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Q81B71 (SYH1_BACCR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 74. 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 1

EC=6.1.1.21
Alternative name(s):
Histidyl-tRNA synthetase 1
Short name=HisRS 1
Gene names
Name:hisS-1
Ordered Locus Names:BC_3317
OrganismBacillus cereus (strain ATCC 14579 / DSM 31) [Reference proteome] [HAMAP]
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length426 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 – 426426Histidine--tRNA ligase 1 HAMAP-Rule MF_00127
PRO_0000136097

Sequences

Sequence LengthMass (Da)Tools
Q81B71 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 4DB7E3D889D43C30

FASTA42648,144
        10         20         30         40         50         60 
MMEMRNVKGT KDYLPEEQVL RNKIKRACED TFERYGCKPL ETPTLNMYEL MSYKYGGGDE 

        70         80         90        100        110        120 
ILKEIYTLQD QGKRELALRY DLTIPFAKVV AMNPNLRLPF KRYEIGKVFR DGPIKQGRFR 

       130        140        150        160        170        180 
EFIQCDVDIV GVESVMAEAE LMAMAFELFR TLNLEITIQY NNRKLLNGIL ESINIPTELT 

       190        200        210        220        230        240 
SDVILSLDKI EKIGIDGVRK DVLERGISEE MADTICNTVL SCLKLTIADF KEAFNNPLVA 

       250        260        270        280        290        300 
DGVNELQQLQ QYLIALGINE NTIFNPFLAR GLTMYTGTVY EIFLKDRSIT SSIGSGGRYD 

       310        320        330        340        350        360 
NIIGAFRGDN MNYPTVGISF GLDVIYTALS QKETISSTAD VFIIPLGTEL QCLQIAQQLR 

       370        380        390        400        410        420 
STTSLKVELE LAGRKLKRAL NYANKENIPY VLIIGEDELS TNTVVLRNMK EGSEVKVPIS 


SLSRYL 

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016877 Genomic DNA. Translation: AAP10257.1.
RefSeqNP_833056.1. NC_004722.1.

3D structure databases

ProteinModelPortalQ81B71.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226900.BC3317.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP10257; AAP10257; BC_3317.
GeneID1205664.
KEGGbce:BC3317.
PATRIC32602595. VBIBacCer54481_3402.

Phylogenomic databases

eggNOGCOG0124.
KOK01892.
OMANKIKRAC.
OrthoDBEOG6BPDH4.
ProtClustDBPRK12420.

Enzyme and pathway databases

BioCycBCER226900:GJEU-3315-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 nameSYH1_BACCR
AccessionPrimary (citable) accession number: Q81B71
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 74 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