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P62374 (SYH_THET2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:TT_C0360
OrganismThermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [Complete proteome] [HAMAP]
Taxonomic identifier262724 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 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 term3D-structure
Complete 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 – 421421Histidine--tRNA ligase HAMAP MF_00127
PRO_0000136283

Secondary structure

............................................................. 421
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62374 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 9DEEE25F2C570A27

FASTA42147,041
        10         20         30         40         50         60 
MTARAVRGTK DLFGKELRMH QRIVATARKV LEAAGALELV TPIFEETQVF EKGVGAATDI 

        70         80         90        100        110        120 
VRKEMFTFQD RGGRSLTLRP EGTAAMVRAY LEHGMKVWPQ PVRLWMAGPM FRAERPQKGR 

       130        140        150        160        170        180 
YRQFHQVNYE ALGSENPILD AEAVVLLYEC LKELGLRRLK VKLSSVGDPE DRARYNAYLR 

       190        200        210        220        230        240 
EVLSPHREAL SEDSKERLEL NPMRILDSKS ERDQALLKEL GVRPMLDFLG EEARAHLKEV 

       250        260        270        280        290        300 
ERHLERLSVP YELEPALVRG LDYYVRTAFE VHHEEIGAQS ALGGGGRYDG LSELLGGPRV 

       310        320        330        340        350        360 
PGVGFAFGVE RVALALEAEG FGLPEEKGPD LYLIPLTEEA VAEAFYLAEA LRPRLRAEYA 

       370        380        390        400        410        420 
LAPRKPAKGL EEALKRGAAF AGFLGEDELR AGEVTLKRLA TGEQVRLSRE EVPGYLLQAL 


G 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017221 Genomic DNA. Translation: AAS80708.1.
RefSeqYP_004335.1. NC_005835.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H4VX-ray2.40B1-421[»]
ProteinModelPortalP62374.
SMRP62374. Positions 2-421.
ModBaseSearch...

Protein-protein interaction databases

STRINGP62374.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2774649.
GenomeReviewsGene locus TT_C0360 in contig AE017221_GR.
PATRIC23951117. VBITheThe54392_0358.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0124.
HOGENOMHBG616575.
OMAIERSINC.
PhylomeDBP62374.
ProtClustDBPRK00037.

Enzyme and pathway databases

BioCycTTHE262724:TT_C0360-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.
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_THET2
AccessionPrimary (citable) accession number: P62374
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 49 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families