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Q7WHL6 (SYA_BORBR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. 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
Synonyms:lovB
Ordered Locus Names:BB3191
OrganismBordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]
Taxonomic identifier257310 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length874 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 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 – 874874Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000075069

Sites

Metal binding5621Zinc Potential
Metal binding5661Zinc Potential
Metal binding6631Zinc Potential
Metal binding6671Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q7WHL6 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 7FEB78F43474C51D

FASTA87494,867
        10         20         30         40         50         60 
MKSSEIRQKF LQFFQSKGHT IVPSSSLVPA NDPTLLFTNS GMVQFKDVFT GKEARAYKRA 

        70         80         90        100        110        120 
TSSQRSVRAG GKHNDLENVG YTARHHTFFE MLGNFSFGDY FKREAIQYAW ELLTQVYRLP 

       130        140        150        160        170        180 
AEKLWVTVYQ EDDEAYDIWA KEVGVPAERI IRIGDNKGAR YASDNFWQMA DTGPCGPCSE 

       190        200        210        220        230        240 
IFYDHGPEIW GGPPGSPEED GDRYIEIWNL VFMQFERDAA GNMERLPKPC VDTGMGLERI 

       250        260        270        280        290        300 
AAVLQHVHSN YEIDLFQKLI AAAARETGVK DLADNSLKVI ADHIRACAFL IVDGIIPSNE 

       310        320        330        340        350        360 
GRGYVLRRIV RRALRHGYKL GQTKPFFHRL VPDLVAEMGE AYPELAQVAE RVAQVLRQEE 

       370        380        390        400        410        420 
ERFGETLEHG MKILDGALAK VAKGDPLDGT TLFTLYDTYG FPVDLTADIC RERGVEVDMA 

       430        440        450        460        470        480 
GFEAAMQRQR EQARAAGKFK MAEGLSYEGA ETRFEGYESL ELSGVKVTAL YVEGTQVEQV 

       490        500        510        520        530        540 
SAGQDAVVVL DATPFYAESG GQVGDTGLLE AGGVRFAVAD TLKIQPGVFG HHGTLEAGAL 

       550        560        570        580        590        600 
KVGDTLLARV DAVRRARTVR NHSATHLMHK ALREVLGAHV QQRGSLVDPD KTRFDFAHDA 

       610        620        630        640        650        660 
PMTAEQIARV EAIVNAEVLA NQATEAKVMA YDDAVKGGAM ALFGEKYGDT VRVLDIGFSR 

       670        680        690        700        710        720 
ELCGGTHVRR TGDIGLFKVV SEGGVAAGVR RIEAITGDNA LAWVQDQNAL LQRAAGVLRA 

       730        740        750        760        770        780 
PAHELPERIV QVQEQLKALE KELEQARTKL AASAGNDLAA TATVEVKGIK VLAASIGDVD 

       790        800        810        820        830        840 
PKALRGMVDN LKDRLKPAVV LLAAGSADGK ISLVGGVTAD LTGRIKAGDL VGFVAGQVGG 

       850        860        870 
KGGGRPDMAM GGGTDLAALP AAVASVQKWV DERL

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX640446 Genomic DNA. Translation: CAE33683.1.
RefSeqNP_889727.1. NC_002927.3.

3D structure databases

ProteinModelPortalQ7WHL6.
SMRQ7WHL6. Positions 1-460.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2660548.
GenomeReviewsGene locus BB3191 in contig BX470250_GR.
KEGGbbr:BB3191.
NMPDRfig|257310.1.peg.3174.
PATRIC21139769. VBIBorBro124907_3252.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG354397.
OMAMFTNSGM.
PhylomeDBQ7WHL6.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycBBRO257310:BB3191-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_BORBR
AccessionPrimary (citable) accession number: Q7WHL6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 50 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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