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B8HSK8 (SYR_CYAP4) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 34. 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:Cyan7425_3671
OrganismCyanothece sp. (strain PCC 7425 / ATCC 29141) [Complete proteome] [HAMAP]
Taxonomic identifier395961 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesCyanothece

Protein attributes

Sequence length585 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 – 585585Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000198892

Regions

Motif126 – 13611"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B8HSK8 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: A03581ECE8D0B38B

FASTA58565,673
        10         20         30         40         50         60 
MSSPLDHLKT QLQRAMVAAY GETLSGADPL LVNASHPKFG DYQSNAPLPL AKQLNQPPRT 

        70         80         90        100        110        120 
IASTIVDHLE VGEAWEPPTI AGPGFINFTL KTSYLASQLE LRLTDPRLGI SAVKLPLRVV 

       130        140        150        160        170        180 
VDFSSPNIAK EMHVGHLRST IIGDCLARIL EFLGHEVLRL NHVGDWGTQF GMLITYLREV 

       190        200        210        220        230        240 
CPEALTAPDA VDLGDLVAFY RQAKQRFDSD PDFQAIARQE VVRLQSGEPD SLHAWQLLCA 

       250        260        270        280        290        300 
QSRREFEKIY NLLDIKLTER GESFYNPLLP QVIQALDQTG LLVEDQGAKC VFLEGYTNKA 

       310        320        330        340        350        360 
GDPQPLIVQK SDGGYIYATT DLAALRYRIE QDQADWIIYV TDAGQSTHFA QVFQVAQRAG 

       370        380        390        400        410        420 
WIPNRIRLVH VPFGLVQGED GKKLKTRSGD TVRLQDLLDE AIDRARNDLV SRLEAEGRQE 

       430        440        450        460        470        480 
TPEFIDHVAQ VVGIGAVKYA DLSQNRTSNY VFSYDKMLSL QGNTAPYLIY AYVRVQGISR 

       490        500        510        520        530        540 
KGQIDLEQLT EQPTLSLQEE EEKLLARHLL QLEDVLAQVT EDLLPNRLCQ YLFELSQKFN 

       550        560        570        580 
QFYDRCPILQ AEEPLRNSRL GLAQLTARTL KLGLSLLGIQ VLERM 

« Hide

References

[1]"Novel metabolic attributes of the genus Cyanothece, comprising a group of unicellular nitrogen-fixing Cyanobacteria."
Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H., Sherman L.A., Pakrasi H.B.
MBio 2:E214-E214(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7425 / ATCC 29141.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001344 Genomic DNA. Translation: ACL45991.1.
RefSeqYP_002484352.1. NC_011884.1.

3D structure databases

ProteinModelPortalB8HSK8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING395961.Cyan7425_3671.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL45991; ACL45991; Cyan7425_3671.
GeneID7289615.
KEGGcyn:Cyan7425_3671.
PATRIC21568307. VBICyaSp30657_3650.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycCSP395961:GJDE-3509-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_CYAP4
AccessionPrimary (citable) accession number: B8HSK8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: April 16, 2014
This is version 34 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