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Q64TQ1 (SYD_BACFR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. 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:BF2379
OrganismBacteroides fragilis (strain YCH46) [Complete proteome] [HAMAP]
Taxonomic identifier295405 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length585 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 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 – 585585Aspartate--tRNA ligase HAMAP MF_00044_B
PRO_0000110824

Sequences

Sequence LengthMass (Da)Tools
Q64TQ1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 49E0B663CEE58369

FASTA58566,169
        10         20         30         40         50         60 
MFRTHTCGEL RISDVNKQVK LSGWVQRSRK MGGMTFVDLR DRYGITQLVF NEEIDAELCE 

        70         80         90        100        110        120 
RANKLGREFV IQIVGTVNER FSKNSHIPTG DIEIIVSELN ILNSAITPPF TIEDNTDGGD 

       130        140        150        160        170        180 
DIRMKYRYLD LRRSAVRSNL ELRHKMTIEV RSYLDKLGFL EVETPVLIGS TPEGARDFVV 

       190        200        210        220        230        240 
PSRMNPGQFY ALPQSPQTLK QLLMVSGFDR YFQIAKCFRD EDLRADRQPE FTQIDCEMSF 

       250        260        270        280        290        300 
VEQEDVITTF EGMAKHLFKV IRNIELTGPF PRMPWSEAMR LYGSDKPDIR FGMQFVELMD 

       310        320        330        340        350        360 
ILKGHGFSVF DNATYIGGIC AEGAAGYTRK QLDALTEFVK KPQIGAKGMV YARIEADGTV 

       370        380        390        400        410        420 
KSSVDKFYIQ EVLQQLKEAF GAKPGDLILI LSGDDAMKTR KQLCELRLEM GNQLGLRDKN 

       430        440        450        460        470        480 
TFACLWVVDF PLFEWSEEEG RLMAMHHPFT SPKPEDIHLL DTNPAAVRAN AYDMVINGVE 

       490        500        510        520        530        540 
VGGGSIRIHD SQLQNKMFEL LGFTPERAQE QFGFLMNAFK FGAPPHGGLA YGLDRWVSLF 

       550        560        570        580 
AGLDSIRDCI AFPKNNSGRD VMLDAPAALD PSQLEELNLI VDIKE 

« Hide

References

[1]"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation."
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004) [PubMed: 15466707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YCH46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006841 Genomic DNA. Translation: BAD49128.1.
RefSeqYP_099662.1. NC_006347.1.

3D structure databases

ProteinModelPortalQ64TQ1.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3083937.
GenomeReviewsGene locus BF2379 in contig AP006841_GR.
KEGGbfr:BF2379.
NMPDRfig|295405.3.peg.2223.
PATRIC21050383. VBIBacFra17906_2298.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG396032.
OMAAFPKTQQ.
ProtClustDBPRK00476.

Enzyme and pathway databases

BioCycBFRA295405:BF2379-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_BACFR
AccessionPrimary (citable) accession number: Q64TQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 56 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