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B3EDE5 (SYD_CHLL2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. 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:Clim_1519
OrganismChlorobium limicola (strain DSM 245 / NBRC 103803) [Complete proteome] [HAMAP]
Taxonomic identifier290315 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupChlorobium

Protein attributes

Sequence length605 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 By similarity 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 – 605605Aspartate--tRNA ligase HAMAP MF_00044_B
PRO_1000090975

Sequences

Sequence LengthMass (Da)Tools
B3EDE5 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: 9134C88D35928130

FASTA60569,203
        10         20         30         40         50         60 
MYRAEESMMP LENRFRTDYC GLLGVGSENR SVRLGGWVHR KRDHGGLIFI DLRDHTGVCQ 

        70         80         90        100        110        120 
LVIQPEQQAL FNAVEHLHAE SVICIEGTVV LRSSETVNTR LASGEIEVVV SSVIIESDAQ 

       130        140        150        160        170        180 
PLPFPVADEV PTSEELRLKY RFIDLRREKI HENIIFRSRL TAMVRRYLEE REFIEIQTPI 

       190        200        210        220        230        240 
LTSSSPEGAR DFLVPSRLHP GKFYALPQAP QQFKQLLMVS GFPRYFQIAP CFRDEDARAD 

       250        260        270        280        290        300 
RSPGEFYQID MEMAFIEQND LFEILEGMFK HLTENMSQKR ITQFPFPRIS YREVMNRFGS 

       310        320        330        340        350        360 
DKPDLRIPLE IQDVTSLFVN SSFKVFASNT KEGTCVKALV LKGRGGESRM FYDKAEKRAR 

       370        380        390        400        410        420 
ELGSAGLAYI QFREEGPKGP IVKFLGEAEM EVLKEQLGLE TGDVVFFGAG KWESTCKIMG 

       430        440        450        460        470        480 
GMRIYFADLF DLDKDELSFC WIVDFPMYEY NEEAKKIDFS HNPFSMPQGE MEALETMQPL 

       490        500        510        520        530        540 
DILAYQYDIV CNGIELSSGA IRNHRPDIMY RAFEIAGYTK EEVDSRFGHM IDAFKLGAPP 

       550        560        570        580        590        600 
HGGIAPGLDR MVMILRDEQN IREVIAFPMN QQAQDLMMSA PSEVMAQQLK ELHLKIDLPP 


VKEAK 

« Hide

References

[1]"Complete sequence of Chlorobium limicola DSM 245."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., Liu Z. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 245 / NBRC 103803.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001097 Genomic DNA. Translation: ACD90570.1.
RefSeqYP_001943549.1. NC_010803.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB3EDE5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6355776.
GenomeReviewsGene locus Clim_1519 in contig CP001097_GR.
KEGGcli:Clim_1519.
PATRIC21375175. VBIChlLim118737_1618.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG396032.
OMAYQLDVEM.
ProtClustDBPRK00476.

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_CHLL2
AccessionPrimary (citable) accession number: B3EDE5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 22, 2008
Last modified: January 25, 2012
This is version 27 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