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B4ETN5 (SYR_PROMH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 37. 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:PMI1103
OrganismProteus mirabilis (strain HI4320) [Complete proteome] [HAMAP]
Taxonomic identifier529507 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

Protein attributes

Sequence length576 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 – 576576Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000095393

Regions

Motif122 – 13211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B4ETN5 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 45892962AD17CFCD

FASTA57664,922
        10         20         30         40         50         60 
MNIQAFLSEK ISMAMSAAGA PADSEPLVRQ SAKVQFGDYQ ANGVMGAAKK MGIPPRQLAE 

        70         80         90        100        110        120 
KILEHLDITD IADKVEIAGP GFINIFLSPV WVAQQAEFAL ADEHLNITKV TPETIVIDYS 

       130        140        150        160        170        180 
SPNVAKQMHV GHLRSTIIGD ASARTLSFLG HNVIRANHLG DWGTQFGMLI AYLEKKQNEN 

       190        200        210        220        230        240 
AADMALADLE EFYREAKKCY DEDEVFAERA RNYVVRLQGG DEYCRTMWRK LVDITMQQNQ 

       250        260        270        280        290        300 
LTYQRLNVTL TEDDIMGESL YNPMLPGIVA DLKAKGLAVE SEGATVVFLD EYKNKEGEPM 

       310        320        330        340        350        360 
GVIIQKKDGG YLYTTTDIAC AKYRHEQLHA NRVLYYIDSR QHQHLMQAWT IVRKAGYIPD 

       370        380        390        400        410        420 
SMSLEHHMFG MMLGKDGRPF KTRSGGTVRL TDLLDEAHER ALTLIREKNP DMDEEELNNI 

       430        440        450        460        470        480 
ARVVGIGAVK YADLSKNRTT DYIFDWDLML SFEGNTAPYM QYAYTRVASI FKRADIDESA 

       490        500        510        520        530        540 
LTQPISLTQP HEKQLALRLV QFDETITQVA REGTPHVMCA YLYDLAQSFS GFYENCPILS 

       550        560        570 
AEDDNVRQSR LKLARLTART LKQGLETLGI ETVDRM 

« Hide

References

[1]"Complete genome sequence of uropathogenic Proteus mirabilis, a master of both adherence and motility."
Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S., Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T., Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Walker D., Whithead S. expand/collapse author list , Thomson N.R., Rather P.N., Parkhill J., Mobley H.L.T.
J. Bacteriol. 190:4027-4037(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HI4320.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM942759 Genomic DNA. Translation: CAR42387.1.
RefSeqYP_002150846.1. NC_010554.1.

3D structure databases

ProteinModelPortalB4ETN5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING529507.PMI1103.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR42387; CAR42387; PMI1103.
GeneID6801055.
KEGGpmr:PMI1103.
PATRIC20516859. VBIProMir120933_1067.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMADGTAVYM.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycPMIR529507:GJIW-1113-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_PROMH
AccessionPrimary (citable) accession number: B4ETN5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: April 16, 2014
This is version 37 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