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B4S8V2 (SYD_PROA2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. 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:Paes_1469
OrganismProsthecochloris aestuarii (strain DSM 271 / SK 413) [Complete proteome] [HAMAP]
Taxonomic identifier290512 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeProsthecochloris

Protein attributes

Sequence length608 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 – 608608Aspartate--tRNA ligase HAMAP MF_00044_B
PRO_1000091026

Sequences

Sequence LengthMass (Da)Tools
B4S8V2 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 15834822BDA1DE60

FASTA60869,789
        10         20         30         40         50         60 
MSLAPGTETD LQNRFRSHFC GRLNTEYENK QVRLAGWIHR KRDHGGLIFI DLRDHTGIAQ 

        70         80         90        100        110        120 
LIIQPEKQEL FQKVERLHVE SVIAVQGTVV KRSEETLNSR IPSGAIEVLV DDVQVESHAV 

       130        140        150        160        170        180 
ALPFPVADEL QTSEELRLTY RFLDLRREKI HQNIVFRSQL ISKVRRYLED HGFMEIQTPI 

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

       250        260        270        280        290        300 
RSPGEFYQVD MEMAFIEQDD LFEILEGMLR YLTETMSTKR ITQFPFPRLS YRDVMNRFGS 

       310        320        330        340        350        360 
DKPDLRVPLE MQDVTELFVG SSFKVFASNT KEGSCIKAMV LKGRGTESRQ FYDKAEKRAR 

       370        380        390        400        410        420 
ELGAPGLAYV QYREEGPKGP IVKFLSEAEL SALQERLAIE TGDVVFFGAG KWEKTCKIMG 

       430        440        450        460        470        480 
GIREYFSDLF ELDRDELSFC WIVDFPLYEF DEKESRIDFS HNPFSMPQGE MDALDTMNPL 

       490        500        510        520        530        540 
DILAYQYDIV CNGIELSSGA IRNHRPDIMY RAFEIAGYSK EEVDKRFGHM IEAFKMGAPP 

       550        560        570        580        590        600 
HGGIAPGLDR LVMILRDEHN IREVIAFPMN QQAQDLMMSA PSDVSRLQLR ELHLKLDLPV 


ETAEQEPG 

« Hide

References

[1]"Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271."
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., Anderson I., Liu Z., Li T., Zhao F. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 271 / SK 413.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001108 Genomic DNA. Translation: ACF46489.1.
RefSeqYP_002016136.1. NC_011059.1.

3D structure databases

ProteinModelPortalB4S8V2.
ModBaseSearch...

Protein-protein interaction databases

STRINGB4S8V2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6460558.
GenomeReviewsGene locus Paes_1469 in contig CP001108_GR.
KEGGpaa:Paes_1469.
PATRIC23042778. VBIProAes37017_1558.

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_PROA2
AccessionPrimary (citable) accession number: B4S8V2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: January 25, 2012
This is version 28 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