQL AAALELLDND 

       370        380        390        400        410        420 
TDQLRQVFYS WVNLPEGGMS TREGTGIDLD DLLDEAIDRA REEVESRLDD RTRGDLDEDD 

       430        440        450        460        470        480 
IDRIARQVGI GAVRYDIVSK QPTKGITFEW DRALDFEAQS APYVQYVHAR CCGILGDVET 

       490        500        510        520        530        540 
DIPDEPDLDP LSEPEERDLL RELARFPAVI EAAADDLTPH TVATYTRDLA ETFNAFYREC 

       550        560        570 
PVLDADPETR AARLALVDGT RTTIANALDA LGVEAPTSM 

« Hide

References

[1]"Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea."
Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., Hood L., Ng W.V.
Genome Res. 14:2221-2234(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY596297 Genomic DNA. Translation: AAV47875.1.
RefSeqYP_137581.1. NC_006396.1.

3D structure databases

ProteinModelPortalQ5UXX8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272569.rrnAC3169.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV47875; AAV47875; rrnAC3169.
GeneID3129268.
KEGGhma:rrnAC3169.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247213.
KOK01887.
OMANFERNSA.

Enzyme and pathway databases

BioCycHMAR272569:GJDH-2844-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.
InterProIPR001278. 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.
ProtoNetSearch...

Entry information

Entry nameSYR_HALMA
AccessionPrimary (citable) accession number: Q5UXX8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: December 7, 2004
Last modified: May 14, 2014
This is version 64 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