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Q6FYU5 (SYH_BARQU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 71. 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:BQ10830
OrganismBartonella quintana (strain Toulouse) (Rochalimaea quintana) [Complete proteome] [HAMAP]
Taxonomic identifier283165 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length498 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 – 498498Histidine--tRNA ligase HAMAP-Rule MF_00127
PRO_0000136112

Sequences

Sequence LengthMass (Da)Tools
Q6FYU5 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 039D63B704C27432

FASTA49856,174
        10         20         30         40         50         60 
MSSKQEKTKA RLPRGFIDRT SAQLYATETM IAQIREVYEL YGFEALETPI FEYTDVLGKF 

        70         80         90        100        110        120 
LPDEDRPNAG VFSLQDEDEQ WMSLRYDLTA PLARYFAENF EILPKPYRSY RLGFVFRNEK 

       130        140        150        160        170        180 
PGPGRFRQFM QFDADIVGTP TVAADAEICM MAADSLEKLG FQHHDYVIRL NNRKILEAVL 

       190        200        210        220        230        240 
EQIGLVGREK AEKRLTVLRA IDKLDKFGLE GVRLLLGKGR LDESGDFTKG AQLKDQEIDS 

       250        260        270        280        290        300 
VLALLTGEAE TAEETLDALR HVVGHHIQGL EGVRELEEMQ AIFAANGYQN RIKIDPSVVR 

       310        320        330        340        350        360 
GLEYYTGPVF EATLLFDVLN DDGQKVVFGS IGGGGRYDGL VARFRGENVP ATGFSIGISR 

       370        380        390        400        410        420 
LITALQNLSK LPVKKTPGPV VVLMMDREPE AVAQYQKMVM QLRKAGIRAE LYLGASGIKA 

       430        440        450        460        470        480 
QMKYADRRQA PCVVIQGSQE RQDRKIQIKD LIEGTRLSRE IKDNQTWRES RPAQITVDEE 

       490 
RLVQAVQDIL ISQNAQKF 

« Hide

References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Toulouse.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX897700 Genomic DNA. Translation: CAF26550.1.
RefSeqYP_032644.1. NC_005955.1.

3D structure databases

ProteinModelPortalQ6FYU5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283165.BQ10830.

Proteomic databases

PRIDEQ6FYU5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF26550; CAF26550; BQ10830.
GeneID2867302.
KEGGbqu:BQ10830.
PATRIC31953547. VBIBarQui58630_1178.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0124.
HOGENOMHOG000018071.
KOK01892.
OMARGDYLIR.
OrthoDBEOG6BPDH4.

Enzyme and pathway databases

BioCycBQUI283165:GHZA-1081-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_BARQU
AccessionPrimary (citable) accession number: Q6FYU5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: July 19, 2004
Last modified: May 14, 2014
This is version 71 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