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Q92G00 (SYA_RICCN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 76. 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:RC1327
OrganismRickettsia conorii (strain ATCC VR-613 / Malish 7) [Complete proteome] [HAMAP]
Taxonomic identifier272944 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length878 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

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 – 878878Alanine--tRNA ligase HAMAP-Rule MF_00036
PRO_0000075190

Sites

Metal binding5671Zinc Potential
Metal binding5711Zinc Potential
Metal binding6691Zinc Potential
Metal binding6731Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q92G00 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: F4E6A0A13379E65A

FASTA87898,838
        10         20         30         40         50         60 
MTKFTTEEVR SKFITYFKAN NHTHVPASSL IPHNDPSLMF VNSGMVQFKN VFTGQGKRPY 

        70         80         90        100        110        120 
NKAVTSQKSL RAGGKHNDLE NVGYTARHHT FFEMLGNFSF GDYFKEQAIY YAWNLLTKEF 

       130        140        150        160        170        180 
ELPKDKLYAT IYHTDDEAAA YWKKIAGFGD DRIIKIKTND NFWSMGDTGP CGPCSEIFYD 

       190        200        210        220        230        240 
HGEQIYGGLP GTKDEDGDRF IEIWNMVFMQ YEQIDKDTSI ELSQKSIDTG MGLERMTAVL 

       250        260        270        280        290        300 
QHVNNNYDID LFQEIINFTE NIVKVKVEGE AKFSYRVIAD HLRASSFLIA DGVIPSNEGR 

       310        320        330        340        350        360 
GYVLRRIMRR SMRHAHMLGS KEPLMYKLLP KLVDLMGNVY PELKRAESFI SSILEQEEIR 

       370        380        390        400        410        420 
FKATLERGLK LLTEETETLT KGNELSGEVA FKLYDTYGFP LDLTEDILKN RDIAVDHKGF 

       430        440        450        460        470        480 
EEQMLMQKAR ARKSWLGSGE SKTDQLWFDI KEQHGSTEFL GYTLNEAKCK IIALIKNNNL 

       490        500        510        520        530        540 
VNDIKEIDTQ FLLISNQTPF YGESGGQIGD IGTIFAKDSE VEVIDTLKYL GSIIIHKCIL 

       550        560        570        580        590        600 
KKGQINVGEN ANFSIDIRYR QNLRIHHSAT HILHAVLHEV LGKHVTQKGS LVAPTYLRFD 

       610        620        630        640        650        660 
ISHSKAVTNE EITLIEDKVN EIIRDNHEVT TTLMATEDAI KQGAMALFGE KYDSEVRVVK 

       670        680        690        700        710        720 
MGETSLELCG GTHVRRTGDI GCFKITSESA IAAGVRRIEA VCGEFVITLM REKDSLLKSI 

       730        740        750        760        770        780 
ESSFKTNKNE LITKVNNILE RNKEVEKELE KTLLASLDLS IEQIEKQSAQ ITGIKLLYKK 

       790        800        810        820        830        840 
VGNIDNKILR QAAENLTKKV EDLIMVYIAE GIGKLSITVA VSKAITDKYN ADIIAKKLSL 

       850        860        870 
FLGGSGGGGQ ASLAQAGGND IGKLTNIHEK LYSLLTVS 

« Hide

References

[1]"Mechanisms of evolution in Rickettsia conorii and R. prowazekii."
Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.
Science 293:2093-2098(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006914 Genomic DNA. Translation: AAL03865.1.
PIRG97865.
RefSeqNP_360964.1. NC_003103.1.

3D structure databases

ProteinModelPortalQ92G00.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272944.RC1327.

Proteomic databases

PRIDEQ92G00.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL03865; AAL03865; RC1327.
GeneID928521.
KEGGrco:RC1327.
PATRIC17890185. VBIRicCon45613_1521.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHOG000156965.
KOK01872.
OMAYDIDIFQ.
OrthoDBEOG6Q2SQ2.

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_RICCN
AccessionPrimary (citable) accession number: Q92G00
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2002
Last sequence update: December 1, 2001
Last modified: June 11, 2014
This is version 76 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

Rickettsia conorii

(strain Malish 7): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries