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Reviewed, UniProtKB/Swiss-Prot B6YS49 (SYD_AZOPC)

Last modified September 22, 2009. Version 8. 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: CFPG_758
OrganismAzobacteroides pseudotrichonymphae genomovar. CFP2 [Complete proteome] [HAMAP]
Taxonomic identifier511995 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesCandidatus Azobacteroides

Protein attributes

Sequence length583 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 By similarity.

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 – 583583Aspartyl-tRNA synthetase HAMAP MF_00044
PRO_1000090958

Sequences

Sequence LengthMass (Da)Tools
B6YS49-1 [UniParc].

Last modified January 20, 2009. Version 1.
Checksum: A7B7DAD0E910005C

FASTA58367,026
        10         20         30         40         50         60 
MYRTNTCGEL RIVNENQEVI LCGWVQKSRR MSGIVFVDLR DRYGITQLIF NKKVNLALYN 

        70         80         90        100        110        120 
KALELGREWV IQIEGKVVKR FNKNSDIPTG DIEIIVSRLR TLNPSEVPPF TIEENTDGGD 

       130        140        150        160        170        180 
DLRMKYRYLD LRRTLIRSNL ELRHQMVFAI RNYLNSHEFM EVETPVLINS TPEGARDFIV 

       190        200        210        220        230        240 
PSRMNMGEFY SLPQSPQLFK QLLMIAGFDR YFQVVKCFRD EDLRTDRQPE FTQVDCEMSF 

       250        260        270        280        290        300 
VEQEDILSIF EGLTKHLFKT IKGLDISGFS RLSYADAIRF YGSDKPDIRF GMQLVEIKDI 

       310        320        330        340        350        360 
TIGRGFDVFD ESEYVGAICA EGCAFYTRKQ LDELTDFVKH PQIGAAGLIY VRYSFDGSLK 

       370        380        390        400        410        420 
SSVDKFYSTV DLQKWIDRVG AKQGDLVLIL YGEKRETQKQ LSRLRLEMGS RLGLRDKKQF 

       430        440        450        460        470        480 
GCLWVIDFPL FEYDNVLNRF FAKHHPFTSP KQEDVCLLET NPEFVRANAF DMVINGIEIG 

       490        500        510        520        530        540 
GGSIRIHNYE LQKKIFALLG FSESYTQSQF GFFVDAFKYG APPHGGIALG LDRFVATFAG 

       550        560        570        580 
LDSIRDCIAF PKNNSGRDTM VGAPSIISRE RLSELNLIVE GWQ 

« Hide

References

[1]"Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT protist cells in termite gut."
Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T., Sakaki Y., Toyoda A., Hattori M., Ohkuma M.
Science 322:1108-1109(2008) [PubMed: 19008447] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AP010656 Genomic DNA. Translation: BAG84021.1.
RefSeqYP_002309432.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID7039309.
GenomeReviewsGene locus CFPG_758 in contig AP010656_GR.
KEGGaps:CFPG_758.

Organism-specific databases

CMRSearch...

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_AZOPC
AccessionPrimary (citable) accession number: B6YS49
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 20, 2009
Last modified: September 22, 2009
This is version 8 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