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Q3AVY5 (SYR_SYNS9) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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:Syncc9902_2134
OrganismSynechococcus sp. (strain CC9902) [Complete proteome] [HAMAP]
Taxonomic identifier316279 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length590 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 – 590590Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242105

Regions

Motif130 – 14011"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q3AVY5 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: E0DE3A6C56EB8460

FASTA59064,955
        10         20         30         40         50         60 
MLSLSQTLDA QLRAAMQRAF PDAEATLDPQ LAAASKPEFG DFQANGALPL AKPLKQPPRQ 

        70         80         90        100        110        120 
IATAIVDQLS GDEAFNALCL APQIAGPGFI NLTIRPERLA EELAARLGTD RLGVPVVEDV 

       130        140        150        160        170        180 
APVVVDFSSP NIAKEMHVGH LRSTIIGDSL ARVLEFRGHS VLRLNHVGDW GTQFGMLITH 

       190        200        210        220        230        240 
LKQVAPETLD TADAVDLGDL VAFYREAKKR FDDDDDFQAT SRDEVVKLQG GDPVSLKAWG 

       250        260        270        280        290        300 
LLCDQSRREF QKLYDRLDIR LTERGESFYN PYLPAVLDGL KAVDLLVTDD GAQCVFLEGV 

       310        320        330        340        350        360 
TGKDGNPLPV IVQKRDGGFN YATTDLAAIR FRFASPPTGD AAQRVIYVTD AGQANHFAGV 

       370        380        390        400        410        420 
FQVAERAGWI PDGARLEHVP FGLVQGEDGK KLKTRAGDTV RLRDLLDEAV ERSEQDLRSR 

       430        440        450        460        470        480 
LQEEERTESD AFISHVATTV GLAAVKYADL SQNRLTNYQF SFDRMLALQG NTAPYLLYAV 

       490        500        510        520        530        540 
VRIAGIARKG GDLGVSNAAL QFSEPQEWAL VRELLKFDRV IVEVEDELLP NRLCSYLFEL 

       550        560        570        580        590 
SQVFNRFYDQ VPVLKAEPEA LSSRLALCRH TADTLRCGLA LLGIPTLERM 

« Hide

References

[1]"Complete sequence of Synechococcus sp. CC9902."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CC9902.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000097 Genomic DNA. Translation: ABB27092.1.
RefSeqYP_378135.1. NC_007513.1.

3D structure databases

ProteinModelPortalQ3AVY5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316279.Syncc9902_2134.

Proteomic databases

PRIDEQ3AVY5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB27092; ABB27092; Syncc9902_2134.
GeneID3741921.
KEGGsye:Syncc9902_2134.
PATRIC23801843. VBISynSp76179_2352.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMAMEHMGFG.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycSSP316279:GJCI-2169-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_SYNS9
AccessionPrimary (citable) accession number: Q3AVY5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 22, 2005
Last modified: May 14, 2014
This is version 59 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