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Reviewed, UniProtKB/Swiss-Prot O51238 (SYA_BORBU)

Last modified January 19, 2010. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alanyl-tRNA synthetase
    EC=6.1.1.7
Alternative name(s):
    Alanine--tRNA ligase
      Short name=AlaRS
Gene names
Name: alaS
Ordered Locus Names: BB_0220
OrganismBorrelia burgdorferi (Lyme disease spirochete) [Complete proteome] [HAMAP]
Taxonomic identifier139 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeBorreliaBorrelia burgdorferi group

Protein attributes

Sequence length594 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036

Subcellular location

Cytoplasm HAMAP MF_00036.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processalanyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

alanine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 594594Alanyl-tRNA synthetase HAMAP MF_00036
PRO_0000075072

Sequences

Sequence LengthMass (Da)Tools
O51238-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 2337B306FD02349A

FASTA59467,773
        10         20         30         40         50         60 
MTLNKLRKKY IDFFKSKKHF EIMGKSLVPE NDPTVLFNTA GMQPLIPYLL GEVHPSGDML 

        70         80         90        100        110        120 
VNVQKCLRTG DIDEVGDLSH LTFFEMLGNW SLGAYFKEYS VKCSFEFLTS SDYLNIPKDS 

       130        140        150        160        170        180 
LYVSVFEGDQ EIPRDTETAK VWESLGISKD RIHYLSKDHN FWGPVGSKGP CGPDTEIYVD 

       190        200        210        220        230        240 
TGKSKCSLDC NITCSCGKYF EIWNNVFMQY NKDENGNYIE LGRKCVDTGM GLERTIAFLQ 

       250        260        270        280        290        300 
GKSSVYDTDA FMPIIKRIEY ISGKIYGQKE DDDRCIRIIS DHVKAACFIL ADSSVVFPSN 

       310        320        330        340        350        360 
LGQGYVLRRL IRRSIRYAKK LGIKSHFLAD LVDSVEAIYR SFYNELTEKK DFIKKELSKE 

       370        380        390        400        410        420 
EEKFFKTLSQ GEQEFIKITR NLPSKTIPGD IAFKLYDTYG FPYEVTEELA IEYGFNVDKL 

       430        440        450        460        470        480 
GFNEHFKKHQ KTSKKGGDKV FKGGLADYTY ETTKLHTATH LLHKALQLVL GDHVRQKGSN 

       490        500        510        520        530        540 
ITAERLRFDF VHSEKMTDDE IKKVEEIVNL QIKNSLSVKK IIMELSEARE KGAMALFGEK 

       550        560        570        580        590 
YDDLVSVYEI DGFSLEVCGG PHVENTNELG TFKIQKEQSS SSGIRRIKAI LIDE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000783 Genomic DNA. Translation: AAC66604.1.
PIRD70127.
RefSeqNP_212354.1.

3D structure databases

SMRO51238. Positions 1-436, 436-591.
ModBaseSearch...

Genome annotation databases

GeneID1195057.
GenomeReviewsGene locus BB_0220 in contig AE000783_GR.
KEGGbbu:BB0220.
NMPDRfig|224326.1.peg.604.
TIGRBB_0220.

Phylogenomic databases

HOGENOMHBG354397.
OMARKCVDTG.

Enzyme and pathway databases

BioCycBBUR224326:BB_0220-MONOMER.
BRENDA6.1.1.7. 142596.

Family and domain databases

HAMAPMF_00036_B. Ala_tRNA_synth_B. Divergent sequence.
[Tree]
InterProIPR018162. Ala-tRNA-synth_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
PfamPF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR00980. TRNASYNTHALA.
SMARTSM00863. tRNA_SAD. 1 hit.
[Graphical view]
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_BORBU
AccessionPrimary (citable) accession number: O51238
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: January 19, 2010
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents