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Protein

Aspartate--tRNA(Asp/Asn) ligase

Gene

aspS

Organism
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).UniRule annotation

Catalytic activityi

ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx).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)LengthDescriptionGraphical viewFeature identifierActions
Sitei82 – 821Important for tRNA non-discriminationUniRule annotation
Binding sitei167 – 1671AspartateUniRule annotation
Binding sitei210 – 2101AspartateUniRule annotation
Metal bindingi352 – 3521Magnesium 2UniRule annotation
Metal bindingi352 – 3521Magnesium 3UniRule annotation
Binding sitei352 – 3521ATPUniRule annotation
Metal bindingi355 – 3551Magnesium 2UniRule annotation
Binding sitei355 – 3551AspartateUniRule annotation
Binding sitei359 – 3591AspartateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi210 – 2123ATPUniRule annotation
Nucleotide bindingi400 – 4034ATPUniRule annotation

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, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciSTOK273063:GJC7-229-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate--tRNA(Asp/Asn) ligaseUniRule annotation (EC:6.1.1.23UniRule annotation)
Alternative name(s):
Aspartyl-tRNA synthetaseUniRule annotation
Short name:
AspRSUniRule annotation
Non-discriminating aspartyl-tRNA synthetaseUniRule annotation
Short name:
ND-AspRSUniRule annotation
Gene namesi
Name:aspSUniRule annotation
Ordered Locus Names:STK_02050
OrganismiSulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Taxonomic identifieri273063 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
Proteomesi
  • UP000001015 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429Aspartate--tRNA(Asp/Asn) ligasePRO_0000111007Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi273063.ST0205.

Structurei

Secondary structure

1
429
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni7 – 93Combined sources
Helixi12 – 143Combined sources
Beta strandi18 – 3114Combined sources
Beta strandi34 – 418Combined sources
Beta strandi44 – 507Combined sources
Helixi57 – 604Combined sources
Beta strandi68 – 7710Combined sources
Beta strandi79 – 813Combined sources
Helixi82 – 843Combined sources
Beta strandi85 – 9612Combined sources
Beta strandi106 – 1083Combined sources
Helixi114 – 1196Combined sources
Helixi121 – 1255Combined sources
Helixi128 – 15023Combined sources
Beta strandi160 – 1645Combined sources
Beta strandi174 – 1774Combined sources
Beta strandi180 – 1845Combined sources
Helixi189 – 19911Combined sources
Beta strandi200 – 20910Combined sources
Beta strandi216 – 2183Combined sources
Beta strandi221 – 23111Combined sources
Helixi235 – 25622Combined sources
Helixi258 – 2647Combined sources
Beta strandi276 – 2794Combined sources
Helixi280 – 28910Combined sources
Helixi302 – 31211Combined sources
Beta strandi315 – 3206Combined sources
Helixi324 – 3263Combined sources
Beta strandi340 – 3489Combined sources
Beta strandi351 – 3599Combined sources
Helixi363 – 37210Combined sources
Helixi377 – 3804Combined sources
Helixi381 – 3844Combined sources
Helixi385 – 3884Combined sources
Beta strandi394 – 4007Combined sources
Helixi401 – 4099Combined sources
Helixi414 – 4163Combined sources
Beta strandi418 – 4203Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WYDX-ray2.30A/B1-429[»]
ProteinModelPortaliQ976I3.
SMRiQ976I3. Positions 1-429.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ976I3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni189 – 1924AspartateUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiarCOG00406. Archaea.
COG0017. LUCA.
HOGENOMiHOG000226032.
KOiK01876.
OMAiKPEICRA.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00044. Asp_tRNA_synth.
InterProiIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004523. Asp-tRNA_synthase_arc.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PANTHERiPTHR22594. PTHR22594. 1 hit.
PTHR22594:SF10. PTHR22594:SF10. 1 hit.
PfamiPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSiPR01042. TRNASYNTHASP.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00458. aspS_nondisc. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q976I3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYRSHFIADV TPEYDGKEVI WAGWVHLLRD LGGKKFIILR DKTGLGQVVV
60 70 80 90 100
DKNSSAFGIS QELTQESVIQ VRGIVKADKR APRGIELHAE EITLLSKAKA
110 120 130 140 150
PLPLDVSGKV KADIDTRLRE RVLDLRRQEM QAVIKIQSLA LKAFRETLYK
160 170 180 190 200
EGFIEIFTPK IIASATEGGA QLFPVIYFGK EAFLAQSPQL YKELMAGVVE
210 220 230 240 250
RVFEVAPAWR AEESDTPFHL AEFISMDVEM AFADYNDVMQ LLEKILHNIV
260 270 280 290 300
KTIKEEGKEE LKILNYEPPE VKIPIKRLKY TEAIEILRSK GYNIKFGDDI
310 320 330 340 350
GTPELRILNE ELKEDLYFIV DWPSDARPFY TKSKSENPEL SESFDLIYKF
360 370 380 390 400
LEIVSGSTRN HKREVLEEAL KKKGLKPESF EFFLKWFDYG MPPHAGFGMG
410 420
LARLMVMLTG IQSVKEIVPF PRDKKRLTP
Length:429
Mass (Da):49,074
Last modified:December 1, 2001 - v1
Checksum:i5BABA8F4D9437D69
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000023 Genomic DNA. Translation: BAK54191.1.
RefSeqiWP_010978146.1. NC_003106.2.

Genome annotation databases

EnsemblBacteriaiBAK54191; BAK54191; STK_02050.
GeneIDi1458094.
KEGGisto:STK_02050.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000023 Genomic DNA. Translation: BAK54191.1.
RefSeqiWP_010978146.1. NC_003106.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WYDX-ray2.30A/B1-429[»]
ProteinModelPortaliQ976I3.
SMRiQ976I3. Positions 1-429.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273063.ST0205.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAK54191; BAK54191; STK_02050.
GeneIDi1458094.
KEGGisto:STK_02050.

Phylogenomic databases

eggNOGiarCOG00406. Archaea.
COG0017. LUCA.
HOGENOMiHOG000226032.
KOiK01876.
OMAiKPEICRA.

Enzyme and pathway databases

BioCyciSTOK273063:GJC7-229-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ976I3.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00044. Asp_tRNA_synth.
InterProiIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004523. Asp-tRNA_synthase_arc.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PANTHERiPTHR22594. PTHR22594. 1 hit.
PTHR22594:SF10. PTHR22594:SF10. 1 hit.
PfamiPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSiPR01042. TRNASYNTHASP.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00458. aspS_nondisc. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 16993 / JCM 10545 / NBRC 100140 / 7.

Entry informationi

Entry nameiSYDND_SULTO
AccessioniPrimary (citable) accession number: Q976I3
Secondary accession number(s): F9VMP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: December 1, 2001
Last modified: December 9, 2015
This is version 101 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, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.