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A5VTT4 (SYH_BRUO2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. 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:
Histidine--tRNA ligase

EC=6.1.1.21
Alternative name(s):
Histidyl-tRNA synthetase
Short name=HisRS
Gene names
Name:hisS
Ordered Locus Names:BOV_A0169
OrganismBrucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512) [Complete proteome] [HAMAP]
Taxonomic identifier444178 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length502 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His). HAMAP-Rule MF_00127

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00127

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00127.

Sequence similarities

Belongs to the class-II 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_processhistidyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

histidine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 502502Histidine--tRNA ligase HAMAP-Rule MF_00127
PRO_1000016318

Sequences

Sequence LengthMass (Da)Tools
A5VTT4 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: BD9DC3BA3B405833

FASTA50255,149
        10         20         30         40         50         60 
MADKADKMKA RLPRGFVDRV PDDLRAAEKM MATIREVYDL YGFEPVETPL VEYTDALGKF 

        70         80         90        100        110        120 
LPDQDRPNEG VFSFQDDDEQ WLSLRYDLTA PLARYVAENF ETLPKPYRSY RNGWVFRNEK 

       130        140        150        160        170        180 
PGPGRFRQFM QFDADTVGAP NVSADAEMCM MMADALERLG IQRGDYAIRV NNRKVLDGVL 

       190        200        210        220        230        240 
DAIGLEGEGN AAKRLNVLRA IDKLDKFGPE GVRLLLGKGR LDESGDFTKG AQLPEAAIEK 

       250        260        270        280        290        300 
VLAFTAAGGA DGAQTIANLQ AVVAGNAKGE EGVQELADMQ ALFFAGGYEG RVKIDPSVVR 

       310        320        330        340        350        360 
GLEYYTGPVF EAELLFDVTN EDGQKVVFGS VGGGGRYDGL VSRFRGEPVP ATGFSIGVSR 

       370        380        390        400        410        420 
LMTALKNLGK LDVSDTVGPV VVLVMDKDTQ NLGRYQKMVS DLRKAGIRAE MYVGGSGMKA 

       430        440        450        460        470        480 
QMKYADRRAA PCVVIQGSQE REAGEVQIKD LVEGKRLSAE IEDNVTWRES RPAQITVRED 

       490        500 
GLVDAVREIL DAQARDRAEQ SK 

« Hide

References

[1]Paulsen I.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25840 / 63/290 / NCTC 10512.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000709 Genomic DNA. Translation: ABQ61997.1.
RefSeqYP_001257239.1. NC_009504.1.

3D structure databases

ProteinModelPortalA5VTT4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING444178.BOV_A0169.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ61997; ABQ61997; BOV_A0169.
GeneID5203917.
KEGGbov:BOV_A0169.
PATRIC17857482. VBIBruOvi136990_0192.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0124.
HOGENOMHOG000018071.
KOK01892.
OMAIFSITKA.
OrthoDBEOG6BPDH4.
ProtClustDBPRK00037.

Enzyme and pathway databases

BioCycBOVI444178:GH2V-2264-MONOMER.

Family and domain databases

Gene3D3.40.50.800. 1 hit.
HAMAPMF_00127. His_tRNA_synth.
InterProIPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR015807. His-tRNA-ligase.
IPR004516. HisRS/HisZ.
[Graphical view]
PANTHERPTHR11476. PTHR11476. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
[Graphical view]
PIRSFPIRSF001549. His-tRNA_synth. 1 hit.
SUPFAMSSF52954. SSF52954. 1 hit.
TIGRFAMsTIGR00442. hisS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYH_BRUO2
AccessionPrimary (citable) accession number: A5VTT4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: February 19, 2014
This is version 48 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