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Q8G864 (SYH_BIFLO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. 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:BL0017
OrganismBifidobacterium longum (strain NCC 2705) [Reference proteome] [HAMAP]
Taxonomic identifier206672 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length466 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
Reference 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 – 466466Histidine--tRNA ligase HAMAP-Rule MF_00127
PRO_0000136114

Sequences

Sequence LengthMass (Da)Tools
Q8G864 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 72729E0E6A7C06C9

FASTA46650,394
        10         20         30         40         50         60 
MAKGASISGF PEWLPSERVV EQRVIDTLRK VFELNGFIGI ETRAVETGAS LLKKGETSKE 

        70         80         90        100        110        120 
IYLLSRLQEV GHESDTPIEE RLGLHFDLTV PLSRYVVEHS GALAFPFKRW QIQKVWRGER 

       130        140        150        160        170        180 
PQEGRFREFV QADIDVIGAG DLPDHYEVEL PLVMVSALEE LRAYGLPKAT VHANNRKLSE 

       190        200        210        220        230        240 
GFYRGLGLTD VEGVLREIDK LDKIGADEVA RLLTETCGAT EAQARACLEL AELTASDGAE 

       250        260        270        280        290        300 
LAAKFDALCE AHGIVKDSEA YTLARQGLDT LAMIVDEAAA IRPGSVIADL KIARGLDYYT 

       310        320        330        340        350        360 
GSVYETFLDG AASLGSICSG GRYDNLASQG NRKYPGVGLS IGLSRLVSYM LHTAGAHANR 

       370        380        390        400        410        420 
VSPAAVLVAV WNEEDRPAAN RIANQLRARG IATDVAPTAA KLGKQIKYAD KLGIPYVWFP 

       430        440        450        460 
ATAAEGAEGA EPAGDEVKNI VTGEQVAADC TSWEPDTVVA QQTVEI 

« Hide

References

[1]"The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract."
Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.
Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCC 2705.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014295 Genomic DNA. Translation: AAN23884.1.
RefSeqNP_695248.1. NC_004307.2.

3D structure databases

ProteinModelPortalQ8G864.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING206672.BL0017.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN23884; AAN23884; BL0017.
GeneID1023039.
KEGGblo:BL0017.
PATRIC21117063. VBIBifLon107831_0018.

Phylogenomic databases

eggNOGCOG0124.
HOGENOMHOG000018071.
KOK01892.
OMANKIKRAC.
OrthoDBEOG6BPDH4.
ProtClustDBPRK00037.

Enzyme and pathway databases

BioCycBLON206672:GI1E-17-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_BIFLO
AccessionPrimary (citable) accession number: Q8G864
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 67 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