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A1K991 (SYA_AZOSB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alanine--tRNA ligase

EC=6.1.1.7
Alternative name(s):
Alanyl-tRNA synthetase
Short name=AlaRS
Gene names
Name:alaS
Ordered Locus Names:azo2780
OrganismAzoarcus sp. (strain BH72) [Complete proteome] [HAMAP]
Taxonomic identifier62928 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAzoarcus

Protein attributes

Sequence length885 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain By similarity. HAMAP MF_00036_B

Catalytic activity

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036_B

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00036_B

Subcellular location

Cytoplasm By similarity HAMAP MF_00036_B.

Domain

Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the 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. HAMAP MF_00036_B

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
RNA-binding
Zinc
tRNA-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processalanyl-tRNA aminoacylation

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

alanine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 885885Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347495

Sites

Metal binding5751Zinc Potential
Metal binding5791Zinc Potential
Metal binding6761Zinc Potential
Metal binding6801Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
A1K991 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: A5615D9260C64B52

FASTA88595,745
        10         20         30         40         50         60 
MKSAEIRAKF LKFFESKGHQ IVASSSLVPH EDPTLLFTNA GMNQFKDVFL GFDKRPYSRA 

        70         80         90        100        110        120 
TTSQKCVRAG GKHNDLENVG YTARHHTFFE MLGNFSFGDY FKRDAITYAW ELLTEVFKLP 

       130        140        150        160        170        180 
KDKLWVTVYA EDDEAYDIWT KEVGVPAERV IRIGDNKGAR YASDNFWMMG DTGPCGPCTE 

       190        200        210        220        230        240 
IFYDHGPHIW GGPPGSPEED GDRYIEIWNN VFMQFNRDEQ GVMHPLPKPS VDTGMGLERI 

       250        260        270        280        290        300 
SAVLQGVHAN YEIDLFKSLI SSAMRAVGTA EALVERARDS MTNTISPSYK VLADHIRACS 

       310        320        330        340        350        360 
FLIADGVIPG NEGRGYVLRR IIRRAIRHGY KLGARAAFFH KMVPDLVAEM GEAYPELKAG 

       370        380        390        400        410        420 
ERRVADVLRQ EEERFFATIE NGMAIVEGEL AAMATAGNTV FNGDTAFKLH DTYGFPLDLT 

       430        440        450        460        470        480 
ADICREREVT VDAAAFDAAM ARQKEQARAA GKFKMAANLD YDGPATTFHG YDKLEAKGNI 

       490        500        510        520        530        540 
LALYKDGVAV NELVEGDLGV VVLDHTPFYA ESGGQAGDRG ELKGAAGIFG VEDTLKIQAS 

       550        560        570        580        590        600 
VFGHHGVVKT GKLAVGQGVA ARVDTAARAA TARNHSVTHL MHKALREVLG PHVQQKGSLV 

       610        620        630        640        650        660 
DPDKTRFDFA HTAPMSAEEI REVEEIVNRE ILANAATEAA VMALDDAQKS GAMMLFGEKY 

       670        680        690        700        710        720 
GDEVRVLSIG SSKELCGGTH VARTGDIGLF KIVVEGGVAA GVRRVEAVTG ENALRYTQEQ 

       730        740        750        760        770        780 
ERRVQGVSAL LKVQPDEVAE RVAGILDNVR ALEKELARLK SKLAASQGED LVAQAVDVGG 

       790        800        810        820        830        840 
AKLLAATLEG ADVPTLRETM DKLKDKLKSA AIVLASVADG KVSLIAGVTA DLTGKVKAGE 

       850        860        870        880 
LVNFVAQQVG GKGGGRPDMA QAGGTEPDKL PAALAAVQAW VSAKL 

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References

[1]"Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp. strain BH72."
Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J., Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C., Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J., Weidner S. expand/collapse author list , Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.
Nat. Biotechnol. 24:1385-1391(2006) [PubMed: 17057704] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BH72.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM406670 Genomic DNA. Translation: CAL95396.1.
RefSeqYP_934283.1. NC_008702.1.

3D structure databases

ProteinModelPortalA1K991.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1K991.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4607616.
GenomeReviewsGene locus azo2780 in contig AM406670_GR.
KEGGazo:azo2780.
PATRIC21013978. VBIAzoSp26047_2818.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAMFTNSGM.
PhylomeDBA1K991.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycASP62928:AZO2780-MONOMER.

Family and domain databases

HAMAPMF_00036_B. Ala_tRNA_synth_B.
[Tree]
InterProIPR002318. Ala-tRNA-synth_IIc.
IPR018162. Ala-tRNA-synth_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR023033. Ala_tRNA_synth_euk/bac.
IPR003156. Pesterase_DHHA1.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
KOK01872.
PANTHERPTHR11777:SF6. PTHR11777:SF6. 1 hit.
PfamPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR00980. TRNASYNTHALA.
SMARTSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMSSF101353. Ala-tRNA-synth_IIc_anticod-bd. 1 hit.
SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
TIGRFAMsTIGR00344. AlaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_AZOSB
AccessionPrimary (citable) accession number: A1K991
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: February 6, 2007
Last modified: January 25, 2012
This is version 43 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