Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histidine--tRNA ligase

Gene

hisS

Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His).

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAminoacyl-tRNA synthetase, Ligase
Biological processProtein biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciTACI273075:G1GT7-103-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Histidine--tRNA ligase (EC:6.1.1.21)
Alternative name(s):
Histidyl-tRNA synthetase
Short name:
HisRS
Gene namesi
Name:hisS
Ordered Locus Names:Ta0099
OrganismiThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Taxonomic identifieri273075 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
Proteomesi
  • UP000001024 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001363281 – 426Histidine--tRNA ligaseAdd BLAST426

Interactioni

Protein-protein interaction databases

STRINGi273075.Ta0099

Structurei

Secondary structure

1426
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi17 – 36Combined sources20
Beta strandi46 – 49Combined sources4
Helixi51 – 54Combined sources4
Helixi61 – 64Combined sources4
Beta strandi67 – 69Combined sources3
Beta strandi75 – 78Combined sources4
Helixi83 – 90Combined sources8
Beta strandi98 – 104Combined sources7
Beta strandi107 – 109Combined sources3
Beta strandi120 – 131Combined sources12
Helixi135 – 151Combined sources17
Turni152 – 156Combined sources5
Beta strandi157 – 164Combined sources8
Helixi165 – 173Combined sources9
Helixi180 – 188Combined sources9
Turni189 – 192Combined sources4
Helixi195 – 204Combined sources10
Helixi209 – 220Combined sources12
Helixi225 – 231Combined sources7
Helixi237 – 251Combined sources15
Turni265 – 269Combined sources5
Beta strandi271 – 279Combined sources9
Beta strandi287 – 292Combined sources6
Helixi296 – 301Combined sources6
Beta strandi307 – 313Combined sources7
Helixi314 – 323Combined sources10
Beta strandi334 – 342Combined sources9
Helixi345 – 356Combined sources12
Turni357 – 359Combined sources3
Beta strandi361 – 364Combined sources4
Helixi371 – 380Combined sources10
Beta strandi384 – 390Combined sources7
Helixi391 – 395Combined sources5
Beta strandi398 – 403Combined sources6
Turni404 – 406Combined sources3
Beta strandi409 – 413Combined sources5
Helixi414 – 416Combined sources3
Helixi417 – 423Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WU7X-ray2.40A/B1-426[»]
ProteinModelPortaliQ9HLX5
SMRiQ9HLX5
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HLX5

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiarCOG00404 Archaea
COG0124 LUCA
HOGENOMiHOG000018073
KOiK01892
OMAiCDFDFIG
OrthoDBiPOG093Z03IG

Family and domain databases

CDDicd00859 HisRS_anticodon, 1 hit
Gene3Di3.40.50.800, 1 hit
HAMAPiMF_00127 His_tRNA_synth, 1 hit
InterProiView protein in InterPro
IPR006195 aa-tRNA-synth_II
IPR004154 Anticodon-bd
IPR036621 Anticodon-bd_dom_sf
IPR015807 His-tRNA-ligase
IPR004516 HisRS/HisZ
IPR033656 HisRS_anticodon
PANTHERiPTHR43707 PTHR43707, 1 hit
PfamiView protein in Pfam
PF03129 HGTP_anticodon, 1 hit
PIRSFiPIRSF001549 His-tRNA_synth, 1 hit
TIGRFAMsiTIGR00442 hisS, 1 hit
PROSITEiView protein in PROSITE
PS50862 AA_TRNA_LIGASE_II, 1 hit

Sequencei

Sequence statusi: Complete.

Q9HLX5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYRLQIEKIR GFRDFYPEDM DVEKFIFKTA EEAAEAFGFR RIDFPSLEYL
60 70 80 90 100
DLYRIKSGEE LLQQTYSFVD KGGREVTLIP EATPSTVRMV TSRKDLQRPL
110 120 130 140 150
RWYSFPKVWR YEEPQAGRYR EHYQFNADIF GSDSPEADAE VIALASSILD
160 170 180 190 200
RLGLQDIYEI RINSRKIMEE IIGGMTSSDP FSVFSIIDRY HKISREEFVD
210 220 230 240 250
QLRSAGIGED GVSMIADLCS GTRGIDEMAR ITGKSSEEIA RMAAVEDLLA
260 270 280 290 300
SYGVKNVRYD FSIVRGLSYY TGIVFEAYDR SGQFRAILGG GRYDNLASLM
310 320 330 340 350
SGESVPAVGF GMGDAVISLL LKRENVQIPR EKKSVYICRV GKINSSIMNE
360 370 380 390 400
YSRKLRERGM NVTVEIMERG LSAQLKYASA IGADFAVIFG ERDLERGVVT
410 420
IRNMYTGSQE NVGLDSVVEH LISQAT
Length:426
Mass (Da):48,229
Last modified:March 1, 2001 - v1
Checksum:i45610EC7EE055B96
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL445063 Genomic DNA Translation: CAC11247.1
RefSeqiWP_010900526.1, NC_002578.1

Genome annotation databases

EnsemblBacteriaiCAC11247; CAC11247; CAC11247
GeneIDi1455755
KEGGitac:Ta0099

Similar proteinsi

Entry informationi

Entry nameiSYH_THEAC
AccessioniPrimary (citable) accession number: Q9HLX5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: March 1, 2001
Last modified: May 23, 2018
This is version 107 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health