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Q8K9E7 (SYA_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BUsg_390
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length883 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-Rule MF_00036

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00036

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00036

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00036.

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-Rule MF_00036

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
tRNA-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processalanyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

alanine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 883883Alanine--tRNA ligase HAMAP-Rule MF_00036
PRO_0000075080

Sites

Metal binding5621Zinc Potential
Metal binding5661Zinc Potential
Metal binding6641Zinc Potential
Metal binding6681Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q8K9E7 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 7D1DB0D46F640AF8

FASTA883102,345
        10         20         30         40         50         60 
MKKTTNEIRQ SFLNFFKEKE HVIVPSSSLI PENDSTLLFT NAGMNQFKEY FLGQKKKFYP 

        70         80         90        100        110        120 
RVTTVQNCLR TGGKHNDLEN VGYTKRHHTF FEMLGNFSFN DYFKKEAITY AWELLTSRKW 

       130        140        150        160        170        180 
FNIDKNKLWI SVYEDDEETY KIWRDIIRIP CHHIVKIGSK NNSQYDSENF WQMGETGPCG 

       190        200        210        220        230        240 
PCTEIFYNYD DSNKSNDFLK DKNESFIEIW NIVFIEFNRI SKTKIVPLIN KSIDTGMGLE 

       250        260        270        280        290        300 
RISAVLQNVH SNYKIDIFQK LIQKISNFTE IKDLNNISLK IIADHIRSCA FLIAENILPS 

       310        320        330        340        350        360 
NEHRGYVLRR IIRRALRHGH KIGIKNNFFY KLVPSLIEIM GDSAKILRKK EKIIEETLKI 

       370        380        390        400        410        420 
EEIQFSQTLD KGLKILNAEI KKSTNKTISG KTAFYLYDTF GFPIDLTSDI CSEKNIKIDF 

       430        440        450        460        470        480 
KGFNIAKEEQ KKRSSIKNKF YKDYNKDIII NDTCIFEGYK KNKTKSLVKY IFIKNESVFL 

       490        500        510        520        530        540 
IYKGQTATIF LDKTSFYPES GGQIGDIGEL YHKKSRFIVE NTKKYGDTIG HYGKLISGKI 

       550        560        570        580        590        600 
IVNDSIYSKI NHVYRNAIQL NHSATHLLHA ALQKVLGKNA IQKGSLVSNT HLRFDFSYSG 

       610        620        630        640        650        660 
NINLSQIQNI ENIINKKIRS NDLIKIKNLS LEEAKKKKAI ALFDYKYQSS VRVVFIKDFS 

       670        680        690        700        710        720 
IELCGGTHTK RTGNIGLFKI IEQSSVSSGI KRIEAVTGQQ AIDYLHIKDN DMQNISFLLK 

       730        740        750        760        770        780 
CQNSKITEKI KKIIIQVEKL EKKTDQLQKR ENIYQIKKLS KKINNIKGIN LLINTFTNYD 

       790        800        810        820        830        840 
QKSMKMIIDQ LKKELKISII IFINKNKNDF TVIIRVTKNL INYITALKII NIFIKKANGK 

       850        860        870        880 
GGGKKEIAEG GGMNIKKLPM ILNYIKSWIT IQLENIKTKN FNN 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM67942.1.
RefSeqNP_660731.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8K9E7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg390.

Proteomic databases

PRIDEQ8K9E7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67942; AAM67942; BUsg_390.
GeneID1005767.
KEGGbas:BUsg390.
PATRIC21247596. VBIBucAph100086_0403.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
KOK01872.
OMAYDIDIFQ.
OrthoDBEOG6Q2SQ2.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-408-MONOMER.

Family and domain databases

HAMAPMF_00036_B. Ala_tRNA_synth_B.
InterProIPR002318. 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.
IPR003156. Pesterase_DHHA1.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
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. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsTIGR00344. alaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_BUCAP
AccessionPrimary (citable) accession number: Q8K9E7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: June 11, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries