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A9VSZ9 (A9VSZ9_BACWK) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 33. 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 1 HAMAP MF_00123

EC=6.1.1.19 HAMAP MF_00123
Alternative name(s):
Arginyl-tRNA synthetase 1 HAMAP MF_00123
Gene names
Name:argS1 HAMAP MF_00123
Ordered Locus Names:BcerKBAB4_2010
OrganismBacillus weihenstephanensis (strain KBAB4) [Complete proteome] [HAMAP] EMBL ABY43238.1
Taxonomic identifier315730 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length562 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 ABY43238.1
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

Motif122 – 13211"HIGH" region By similarity HAMAP MF_00123

Sequences

Sequence LengthMass (Da)Tools
A9VSZ9 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: C47587DFD8A2DEFA

FASTA56264,599
        10         20         30         40         50         60 
MNYKTQFAKS LSNIFTNELT KNQILDLIET PKQDEFGDAA FPCFSLAKQY KKSPAIIAKE 

        70         80         90        100        110        120 
LAEKLNDPFF TKVEAVGPYV NVFFNRETVS DKVLKTILAE KEEYGQNHFG CEKTVVIDYS 

       130        140        150        160        170        180 
SPNIAKPFSM GHLRSTMIGN SLKHIAEKCG YEVVGINYIG DWGTQFGKLI TAYKKWGNEE 

       190        200        210        220        230        240 
VVKEDPIREL FKLYVQFHEE AKENKELEEE GRAWFKKLEE GDEEAVELWN WFRHESLKEF 

       250        260        270        280        290        300 
SRIYELLGVE FTNFQGEAFY NDKMEDFIEI LEEHDLLEES EGALVVNLEE EGMPPCLIRK 

       310        320        330        340        350        360 
SDGATIYATR DLTAALYRQN TYEFDKALYV VGPEQSLHFN QFFTVLKKLG YTWVDGMEHV 

       370        380        390        400        410        420 
PFGFILKDGK KMSTRKGRII LLEEVLEEAV ALAEQNIEEK NPNLKQKEDV AKQVGVGAVI 

       430        440        450        460        470        480 
FHDLKNERMH NIEFSLENML KFEGETGPYV QYTHARACSI LRKESVEFET CTFALKDDYS 

       490        500        510        520        530        540 
WSVVKLLNKF PQVIEAAFNK NEPSTISKYV LDVAQAFNKY YGNVRILEES EEKESRLALA 

       550        560 
YAVTVVLKEG LRLLGVGAPE EM 

« Hide

References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000903 Genomic DNA. Translation: ABY43238.1.
RefSeqYP_001644866.1. NC_010184.1.

3D structure databases

ProteinModelPortalA9VSZ9.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9VSZ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000079309; EBBACP00000077243; EBBACG00000079300.
GeneID5842223.
GenomeReviewsGene locus BcerKBAB4_2010 in contig CP000903_GR.
KEGGbwe:BcerKBAB4_2010.
PATRIC19008593. VBIBacWei55973_2615.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000002259.
HOGENOMHBG695395.
OMAFHEEAEK.
ProtClustDBPRK12451.

Family and domain databases

HAMAPMF_00123. Arg_tRNA_synth.
[Tree]
InterProIPR001278. 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.
ProtoNetSearch...

Entry information

Entry nameA9VSZ9_BACWK
AccessionPrimary (citable) accession number: A9VSZ9
Entry history
Integrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: January 25, 2012
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)