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Protein

Aspartate--tRNA(Asp) ligase

Gene

aspS

Organism
Thermus thermophilus
Status
Reviewed-Annotation score: Annotation score: 3 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).UniRule annotation

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei177AspartateUniRule annotation1
Binding sitei223AspartateUniRule annotation1
Binding sitei232ATPUniRule annotation1
Binding sitei442AspartateUniRule annotation1
Binding sitei476ATPUniRule annotation1
Binding sitei483AspartateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi223 – 225ATPUniRule annotation3
Nucleotide bindingi528 – 531ATPUniRule annotation4

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

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001109711 – 580Aspartate--tRNA(Asp) ligaseAdd BLAST580

Proteomic databases

PRIDEiP36419.

Interactioni

Subunit structurei

Homodimer.UniRule annotation2 Publications

Protein-protein interaction databases

STRINGi262724.TTC0359.

Structurei

Secondary structure

1580
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 9Combined sources3
Helixi12 – 14Combined sources3
Beta strandi18 – 30Combined sources13
Beta strandi35 – 41Combined sources7
Beta strandi44 – 50Combined sources7
Beta strandi52 – 54Combined sources3
Helixi57 – 60Combined sources4
Beta strandi68 – 77Combined sources10
Turni86 – 89Combined sources4
Beta strandi90 – 101Combined sources12
Helixi113 – 115Combined sources3
Helixi124 – 129Combined sources6
Helixi131 – 134Combined sources4
Helixi138 – 160Combined sources23
Beta strandi170 – 172Combined sources3
Beta strandi176 – 179Combined sources4
Beta strandi183 – 185Combined sources3
Beta strandi192 – 195Combined sources4
Helixi201 – 209Combined sources9
Beta strandi213 – 222Combined sources10
Beta strandi233 – 244Combined sources12
Helixi247 – 265Combined sources19
Beta strandi276 – 278Combined sources3
Helixi279 – 286Combined sources8
Beta strandi287 – 290Combined sources4
Helixi303 – 306Combined sources4
Beta strandi307 – 309Combined sources3
Helixi313 – 316Combined sources4
Beta strandi317 – 327Combined sources11
Helixi331 – 343Combined sources13
Beta strandi350 – 355Combined sources6
Beta strandi358 – 361Combined sources4
Helixi364 – 367Combined sources4
Helixi368 – 370Combined sources3
Helixi371 – 378Combined sources8
Beta strandi385 – 392Combined sources8
Helixi393 – 410Combined sources18
Beta strandi420 – 424Combined sources5
Beta strandi427 – 429Combined sources3
Turni433 – 435Combined sources3
Beta strandi440 – 442Combined sources3
Turni451 – 454Combined sources4
Helixi455 – 458Combined sources4
Helixi460 – 462Combined sources3
Beta strandi464 – 472Combined sources9
Beta strandi475 – 483Combined sources9
Helixi487 – 497Combined sources11
Turni501 – 503Combined sources3
Helixi504 – 507Combined sources4
Helixi509 – 514Combined sources6
Beta strandi522 – 528Combined sources7
Helixi529 – 537Combined sources9
Helixi542 – 545Combined sources4
Beta strandi546 – 548Combined sources3
Turni557 – 560Combined sources4
Beta strandi561 – 564Combined sources4
Helixi567 – 572Combined sources6
Beta strandi575 – 577Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP36419.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni201 – 204AspartateUniRule annotation4

Sequence similaritiesi

Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C9M. Bacteria.
COG0173. LUCA.

Family and domain databases

Gene3Di3.30.1360.30. 1 hit.
HAMAPiMF_00044. Asp_tRNA_synth_type1. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EFWX-ray3.00A/B1-580[»]
1G51X-ray2.40A/B1-580[»]
1L0WX-ray2.01A/B1-580[»]
ProteinModelPortaliP36419.
SMRiP36419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi262724.TTC0359.

Proteomic databases

PRIDEiP36419.

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

Gene3Di3.30.1360.30. 1 hit.
HAMAPiMF_00044. Asp_tRNA_synth_type1. 1 hit.
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...

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: November 30, 2016
This is version 122 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.