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A9IVY8 (SYA_BART1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. 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:BT_1489
OrganismBartonella tribocorum (strain CIP 105476 / IBS 506) [Complete proteome] [HAMAP]
Taxonomic identifier382640 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella

Protein attributes

Sequence length888 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 – 888888Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347504

Sites

Metal binding5641Zinc Potential
Metal binding5681Zinc Potential
Metal binding6761Zinc Potential
Metal binding6801Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
A9IVY8 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 7F364B63C123A164

FASTA88898,353
        10         20         30         40         50         60 
MNSVNNIRST FLDYFHRNGH QVLSSSPLVP RNDPTLMFTN AGMVQFKNVF TGLEQHLYKK 

        70         80         90        100        110        120 
ATTAQKCVRA GGKHNDLDNV GYTARHHTFF EMLGNFSFGD YFKEEAIFLS WDLLTKEFCL 

       130        140        150        160        170        180 
PKDKLLVTVY QSDDVAAELW RKISGLPDEK IVRIATADNF WAMGDTGPCG PCSEIFYDHG 

       190        200        210        220        230        240 
DEIWGGPPGS MEEDGDRFIE IWNLVFMQYE QLSKEERVDL PHPSIDTGMG LERIAAVLQG 

       250        260        270        280        290        300 
VHDNYDIDLF RVLIGASEKI TGIKATGDFV ASHRVIADHL RSSAFLIADG VLPSNEGRGY 

       310        320        330        340        350        360 
VLRRIMRRAM RHAHLLGAKE PLMWQLLPAL ICEMGQAYPE LVRAESLISE TLKLEEIRFR 

       370        380        390        400        410        420 
KTLERGLGLL NEESAKLKEG DHLNGEVAFK LYDTYGFPLD LTQDVLRRRG ISVDVDAFDK 

       430        440        450        460        470        480 
AMERQKEEAR AHWSGSGEAV TETIWFSVRD QVGVTEFLGY ETEKAEGIIT ALVCDGKIVD 

       490        500        510        520        530        540 
EVSSGQKAIL VLNQTPFYGE SGGQIGDSGI ISGEDFIFEV HDTQKKADGV FIHLGKVKSG 

       550        560        570        580        590        600 
HAKISDCVQL TVDVVRRKKI RANHSATHLL HEALRQVLGS HVTQKGSLVS PERLRFDFSH 

       610        620        630        640        650        660 
PKSVSLEELK KIEDLANEIV LQNNKVTTRL MAVDEAISEG AMALFGEKYE DEVRVVSMGA 

       670        680        690        700        710        720 
PLEQGGLKKH WSIELCGGTH VERTGDIGLI HIVSESSVSA GVRRIEALTG AAARLYLCRQ 

       730        740        750        760        770        780 
DVRIREISDL LKTSSSDLEE RVRSLLDERR KFEKELNDVR KKMVLNGKIT ESGQGDITII 

       790        800        810        820        830        840 
NGLSFMRHIV KNILPRDLKA LVDAGKKQIG SGVVAFITIS EDGKGSAVVG VTDDLTDKLN 

       850        860        870        880 
AVDLVRILSN VLGGQGGGGR SDMAQAGGPD GNKANEAFAA LKDFLEKT

« Hide

References

[1]"Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors."
Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.
Nat. Genet. 39:1469-1476(2007) [PubMed: 18037886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CIP 105476 / IBS 506.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM260525 Genomic DNA. Translation: CAK01835.1.
RefSeqYP_001609830.1. NC_010161.1.

3D structure databases

ProteinModelPortalA9IVY8.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9IVY8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5830874.
GenomeReviewsGene locus BT_1489 in contig AM260525_GR.
PATRIC20550787. VBIBarTri113218_1534.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG354397.
OMAGESKTDQ.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycBTRI382640:BT_1489-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]
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_BART1
AccessionPrimary (citable) accession number: A9IVY8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: February 5, 2008
Last modified: January 25, 2012
This is version 28 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

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