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Protein

Alanine--tRNA ligase

Gene

alaS

Organism
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi456 – 4561ZincSequence analysis
Metal bindingi460 – 4601ZincSequence analysis
Metal bindingi558 – 5581ZincSequence analysis
Metal bindingi562 – 5621ZincSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, tRNA-binding, Zinc

Enzyme and pathway databases

BioCyciBBUR224326:G9SO-220-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine--tRNA ligase (EC:6.1.1.7)
Alternative name(s):
Alanyl-tRNA synthetase
Short name:
AlaRS
Gene namesi
Name:alaS
Ordered Locus Names:BB_0220
OrganismiBorrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Taxonomic identifieri224326 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesBorreliaceaeBorreliella
Proteomesi
  • UP000001807 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 594594Alanine--tRNA ligasePRO_0000075072Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi224326.BB_0220.

Structurei

3D structure databases

ProteinModelPortaliO51238.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Consists of two domains; the N-terminal catalytic domain (in this organism this is shorter than usual) and the editing domain; the C-terminal C-Ala domain found in most orthologs is missing. The editing domain removes incorrectly charged amino acids (By similarity).By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CIM. Bacteria.
COG0013. LUCA.
KOiK01872.
OMAiRKCVDTG.

Family and domain databases

HAMAPiMF_00036_B. Ala_tRNA_synth_B. 1 hit.
InterProiIPR002318. Ala-tRNA-lgiase_IIc.
IPR018162. Ala-tRNA-ligase_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR023033. Ala_tRNA_ligase_euk/bac.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR00980. TRNASYNTHALA.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF101353. SSF101353. 1 hit.
SSF55186. SSF55186. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O51238-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLNKLRKKY IDFFKSKKHF EIMGKSLVPE NDPTVLFNTA GMQPLIPYLL
60 70 80 90 100
GEVHPSGDML VNVQKCLRTG DIDEVGDLSH LTFFEMLGNW SLGAYFKEYS
110 120 130 140 150
VKCSFEFLTS SDYLNIPKDS LYVSVFEGDQ EIPRDTETAK VWESLGISKD
160 170 180 190 200
RIHYLSKDHN FWGPVGSKGP CGPDTEIYVD TGKSKCSLDC NITCSCGKYF
210 220 230 240 250
EIWNNVFMQY NKDENGNYIE LGRKCVDTGM GLERTIAFLQ GKSSVYDTDA
260 270 280 290 300
FMPIIKRIEY ISGKIYGQKE DDDRCIRIIS DHVKAACFIL ADSSVVFPSN
310 320 330 340 350
LGQGYVLRRL IRRSIRYAKK LGIKSHFLAD LVDSVEAIYR SFYNELTEKK
360 370 380 390 400
DFIKKELSKE EEKFFKTLSQ GEQEFIKITR NLPSKTIPGD IAFKLYDTYG
410 420 430 440 450
FPYEVTEELA IEYGFNVDKL GFNEHFKKHQ KTSKKGGDKV FKGGLADYTY
460 470 480 490 500
ETTKLHTATH LLHKALQLVL GDHVRQKGSN ITAERLRFDF VHSEKMTDDE
510 520 530 540 550
IKKVEEIVNL QIKNSLSVKK IIMELSEARE KGAMALFGEK YDDLVSVYEI
560 570 580 590
DGFSLEVCGG PHVENTNELG TFKIQKEQSS SSGIRRIKAI LIDE
Length:594
Mass (Da):67,773
Last modified:June 1, 1998 - v1
Checksum:i2337B306FD02349A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000783 Genomic DNA. Translation: AAC66604.1.
PIRiD70127.
RefSeqiNP_212354.1. NC_001318.1.
WP_010889708.1. NC_001318.1.

Genome annotation databases

EnsemblBacteriaiAAC66604; AAC66604; BB_0220.
GeneIDi1195057.
KEGGibbu:BB_0220.
PATRICi20557054. VBIBorBur75917_0618.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000783 Genomic DNA. Translation: AAC66604.1.
PIRiD70127.
RefSeqiNP_212354.1. NC_001318.1.
WP_010889708.1. NC_001318.1.

3D structure databases

ProteinModelPortaliO51238.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224326.BB_0220.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC66604; AAC66604; BB_0220.
GeneIDi1195057.
KEGGibbu:BB_0220.
PATRICi20557054. VBIBorBur75917_0618.

Phylogenomic databases

eggNOGiENOG4105CIM. Bacteria.
COG0013. LUCA.
KOiK01872.
OMAiRKCVDTG.

Enzyme and pathway databases

BioCyciBBUR224326:G9SO-220-MONOMER.

Family and domain databases

HAMAPiMF_00036_B. Ala_tRNA_synth_B. 1 hit.
InterProiIPR002318. Ala-tRNA-lgiase_IIc.
IPR018162. Ala-tRNA-ligase_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR023033. Ala_tRNA_ligase_euk/bac.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR00980. TRNASYNTHALA.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF101353. SSF101353. 1 hit.
SSF55186. SSF55186. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSYA_BORBU
AccessioniPrimary (citable) accession number: O51238
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: September 7, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.