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A2C016 (SYR_PROM1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. 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:NATL1_02621
OrganismProchlorococcus marinus (strain NATL1A) [Complete proteome] [HAMAP]
Taxonomic identifier167555 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length607 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 – 607607Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000018087

Regions

Motif147 – 15711"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
A2C016 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 2CAF8267062EDB13

FASTA60768,529
        10         20         30         40         50         60 
MLEISARLEE ALNRAFTKVF PQEDRSSKTS SILTGSNLVP ASKPEFGDFQ INCALSLAKE 

        70         80         90        100        110        120 
INRPPRDIAQ QIAKQLQQDN DFVRICNPPL IAGPGFINLS INSKTLISEI HFRLNDKRLG 

       130        140        150        160        170        180 
VPLKKFNTDK IEEEKSNNRV IIDFSSPNIA KEMHVGHLRS TIIGDSLARV LEFCGYEVLR 

       190        200        210        220        230        240 
LNHVGDWGTQ FGMLITHLKE VVPEVLHTKD VVEISDLVNF YRQAKKRFDE DQIFQNKSRS 

       250        260        270        280        290        300 
EVVNLQAGDK ESLIAWQLLC NQSRKEFQKI YDRLDIKLTE RGESFYNKFL VDVINDLKNK 

       310        320        330        340        350        360 
KLLINDQGAQ CIFLDGLVGK DGKPQPIIIQ KSDGGFNYAT TDLAAIKYRL TIPPHGDGAC 

       370        380        390        400        410        420 
RLIYVTDAGQ ASHFSGVFQI AKLANWIPTD CQIEHVPFGL VQGEDGKKLK TRSGETIRLV 

       430        440        450        460        470        480 
DLLDEAIQRA RDDLKNRLNT ESRSENENFI DKVSTTVGIA SIKYADLSQN RISNYQFSFD 

       490        500        510        520        530        540 
KMLSLQGNTA PYLLYALVRI AGISRKGGDL NVSSQNIQFN ESQEWDLIRK LLQLDSIIAE 

       550        560        570        580        590        600 
VEKELLPNRL CGYLFELSQT FNRFYDQVPI LKASEPSRAS RLVLCSITAD TLKLGMSLLG 


IPTLERM 

« 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: NATL1A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000553 Genomic DNA. Translation: ABM74826.1.
RefSeqYP_001014091.1. NC_008819.1.

3D structure databases

ProteinModelPortalA2C016.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167555.NATL1_02621.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM74826; ABM74826; NATL1_02621.
GeneID4780407.
KEGGpme:NATL1_02621.
PATRIC23018047. VBIProMar31285_0269.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMAYVKFHDE.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycPMAR167555:GI3K-266-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_PROM1
AccessionPrimary (citable) accession number: A2C016
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 20, 2007
Last modified: May 14, 2014
This is version 51 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