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Q2NE12 (SYR_METST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:Msp_1574
OrganismMethanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3) [Complete proteome] [HAMAP]
Taxonomic identifier339860 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanosphaera

Protein attributes

Sequence length560 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 – 560560Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242131

Regions

Motif122 – 13211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q2NE12 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 23080817D7E97A69

FASTA56064,597
        10         20         30         40         50         60 
MYSKLKTEIN ESIKEALTKL RIKYDDEIIL EEPPNPSMGD MSTNIAFSLA SKLKKSPVEI 

        70         80         90        100        110        120 
AQEIKENIKL PLYFEKVETK GPYINFYINY TLFTTKVVNY IDKNYGELPE KDERILLEHT 

       130        140        150        160        170        180 
SANPNGPLHV GHLRNAILGD SLKRILQHAG YKVEAQYYVN DMGRQIAIIV WGMDKFNYTV 

       190        200        210        220        230        240 
DDDKKADHAI GEVYYKCNQQ LEANPEYNQE IDDILRKYEE GTDAALIDAF QGVVEYCIDG 

       250        260        270        280        290        300 
IKETLKDLNI KMNLFKWEST FLRNGSVDDV LEKLQPFTIQ KDILYLPLER YNVDKELVLR 

       310        320        330        340        350        360 
RSNGTSLYAT RDLAYHQYKT KNSDISLDIL GADHKLAAKQ LGLALELSNN RAPEVVFYEF 

       370        380        390        400        410        420 
IDLPEGSMST RKGVFISVDE FIEQSVEHAK EELIRRDLDL TEKQIEEVSK IVGVGSIRFY 

       430        440        450        460        470        480 
INQISPEKPI TFKWEEALSF ERGCASIQYA HARACKLLAK SDYNEFEEVR CDYELDDEEK 

       490        500        510        520        530        540 
DLIKTLSQFT EVICQSAQER RVHHLAQYTL SLSKAFNKFY KSKQVIGSEH EKLRLKLVDA 

       550        560 
SRITLKNSLK LLGIKSPEFM 

« Hide

References

[1]"The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis."
Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R., Gottschalk G., Thauer R.K.
J. Bacteriol. 188:642-658(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000102 Genomic DNA. Translation: ABC57941.1.
RefSeqYP_448584.1. NC_007681.1.

3D structure databases

ProteinModelPortalQ2NE12.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING339860.Msp_1574.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC57941; ABC57941; Msp_1574.
GeneID3855800.
KEGGmst:Msp_1574.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247213.
KOK01887.
OMAMEHMGFG.

Enzyme and pathway databases

BioCycMSTA339860:GJEZ-1577-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_METST
AccessionPrimary (citable) accession number: Q2NE12
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: February 7, 2006
Last modified: May 14, 2014
This is version 52 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