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Protein

Aspartate--tRNA(Asp) ligase

Gene

aspS

Organism
Thermus thermophilus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei177 – 1771Aspartate
Binding sitei223 – 2231Aspartate
Binding sitei232 – 2321ATP
Binding sitei442 – 4421Aspartate
Binding sitei476 – 4761ATP
Binding sitei483 – 4831Aspartate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi223 – 2253ATP
Nucleotide bindingi528 – 5314ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.1.1.12. 2305.
SABIO-RKP36419.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate--tRNA(Asp) ligase (EC:6.1.1.12)
Alternative name(s):
Aspartyl-tRNA synthetase
Short name:
AspRS
Discriminating aspartyl-tRNA synthetase
Short name:
D-AspRS
Gene namesi
Name:aspS
OrganismiThermus thermophilus
Taxonomic identifieri274 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 580580Aspartate--tRNA(Asp) ligasePRO_0000110971Add
BLAST

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi262724.TTC0359.

Structurei

Secondary structure

1
580
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 93Combined sources
Helixi12 – 143Combined sources
Beta strandi18 – 3013Combined sources
Beta strandi35 – 417Combined sources
Beta strandi44 – 507Combined sources
Beta strandi52 – 543Combined sources
Helixi57 – 604Combined sources
Beta strandi68 – 7710Combined sources
Turni86 – 894Combined sources
Beta strandi90 – 10112Combined sources
Helixi113 – 1153Combined sources
Helixi124 – 1296Combined sources
Helixi131 – 1344Combined sources
Helixi138 – 16023Combined sources
Beta strandi170 – 1723Combined sources
Beta strandi176 – 1794Combined sources
Beta strandi183 – 1853Combined sources
Beta strandi192 – 1954Combined sources
Helixi201 – 2099Combined sources
Beta strandi213 – 22210Combined sources
Beta strandi233 – 24412Combined sources
Helixi247 – 26519Combined sources
Beta strandi276 – 2783Combined sources
Helixi279 – 2868Combined sources
Beta strandi287 – 2904Combined sources
Helixi303 – 3064Combined sources
Beta strandi307 – 3093Combined sources
Helixi313 – 3164Combined sources
Beta strandi317 – 32711Combined sources
Helixi331 – 34313Combined sources
Beta strandi350 – 3556Combined sources
Beta strandi358 – 3614Combined sources
Helixi364 – 3674Combined sources
Helixi368 – 3703Combined sources
Helixi371 – 3788Combined sources
Beta strandi385 – 3928Combined sources
Helixi393 – 41018Combined sources
Beta strandi420 – 4245Combined sources
Beta strandi427 – 4293Combined sources
Turni433 – 4353Combined sources
Beta strandi440 – 4423Combined sources
Turni451 – 4544Combined sources
Helixi455 – 4584Combined sources
Helixi460 – 4623Combined sources
Beta strandi464 – 4729Combined sources
Beta strandi475 – 4839Combined sources
Helixi487 – 49711Combined sources
Turni501 – 5033Combined sources
Helixi504 – 5074Combined sources
Helixi509 – 5146Combined sources
Beta strandi522 – 5287Combined sources
Helixi529 – 5379Combined sources
Helixi542 – 5454Combined sources
Beta strandi546 – 5483Combined sources
Turni557 – 5604Combined sources
Beta strandi561 – 5644Combined sources
Helixi567 – 5726Combined sources
Beta strandi575 – 5773Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EFWX-ray3.00A/B1-580[»]
1G51X-ray2.40A/B1-580[»]
1L0WX-ray2.01A/B1-580[»]
ProteinModelPortaliP36419.
SMRiP36419. Positions 1-580.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36419.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni201 – 2044Aspartate

