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Q3A6K6 (SYR_PELCD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Pcar_0742
OrganismPelobacter carbinolicus (strain DSM 2380 / Gra Bd 1) [Complete proteome] [HAMAP]
Taxonomic identifier338963 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Desulfuromonadales › Pelobacteraceae › Pelobacter ›

Protein attributes

Sequence length554 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: 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 – 554554Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242062

Regions

Motif129 – 13911"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q3A6K6 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 117FE0BBF0269B23

FASTA55462,387
        10         20         30         40         50         60 
MKQRLRQYIG EALQACFDQQ QLHSGTIPEI NLEVPAHAEH GDFSTNVAMA MARAEKKAPR 

        70         80         90        100        110        120 
KIAETIVAAL GEGGGMWSRV EIAGPGFINF YLTPRCWFGV LDEVVRRGDL FGRTHTGNGR 

       130        140        150        160        170        180 
KVQVEFVSAN PTGPLHIGHG RGAATGDAVA AVLGAAGYEV QREYYINDAG NQMLTLGRSL 

       190        200        210        220        230        240 
LLRYRELLGE TIEFPTDCYQ GVYVIDLARE VLESEGERLR DLPEEEALRF FANYGGDKIR 

       250        260        270        280        290        300 
AGIDEDLAAF GVRFDNWYSE QSLYDRQEVE RGIALLKERG LTYEKDGAIW FRTTDYGDDK 

       310        320        330        340        350        360 
DRVLIRSNGA TTYFASDVAY HKEKFERGFD TVIDVWGADH HGYVPRMKAV LAGLDRNPED 

       370        380        390        400        410        420 
LQIILVQLVN LLRGGQQVAM STRSGEFVTL REVIDEVGRD ACRFFFLMRR SDSQLDFDLD 

       430        440        450        460        470        480 
LAKKQSTENP VYYVQYAHAR VCSINRNAED QGVAMPELGE VDFDCLTLED ELALTKLLSR 

       490        500        510        520        530        540 
YPEVVDGAAE HFEPHRVVFY LQELAARFHS YYNKGRVLVD DPDVSRARLY LVNCVRTVLH 

       550 
NALVLLGVSA PERM

« Hide

References

[1]"Complete sequence of Pelobacter carbinolicus DSM 2380."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2380 / Gra Bd 1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000142 Genomic DNA. Translation: ABA88001.1.
RefSeqYP_006716438.1. NC_007498.2.

3D structure databases

ProteinModelPortalQ3A6K6.
ModBaseSearch...

Protein-protein interaction databases

STRING338963.Pcar_0742.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA88001; ABA88001; Pcar_0742.
GeneID3722948.
KEGGpca:Pcar_0742.
PATRIC22887484. VBIPelCar86875_0811.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMAHTSANPN.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycPCAR338963:GKDU-836-MONOMER.

Family and domain databases

Gene3D3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPMF_00123. Arg_tRNA_synth.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-ligase_Ia.
IPR015945. Arg-tRNA-synth_Ia_core.
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]
SUPFAMSSF55190. Arg-tRNA-synth_Ic_N. 1 hit.
SSF47323. tRNAsyn_1a_bind. 1 hit.
TIGRFAMsTIGR00456. argS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYR_PELCD
AccessionPrimary (citable) accession number: Q3A6K6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 22, 2005
Last modified: May 29, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

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