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A7HH87 (SYA_ANADF) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 34. 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:Anae109_3904
OrganismAnaeromyxobacter sp. (strain Fw109-5) [Complete proteome] [HAMAP]
Taxonomic identifier404589 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length904 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 – 904904Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347489

Sites

Metal binding5941Zinc Potential
Metal binding5981Zinc Potential
Metal binding6951Zinc Potential
Metal binding6991Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
A7HH87 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 06D8C3289D861DC3

FASTA90498,558
        10         20         30         40         50         60 
MKTAAQIREL FLRFFEEKAH RRVPSSSLVP QNDPTLLFTN AGMNQFKDVF TGREKRDYSR 

        70         80         90        100        110        120 
ATTAQKCVRA GGKHNDLENV GFTARHHTFF EMLGNFSFGD YFKKEAIAWA WELVTSERWL 

       130        140        150        160        170        180 
AISKERLAAT VFAGEGTLPW DEEAYRLWEA QGVPPERIHK LGAKDNFWAM GDTGPCGPCS 

       190        200        210        220        230        240 
ELHFFQGNDI PCAEEKAGRT CQGVACDCDR WLEIWNLVFM QFERGADGGL TPLPKPSIDT 

       250        260        270        280        290        300 
GAGLERMAAV VQGKRSNYDI DAFQSIIRAI EKLAGKRYGA TDADDDVSMR VIADHARATT 

       310        320        330        340        350        360 
FLVGDGVLPA NEGRGYVLRR IMRRAIRHGK RLGLERPFLA DVCEAVMEEM GGAYPETREN 

       370        380        390        400        410        420 
RAFIVKVAGQ EEESFRRTLD KGLAILETEM RKAIPPETHL GKPATPPPSA PRPVIDGKLA 

       430        440        450        460        470        480 
FQLYDTFGFP LDLTRVIAAE RGFDVDEQGF DRNMAEQRAR SEWKGSGEQA VGDLHKQIAS 

       490        500        510        520        530        540 
ELGETRFLGY EAPTARAEVK ALLANGARAA KAARGDKVEV VTAATPFYGE SGGQVGDQGS 

       550        560        570        580        590        600 
IAAPGGRVRV EDTRRPVPGL VTHVGVVEEG ELAVGDLVEL AVDDRRRDLI RANHSATHLL 

       610        620        630        640        650        660 
QLALRETLGD HVKQAGSIVA PDYLRFDFSH FQPLSEEELN AIERRVNELV RENAETETAV 

       670        680        690        700        710        720 
LKLEDARQSG AMMIFGEKYG DVVRVVRLGP SKELCGGTHV RRTGDIAFFK IGSEESIAAG 

       730        740        750        760        770        780 
VRRIVAYTGP QAIELSQREA DELRRAAALF KAGAFEVAQK IEQTQKRVKD LERALDEAKG 

       790        800        810        820        830        840 
KIASAQSGDL AAQARDVKGA KVLAVRVQGD GKSLRELADK LRDRLGTGVV ALGAEQDGKA 

       850        860        870        880        890        900 
ILLVAVTKDL TARLKAGELV KEAAKLVGGS GGGKPDLAQA GGSDPAGLEK ALAKVQELAV 


AALG 

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References

[1]"Complete sequence of Anaeromyxobacter sp. Fw109-5."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Lykidis A., Fields M., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Fw109-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000769 Genomic DNA. Translation: ABS28083.1.
RefSeqYP_001381067.1. NC_009675.1.

3D structure databases

ProteinModelPortalA7HH87.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7HH87.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5377443.
GenomeReviewsGene locus Anae109_3904 in contig CP000769_GR.
KEGGafw:Anae109_3904.
NMPDRfig|404589.4.peg.3351.
PATRIC20933301. VBIAnaSp113478_4090.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAGESKTDQ.
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_ANADF
AccessionPrimary (citable) accession number: A7HH87
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 11, 2007
Last modified: January 25, 2012
This is version 34 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