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A6TNX2 (SYR_ALKMQ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 46. 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:Amet_1714
OrganismAlkaliphilus metalliredigens (strain QYMF) [Complete proteome] [HAMAP]
Taxonomic identifier293826 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeAlkaliphilus

Protein attributes

Sequence length566 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 – 566566Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000198868

Regions

Motif123 – 13311"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
A6TNX2 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: F9D4CEF14B37CAB2

FASTA56664,448
        10         20         30         40         50         60 
MSDFKQKVSE LLGTQIEGIG QRELLEMIEV PPNSEMGDFA FPCFRLAKTF RKAPQVIAEE 

        70         80         90        100        110        120 
LVAKIQLTDD FEKVDNTGGY LNFFVNRNTY AKAVIQEVLS KGDQYGSRNL GEGKNICIDY 

       130        140        150        160        170        180 
SAPNVAKPFH VGHLRSTVIG NSLYRIYDFL GYNCIGINHL GDWGTQFGKV IVAYKNWGDK 

       190        200        210        220        230        240 
AEIEKEPINT LLALYVKFHD EAEKNPDLED EARGWFTKME KGDEEALSLW KWFSSETIKE 

       250        260        270        280        290        300 
LKKIYALLDV HFDHYSGESF YNDKMDVVID ELNKQNLLKE SQGANIVDLE EYNMPPCLVQ 

       310        320        330        340        350        360 
KKDGSTLYAT RDIAAAIYRK NTFNFEKCLY VTDYSQNLHF AQWFKVIELM GYDWAKDIEH 

       370        380        390        400        410        420 
ISFGRVTHEG RRIQSRKGSV VLLEEVLNGA VERISEIIEE KNPNVENKEQ VAKDVGIGAI 

       430        440        450        460        470        480 
VFNDLSNNRI KDISFSWDTA FSFEGETGPY VQYTHARASS VLRKAEVAIT DHINAAHLTD 

       490        500        510        520        530        540 
DVTMNVIKTI EQFPQVIVDA QRKNEPSIIT RHIVNIAQAF NRFYHDHPIL VEDEELKMAR 

       550        560 
LAVVQAVKQV LSVGLSLIGI KAPEKM 

« Hide

References

[1]"Complete sequence of Alkaliphilus metalliredigens QYMF."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J., Fields M., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: QYMF.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000724 Genomic DNA. Translation: ABR47890.1.
RefSeqYP_001319549.1. NC_009633.1.

3D structure databases

ProteinModelPortalA6TNX2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING293826.Amet_1714.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR47890; ABR47890; Amet_1714.
GeneID5311768.
KEGGamt:Amet_1714.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247211.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycAMET293826:GI5P-1741-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_ALKMQ
AccessionPrimary (citable) accession number: A6TNX2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: August 21, 2007
Last modified: April 16, 2014
This is version 46 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