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C9M. Bacteria.
COG0173. LUCA.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.30.1360.30. 1 hit.
HAMAPiMF_00044. Asp_tRNA_synth.
InterProiIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004524. Asp-tRNA-ligase_bac/mit.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR004115. GAD-like.
IPR029351. GAD_dom.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PANTHERiPTHR22594. PTHR22594. 2 hits.
PTHR22594:SF5. PTHR22594:SF5. 2 hits.
PfamiPF02938. GAD. 1 hit.
PF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSiPR01042. TRNASYNTHASP.
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF55261. SSF55261. 1 hit.
TIGRFAMsiTIGR00459. aspS_bact. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P36419-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRTHYAGSL RETHVGEEVV LEGWVNRRRD LGGLIFLDLR DREGLVQLVA
60 70 80 90 100
HPASPAYATA ERVRPEWVVR AKGLVRLRPE PNPRLATGRV EVELSALEVL
110 120 130 140 150
AEAKTPPFPV DAGWRGEEEK EASEELRLKY RYLDLRRRRM QENLRLRHRV
160 170 180 190 200
IKAIWDFLDR EGFVQVETPF LTKSTPEGAR DFLVPYRHEP GLFYALPQSP
210 220 230 240 250
QLFKQMLMVA GLDRYFQIAR CFRDEDLRAD RQPDFTQLDL EMSFVEVEDV
260 270 280 290 300
LELNERLMAH VFREALGVEL PLPFPRLSYE EAMERYGSDK PDLRFGLELK
310 320 330 340 350
EVGPLFRQSG FRVFQEAESV KALALPKALS RKEVAELEEV AKRHKAQGLA
360 370 380 390 400
WARVEEGGFS GGVAKFLEPV REALLQATEA RPGDTLLFVA GPRKVAATAL
410 420 430 440 450
GAVRLRAADL LGLKREGFRF LWVVDFPLLE WDEEEEAWTY MHHPFTSPHP
460 470 480 490 500
EDLPLLEKDP GRVRALAYDL VLNGVEVGGG SIRIHDPRLQ ARVFRLLGIG
510 520 530 540 550
EEEQREKFGF FLEALEYGAP PHGGIAWGLD RLLALMTGSP SIREVIAFPK
560 570 580
NKEGKDPLTG APSPVPEEQL RELGLMVVRP
Length:580
Mass (Da):66,030
Last modified:June 1, 1994 - v1
Checksum:i510C79B25CF95D4E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70943 Genomic DNA. Translation: CAA50282.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70943 Genomic DNA. Translation: CAA50282.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EFWX-ray3.00A/B1-580[»]
1G51X-ray2.40A/B1-580[»]
1L0WX-ray2.01A/B1-580[»]
ProteinModelPortaliP36419.
SMRiP36419. Positions 1-580.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi262724.TTC0359.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105C9M. Bacteria.
COG0173. LUCA.

Enzyme and pathway databases

BRENDAi6.1.1.12. 2305.
SABIO-RKP36419.

Miscellaneous databases

EvolutionaryTraceiP36419.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.30.1360.30. 1 hit.
HAMAPiMF_00044. Asp_tRNA_synth.
InterProiIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004524. Asp-tRNA-ligase_bac/mit.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR004115. GAD-like.
IPR029351. GAD_dom.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PANTHERiPTHR22594. PTHR22594. 2 hits.
PTHR22594:SF5. PTHR22594:SF5. 2 hits.
PfamiPF02938. GAD. 1 hit.
PF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSiPR01042. TRNASYNTHASP.
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF55261. SSF55261. 1 hit.
TIGRFAMsiTIGR00459. aspS_bact. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Sequence, overproduction and crystallization of aspartyl-tRNA synthetase from Thermus thermophilus. Implications for the structure of prokaryotic aspartyl-tRNA synthetases."
    Poterszman A., Plateau P., Moras D., Blanquet S., Mazuric M.-H., Kreutzer R., Kern D.
    FEBS Lett. 325:183-186(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: VK1.
  2. "Crystal structure of a prokaryotic aspartyl tRNA-synthetase."
    Delarue M., Poterszman A., Nikonov S., Garber M., Moras D., Thierry J.-C.
    EMBO J. 13:3219-3229(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  3. "Synthesis and recognition of aspartyl-adenylate by Thermus thermophilus aspartyl-tRNA synthetase."
    Poterszman A., Delarue M., Thierry J.C., Moras D.
    J. Mol. Biol. 244:158-167(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH AMP AND ASPARTYL-AMP.
  4. "An intermediate step in the recognition of tRNA(Asp) by aspartyl-tRNA synthetase."
    Briand C., Poterszman A., Eiler S., Webster G., Thierry J.-C., Moras D.
    J. Mol. Biol. 299:1051-1060(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH TRNA(ASP).
  5. "Comparative analysis of space-grown and earth-grown crystals of an aminoacyl-tRNA synthetase: space-grown crystals are more useful for structural determination."
    Ng J.D., Sauter C., Lorber B., Kirkland N., Arnez J., Giege R.
    Acta Crystallogr. D 58:645-652(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS).

Entry informationi

Entry nameiSYD_THETH
AccessioniPrimary (citable) accession number: P36419
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: December 9, 2015
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.