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Q1LT63 (SYN_BAUCH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Asparagine--tRNA ligase
EC=6.1.1.22
Alternative name(s):
Asparaginyl-tRNA synthetase
Short name=AsnRS
Gene names
Name:asnS
Ordered Locus Names:BCI_0408
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia

Protein attributes

Sequence length467 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn). HAMAP MF_00534

Subunit structure

Homodimer By similarity. HAMAP MF_00534

Subcellular location

Cytoplasm HAMAP MF_00534.

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 processasparaginyl-tRNA aminoacylation

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

asparagine-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 – 467467Asparagine--tRNA ligase HAMAP MF_00534
PRO_1000051380

Sequences

Sequence LengthMass (Da)Tools
Q1LT63 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 79F9BDE893AFFDF6

FASTA46753,150
        10         20         30         40         50         60 
MIILPIAKIL QGIILAADHE VIVQGWVRTR RDSKAGISFL SIYDGSCLDS LQVIINHDLP 

        70         80         90        100        110        120 
NYKSDVLHLT TGCSVVITGS IVTSIGVGQH FEIQAKNIKV LGWVKNPETY PITAKKHSLE 

       130        140        150        160        170        180 
FLREVAHLRP RTNIIGAVTR VRHTLAQAIH RFMHIEGFFW VSTPLITTFN CEGAGEMFRV 

       190        200        210        220        230        240 
STLDLENLPY TSKGKINYEK DFFGKEAFLT VSGQLNGESY ACALSKIYTF GPTFRAENSN 

       250        260        270        280        290        300 
TSRHLAEFWM VEPEVAFANL TDIAILAEKM LKYIFNAILI ERVDDINFFA EQINKNIIKR 

       310        320        330        340        350        360 
LEQFISSNFA QIDYTEAIDI LQNCKQKFDH TVFWGMDLFA EHERYLADKH FQAPVVVTNY 

       370        380        390        400        410        420 
PKDIKAFYMR INDDGKTVAA MDVLAPGIGE IIGGSQREER LAKLDQRLAD RGLNIEDYWW 

       430        440        450        460 
YRDLRSYGTV PHSGFGLGLE RLMIYITGMH NIRDVIPFPR NPRQASF

« Hide

References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000238 Genomic DNA. Translation: ABF13990.1.
RefSeqYP_588851.1. NC_007984.1.

3D structure databases

ProteinModelPortalQ1LT63.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1LT63.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4056737.
GenomeReviewsGene locus BCI_0408 in contig CP000238_GR.
KEGGbci:BCI_0408.
PATRIC21074323. VBIBauCic75062_0390.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0017.
HOGENOMHBG745843.
OMAAIHRFFH.
PhylomeDBQ1LT63.
ProtClustDBPRK03932.

Enzyme and pathway databases

BioCycBCIC186490:BCI_0408-MONOMER.

Family and domain databases

HAMAPMF_00534. Asn_tRNA_synth.
[Tree]
InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004522. Asn-tRNA-synth_IIb.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR004365. NA-bd_OB_tRNA-helicase.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KOK01893.
PANTHERPTHR22594. aa-tRNA-synt_II. 1 hit.
PTHR22594:SF6. PTHR22594:SF6. 1 hit.
PfamPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
PRINTSPR01042. TRNASYNTHASP.
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
TIGRFAMsTIGR00457. AsnS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYN_BAUCH
AccessionPrimary (citable) accession number: Q1LT63
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 30, 2006
Last modified: January 25, 2012
This is version 47 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

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