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B4S6D8 (SYR_PROA2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 38. 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:Paes_2238
OrganismProsthecochloris aestuarii (strain DSM 271 / SK 413) [Complete proteome] [HAMAP]
Taxonomic identifier290512 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeProsthecochloris

Protein attributes

Sequence length551 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 – 551551Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000095391

Regions

Motif123 – 13311"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B4S6D8 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: EBA1428DFEBA1912

FASTA55161,934
        10         20         30         40         50         60 
MQEYLIASIQ QALLASGIEP PKEITIEKPS NKQFGDFSTN IALTLAKECR KNPRQLAEEI 

        70         80         90        100        110        120 
SAKLEFRPET VDKTTIAGPG FINFYLTPAF IMQSVEQVLN EGDQFGKTCT GKGQKAIVEY 

       130        140        150        160        170        180 
VSANPTGPLT IGRGRGGVLG DCIANLLESQ GYKVTREYYF NDAGRQMTIL AESVRLRYLE 

       190        200        210        220        230        240 
CCGEAIAFPD THYQGDYISD IAAKLFEKHG VELKEVSQLD EFKQIAETYI FASIKNTLHR 

       250        260        270        280        290        300 
LNIHHDSFFN EHKLYQTGQN GKSPNEQVID ALDKAGYISN YDGAVWFTTT KLGQEKDKVL 

       310        320        330        340        350        360 
IKSTGEPSYR LPDIAYHVTK YERAFSEIIN VFGADHIDEY PDVIEALRIL GYDPGRIKVA 

       370        380        390        400        410        420 
INQFVTTTVN GETVKMSTRK GNADLLDDLI DDVGADATRL FFIMRSKDSH LNFDVELAKK 

       430        440        450        460        470        480 
QSRDNPVFYL QYAHARICSL VKLAEQEIGF TQSDIGVHLM QNLDSPHELQ LGLALLDFPE 

       490        500        510        520        530        540 
VISSAVRMLE PQKMVEYLHH VAELYHRFYQ ECPILKAEPD ICKARLFLSL ATRQVLQNGF 

       550 
RILGVTAPTA M 

« Hide

References

[1]"Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 271 / SK 413.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001108 Genomic DNA. Translation: ACF47240.1.
RefSeqYP_002016887.1. NC_011059.1.

3D structure databases

ProteinModelPortalB4S6D8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290512.Paes_2238.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF47240; ACF47240; Paes_2238.
GeneID6460687.
KEGGpaa:Paes_2238.
PATRIC23044426. VBIProAes37017_2377.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMAPDIAYHI.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycPAES290512:GHUT-2287-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_PROA2
AccessionPrimary (citable) accession number: B4S6D8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: May 14, 2014
This is version 38 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