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Protein

Aspartate--tRNA(Asp) ligase

Gene

aspS

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).UniRule annotation

Catalytic activityi

ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp).UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 3 Mg2+ cations per subunit. The strongest magnesium site (Mg1) is bound to the beta- and gamma-phosphates of ATP and four water molecules complete its coordination sphere.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei85Important for tRNA discriminationUniRule annotation1
Binding sitei170AspartateUniRule annotation1
Binding sitei214AspartateUniRule annotation1
Metal bindingi361Magnesium 2UniRule annotation1
Metal bindingi361Magnesium 3UniRule annotation1
Binding sitei361ATPUniRule annotation1
Metal bindingi364Magnesium 2UniRule annotation1
Binding sitei364AspartateUniRule annotation1
Binding sitei368AspartateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi214 – 216ATPUniRule annotation3
Nucleotide bindingi222 – 224ATPUniRule annotation3
Nucleotide bindingi409 – 412ATPUniRule annotation4

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate--tRNA(Asp) ligaseUniRule annotation (EC:6.1.1.12UniRule annotation)
Alternative name(s):
Aspartyl-tRNA synthetaseUniRule annotation
Short name:
AspRSUniRule annotation
Discriminating aspartyl-tRNA synthetaseUniRule annotation
Short name:
D-AspRSUniRule annotation
Gene namesi
Name:aspSUniRule annotation
Ordered Locus Names:PH1020
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001110041 – 438Aspartate--tRNA(Asp) ligaseAdd BLAST438

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

IntActiO58776. 1 interactor.
MINTiMINT-1501366.
STRINGi70601.PH1020.

Structurei

3D structure databases

ProteinModelPortaliO58776.
SMRiO58776.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni192 – 195AspartateUniRule annotation4

Sequence similaritiesi

Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiarCOG00406. Archaea.
COG0017. LUCA.
HOGENOMiHOG000226032.
KOiK01876.
OMAiWVHEIRD.
OrthoDBiPOG093Z02FK.

Family and domain databases

HAMAPiMF_02075. Asp_tRNA_synth_type2. 1 hit.
InterProiView protein in InterPro
IPR004364. aa-tRNA-synt_II.
IPR006195. aa-tRNA-synth_II.
IPR004523. Asp-tRNA_synthase_2.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
PfamiView protein in Pfam
PF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
PRINTSiPR01042. TRNASYNTHASP.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00458. aspS_nondisc. 1 hit.
PROSITEiView protein in PROSITE
PS50862. AA_TRNA_LIGASE_II. 1 hit.

Sequencei

Sequence statusi: Complete.

O58776-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRTHYSNEI TEELNGKRVK VAGWVQEVKD LGGIKFIWIR DREGIVQVTA
60 70 80 90 100
PKKKVSQEIF KLIPKLNSED VIVVEGIVNF TPKAKLGFEV IPEKLEVISR
110 120 130 140 150
AKTPLPLDPT GKVKAELDTR LDNRFMDLRN PKVMAIFKIR SSVFRAVREF
160 170 180 190 200
FYSEGFIEIH TPKIIATATE GGTELFPLKY FERDAFLAQS PQLYKQMMMA
210 220 230 240 250
TGLDKVFEIA PIFRAEEHNT TRHLNEAWSI DAEMAFIENE GEVMDLLERL
260 270 280 290 300
ISYVINYVRE HNEKELKTLE FELNEPKRPF PRITYDKALE ILSDLGKEIP
310 320 330 340 350
WGEDIDTEGE KLLGKYMAEN EGADLYFIYR YPSEAKPFYI MKYDEKPEVC
360 370 380 390 400
RAFDLEYRGV EISSGGQREH RHDVLLEQIK EKGLNPKSFE FYLKAFEYGM
410 420 430
PPHGGFGLGA ERLIMRMLDI GNIREVILFP RDRRRLVP
Length:438
Mass (Da):50,869
Last modified:August 1, 1998 - v1
Checksum:i5B62A7B281A3B4E9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30117.1.
PIRiG71094.
RefSeqiWP_010885107.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA30117; BAA30117; BAA30117.
GeneIDi1443342.
KEGGipho:PH1020.

Similar proteinsi

Entry informationi

Entry nameiSYD_PYRHO
AccessioniPrimary (citable) accession number: O58776
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: August 30, 2017
This is version 124 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

Complete proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families