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B1MLU2 (SYR_MYCA9) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 43. 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:MAB_1433
OrganismMycobacterium abscessus (strain ATCC 19977 / DSM 44196) [Complete proteome] [HAMAP]
Taxonomic identifier561007 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium abscessus

Protein attributes

Sequence length550 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 – 550550Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_1000095382

Regions

Motif130 – 14011"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
B1MLU2 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: CB0FE1DE15A92015

FASTA55059,679
        10         20         30         40         50         60 
MTPADLADLL RSTATTVLDE RGLDTSALPA VVTVERPRNP EHGDYATNVA LQVAKKVGVA 

        70         80         90        100        110        120 
PRDLAGWLVE ALVSHAAIAG AEIAGPGFVN LRIAADAQGT IVANILKAGE TYGNSDAQGT 

       130        140        150        160        170        180 
HTINLEFVSA NPTGPIHIGG TRWAAVGDAL GRLLARQGAK VTREYYFNDH GAQIDRFVRS 

       190        200        210        220        230        240 
LIASAEGKEA PEDGYAGDYI ADIAKQVITQ RPEALTLTEP ERSEVFREIG VDLMFTHIKE 

       250        260        270        280        290        300 
SLHEFGTDFD VFTHEDSMHT SGRVQEAIAQ LRKTGNIYEK DGASWLRSSN FGDDKDRVVI 

       310        320        330        340        350        360 
KSDGNPAYIA GDIAYYLDKR ERGFDLCIYM LGADHHGYIA RLKAVAAALG YDADSVEVLI 

       370        380        390        400        410        420 
GQMVNLVRDG QPVRMSKRAG TVITLDDLVD AIGVDAARYA LIRSSVDTSI DIDLELWASA 

       430        440        450        460        470        480 
SSENPVYYVQ YAHARLCALA RNAADLGLQH STEHLELLTH EKEGALIRGL GEFGRILQNA 

       490        500        510        520        530        540 
AALREPHRVA RYLEDIAGDY HRFYDSCRVL PQGDETPGDL HAARLALCLA TRQVIANGLD 

       550 
ILGVSAPERM 

« Hide

References

[1]"Acquisition of foreign virulence genes by the cystic fibrosis pathogen Mycobacterium abscessus."
Genoscope
Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L., Gaillard J.L.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19977 / DSM 44196.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU458896 Genomic DNA. Translation: CAM61519.1.
RefSeqYP_001702173.1. NC_010397.1.

3D structure databases

ProteinModelPortalB1MLU2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING561007.MAB_1433.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM61519; CAM61519; MAB_1433.
GeneID5967478.
KEGGmab:MAB_1433.
PATRIC17974553. VBIMycAbs55940_1470.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycMABS561007:GJTG-1436-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_MYCA9
AccessionPrimary (citable) accession number: B1MLU2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: April 16, 2014
This is version 43 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