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Reviewed, UniProtKB/Swiss-Prot Q8A9E3 (SYD_BACTN)

Last modified November 3, 2009. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Aspartyl-tRNA synthetase
    EC=6.1.1.12
Alternative name(s):
    Aspartate--tRNA ligase
      Short name=AspRS
Gene names
Name: aspS
Ordered Locus Names: BT_0872
OrganismBacteroides thetaiotaomicron [Complete proteome] [HAMAP]
Taxonomic identifier818 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length587 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp). HAMAP MF_00044

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm. HAMAP MF_00044

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 processaspartyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

aspartate-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 587587Aspartyl-tRNA synthetase HAMAP MF_00044
PRO_0000110830

Sequences

Sequence LengthMass (Da)Tools
Q8A9E3-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 09D82A4A57016A29

FASTA58766,563
        10         20         30         40         50         60 
MFRTHTCGEL RISDVNKQIT LSGWVQRSRK MGGMTFIDLR DRYGITQLVF NEEINAELCD 

        70         80         90        100        110        120 
RANKLGREFV IQITGTVNER FSKNANIPTG DIEIIVSELN VLNTAMTPPF TIEDNTDGGD 

       130        140        150        160        170        180 
DIRMKYRYLD LRRNAVRSNL ELRHKMTIEV RKYLDSLGFI EVETPVLIGS TPEGARDFVV 

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

       250        260        270        280        290        300 
VEQEDIISTF EGMAKHLFKT LRGVELTEPF QRMPWADAMK YYGSDKPDLR FGMKFVELMD 

       310        320        330        340        350        360 
IMKGHGFSVF DNAAYVGGIC AEGAATYTRK QLDALTEFVK KPQIGAKGMV YARVEADGTV 

       370        380        390        400        410        420 
KSSVDKFYTQ EVLQQMKEAF GAKPGDLILI LSGDDVMKTR KQLCELRLEM GSQLGLRDKN 

       430        440        450        460        470        480 
KFVCLWVIDF PMFEWSEEEG RLMAMHHPFT HPKEEDIPLL DTDPAAVRAD AYDMVVNGVE 

       490        500        510        520        530        540 
VGGGSIRIHD AQLQARMFEI LGFTPEKAQA QFGFLMNAFK YGAPPHGGLA YGLDRWVSLF 

       550        560        570        580 
AGLDSIRDCI AFPKNNSGRD VMLDAPSEID QTQLDELNLI VDIKENK 

« Hide

References

[1]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed: 12663928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

AE015928 Genomic DNA. Translation: AAO75979.1.
RefSeqNP_809785.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1073405.
GenomeReviewsGene locus BT_0872 in contig AE015928_GR.
KEGGbth:BT_0872.
NMPDRfig|226186.1.peg.872.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8A9E3.
OMAVDRRRDH.

Enzyme and pathway databases

BioCycBTHE226186:BT_0872-MON.
BRENDA6.1.1.12. 21018.

Family and domain databases

HAMAPMF_00044.
[Tree]
InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR002312. Asp-tRNA-synth_IIb.
IPR020564. Asp-tRNA-synth_IIb_bac-type.
IPR004524. Asp-tRNA-synth_IIb_bac/mt.
IPR018153. Asp-tRNA-synth_IIb_C_bac/mt.
IPR004115. GAD_dom.
IPR012340. NA-bd_OB-fold.
IPR004365. NA_bd_OB_tRNA-helicase.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
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.
TIGRFAMsTIGR00459. aspS_bact. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYD_BACTN
AccessionPrimary (citable) accession number: Q8A9E3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents