Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q668A0 (SYH_YERPS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 66. 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:YPTB2840
OrganismYersinia pseudotuberculosis serotype I (strain IP32953) [Complete proteome] [HAMAP]
Taxonomic identifier273123 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length424 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 – 424424Histidine--tRNA ligase HAMAP-Rule MF_00127
PRO_0000136306

Sequences

Sequence LengthMass (Da)Tools
Q668A0 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: B6DAD3B591E6703D

FASTA42447,262
        10         20         30         40         50         60 
MAKNIQAIRG MNDYLPADTA IWQRIESILK QVLSGYGYSE IRMPIVEQTP LFKRAIGEVT 

        70         80         90        100        110        120 
DVVEKEMYTF DDRNGESLTL RPEGTAGCVR AGIEHGLLYN QEQRLWYIGP MFRYERPQKG 

       130        140        150        160        170        180 
RYRQFHQLGA EVFGLPGPDI DAELILLTAR WWRALGIFEH VKLELNSIGS LAARADYREA 

       190        200        210        220        230        240 
LVAFLEQHVE VLDEDCKRRM YSNPLRVLDS KNPDVQQLLD DAPKLSDYLD EESKQHFAGL 

       250        260        270        280        290        300 
CELLDKASIP YTVNERLVRG LDYYNRTVFE WVTHSLGAQG TVCAGGRYDG LVEQLGGRAT 

       310        320        330        340        350        360 
PAVGFAMGLE RLVLLVQAVN ADFQVPATVD AYVISSGEGA QSAAMLLAES LRDALPTLKI 

       370        380        390        400        410        420 
MTNYGGGNVK KQFTRADKWG ARVALMLGES EVAAQQVVVK DLRNGEQETL AQADVAARLA 


LMLG 

« Hide

References

[1]"Insights into the evolution of Yersinia pestis through whole-genome comparison with Yersinia pseudotuberculosis."
Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., Simonet M., Chenal-Francisque V., Souza B. expand/collapse author list , Dacheux D., Elliott J.M., Derbise A., Hauser L.J., Garcia E.
Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IP32953.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX936398 Genomic DNA. Translation: CAH22078.1.
RefSeqYP_071347.1. NC_006155.1.

3D structure databases

ProteinModelPortalQ668A0.
SMRQ668A0. Positions 4-424.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273123.YPTB2840.

Proteomic databases

PRIDEQ668A0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH22078; CAH22078; YPTB2840.
GeneID2955801.
KEGGyps:YPTB2840.
PATRIC18644807. VBIYerPse22266_3454.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0124.
HOGENOMHOG000018072.
KOK01892.
OMACGGGNFK.
OrthoDBEOG6BPDH4.

Enzyme and pathway databases

BioCycYPSE273123:GI1M-2934-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_YERPS
AccessionPrimary (citable) accession number: Q668A0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: October 11, 2004
Last modified: May 14, 2014
This is version 66 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