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Q9KDE6 (SYA_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. 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:BH1267
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length879 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 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 – 879879Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000075055

Sites

Metal binding5661Zinc Potential
Metal binding5701Zinc Potential
Metal binding6681Zinc Potential
Metal binding6721Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q9KDE6 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 4BC9C5CC397A7F41

FASTA87997,742
        10         20         30         40         50         60 
MKYLTSAQVR QMFLDFFKEK GHDVEPSASL VPHDDPSLLW INSGVATLKK YFDGRVIPEN 

        70         80         90        100        110        120 
PRITNAQKSI RTNDIENVGK TARHHTFFEM LGNFSIGDYF KEEAIEWAWE FLTSEKWIGF 

       130        140        150        160        170        180 
DKEKLSVTVH PEDDEAYSYW KEKIGIPEER IIRLEGNFWD IGEGPSGPNT EIFYDRGPEY 

       190        200        210        220        230        240 
GDQPNDPELY PGGENDRYLE VWNLVFSQFN HNPDGSYTPL PKKNIDTGMG LERMVSVIQN 

       250        260        270        280        290        300 
VPTNFETDLF MPIIRATEKI SGTEYGSHHE ADVSFKVIAD HIRTVTFAIG DGALPSNEGR 

       310        320        330        340        350        360 
GYVLRRLLRR AVRYAKQIGI DRPFMYELVP VVGDIMVDFY PEVKEKAAFI QKVVKTEEER 

       370        380        390        400        410        420 
FHETLNEGLS ILEKVIDKAK SEGASTISGS DVFRLYDTYG FPVDLTEEYV EEQGLQVDLD 

       430        440        450        460        470        480 
GFEAEMERQR ERARTARQQA GSMQVQDEVL GQITVDSTFI GYKQLSTETT IETIVLDKTV 

       490        500        510        520        530        540 
ADYVGAGQEA KVILKETPFY AESGGQVADK GIIRGANGFA VVSDVQKAPN GQHLHTVIVK 

       550        560        570        580        590        600 
EGTLQVNDQV QAIVEETERS GIVKNHTATH LLHRALKDVL GEHVNQAGSL VSEERLRFDF 

       610        620        630        640        650        660 
SHFGQVTDEE KEKIERIVNE KIWQAIKVNI STKTLDEAKA IGAMALFGEK YGDIVRVVEV 

       670        680        690        700        710        720 
GDYSIELCGG CHVTNTSEIG LFKIVSESGI GAGVRRIEAV TGKEAFLFMA KQLDLLKETA 

       730        740        750        760        770        780 
ATVKAKNVKD VPVRVEALQQ QIRELQRENE SLNAKLGNME AGSLVNEVQK IEGVPVLAKA 

       790        800        810        820        830        840 
ISGADMDGLR SIVDKLKQEI PSVVIVLGTA SEGKVNIVAG VTKDLINKGY HAGKLVKEVA 

       850        860        870 
TRCGGGGGGR PDMAQAGGKQ PEKLQDALSF VYEYVKSIS 

« Hide

References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000004 Genomic DNA. Translation: BAB04986.1.
PIRC83808.
RefSeqNP_242133.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9KDE6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000053773; EBBACP00000052412; EBBACG00000053764.
GeneID894263.
GenomeReviewsGene locus BH1267 in contig BA000004_GR.
KEGGbha:BH1267.
NMPDRfig|272558.1.peg.1267.
PATRIC18939596. VBIBacHal18977_1316.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000001776.
HOGENOMHBG354397.
OMAMFTNSGM.
PhylomeDBQ9KDE6.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycBHAL272558:BH1267-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_BACHD
AccessionPrimary (citable) accession number: Q9KDE6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 69 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