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Q4UJT5 (SYA_RICFE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 61. 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:RF_1353
OrganismRickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi) [Complete proteome] [HAMAP]
Taxonomic identifier315456 [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_0000075191

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q4UJT5 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: CA941B9A40D10B98

FASTA87899,621
        10         20         30         40         50         60 
MTKFTTEEVR SKFITYFKAN NHTHVPASSL IPHNDPSLMF VNSGMVQFKN VFTGQEKRPY 

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

       130        140        150        160        170        180 
ELPKDKLYVT VYHTDEEAAS YWKKIAGFRD DRIIRIKTND NFWSMGDTGP CGPCSEIFYD 

       190        200        210        220        230        240 
HGEQIYGGLP GTKDEDGDRF IEIWNMVFMQ YEQIDKDTRI ELPQKSIDTG MGLERMTAVL 

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

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

       370        380        390        400        410        420 
FKTTLERGLK LLTEETETLT KGNELSGEIA FKLYDTYGFP LDLTEDILKN RDISVDHKRF 

       430        440        450        460        470        480 
EEQMLAQKER ARKSWLGSGE SKTDQLWFDI KEQHGSTEFL GYTLNEAECK IIALIKDNNL 

       490        500        510        520        530        540 
VNDIKEIDTQ FLLISNQTPF YGESGGQMGD IGMIFSKDSE IEVIDTLKYL GSIIVHKCIL 

       550        560        570        580        590        600 
KKGQIKIGEN ANFSIDIKYR QNLRIHHSAT HILHAVLHEV LGKHVTQKGS LVAPTYLRFD 

       610        620        630        640        650        660 
ISHSKAVTNE EITLIEDKVN EIIRDNHEVD TTLMTTEDAV KQGAMALFGE KYDSEVRVVK 

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

       730        740        750        760        770        780 
ESSLKTNKNE LITKVNNILE RNKELEKELE KVHLARLDLS IEQIEKQAED IKGVKLIYRY 

       790        800        810        820        830        840 
IENLDNKVLR QAAENLTKKV EDLIVVYITG NNDKLSITVA VSKAITDKYK AGIIAKELSL 

       850        860        870 
FLGGSGGGGQ ASLAQAGGND IGKLTNIQEK LHGLLTVS 

« Hide

References

[1]"The genome sequence of Rickettsia felis identifies the first putative conjugative plasmid in an obligate intracellular parasite."
Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E., Parinello H., Claverie J.-M., Raoult D.
PLoS Biol. 3:1-12(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-1525 / URRWXCal2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000053 Genomic DNA. Translation: AAY62204.1.
RefSeqYP_247369.1. NC_007109.1.

3D structure databases

ProteinModelPortalQ4UJT5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING315456.RF_1353.

Proteomic databases

PRIDEQ4UJT5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAY62204; AAY62204; RF_1353.
GeneID3400909.
KEGGrfe:RF_1353.
PATRIC17893638. VBIRicFel64634_1629.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHOG000156965.
KOK01872.
OMAYDIDIFQ.
OrthoDBEOG6Q2SQ2.

Enzyme and pathway databases

BioCycRFEL315456:GKEK-1390-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_RICFE
AccessionPrimary (citable) accession number: Q4UJT5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: July 5, 2005
Last modified: June 11, 2014
This is version 61 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 felis (Rickettsia azadi)

Rickettsia felis (strain URRWXCal2): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries