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Q1QLI9 (SYD_NITHX) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aspartate--tRNA ligase

EC=6.1.1.12
Alternative name(s):
Aspartyl-tRNA synthetase
Short name=AspRS
Gene names
Name:aspS
Ordered Locus Names:Nham_2111
OrganismNitrobacter hamburgensis (strain X14 / DSM 10229) [Complete proteome] [HAMAP]
Taxonomic identifier323097 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter

Protein attributes

Sequence length590 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp). HAMAP MF_00044_B

Subunit structure

Homodimer By similarity. HAMAP MF_00044_B

Subcellular location

Cytoplasm By similarity HAMAP MF_00044_B.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processtRNA aminoacylation for protein translation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

aspartate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 590590Aspartate--tRNA ligase HAMAP MF_00044_B
PRO_1000006716

Sequences

Sequence LengthMass (Da)Tools
Q1QLI9 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: E70F0C0B8D2E9949

FASTA59066,735
        10         20         30         40         50         60 
MHRYRSHTCG ALRDSHIDQT VRLSGWCHRI RDHGGVLFID LRDHYGLTQC VADPDSPAFA 

        70         80         90        100        110        120 
QAEKLRSEWV VRIDGKARLR PAGTENPELP TGQIEIYINE IEVLGPADEL PLPVFGEQEY 

       130        140        150        160        170        180 
PEDIRLKYRF LDLRREKLHQ NIMTRGAIVD SMRKRMKEQG FFEFQTPILT ASSPEGARDF 

       190        200        210        220        230        240 
LVPSRIHPGK FYALPQAPQQ YKQLLMMSGF DRYFQIAPCF RDEDPRADRL PGEFYQLDLE 

       250        260        270        280        290        300 
MSFVEQDDVF AAVEPVVTGV FEEFAKGKPV TKNWPRIPFA ESLRKYGTDK PDLRNPLLMQ 

       310        320        330        340        350        360 
DVSQHFRGSG FKVFARMLED SKNQVWAIPG PGGGSRAFCD RMNSWAQGEG QPGLGYIMWR 

       370        380        390        400        410        420 
EGGEGAGPLA NNIGPERTEA IRQQLGLKAG DAAFFVAGDP AKFWKFAGLA RTKLGEELNV 

       430        440        450        460        470        480 
IDKDRFELAW IVDFPMYEYN EDEKKVDFSH NPFSMPQGGL DALNNQDPLT IKAFQYDITC 

       490        500        510        520        530        540 
NGYEIASGGI RNHRPEAMVK AFEIAGYGEN DVVERFGGMY RAFQYGAPPH GGMAAGVDRV 

       550        560        570        580        590 
VMLLCGTTNL REISLFPMNQ RAEDLLMGAP SDVTPKQLRE LHIRLNLPQD 

« Hide

References

[1]"Complete sequence of chromosome of Nitrobacter hamburgensis X14."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L., O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T., Gentry M.E., Bruce D., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: X14 / DSM 10229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000319 Genomic DNA. Translation: ABE62908.1.
RefSeqYP_577368.1. NC_007964.1.

3D structure databases

ProteinModelPortalQ1QLI9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1QLI9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4031941.
GenomeReviewsGene locus Nham_2111 in contig CP000319_GR.
KEGGnha:Nham_2111.
NMPDRfig|323097.3.peg.3233.
PATRIC22691960. VBINitHam61822_2997.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0173.
HOGENOMHBG396032.
OMAYQLDVEM.
PhylomeDBQ1QLI9.
ProtClustDBPRK00476.

Enzyme and pathway databases

BioCycNHAM323097:NHAM_2111-MONOMER.

Family and domain databases

HAMAPMF_00044_B. Asp_tRNA_synth_B.
[Tree]
InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004524. Asp-tRNA-synth_IIb_bac/mt.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR004115. GAD_dom.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR004365. NA-bd_OB_tRNA-helicase.
[Graphical view]
Gene3DG3DSA:3.30.1360.30. GAD_dom. 1 hit.
G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KOK01876.
PANTHERPTHR22594. aa-tRNA-synt_II. 1 hit.
PTHR22594:SF5. AspS_bac. 1 hit.
PfamPF02938. GAD. 1 hit.
PF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
PRINTSPR01042. TRNASYNTHASP.
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
SSF55261. SSF55261. 1 hit.
TIGRFAMsTIGR00459. AspS_bact. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYD_NITHX
AccessionPrimary (citable) accession number: Q1QLI9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 16, 2006
Last modified: January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families