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C4LJN2 (C4LJN2_CORK4) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Arginine--tRNA ligase HAMAP MF_00123

EC=6.1.1.19 HAMAP MF_00123
Alternative name(s):
Arginyl-tRNA synthetase HAMAP MF_00123
Gene names
Name:argS HAMAP MF_00123
Ordered Locus Names:ckrop_1292
OrganismCorynebacterium kroppenstedtii (strain DSM 44385 / CCUG 35717) [Complete proteome] [HAMAP]
Taxonomic identifier645127 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length594 AA.
Sequence statusComplete.
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. HAMAP MF_00123

Subcellular location

Cytoplasm By similarity HAMAP MF_00123.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. HAMAP MF_00123

Ontologies

Keywords
   Biological processProtein biosynthesis HAMAP MF_00123
   Cellular componentCytoplasm HAMAP MF_00123
   LigandATP-binding HAMAP MF_00123
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase HAMAP MF_00123 EMBL ACR18037.1
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

Regions

Motif170 – 18011"HIGH" region By similarity HAMAP MF_00123

Sequences

Sequence LengthMass (Da)Tools
C4LJN2 [UniParc].

Last modified July 7, 2009. Version 1.
Checksum: 3826535A7BEA2045

FASTA59465,014
        10         20         30         40         50         60 
MSWHQRSALT NGSINRNRQR AGTALGSDRE PRRGAVHCGP MTPEELSTLI ATRAESVLSH 

        70         80         90        100        110        120 
HGKDASVLPL TVTVERPRNP EHGDYATNLA LQIAKKVGTS PRELAGWLAE DLATNSAIET 

       130        140        150        160        170        180 
VDVAGPGFLN IRLAAAAQGE IVGRILAEGE RFGSSSELSD EVINLEFVSA NPTGPIHLGG 

       190        200        210        220        230        240 
TRWAAVGDAL GRIFAFRGAS ITREYYFNDH GRQIDRFARS LVAAALGQPT PEDGYGGEYI 

       250        260        270        280        290        300 
QDIASSVVDK HPEATQLPLE ERQELFRKEG VDLMFAHIKR TLHEFGTDFD VFFHENSLFE 

       310        320        330        340        350        360 
SGAVDQAIQK LKDNGNLYEA DGAWWLRSTS FGDDKDRVVI KSDGDAAYIA GDIAYIRDKI 

       370        380        390        400        410        420 
ERGHNLCIYM LGADHHGYIA RLKAAAQALG YDPTQVEVLI GQMVNLVRDG KAVKMSKRAG 

       430        440        450        460        470        480 
TVITLDDLVE LIGVDAARYA LIRSSVDQTL DIDMDLWARQ TNDNPVFYVQ YAHARLCSLG 

       490        500        510        520        530        540 
RKAQAAGILV KDPDYSLLVN DYEGALIRTL GEFPSVVGTA AELREPHRIA RYMEELAGTF 

       550        560        570        580        590 
HRFYDSCQIL PKKSEPTGDE AAPIVHARLA LAQATRQTIA NALSLLGVSA PERM 

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References

[1]"Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385 revealed insights into the physiology of a lipophilic corynebacterium that lacks mycolic acids."
Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P., Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S., Weisshaar B., Goesmann A., Droege M., Puehler A.
J. Biotechnol. 136:22-30(2008) [PubMed: 18430482] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44385 / CCUG 35717.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001620 Genomic DNA. Translation: ACR18037.1.
RefSeqYP_002906580.1. NC_012704.1.

3D structure databases

ProteinModelPortalC4LJN2.
ModBaseSearch...

Protein-protein interaction databases

STRINGC4LJN2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7875581.
GenomeReviewsGene locus ckrop_1292 in contig CP001620_GR.
KEGGckp:ckrop_1292.
PATRIC21517933. VBICorKro120627_1329.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAFDVYFHE.
ProtClustDBPRK01611.

Family and domain databases

HAMAPMF_00123. Arg_tRNA_synth.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-synth_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]
Gene3DG3DSA:3.30.1360.70. Arg-tRNA-synth_Ic_N. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KOK01887.
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.
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 nameC4LJN2_CORK4
AccessionPrimary (citable) accession number: C4LJN2
Entry history
Integrated into UniProtKB/TrEMBL: July 7, 2009
Last sequence update: July 7, 2009
Last modified: January 25, 2012
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)