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Reviewed, UniProtKB/Swiss-Prot A1W7D0 (SYA_ACISJ)

Last modified November 3, 2009. Version 27. 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:
    Alanyl-tRNA synthetase
    EC=6.1.1.7
Alternative name(s):
    Alanine--tRNA ligase
      Short name=AlaRS
Gene names
Name: alaS
Ordered Locus Names: Ajs_1979
OrganismAcidovorax sp. (strain JS42) [Complete proteome] [HAMAP]
Taxonomic identifier232721 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length874 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Cytoplasm By similarity.

Domain

The C-terminal C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs By similarity.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 874874Alanyl-tRNA synthetase HAMAP MF_00036
PRO_0000347472

Regions

Zinc finger180 – 19314C2H2-type HAMAP MF_00036

Sequences

Sequence LengthMass (Da)Tools
A1W7D0-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: E37B8D88D7301B45

FASTA87494,392
        10         20         30         40         50         60 
MSTPTFSVAD IRKTFLDFFA AKGHTVVASS PLVPGNDPTL MFTNSGMVQF KDVFLGTDKR 

        70         80         90        100        110        120 
PYVRATSVQT CLRAGGKHND LENVGYTARH HTFFEMLGNW SFGDYFKRES LKWAWELLTE 

       130        140        150        160        170        180 
VYKLPPERLL ATVYAEDDEA YDIWTKEIGL PPERVIRIGD NKGGRYKSDN FWMMADTGPC 

       190        200        210        220        230        240 
GPCSEIFYDH GEHIAGGPPG SPDEDGDRFI EIWNNVFMQF DMDEQGNVKP LPAPCVDTGM 

       250        260        270        280        290        300 
GLERLAAILQ HVHSNYEIDL FDALIKAAAR ETGTSDLTNP SLKVIADHIR ATAFLVADGV 

       310        320        330        340        350        360 
IPSNEGRGYV QRRIVRRAIR HGYKLGRKTP FFHKLVQDLV QQMGDAYPKI REQQARITDV 

       370        380        390        400        410        420 
LRVEEERFFE TLAHGMEILD SALAGGAKTL PGDVAFKLHD TYGFPLDLTN DVCRERGVNV 

       430        440        450        460        470        480 
DEAGFATAME HQKSTARAAG KFKMDRALEY TGAANQFTGY EQLAESAKIV ALYVDGTSTA 

       490        500        510        520        530        540 
ALHAGQSGVV VLDRTPFYAE SGGQVGDQGT IGAGSACFTV ADTQKIKADV YGHHGTLEAG 

       550        560        570        580        590        600 
TLNVGDTVQA QVDLQLRAAT MRNHSVTHLM HKALREVLGD HVQQKGSLVN AERTRFDFAH 

       610        620        630        640        650        660 
NAPLTAAQIR EIERLVNAEV LANTDTNARL MDIESAQKTG AMMLFGEKYG ETVRVLDIGT 

       670        680        690        700        710        720 
SRELCGGTHV RRTGDIGLFK VVAEGGVAAG VRRIEAVTGE NALAYLQSLE STVDQAAAAL 

       730        740        750        760        770        780 
KAPPAELTAR IGGALDQIKT LEKELAALKG KLASSQGDEL AGQAVDVKGI KVLAARLEGA 

       790        800        810        820        830        840 
DAKTLRETMD KLKDKLKTAA IVLAAVDGDK VQLAAGVTAD SIGRVKAGDL VNFVAAQVGG 

       850        860        870 
KGGGKPDMAM AGGTNAAALP QALAAVQGWV GERI 

« Hide

References

[1]"Complete sequence of chromosome 1 of Acidovorax sp. JS42."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000539 Genomic DNA. Translation: ABM42155.1.
RefSeqYP_986231.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA1W7D0.

Genome annotation databases

GeneID4674560.
GenomeReviewsGene locus Ajs_1979 in contig CP000539_GR.
KEGGajs:Ajs_1979.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMATLMFTNS.

Family and domain databases

HAMAPMF_00036.
[Tree]
InterProIPR002318. Ala-tRNA-synth_IIc.
IPR018165. Ala-tRNA-synth_IIc_cons-reg.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR003156. Pesterase_DHHA1.
IPR012947. tRNA_SAD.
[Graphical view]
PfamPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR00980. TRNASYNTHALA.
TIGRFAMsTIGR00344. alaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_ACISJ
AccessionPrimary (citable) accession number: A1W7D0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: February 6, 2007
Last modified: November 3, 2009
This is version 27 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