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Q68VQ7 (SYA_RICTY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 58. 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:RT0845
OrganismRickettsia typhi (strain ATCC VR-144 / Wilmington) [Complete proteome] [HAMAP]
Taxonomic identifier257363 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length877 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.

Subcellular location

Cytoplasm By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 877877Alanine--tRNA ligase HAMAP-Rule MF_00036
PRO_0000075193

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q68VQ7 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: CF51798B7FC0016E

FASTA87799,125
        10         20         30         40         50         60 
MTKFTTEEVR SKFITYFKAN NHTHVPASSL IPDNDPSLMF VNSGMVQFKN VFTGQEKRSY 

        70         80         90        100        110        120 
NKAVTSQKSL RAGGKHNDLE HVGYTARHHT FFEMLGNFSF GDYFKEQAIY YTWDLLTKEF 

       130        140        150        160        170        180 
ELPKDKLYVT IYHTDDTAAS YWEKISGLRD DRIIKIKTND NFWSMGDTGP CGPCSEIFYD 

       190        200        210        220        230        240 
HGEEIYGGLP GTKDEDCDRF IEIWNMVFMQ YEQINKETRI ELPKKSIDTG MGLERMTAVL 

       250        260        270        280        290        300 
QHVNNNYDID LFQEIINFTE NIVKVKVDGE AKFSYRVIAD HLRASSFLIA DGIIPSNEGR 

       310        320        330        340        350        360 
GYVLRRIMRR AMRHAHMLGA KEPLMYKLLP KLVDLMGNIY PELKIAEGFI SSILEQEEIR 

       370        380        390        400        410        420 
FKTTLERGLK LLTEETKTLT KGNKLSGEVA FKLYDTYGFP LDLTEDILKN RDIAVDHKGF 

       430        440        450        460        470        480 
EELMLIQKER ARTSWLGSGE SKTDQLWFDI KEQYGSTEFL GYTLNEAKCK IIALIKNNNL 

       490        500        510        520        530        540 
ADTIQEVDTQ FLLIANQTPF YGESGGQMGD IGMIFSQDSE VEVIDTLKYL RSIIVHKCIL 

       550        560        570        580        590        600 
KKGKINIGEN ANFNIDIKYR KNLRIHHSAT HILHAVLHKI LGKQVIQKGS LVTSTYLRFD 

       610        620        630        640        650        660 
INHSKAITNE EITLIEDKVN EIIRNNHEVN TTVMFTEDAI KQGAIALFGE KYDSEVRVVK 

       670        680        690        700        710        720 
IGETSLELCC GTHVKRTGDI GAFKIISESS IAAGVRRIEA VCGEFVIKLI REKDNLIKLI 

       730        740        750        760        770        780 
ESSVKTNKNE LITKVTNILE RNKELEKELE KAHLAGLDLS IEQIKKQAEQ IAGIKLLYKK 

       790        800        810        820        830        840 
VGNINNKILR QAAENLTQKL ENLIVVYIAH GVGKLSITVA VSKAITDKFN AGIIAKELSL 

       850        860        870 
FLGGSGGGGK ASIAQSGGND IVNLTNINKK LLSLIVT 

« Hide

References

[1]"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae."
McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. expand/collapse author list , Hong C., Yu X.-J., Walker D.H., Weinstock G.M.
J. Bacteriol. 186:5842-5855(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-144 / Wilmington.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017197 Genomic DNA. Translation: AAU04299.1.
RefSeqYP_067781.1. NC_006142.1.

3D structure databases

ProteinModelPortalQ68VQ7.
ModBaseSearch...

Protein-protein interaction databases

STRING257363.RT0845.

Proteomic databases

PRIDEQ68VQ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU04299; AAU04299; RT0845.
GeneID2959272.
KEGGrty:RT0845.
PATRIC17910942. VBIRicTyp34752_0862.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHOG000156965.
KOK01872.
OMAEWFDFPK.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycRTYP257363:GJEQ-885-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.
IPR012947. tRNA_SAD.
[Graphical view]
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_RICTY
AccessionPrimary (citable) accession number: Q68VQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: October 11, 2004
Last modified: May 1, 2013
This is version 58 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

Rickettsia typhi

Rickettsia typhi (strain Wilmington): entries and gene names

SIMILARITY comments

Index of protein domains and families