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A0B5P0 (SYR_METTP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 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:Mthe_0216
OrganismMethanosaeta thermophila (strain DSM 6194 / PT) (Methanothrix thermophila (strain DSM 6194 / PT)) [Complete proteome] [HAMAP]
Taxonomic identifier349307 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosaetaceaeMethanosaeta

Protein attributes

Sequence length558 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 – 558558Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000018066

Regions

Motif119 – 12911"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
A0B5P0 [UniParc].

Last modified November 28, 2006. Version 1.
Checksum: 97EDC2D8F9C91E14

FASTA55863,436
        10         20         30         40         50         60 
MFLDFMSEVE GILKEGLDRC GLSVPLENSL DLSPHADLST TIAFRLSPVL RKDPKDVAAE 

        70         80         90        100        110        120 
IYNSMGSPSR WVDRAELVGP YINFYMSRNF LDNVVTKAQG EDAWWGRRSG SVVVEHTSAN 

       130        140        150        160        170        180 
PDGPLHVGHI RNSVIGDTIV RILRRAGYNV EAQYYVNDMG RQTAMVVWGC DHLDLDDSKP 

       190        200        210        220        230        240 
DHAIARVYIA AHKIMNEKPE LSAEVDELMR RYESRDPEIV KKFQRAARYA ISGIERTLHR 

       250        260        270        280        290        300 
MNIHHDSYKW ESEFVWDGSV DEILEMLERT GRTVLKDGAL QLDLSEEGFE KSLVLRRADG 

       310        320        330        340        350        360 
TTLYTTRDLA YHKWKAENYE RVVEVLGADH KLISAQLRTA LRMLGIGEPE VVIFEFVSLP 

       370        380        390        400        410        420 
DGSMSTRRGK FISADELLDE VEKQAYLEVT KRRPEMDEEF RRDVAGKVAV GAVRYDIVRV 

       430        440        450        460        470        480 
SADKATTFDW KTALDFEKLS APFIQYSHAR ACSIINKAGE LDEFDPGLLR DDYEIALIKK 

       490        500        510        520        530        540 
IAEFDLVIER AARELKPHQL ATYARELAER FNLFYRYDPV LDAKPVELRN ARLGLVRASR 

       550 
NALSATLDTL GIDAPESM 

« Hide

References

[1]"Complete sequence of Methanosaeta thermophila PT."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Smith K.S., Ingram-Smith C., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6194 / PT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000477 Genomic DNA. Translation: ABK14014.1.
RefSeqYP_842654.1. NC_008553.1.

3D structure databases

ProteinModelPortalA0B5P0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349307.Mthe_0216.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK14014; ABK14014; Mthe_0216.
GeneID4462997.
KEGGmtp:Mthe_0216.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247213.
KOK01887.
OMANPNGPLH.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycMMET349307:GHKI-222-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.
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. 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.
ProtoNetSearch...

Entry information

Entry nameSYR_METTP
AccessionPrimary (citable) accession number: A0B5P0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 28, 2006
Last modified: April 16, 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