Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q2KY92 (SYH_BORA1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. 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:
Histidine--tRNA ligase

EC=6.1.1.21
Alternative name(s):
Histidyl-tRNA synthetase
Short name=HisRS
Gene names
Name:hisS
Ordered Locus Names:BAV2343
OrganismBordetella avium (strain 197N) [Complete proteome] [HAMAP]
Taxonomic identifier360910 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Subunit structure

Homodimer By similarity. HAMAP MF_00127

Subcellular location

Cytoplasm By similarity HAMAP 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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Histidine--tRNA ligase HAMAP MF_00127
PRO_1000016315

Sequences

Sequence LengthMass (Da)Tools
Q2KY92 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 914D6819BD979D53

FASTA42847,191
        10         20         30         40         50         60 
MTQAFQKVSA IRGMNDVLPG PSAQWERFEE IVRAWLQGYG YRNVRTPILE QTRLFTRGIG 

        70         80         90        100        110        120 
EVTDIVEKEM YTFTDALNGE SLTMRPEMTA GVVRAAIEHN MLYERPHRVY SIGPVFRHER 

       130        140        150        160        170        180 
PQRGRYRQFH QIDVEALGFA GPDIDAELIV MLGRLWNTLG LADIRLELNS LGQPAERAAH 

       190        200        210        220        230        240 
RAALIEYLEK HVDILDEDGK RRLYTNPLRV LDTKNPALQE MANAAPRLFD FLGEASRAHF 

       250        260        270        280        290        300 
DGVCQRLDDA GIGYSLNPRL VRGLDYYNLT VFEWVTDRLG SQGTVCGGGR YDGLIELLGG 

       310        320        330        340        350        360 
KPAPAVGFAI GVERLLDLWE QSAGQQTPPE CEVYVVHQGE GAQRLAARVG EDLRDAGLSV 

       370        380        390        400        410        420 
IVHAGAASFK SQFKRADASG ARVAVILGDD EVATKTASVK YLRADAAGEG AQDKVALATL 


ASVLKSKG 

« Hide

References

[1]"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
J. Bacteriol. 188:6002-6015(2006) [PubMed: 16885469] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 197N.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM167904 Genomic DNA. Translation: CAJ49953.1.
RefSeqYP_786857.1. NC_010645.1.

3D structure databases

ProteinModelPortalQ2KY92.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2KY92.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6265925.
GenomeReviewsGene locus BAV2343 in contig AM167904_GR.
KEGGbav:BAV2343.
NMPDRfig|521.1.peg.108.
PATRIC21130923. VBIBorAvi43433_2369.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG616575.
OMAIERSINC.
ProtClustDBPRK00037.

Enzyme and pathway databases

BioCycABAU360910:BAV2343-MONOMER.

Family and domain databases

HAMAPMF_00127. His_tRNA_synth.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR015807. His-tRNA-synth_IIa_subgr.
IPR004516. His-tRNA_synth_IIA.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
KOK01892.
PANTHERPTHR11476. His-tRNA_synth. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PIRSFPIRSF001549. His-tRNA_synth. 1 hit.
SUPFAMSSF52954. Anticodon_bd. 1 hit.
TIGRFAMsTIGR00442. HisS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYH_BORA1
AccessionPrimary (citable) accession number: Q2KY92
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 7, 2006
Last modified: January 25, 2012
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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families