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Reviewed, UniProtKB/Swiss-Prot A1TJ83 (SYR_ACIAC)

Last modified November 3, 2009. Version 22. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Arginyl-tRNA synthetase
    EC=6.1.1.19
Alternative name(s):
    Arginine--tRNA ligase
      Short name=ArgRS
Gene names
Name: argS
Ordered Locus Names: Aave_0414
OrganismAcidovorax avenae subsp. citrulli (strain AAC00-1) [Complete proteome] [HAMAP]
Taxonomic identifier397945 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length569 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). HAMAP MF_00123

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm. HAMAP 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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

arginine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 569569Arginyl-tRNA synthetase HAMAP MF_00123
PRO_1000017982

Regions

Motif128 – 13811"HIGH" region HAMAP MF_00123

Sequences

Sequence LengthMass (Da)Tools
A1TJ83-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 5A0F4FADD80424F3

FASTA56962,896
        10         20         30         40         50         60 
MLSVKQELLA ALAGELEKLS PGSAGRAAFE SPKVAAHGDF ACTAAMQLAK PLKLNPRALG 

        70         80         90        100        110        120 
EQLKAALEAT PAFARWVDAI EIAGPGFLNI RLKAAAKQEI VREVLSAGDR FGYQKDNGQR 

       130        140        150        160        170        180 
VLVEFVSANP TGPLHVGHGR QAALGDAICN LFSTQGWSVH REFYYNDAGV QIDTLTKSTQ 

       190        200        210        220        230        240 
LRARGFKPGD ECWPTDPENP ASKTFYNGDY IQDIANDFLA KKTVKADDRE FTANGDVEDY 

       250        260        270        280        290        300 
DNIRQFAVAY LRNEQDKDLQ AFNLHFDQYY LESSLYTSGR VEATVNRLVE KGHTYEQDGA 

       310        320        330        340        350        360 
LWLKSTDYGD DKDRVMRKKD GTYTYFVPDV AYHIAKWERG FAKVVNIQGT DHHGTIARVR 

       370        380        390        400        410        420 
AGLQAADVGI PQGYPDYVLH TMVRVVKGGK EVKIGKRAGS YVTLRDLIEW TSKDAVRFFL 

       430        440        450        460        470        480 
LSRKPDTEYT FDVDLAVAQN NDNPVYYVQY AHARIQSVLR AWAEAGGGDV ASLKDVDLSA 

       490        500        510        520        530        540 
LEGPQAQALM LQLAKYPEML TAAAEGEAPH DVTFYLRDLA ASYHSYYDAE RILVDDEAVK 

       550        560 
RARLALVAAT AQVLHNGLKV LGVDAPARM 

« Hide

References

[1]"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000512 Genomic DNA. Translation: ABM31021.1.
RefSeqYP_968795.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA1TJ83.

Genome annotation databases

GeneID4668362.
GenomeReviewsGene locus Aave_0414 in contig CP000512_GR.
KEGGaav:Aave_0414.
NMPDRfig|397945.5.peg.369.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAADHHGYV.

Family and domain databases

HAMAPMF_00123.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-synth_Ic.
IPR015945. Arg-tRNA-synth_Ic_core.
IPR005148. Arg-tRNA-synth_Ic_N.
IPR008909. DALR_anticod_bd.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11956. Arg_tRNA-synt_1c. 1 hit.
PfamPF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSPR01038. TRNASYNTHARG.
TIGRFAMsTIGR00456. argS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYR_ACIAC
AccessionPrimary (citable) accession number: A1TJ83
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: November 3, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents