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B4R8T9 (SYR_PHEZH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 36. 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:PHZ_c2895
OrganismPhenylobacterium zucineum (strain HLK1) [Complete proteome] [HAMAP]
Taxonomic identifier450851 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaePhenylobacterium

Protein attributes

Sequence length593 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 – 593593Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000095388

Regions

Motif123 – 13311"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B4R8T9 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 27945A89A03EC77D

FASTA59364,241
        10         20         30         40         50         60 
MSDLKTALGE AVEAAFAAEG VPAELARVTA SDRPDLADFQ SNGALAAAKR VGKNPREIAT 

        70         80         90        100        110        120 
AVAGRLQGDP RLASVEIAGP GFLNLKVADA ALAARADAIA ADPRAGAGTV PAPRRVIVDY 

       130        140        150        160        170        180 
GGPNVAKPMH VGHLRASIIG ESVKRLYRFR GDTVIGDAHF GDWGYQMGLL IGAVCDEDAE 

       190        200        210        220        230        240 
IRALVDQLNA SGDPNGEIPA AFERVTLADL DRLYPLAAAK GKEDPAYRDR ARKLTADLQA 

       250        260        270        280        290        300 
HKPGCYLLWR RFRDVTQVAL ERDFHALGVD FDWWKGESDV DHLIQPMVAE LADKGLLVDD 

       310        320        330        340        350        360 
QGARIVRVAR EGDKRELPPL LVVSSEGSAM YGTTDLATIL DRKREFDPQL VIYCVDQRQA 

       370        380        390        400        410        420 
DHFEIVFRAA YLAGYAEEGQ LEHIGFGTMN GTDGKPFKTR EGGVLKLADL IEMTRSKARE 

       430        440        450        460        470        480 
RLHEAGLGED LPAEEFEDIA GKVAVAALKF ADLSNFRGTS YVFDLDRFTS FEGKTGPYLL 

       490        500        510        520        530        540 
YQAVRVKSLL RKAEAEGAQA GPVTVAEPAE RDLVLTLDAF ETALQEAYDK KAPNALAEHA 

       550        560        570        580        590 
YRLSQAFSKF YAACPILAAP PPVRGSRLTL AQATLRQLEL ALDILGIAVP ERM 

« Hide

References

[1]"Complete genome of Phenylobacterium zucineum - a novel facultative intracellular bacterium isolated from human erythroleukemia cell line K562."
Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.
BMC Genomics 9:386-386(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HLK1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000747 Genomic DNA. Translation: ACG79304.1.
RefSeqYP_002131733.1. NC_011144.1.

3D structure databases

ProteinModelPortalB4R8T9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING450851.PHZ_c2895.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACG79304; ACG79304; PHZ_c2895.
GeneID6788842.
KEGGpzu:PHZ_c2895.
PATRIC22929044. VBIPheZuc44517_3582.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMAKCFDILG.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycPZUC450851:GHUG-2934-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.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR001278. 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. 1 hit.
[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.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYR_PHEZH
AccessionPrimary (citable) accession number: B4R8T9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: May 14, 2014
This is version 36 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