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Q1Q8I7 (SYR_PSYCK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 54. 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:Pcryo_2239
OrganismPsychrobacter cryohalolentis (strain K5) [Complete proteome] [HAMAP]
Taxonomic identifier335284 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter

Protein attributes

Sequence length609 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 – 609609Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242074

Regions

Motif132 – 14211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q1Q8I7 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 28EDD431089B892F

FASTA60967,402
        10         20         30         40         50         60 
MSQAQIDTLT SLFDSAIAVL KNDGELPADW QNNSQITRTK DTSHGDFASN IALTAAKAAK 

        70         80         90        100        110        120 
ANPRQVAEKI VNALPENQDI RQIEIAGPGF INVFLNTEAK FAVLDDIFNL QNGFGLSKQF 

       130        140        150        160        170        180 
DGQKIQVEFV SANPTSSLHV GHGRGAAFGM SVSNLLEAIG YDVTREYYVN DAGRQMDILA 

       190        200        210        220        230        240 
TSTYLRYLET NGETVTFPVN GYQGDYVSDI AQTLKTQHAD TYVHRFADIA ENVPEDAQFE 

       250        260        270        280        290        300 
INADGEKVLL SGDKEAHIDG LIANSKALLG NGYELFLNAA LSSILADIKD DLNDFGVSYE 

       310        320        330        340        350        360 
CWFSERSIDS EIEPVLQILE DKGYLYEKDG NIWFKSTDFG DEKDRVVRRA NGQSTYFASD 

       370        380        390        400        410        420 
IAYHKNKFDR GFDKVVNVWG ADHHGYVPRV KAALLALGID ADRLDVVLVQ FVALWRGDEK 

       430        440        450        460        470        480 
VQMSSRSGKF VTLRELRHEV GNDAARFYYV ARKPEVHVDF DLELAKSQSK DNLVYYIQYA 

       490        500        510        520        530        540 
HARVCRVLEK LETSGLSVDD AIGAAQQELL VAPSEEELIK LLAAYPATLM RSATGYEPHI 

       550        560        570        580        590        600 
LTNYLKELAA LFHGWYDSNR ILPVSLTSGE TPSADEMAMM QARLRLSKAV RQVISNGLGL 


LGLSAPSSM 

« Hide

References

[1]"Complete sequence of chromosome of Psychrobacter cryohalolentis K5."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000323 Genomic DNA. Translation: ABE76016.1.
RefSeqYP_581500.1. NC_007969.1.

3D structure databases

ProteinModelPortalQ1Q8I7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335284.Pcryo_2239.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE76016; ABE76016; Pcryo_2239.
GeneID4035537.
KEGGpcr:Pcryo_2239.
PATRIC23064111. VBIPsyCry128170_2368.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMANPNGPLH.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycPCRY335284:GHE9-2283-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. 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_PSYCK
AccessionPrimary (citable) accession number: Q1Q8I7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: May 16, 2006
Last modified: April 16, 2014
This is version 54 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