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Q4FM10 (SYR_PELUB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 60. 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:SAR11_0970
OrganismPelagibacter ubique (strain HTCC1062) [Complete proteome] [HAMAP]
Taxonomic identifier335992 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSAR11 clusterCandidatus Pelagibacter

Protein attributes

Sequence length577 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 – 577577Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242061

Regions

Motif132 – 14211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q4FM10 [UniParc].

Last modified August 30, 2005. Version 1.
Checksum: E5ADC3D72F8EB0C6

FASTA57766,292
        10         20         30         40         50         60 
MNIFDLYLDK IIILIKKLNK DGSLELPESL NGVNVDIPPS NFDCDISTNV AMVLSKANKK 

        70         80         90        100        110        120 
SPIDIANILI ELIKNEDEKI ESISAAKPGF INIKFKTIYW NNFIKSINQN HKDYGVNNKE 

       130        140        150        160        170        180 
KKQKYLIEFV SANPTGPLHV GHCRGAILGD VISNILIFNK HDVSKEYYVN DYGNQILNFT 

       190        200        210        220        230        240 
KSVFFRIREI LFNEKFPIEN SDLYPGDYLV GIAKNIIKSN KVLKFDKFEN VSKELTLLSV 

       250        260        270        280        290        300 
SESLKLIKNN LSNLGIVHDR FTSETDIVLN NEVQKAIDKL KEKKLVYSGK IKAPKGEDDE 

       310        320        330        340        350        360 
NWVEREQLLF KSTDFGDDKD RALQKSDKSW TYFASDVAYH DNKLNRNYDT LINILGADHA 

       370        380        390        400        410        420 
GYIKRITSVV EALSGDKKKL ICKVSQLVKL IKDGKPFKMS KRKGDYITVE DLIAEVGKDA 

       430        440        450        460        470        480 
TRFIMLNRSS DVELDFDFTK VKEKSKDNPL YYVQYCYARI SSVFRHVNLN IENDLNIKDY 

       490        500        510        520        530        540 
EFAYTGDEIK ILKKIAEWPK CIEAASLRLE PHRIPVYLYE LSSEFHSYWN MGKEDQSKRF 

       550        560        570 
INEQKKISND KLVFLKVISN VIKSGMDIVG VDTPQKM 

« Hide

References

[1]"Genome streamlining in a cosmopolitan oceanic bacterium."
Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D., Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M., Carrington J.C., Mathur E.J.
Science 309:1242-1245(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HTCC1062.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000084 Genomic DNA. Translation: AAZ21778.1.
RefSeqYP_266382.1. NC_007205.1.

3D structure databases

ProteinModelPortalQ4FM10.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335992.SAR11_0970.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ21778; AAZ21778; SAR11_0970.
GeneID3516577.
KEGGpub:SAR11_0970.
PATRIC31991421. VBICanPel5618_0961.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMARFIMLTR.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycCPEL335992:GH3Z-977-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_PELUB
AccessionPrimary (citable) accession number: Q4FM10
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: August 30, 2005
Last modified: April 16, 2014
This is version 60 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