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A8EWI6 (SYA_ARCB4) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. 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:Abu_2092
OrganismArcobacter butzleri (strain RM4018) [Complete proteome] [HAMAP]
Taxonomic identifier367737 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeArcobacter

Protein attributes

Sequence length851 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 – 851851Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347491

Sites

Metal binding5541Zinc Potential
Metal binding5581Zinc Potential
Metal binding6561Zinc Potential
Metal binding6601Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
A8EWI6 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 7005E6118CA73F87

FASTA85194,966
        10         20         30         40         50         60 
MDIRKEYLEF FRSKGHEVIS SMPLVPDDPT LMFTNAGMVQ FKDIFTGAVP TPKNKRATSC 

        70         80         90        100        110        120 
QLCVRAGGKH NDLENVGYTA RHHTLFEMLG NFSFGDYFKE DAIAYAWEFV TVNLALPIDK 

       130        140        150        160        170        180 
LWVTVHNNDD EAFDIWSKYI NPSRIMRFGD KDNFWSMGDT GACGPCSEIF YDQGEENFNG 

       190        200        210        220        230        240 
EEDYMGGDGD RFLEIWNLVF MQYERTADGK LNPLPKPSID TGMGLERVIA IKEGVFNNFD 

       250        260        270        280        290        300 
SSNFKPIIKK IEEISSKNAT SENIGSYRVI ADHLRACSFM LSQGILFGNE GRPYVLRRIL 

       310        320        330        340        350        360 
RRAVRHGYLI GFRKPFMAKL LDTLIEIMGG HYTELVENKN FIEEQLTLEE DRFFKTIDLG 

       370        380        390        400        410        420 
MSLFNEELEK TKDIFSGVTA FKLYDTYGFP LDLTEDMLRD RGLKVDLAKF DELMNNQKAM 

       430        440        450        460        470        480 
AKAAWKGSGD TSNEGDFKQL LEKFGSNEFV GYNNTTYKSK IIALLDEHFK EVKILEKDST 

       490        500        510        520        530        540 
GWVMLDKTPF YATSGGQNGD IGALEDNKHI AIVEETTKFH GLNLSKVKVV NSSLKQGESV 

       550        560        570        580        590        600 
DAIVVNRNEV AKHHSATHLL QSALKIVLGD TVSQAGSLND ASRLRFDFTY PKAMTKEQID 

       610        620        630        640        650        660 
EVEDLVNSMI ARGISGNVEE LPIEQAKKKG AIAMFGEKYG DVVRVVSFED VSVEFCGGTH 

       670        680        690        700        710        720 
VRNTADIGSF YIVKESGVSA GVRRIEAVCG TAAIKYTKDI ISKMNEIQAE VKNSDVILGI 

       730        740        750        760        770        780 
KKLKEQIKDL KKEIETSQSK TSSPIEETII NDTKVIVSVV ENGDLKKIVD DTKNANEKVA 

       790        800        810        820        830        840 
IFLLQAKDDK VLIVAGSKNT NIKAGDWIKN IAPIVGGGGG GRPDFAQAGG KDTSKIQEAK 

       850 
TKALDYAKEN L 

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References

[1]"The complete genome sequence and analysis of the Epsilonproteobacterium Arcobacter butzleri."
Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M., Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A., Rogosin A., Stanker L.H., Mandrell R.E.
PLoS ONE 2:E1358-E1358(2007) [PubMed: 18159241] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RM4018.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000361 Genomic DNA. Translation: ABV68309.1.
RefSeqYP_001490979.1. NC_009850.1.

3D structure databases

ProteinModelPortalA8EWI6.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8EWI6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5623611.
GenomeReviewsGene locus Abu_2092 in contig CP000361_GR.
KEGGabu:Abu_2092.
PATRIC20965548. VBIArcBut20197_2038.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAMFTNSGM.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycABUT367737:ABU_2092-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_ARCB4
AccessionPrimary (citable) accession number: A8EWI6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: November 13, 2007
Last modified: January 25, 2012
This is version 31 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