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Q2FS66 (SYR_METHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. 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:Mhun_2837
OrganismMethanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1) [Reference proteome] [HAMAP]
Taxonomic identifier323259 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanospirillaceaeMethanospirillum

Protein attributes

Sequence length555 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
Reference 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 – 555555Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000242132

Regions

Motif117 – 12711"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q2FS66 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 22FFA23E06B51378

FASTA55561,994
        10         20         30         40         50         60 
MYRTTCDAIA AILRQHTGKE DVMLTDGGDH ADVASTIAFS LAKELRKAPA IIAQEIAGAI 

        70         80         90        100        110        120 
SDQVMAETGA ETRAVGPYVN FIFGAEYCMN VLEQAVREGY GKGQEKSERV VLEHTSANPN 

       130        140        150        160        170        180 
GPLHVGHIRN TIIGDTLARC FRKAGYPLEV QYYVNDMGRQ IAIVAWGIAT QGADIHAEGK 

       190        200        210        220        230        240 
GDHLIADVYI EANRHLEKEP ALNAEIDRLM QLVESGDPDT ISQFKIPVKR CLDGFKDTLA 

       250        260        270        280        290        300 
AMHVKHDRFI YESDFIRNGD TAKVLSRISH LPEARIEETL SLDLSAFGFE KNYILRRSDG 

       310        320        330        340        350        360 
TSVYAARDIA FHIWKGHNFD RVIDVLGADH KLIGTQLQAT LEILGERVPE IVFFEFVSLP 

       370        380        390        400        410        420 
EGSMSTRKGK FISADELIAE TERRAMEEVT ARRSELSEEE RKKIAHSVAI SAIRYDIIRT 

       430        440        450        460        470        480 
IPEKSTVFDW KEALDFEKQS GPYIQYAHAR ACSILEKAES YTPCFEAEGE GEIALTKQIA 

       490        500        510        520        530        540 
LFPKVITEVV TELKPHLLAI YARELADIFN SFYHAEPVLR AEGKIRDRRL TLVDATRNTL 

       550 
KEALETLGID ALRAM 

« Hide

References

[1]"Complete sequence of Methanospirillum hungatei JF-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Ivanova N., McInerney M.J., Brockman F., Culley D., Ferry J.G., Gunsalus R.P., Morrison M., Plugge C., Scholten J., Stams A.J.M., Boone D.R., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27890 / DSM 864 / NBRC 100397 / JF-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000254 Genomic DNA. Translation: ABD42529.1.
RefSeqYP_504248.1. NC_007796.1.

3D structure databases

ProteinModelPortalQ2FS66.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323259.Mhun_2837.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD42529; ABD42529; Mhun_2837.
GeneID3923106.
KEGGmhu:Mhun_2837.

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247213.
KOK01887.
OMAMEHMGFG.

Enzyme and pathway databases

BioCycMHUN323259:GH0L-2878-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_METHJ
AccessionPrimary (citable) accession number: Q2FS66
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 21, 2006
Last modified: May 14, 2014
This is version 51 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