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A8ICW8 (SYA_AZOC5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 32. 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:AZC_2854
OrganismAzorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / ORS 571) [Complete proteome] [HAMAP]
Taxonomic identifier438753 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesXanthobacteraceaeAzorhizobium

Protein attributes

Sequence length881 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 – 881881Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347496

Sites

Metal binding5631Zinc Potential
Metal binding5671Zinc Potential
Metal binding6721Zinc Potential
Metal binding6761Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
A8ICW8 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: C967993014278427

FASTA88194,871
        10         20         30         40         50         60 
MSGVNEIRSS FIDYFVKNGH EAVASSPLVP RNDPTLMFTN AGMVQFKNVF TGVEKRPYSR 

        70         80         90        100        110        120 
AVTAQKCVRA GGKHNDLDNV GYTARHHTFF EMLGNFSFGD YFKDRAIELA WNLITKEWDL 

       130        140        150        160        170        180 
PKDRLLATVY YDDDVAYDLW KKVAGLPDSR IIRIPTSDNF WAMGDTGPCG PCSEIFFDHG 

       190        200        210        220        230        240 
DHIPGGPPGS PDEDGDRFIE IWNLVFMQYE QLPGERLNLP RPSIDTGMGL ERISALLQGT 

       250        260        270        280        290        300 
HDNYETDLMR AIIAEVQELT NVPSNGPQKA SHRVIADHLR SSVFLVADGV LPSNEGRGYV 

       310        320        330        340        350        360 
LRRIMRRAMR HAQLLGAREP LMHRLVPVLV REMGRAYPEI VRAEALATET LLLEETRFRR 

       370        380        390        400        410        420 
TLERGLSLLE EESAGLVSGA RFPGEVAFKL YDTYGFPLDL TEDALRGRGI EVEREAFDAA 

       430        440        450        460        470        480 
MERQKAEARA NWSGSGEAAT DTVWFGVRER EGATEFLGYD TETAEGAVRA LVQEGKEVSE 

       490        500        510        520        530        540 
LPAGARGFVV LNQTPFYGES GGQVGDSGLV SGEGVKACVL NTQKKLGDVF VHDVEVTEGT 

       550        560        570        580        590        600 
LKIGTPLALE VDHARRSAVR ANHSATHLLH EALRRVLGDH VAQKGSLVAP DRLRFDFSHP 

       610        620        630        640        650        660 
KPLTADELAQ VEDIANTYVL RNEPVETRLM AVDDAVASGA RALFGEKYGD EVRVVSMGTD 

       670        680        690        700        710        720 
SGNGAPFSVE LCGGTHVKRT GDIGIVTVLA DSGVAAGVRR LEALTATAAR RHLNAASTAL 

       730        740        750        760        770        780 
QTTAGTLKVS TAEVEARVAA LVEERRKLER DLAEARKKLA MGGGGESGPA VIEVNGTRYL 

       790        800        810        820        830        840 
RIAISGADPK DLKAIVDEGK TKIGSGVVAV ANTAADGKGA LVVGVTADLA GKFDAQKLVR 

       850        860        870        880 
IGVEVLGGKG GGGRPDMAQG GGPDGAKADA ALAAIESALG A 

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References

[1]"Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium caulinodans ORS571."
Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T., Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B., Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43989 / DSM 5975 / ORS 571.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009384 Genomic DNA. Translation: BAF88852.1.
RefSeqYP_001525770.1. NC_009937.1.

3D structure databases

ProteinModelPortalA8ICW8.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8ICW8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5688279.
GenomeReviewsGene locus AZC_2854 in contig AP009384_GR.
KEGGazc:AZC_2854.
PATRIC21022479. VBIAzoCau17976_2989.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG354397.
OMAMFTNSGM.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycACAU438753:AZC_2854-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_AZOC5
AccessionPrimary (citable) accession number: A8ICW8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: December 4, 2007
Last modified: January 25, 2012
This is version 32 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