Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B7H2A9 (SYR_ACIB3) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 34. 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:ABBFA_003380
OrganismAcinetobacter baumannii (strain AB307-0294) [Complete proteome] [HAMAP]
Taxonomic identifier557600 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length596 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 – 596596Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000198865

Regions

Motif128 – 13811"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B7H2A9 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: CE748F8F74F0A64C

FASTA59666,306
        10         20         30         40         50         60 
MNTAIQAALD HAVQTLQQEG VLPSDWNNSS NLTRTKDRSH GDFASNIAMI GSKAAGMKPR 

        70         80         90        100        110        120 
DLAEKILAAL PEVADISKAE IAGPGFINFF LNADQRFAIL DQIQAQKESF GRSQSNAAKK 

       130        140        150        160        170        180 
IQVEFVSANP TSSLHVGHGR GAAYGMTVAN LLEATGAKVD REYYVNDAGR QMDILATSTY 

       190        200        210        220        230        240 
LRYLELLGQN LVFPKNAYQG DYVKEIAQGI IDKDGDAYVR EVANVYKDVP EDVQYAEELD 

       250        260        270        280        290        300 
SEGNKVVLSG DKEKHIDGLI ANSQQLLGEG YRVFHQAALH AILDDIKDDL ADFGVTFNQW 

       310        320        330        340        350        360 
FSEASLSAKI DEALETLDQR GFLYEKDGNI WFKSTEFGDE KDRVVKRRNG QTTYFASDIA 

       370        380        390        400        410        420 
YHLNKLQRGY TDLVDIWGSD HHGYISRVKA AIDAMGYDSK KLTVLLVQFV SLWRGGEMVQ 

       430        440        450        460        470        480 
MSSRSGQFVT LRDLRKEVGN DAARFYYVMR KSEQHIDFDL DLAVSQSKDN AVYYIQYAHA 

       490        500        510        520        530        540 
RICRMLEKAA STGLQFEVSA ARSHAARLSL DAETEILAKL AAYPDVVLRA ANAYEPHQVG 

       550        560        570        580        590 
NYLKELAALF HGWYNEHKVL SDDAELTQAR LLLSINVQQV LRNGLELLGV SAPEAM 

« Hide

References

[1]"Comparative genome sequence analysis of multidrug-resistant Acinetobacter baumannii."
Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J., MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M., Bonomo R.A., Gill S.R.
J. Bacteriol. 190:8053-8064(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AB307-0294.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001172 Genomic DNA. Translation: ACJ57690.1.
RefSeqYP_002327254.1. NC_011595.1.

3D structure databases

ProteinModelPortalB7H2A9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557600.ABBFA_003380.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ57690; ACJ57690; ABBFA_003380.
GeneID7060113.
KEGGabb:ABBFA_003380.
PATRIC20708227. VBIAciBau42682_3262.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycABAU557600:GKC3-3389-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.
InterProIPR001278. 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. 2 hits.
[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.
ProtoNetSearch...

Entry information

Entry nameSYR_ACIB3
AccessionPrimary (citable) accession number: B7H2A9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: April 16, 2014
This is version 34 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