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A2CDB7 (SYR_PROM3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 49. 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:P9303_27471
OrganismProchlorococcus marinus (strain MIT 9303) [Complete proteome] [HAMAP]
Taxonomic identifier59922 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length603 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 – 603603Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000018088

Regions

Motif143 – 15311"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
A2CDB7 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 40220DA99C9ADAB8

FASTA60366,379
        10         20         30         40         50         60 
MLSLAHALES QLRAAIDRAF PEAAASARES GTGLDPQLAP ASKPEFGDFQ ANAALPLAKP 

        70         80         90        100        110        120 
LKQPPRQIAA AIVDQLMVDT AFNAICLTPD IAGPGFINLT VRPECLAAEV QARLADARLG 

       130        140        150        160        170        180 
VPLVEGDNDG QQPTPVVVDF SSPNIAKEMH VGHLRSTIIG DSLARVLEFR GHPVLRLNHV 

       190        200        210        220        230        240 
GDWGTQFGML ITHLKQVAPE ALETADAVDL GDLVVFYRQA KQRFDDDEAF QTTSREEVVK 

       250        260        270        280        290        300 
LQGGDPLSLK AWSLLCDQSR REFQKIYDRL DVRLNERGES FYNAYLESVV EDLNVSGLLV 

       310        320        330        340        350        360 
SDDGAQCVFL EGVTGKDGKP LPVIVQKSDG GFNYATTDLA AMRYRFAAPP QGDGARRVIY 

       370        380        390        400        410        420 
VTDAGQANHF AGVFQVAQRA GWIPDAGRLQ HVPFGLVQGE DGKKLKTRAG DTVRLRELLD 

       430        440        450        460        470        480 
EAVERAESDL RRRLQEEGRD EDESFIEQVA TTVGLAAVKY ADLSQNRITN YQFSFDRMLA 

       490        500        510        520        530        540 
LQGNTAPYLL YAVVRIAGIA RKGGDLDVTT AELQFSETQE WALVRELLKF DAVIAEVEEE 

       550        560        570        580        590        600 
LLPNRLCTYL FELSQVFNRF YDQVPVLKAE QPSRSCRLAL CRLTADTLKL GLSLLGIPTL 


ERM 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9303.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000554 Genomic DNA. Translation: ABM79477.1.
RefSeqYP_001018742.1. NC_008820.1.

3D structure databases

ProteinModelPortalA2CDB7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59922.P9303_27471.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM79477; ABM79477; P9303_27471.
GeneID4777617.
KEGGpmf:P9303_27471.
PATRIC23003049. VBIProMar17757_2808.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMAYVKFHDE.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycPMAR59922:GH54-2854-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_PROM3
AccessionPrimary (citable) accession number: A2CDB7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 20, 2007
Last modified: May 14, 2014
This is version 49 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