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Q12U25 (SYA_METBU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. 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:Mbur_2186
OrganismMethanococcoides burtonii (strain DSM 6242) [Complete proteome] [HAMAP]
Taxonomic identifier259564 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanococcoides

Protein attributes

Sequence length923 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_A

Catalytic activity

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036_A

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00036_A

Subcellular location

Cytoplasm By similarity HAMAP MF_00036_A.

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_A

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 – 923923Alanine--tRNA ligase HAMAP MF_00036_A
PRO_0000347885

Sites

Metal binding6111Zinc By similarity
Metal binding6151Zinc By similarity
Metal binding7141Zinc By similarity
Metal binding7181Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q12U25 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: B674C89E48E056C9

FASTA923103,461
        10         20         30         40         50         60 
MLEDEYQIDF FSDNGFVRKQ CPTCGNFFWT RDIERSTCGD APCDPYSFIG NPVFKKELEL 

        70         80         90        100        110        120 
PDMREFYLNF FEEQGHTRIE RYPVIARWRD DIYLTIASIA DFQPFVTSGQ VPPPANPLTI 

       130        140        150        160        170        180 
SQPCIRLSDL DAVGKSGRHL TTFEMMAHHA FNTKNEEIYW KEHTLELCDG LLNSLGADPM 

       190        200        210        220        230        240 
AVTYKEEPWA GGGNAGACVE VLIGGLEVAT LVFMNLKKDK NGDIDIKGDM YSKMENYIVD 

       250        260        270        280        290        300 
TGYGLERLVW ASKGSPTIYD AIFPSIVNEL MGLAGIEHEL ENNEYSHILS QNARLAGLMD 

       310        320        330        340        350        360 
ISEKANLLEL RKQVAASIGI TADKLSSIME PVENVYAIAD HTRCLTFMIG DGIIPSNVKA 

       370        380        390        400        410        420 
GYLARLVIRR TLRMMKDLGI MIPISEIIQM HINNLPEYPE FQKRFDVIKD ILEHEERKFA 

       430        440        450        460        470        480 
ETLERGRRMM EKSARHYKES GEKMPLETII DMYDSHGIPP EISKAVASDV GVEVDLPDNF 

       490        500        510        520        530        540 
YSLVADKHSQ SEEKEEKVVP FADKIARLPK TKRLFYDEPN RMDFDAVVLE VFDNHIVLDN 

       550        560        570        580        590        600 
TLMYPEGGGQ PADHGTLTVE DVVLKVVDTQ MYDGVVVHTI NEIEDELHIR KGDMVVGRVN 

       610        620        630        640        650        660 
EKRRMAHARH HTATHIINDA AREVLGSHIW QTGAQKFADR ARLDISHYKR ITQEEANQIE 

       670        680        690        700        710        720 
IIANHTVMKN KRIISDWMDR TEAEQKYGFR LYQGGVPPGK MIRVLQVGND IEACAGTHCT 

       730        740        750        760        770        780 
NTGLVGPIKI LKTERIQDGV ERLEYAAGEA AIIAMQDIET LVRDSSETLR VSAEQLPSTI 

       790        800        810        820        830        840 
ERFFDEWKEL KKENNKLKEE LAHSRVSQLV NDAEDVNGIR IITKAIPHAD SEELTKTAGE 

       850        860        870        880        890        900 
LTQESNVVAI LISEMDGVKI VATAGDDAVK RGVNVGAIVK EMSTMVGGGG GGRPNMARGG 

       910        920 
GTDPSGMDNA LSRSVELLKE QLN 

« Hide

References

[1]"Complete sequence of Methanococcoides burtonii DSM 6242."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Kadner K., Aerts A., Dehal P., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Anderson I., Franzmann P., Thomas T., Saunders N., Cavicchioli R., Sowers K., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6242.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000300 Genomic DNA. Translation: ABE53051.1.
RefSeqYP_566801.1. NC_007955.1.

3D structure databases

ProteinModelPortalQ12U25.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ12U25.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3997042.
GenomeReviewsGene locus Mbur_2186 in contig CP000300_GR.
KEGGmbu:Mbur_2186.
NMPDRfig|259564.8.peg.2090.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04130.
HOGENOMHBG392147.
OMAMFTNSGM.
PhylomeDBQ12U25.
ProtClustDBPRK13902.

Enzyme and pathway databases

BioCycMBUR259564:MBUR_2186-MONOMER.

Family and domain databases

HAMAPMF_00036_A. Ala_tRNA_synth_A.
[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.
IPR022429. Ala-tRNA_synth_arc.
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.
TIGRFAMsTIGR03683. A-tRNA_syn_arch. 1 hit.
TIGR00344. AlaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_METBU
AccessionPrimary (citable) accession number: Q12U25
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: August 22, 2006
Last modified: January 25, 2012
This is version 42 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