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Q1RKG2 (SYA_RICBR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Ordered Locus Names:RBE_0071
OrganismRickettsia bellii (strain RML369-C) [Complete proteome] [HAMAP]
Taxonomic identifier336407 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia

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 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 – 877877Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000278068

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q1RKG2 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 983BD61A275CF38F

FASTA87798,911
        10         20         30         40         50         60 
MSKFTTEEIR SKFISYFKAN NHTHVSSSPL IPHNDPSLMF VNSGMVQFKN VFTGQEKRPY 

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

       130        140        150        160        170        180 
ELPKDKLYAT VYHTDDEAAS YWKKIAGFSD DRIIRIKTND NFWSMGDLGP CGPCSEIFYD 

       190        200        210        220        230        240 
HGEQIYGGLP GTKDEDGDRF IEIWNMVFMQ YEQINKDTRI DLPKKSIDTG MGLERMTAVL 

       250        260        270        280        290        300 
QHVNNNYDID LFQEIISFTE NILKVKVEAE AKFSYRVIAD HLRACSFLIA DGVVPSSEGR 

       310        320        330        340        350        360 
GYVLRRIMRR AMRHAHILGS KEPLMYKLLP KLVDLMGNTY PELKRAESFI SSILEQEEIR 

       370        380        390        400        410        420 
FKTTLERGLK LLSEETENLN AGGRLSGEVA FKLYDTYGFP LDLTEDILKN RNIAVDHQGF 

       430        440        450        460        470        480 
EQQMLEQKEC ARKSWLGSGE SKTDQLWFDI KAKYGSTEFL GYNLNEADGK IVALIKDNAL 

       490        500        510        520        530        540 
VNDISEIDTQ FLLIANQTPF YGESGGQMGD IGVIKTQNCE IEVIDTLKYL GFIIVHKCVL 

       550        560        570        580        590        600 
KKGKVITDEN ANFSIDVKYR QNLRIHHSAT HLLHAVLHQI LGKHVTQKGS LVATSYLRFD 

       610        620        630        640        650        660 
ISHPKALTPE EIVLIEDKVN EIIRDNHEVD TTLMSTEDAV KQGAMALFGE KYDSEVRVVK 

       670        680        690        700        710        720 
MGETSLELCG GTHVRHTGDI GCFKITSESA IAAGIRRIEA VCGEFVIKLI REKEGLLKNI 

       730        740        750        760        770        780 
ENSLKTNKNE LVSKVNNILE RNKELEKELE KTYLASLDLS VEQIEKQAEK IKEIKLIYCH 

       790        800        810        820        830        840 
VENLDNKILR QAAENLTKKV EDLVVVYVGN NSSKLSITVG ISRAITDKFN AGFIAKELSL 

       850        860        870 
FLGGSGGGGQ PSIAQAGGSD LAKLPKVKDQ LQSLLDA

« Hide

References

[1]"Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens."
Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D.
PLoS Genet. 2:733-744(2006) [PubMed: 16703114] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RML369-C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000087 Genomic DNA. Translation: ABE04152.1.
RefSeqYP_537241.1. NC_007940.1.

3D structure databases

ProteinModelPortalQ1RKG2.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1RKG2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3994975.
GenomeReviewsGene locus RBE_0071 in contig CP000087_GR.
KEGGrbe:RBE_0071.
PATRIC17881387. VBIRicBel102610_0078.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAGESKTDQ.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycRBEL336407:RBE_0071-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_RICBR
AccessionPrimary (citable) accession number: Q1RKG2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: May 16, 2006
Last modified: January 25, 2012
This is version 41 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 bellii strain RML369-C

Rickettsia bellii (strain RML369-C): entries and gene names

SIMILARITY comments

Index of protein domains and families

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