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Q6MI59 (SYD_BDEBA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 60. 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:Bd3311
OrganismBdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100) [Complete proteome] [HAMAP]
Taxonomic identifier264462 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaBdellovibrionalesBdellovibrionaceaeBdellovibrio

Protein attributes

Sequence length642 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 – 642642Aspartate--tRNA ligase HAMAP MF_00044_B
PRO_0000110833

Sequences

Sequence LengthMass (Da)Tools
Q6MI59 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 273C93A64D23BA1F

FASTA64272,343
        10         20         30         40         50         60 
MPLVEGPLYR FCYGEYKNMV FDCNGTICKS GAHEQGRHMK FVKELKRTHY CGSLGVSQAG 

        70         80         90        100        110        120 
QKVVLMGWVD VRRDHGSLVF IDLRDREGIV QVVLDPNKAE TASSKNLRGE FVLAVEGVVR 

       130        140        150        160        170        180 
ARPDGMKNAK IKTGEVEVEA IRCEILNESA VPPFQVSDTN VNEMLRLKYR YLDLRSARLS 

       190        200        210        220        230        240 
SHLITRHKVA QLVRRFLSDN GFLEVETPIL YKSTPEGARD YLVPSRVNPG HFYALPQSPQ 

       250        260        270        280        290        300 
TLKQLLMISG YDRYFQIARC FRDEDLRADR QPEFSQIDME MSYIDQEDIM EMNEKLLRTI 

       310        320        330        340        350        360 
WKEIKGIDVG AIPRMTYQEA MDRYGIDKPD TRFGVEIKDL KSIVTGSGFK VFDDVLARGG 

       370        380        390        400        410        420 
IVRGIAAPKG GSYSRGQLDK LTDMAKRAGA KGLVWIKSEA DGTLSSSVSK FFSPEKLAEM 

       430        440        450        460        470        480 
FKACGGEAGD CALVVADDYD TACAALSTLR LHLGRELNLI DNSKYKFLWV VDFPLLEYSP 

       490        500        510        520        530        540 
DEKRWVARHH PFTSPKDEFA QDLVNNNEAA YGKMLAKAYD LVCNGYEMGG GSIRIYRNEI 

       550        560        570        580        590        600 
QQAMFRLLGM SEEETQHKFG FFLEALKYGT PPHGGIAWGM DRLVMLLCET DAIREVIAFP 

       610        620        630        640 
KTAKATDLMS DCPSEVNRDQ LAEVGVRLST LAEKHLEDLK KS 

« Hide

References

[1]"A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a genomic perspective."
Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C., Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E., Schuster S.C.
Science 303:689-692(2004) [PubMed: 14752164] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15356 / DSM 50701 / NCIB 9529 / HD100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX842655 Genomic DNA. Translation: CAE78121.1.
RefSeqNP_970062.1. NC_005363.1.

3D structure databases

ProteinModelPortalQ6MI59.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2736950.
GenomeReviewsGene locus Bd3311 in contig BX842601_GR.
KEGGbba:Bd3311.
NMPDRfig|264462.1.peg.3035.
PATRIC21080950. VBIBdeBac73187_3030.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG396032.
OMAAFPKTQQ.
PhylomeDBQ6MI59.

Enzyme and pathway databases

BioCycBBAC264462:BD3311-MONOMER.

Family and domain databases

HAMAPMF_00044_B. Asp_tRNA_synth_B. Divergent sequence.
[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_BDEBA
AccessionPrimary (citable) accession number: Q6MI59
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 60 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