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Q63C01 (SYR1_BACCZ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. 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 1

EC=6.1.1.19
Alternative name(s):
Arginyl-tRNA synthetase 1
Short name=ArgRS 1
Gene names
Name:argS1
Ordered Locus Names:BCE33L1974
OrganismBacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP]
Taxonomic identifier288681 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length562 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 – 562562Arginine--tRNA ligase 1 HAMAP-Rule MF_00123
PRO_0000241981

Regions

Motif122 – 13211"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q63C01 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 35EBD962DE643E09

FASTA56264,425
        10         20         30         40         50         60 
MDYKTQFAES LSNIFTNELT QKQILDLIET PKQDEFGDAA FPCFSLAKQY KKSPAIIAKE 

        70         80         90        100        110        120 
VAEKLSDPFF TKVEAVGPYV NVFFNRDTVS DAVLKTILAE KEEYGQNHFG CEKTVVIDYS 

       130        140        150        160        170        180 
SPNIAKPFSM GHLRSTMIGN SLKHIAEKCG YEVVGINYIG DWGTQFGKLI TAYKKWGNEA 

       190        200        210        220        230        240 
VVKEDPIREL FKLYVQFHEE IKDDEELEEE GRAWFKKLEE GDEEAVELWN WFRHESLKEF 

       250        260        270        280        290        300 
SRIYELLGVE FTNFQGEAFY NNLMEDFIGI LEEHDLLEES EGALVVNLEE EGMPPCLIRK 

       310        320        330        340        350        360 
SDGATIYATR DLTAALYRQN TFGFDKALYV VGPEQSLHFN QFFTVLKKLG YTWVDGMEHV 

       370        380        390        400        410        420 
PFGFILKDGK KMSTRKGRVI LLEEVLEEAI ELAKQNIEEK NPNLKQKEEV AKQVGAGAVI 

       430        440        450        460        470        480 
FHDLKNERMH NIEFSLENML KFEGETGPYV QYTHARACSI LRKESVEFET CTFTLKDDYS 

       490        500        510        520        530        540 
WNIVKLLNKF PEVIEAACNK NEPSVISKYV LDVAQSFNKY YGNVRILDEN AEKDSRLALV 

       550        560 
YAVTVVLKEG LRLLGVEAPE EM 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000001 Genomic DNA. Translation: AAU18282.1.
RefSeqYP_083566.1. NC_006274.1.

3D structure databases

ProteinModelPortalQ63C01.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING288681.BCZK1974.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU18282; AAU18282; BCE33L1974.
GeneID3026695.
KEGGbcz:BCZK1974.
PATRIC18887480. VBIBacCer95304_2079.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
KOK01887.
OMAYVKFHDE.
OrthoDBEOG6JB13C.

Enzyme and pathway databases

BioCycBCER288681:GHG7-2047-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 nameSYR1_BACCZ
AccessionPrimary (citable) accession number: Q63C01
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: October 25, 2004
Last modified: May 14, 2014
This is version 70 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