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Q9YB39 (SYR_AERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. 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:APE_1756
OrganismAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) [Complete proteome] [HAMAP]
Taxonomic identifier272557 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum

Protein attributes

Sequence length644 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

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 – 644644Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000151642

Regions

Motif129 – 13911"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q9YB39 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 076E18F55C0B5A08

FASTA64472,173
        10         20         30         40         50         60 
MASSIDPLTR LHGILSSYLS EVLGVDRSVV ERLLAPPPRK EYGDLGFPLM RFARSSNASA 

        70         80         90        100        110        120 
DSIVESLRGK LWERGITWAS PTLEAGYLNI VFDVEKLGDE VFRLLASGWR PSTARTSRPE 

       130        140        150        160        170        180 
TIVVEHTSAN PIHPLHLGHA RNSSLGDALA RLLEARGHRV NRRFYVDDVG RQAVVASLGF 

       190        200        210        220        230        240 
KLSGVTPREL ASRMGVKVDH AVGWVYAVTH NALETVTARK RGDTSKVDEA LSTLARLKER 

       250        260        270        280        290        300 
GDREVFDRIL EAVGSLDDPE GLVSEMMRKY ERGEEPEKSL IRGVVSAVLE GFRETLGRFG 

       310        320        330        340        350        360 
VDFDDWDWES DLLWSGLVNK IIEEARRSPF LTTHKDAIAL DIPRIVREVL ARDPEAASTI 

       370        380        390        400        410        420 
KLPRSLEIPP LILVRSDGTT LYTTRDLAYS VYKFRVTGAD RVINVIGADQ RLPQLQIRLA 

       430        440        450        460        470        480 
LLGLGYRREA LNMMHYDYEI VSLPGRRMSS RRGEYVTLDE LLEMAKARSV REVESRNPGA 

       490        500        510        520        530        540 
DRDWIESTAE KIAVGAVRFA LVRPGRLKPI TLDVERILDL KENTAPYLQY TYARASSILE 

       550        560        570        580        590        600 
KHGEIDYLKA HPASLEEGSR RELFVEALRF PLVSAKAADD LAPEDLASYL LRLADMFNSW 

       610        620        630        640 
YQKDSVIHEE WEGARHAKAA LVLLVKSVIG EGLRLLGVEP LEKM 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000002 Genomic DNA. Translation: BAA80759.1.
PIRB72559.
RefSeqNP_148147.1. NC_000854.2.

3D structure databases

ProteinModelPortalQ9YB39.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272557.APE_1756.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA80759; BAA80759; APE_1756.
GeneID1446221.
KEGGape:APE_1756.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247213.
KOK01887.
OMADGTAVYM.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycAPER272557:GJD6-1188-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00123. Arg_tRNA_synth.
InterProIPR001278. 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. 2 hits.
[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.
ProtoNetSearch...

Entry information

Entry nameSYR_AERPE
AccessionPrimary (citable) accession number: Q9YB39
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 92 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