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Q46HI6 (SYR_PROMT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 59. 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:PMN2A_1554
OrganismProchlorococcus marinus (strain NATL2A) [Complete proteome] [HAMAP]
Taxonomic identifier59920 [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_0000242066

Regions

Motif147 – 15711"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q46HI6 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 8152D8E8A0D7F24A

FASTA60768,661
        10         20         30         40         50         60 
MLEISARLEE ALNRAFIKVF PQEDRSSKTS SILTGSNLVP ASKPEFGDFQ INCALSLAKE 

        70         80         90        100        110        120 
IKQPPREIAQ KIANQLQKDN DFVRMCNPPR IAGPGFINLS INSKTLISEI HVRLNDKRLG 

       130        140        150        160        170        180 
VPLKKFSTDK IEEGKSNNRV ILDFSSPNIA KEMHVGHLRS TIIGDSLARI LEFRGYEVLR 

       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 NGKPQPIIIQ KSDGGFNYAT TDLAAIKYRL TIPPHGDGAC 

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

       430        440        450        460        470        480 
DLLDEAIQRA KNDLKNRLNT ERRSENENFI DKVSTTVGIA SIKYADLSQN RISNYQFSFD 

       490        500        510        520        530        540 
KMLSLQGNTA PYLLYALVRI AGISRKGGDL NVSSHNIQFN ESQEWELIRK LLQLDYIIAE 

       550        560        570        580        590        600 
VEKELLPNRL CGYLFELSQT FNRFYDQVPI LKASEPSRAS RLILCSITAD 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: NATL2A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000095 Genomic DNA. Translation: AAZ59042.1.
RefSeqYP_292745.1. NC_007335.2.

3D structure databases

ProteinModelPortalQ46HI6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59920.PMN2A_1554.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ59042; AAZ59042; PMN2A_1554.
GeneID3606952.
KEGGpmn:PMN2A_1554.
PATRIC23022583. VBIProMar14922_0250.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMAYVKFHDE.
OrthoDBEOG6JB13C.
PhylomeDBQ46HI6.

Enzyme and pathway databases

BioCycPMAR59920:GI1O-247-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_PROMT
AccessionPrimary (citable) accession number: Q46HI6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: September 13, 2005
Last modified: July 9, 2014
This is version 59 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