Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot B0VAI3 (SYA_ACIBY)

Last modified November 3, 2009. Version 10. 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: ABAYE2595
OrganismAcinetobacter baumannii (strain AYE) [Complete proteome] [HAMAP]
Taxonomic identifier509173 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length878 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 – 878878Alanyl-tRNA synthetase HAMAP MF_00036
PRO_0000347475

Regions

Zinc finger177 – 19014C2H2-type HAMAP MF_00036

Sequences

Sequence LengthMass (Da)Tools
B0VAI3-1 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 48DC937CBAF0C6F6

FASTA87896,528
        10         20         30         40         50         60 
MTSAEIREAF LRYFETQGHT RVASSSLVPA NDPTLLFTNA GMNQFKDCFL GLEKRDYVRA 

        70         80         90        100        110        120 
TTSQKCVRAG GKHNDLDNVG YTARHHTFFE MLGNFSFGDY FKRDALKFAW EFLTSEQWLA 

       130        140        150        160        170        180 
LPKDKLYVTV YHTDDEAYDI WNKEIGLAPE RIIRIGDNKG EKYASDNFWA MGDTGPCGPC 

       190        200        210        220        230        240 
SEIFFDHGEH IWGGLPGSPE EDGDRFIEIW NNVFMQFNRT ADGVLHPLPA PSVDTGMGLE 

       250        260        270        280        290        300 
RISAVLQHVN SNYDIDLFQH LLKAAANIIG IEDEGQPSLR VVADHARSCC FLIADGVNPS 

       310        320        330        340        350        360 
NEGRGYVLRR IIRRAVRHGN KLGATGTFFY KMLQPLIEVM GQAYPELEAR REVIEATLIR 

       370        380        390        400        410        420 
EEEQFAKTLE QGLKLLEGEL AQLKDKTIPG ATVFKLYDTY GFPTDLTADI ARERGFIIDE 

       430        440        450        460        470        480 
AGFEVEMAAQ RQRARDAGKF AVDYNNIVKV EGETQFDGYT NTTGQGQIVA IYKDGVQVDE 

       490        500        510        520        530        540 
VSEGDEALIV LNQTPFYAES GGQIGDTGIF KNETGIFEVQ DTKKSGGAFV HQGIVTVGNL 

       550        560        570        580        590        600 
KTSQNVEAIV KADIREATAR NHSATHLLHA ALRQILGSHV QQKGSLVASD ILRFDFANDQ 

       610        620        630        640        650        660 
PVSFEQLQQV ERLVNAEIIA NTAVTTELLD IETAKAKGAM MLFGEKYGDE VRVLSMGSVI 

       670        680        690        700        710        720 
DEKNFSIELC GGIHVKRTGD IGLFKITSEG GVAAGVRRIE AVTGTKALEV VQKADHDIQH 

       730        740        750        760        770        780 
INSLLKAQKD QTVERVQANV ELVSALQKQI EQLNQKLANF QAADLIDQVQ TIAGRQTLIT 

       790        800        810        820        830        840 
TVQGVDAKAL RNLHDSVKSK LENAVIVLAG VEGDKVSLLA SVASQYTANL KAGDIIKHLA 

       850        860        870 
TELGGKGGGK PDLAQGGAPL NEKFGQVMAA LPAWLEQK 

« Hide

References

[1]"Comparative analysis of Acinetobacters: three genomes for three lifestyles."
Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., Weissenbach J., Cruveiller S.
PLoS ONE 3:E1805-E1805(2008) [PubMed: 18350144] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CU459141 Genomic DNA. Translation: CAM87432.1.
RefSeqYP_001714409.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6003180.
GenomeReviewsGene locus ABAYE2595 in contig CU459141_GR.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAGEFVIKL.

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_ACIBY
AccessionPrimary (citable) accession number: B0VAI3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: April 8, 2008
Last modified: November 3, 2009
This is version 10 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