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B2IHX3 (SYA_BEII9) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 25. 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:
Alanine--tRNA ligase

EC=6.1.1.7
Alternative name(s):
Alanyl-tRNA synthetase
Short name=AlaRS
Gene names
Name:alaS
Ordered Locus Names:Bind_2405
OrganismBeijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIB 8712) [Complete proteome] [HAMAP]
Taxonomic identifier395963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBeijerinckiaceaeBeijerinckia

Protein attributes

Sequence length898 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.

Sequence caution

The sequence ACB96016.1 differs from that shown. Reason: Erroneous initiation.

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 – 898898Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347506

Sites

Metal binding5641Zinc Potential
Metal binding5681Zinc Potential
Metal binding6821Zinc Potential
Metal binding6861Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
B2IHX3 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: 5121E2BAF059BC1C

FASTA89897,547
        10         20         30         40         50         60 
MNGVNEIRAA FLDFFRKNGH EIVPSSPLVP RNDPTLMFTN AGMVQFKNLF TGVEKRPYTR 

        70         80         90        100        110        120 
ASTAQKCVRA GGKHNDLDNV GYTARHHTFF EMLGNFSFGD YFKPLAIELA WKLITEVFDL 

       130        140        150        160        170        180 
PKDRLLVTVY HDDDEAYDLW KKIAGFPDSK IIRIATSDNF WAMGDTGPCG PCSEIFYDQG 

       190        200        210        220        230        240 
EKLFGGPPGS ADEDGDRFLE FWNLVFMQFE QRGPGDRIAL PKPSIDTGMG LERIAALLQG 

       250        260        270        280        290        300 
VTSNYDIDLM RALILAVAQA TGVDPDGPMR ASHRVIADHL RASSFLIADG VLPSNEGRGY 

       310        320        330        340        350        360 
VLRRIMRRAM RHAQLLGAQE PLLWRLVPAL TREMGQAYPE LLRAEALIVE TLRLEETRFR 

       370        380        390        400        410        420 
ATLARGLTIL EDETRHLSEG GVLSGEVAFK LYDTYGFPLD LTQDALRAKS LGVDMEGFEK 

       430        440        450        460        470        480 
AMARQRAEAR KAWSGSGEAA TDTHWFALRE QLGATDFLGY DTEKAEALIQ AILQDGKEVL 

       490        500        510        520        530        540 
RLEAGQSGAI VLNQTPFYGE SGGQVGDTGL IIAPGMRFKV ENTHKKLGDL FIHEGIVEEG 

       550        560        570        580        590        600 
AVVPGLEVRT LVDHSRRTAV RANHSATHLL HEALRQVLGD HIAQKGSLVA PDRLRFDFSH 

       610        620        630        640        650        660 
PKPVTPEEWT QIEDIANSVI LENAPVTTKL MSIEDAMGSG ARALFGEKYG DEVRVVSMGY 

       670        680        690        700        710        720 
DEDKADDSTD GRIAPPFSVE LCGGTHVART GDIGLLTIIS ESAVAAGVRR IEAKTGSSAR 

       730        740        750        760        770        780 
HHLNTQASLL HSLAAQLKSP EDEASKRLSA LIEERRKLDR ELSEARKKLA MGGGSSNGAD 

       790        800        810        820        830        840 
SPLREIGGIK FFRRAVTGVE MKDLKSLADE AKQTIGSGIV AIVGVGSDNK ASVVVGVTDD 

       850        860        870        880        890 
LIDRFDAVAL VRLAAGKLGG KGGGGRKDLA QAGGPDGEAA EAALTAIEES LGSSLPTP 

« Hide

References

[1]"Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC 9039."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N. expand/collapse author list , Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9039 / DSM 1715 / NCIB 8712.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001016 Genomic DNA. Translation: ACB96016.1. Different initiation.
RefSeqYP_001833505.1. NC_010581.1.

3D structure databases

ProteinModelPortalB2IHX3.
ModBaseSearch...

Protein-protein interaction databases

STRINGB2IHX3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6199545.
GenomeReviewsGene locus Bind_2405 in contig CP001016_GR.
KEGGbid:Bind_2405.
PATRIC21087739. VBIBeiInd21058_2793.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG354397.
ProtClustDBPRK00252.

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_BEII9
AccessionPrimary (citable) accession number: B2IHX3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: January 25, 2012
This is version 25 of the entry and version 2 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