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Q493M6 (SYA_BLOPB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:BPEN_174
OrganismBlochmannia pennsylvanicus (strain BPEN) [Complete proteome] [HAMAP]
Taxonomic identifier291272 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › ant endosymbionts › Candidatus Blochmannia

Protein attributes

Sequence length879 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

Subunit structure

Homotetramer 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 – 879879Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000075068

Sites

Metal binding5651Zinc Potential
Metal binding5691Zinc Potential
Metal binding6671Zinc Potential
Metal binding6711Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q493M6 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: AB11E160B35B1A04

FASTA87999,895
        10         20         30         40         50         60 
MYKNIDDIRQ EFLNFFKKKG HKIISSSTLI PNSDQTLLFT NSGMNQFKNI FLGIDKPLFK 

        70         80         90        100        110        120 
RVATAQRCVR AGGKHNDLNN VGYTERHLTF FEMLGNFSFG DYFKNEAIQF AWELLTDVNW 

       130        140        150        160        170        180 
FNLSKNKLWV TVHNCDGESY DIWSNQIDIP NEHIVKIGSN TNDFCDSDNF WQMGNIGPCG 

       190        200        210        220        230        240 
PCSEIFYDRG DRFQGGPPGS LEEFGERYVE IWNLVFIQFD RQENGRLLSL PMLSVDTGMG 

       250        260        270        280        290        300 
LERITSILQG VNSNFSIDVF KKLISSISRI MKINDIYINR SVYVIADHIR ACSFLIQDGV 

       310        320        330        340        350        360 
LPANEGRGYV LRRIIRRAIL HGKKLGVNDI FFYKLVSPLI KYMQHIADIL HEKKDFIAEI 

       370        380        390        400        410        420 
LLSEEKLFQD TLKRGLELLE KQLIRLKGNC LNGEIAFNLY DTYGFPFELT QDVCLKRGIH 

       430        440        450        460        470        480 
VDQEGFDQAM LTQKKYTKEL NKFDISYEKL SLCNVSSIFV GYDKLICKSR VMALFQNNKS 

       490        500        510        520        530        540 
INKIYTKEEG IVILNNTPFY GESGGQIGDC GQLNTISGFF QVSNTKKYGQ TIGHLGIVNS 

       550        560        570        580        590        600 
GTISVGEEIV AQVDQHKRKC ISLNHSATHL LRAALSQVLG SHVTQKGSLV NDRYLRFDFY 

       610        620        630        640        650        660 
HHATMTTTQM NTVENIVNEQ IWKNAPITVD VMPIELARNS GAVILINKQY DKKVRVLKIG 

       670        680        690        700        710        720 
NFSTELCGGT HAEHTGEIGV FMITKECSIA AGIRRVEAVT NNVALSAIHQ YKMLLKNIFQ 

       730        740        750        760        770        780 
STQSDDKNIL SKIHEFKCRY QKLEKEIDTL RNQQIIQQSL SFIKDVYYIK DVRILVKQVV 

       790        800        810        820        830        840 
NMTSKTLFNM TDCIKHQLKS GVIVLINLNT NKKINLVVAV TKDLIERNRI NALSLVHYII 

       850        860        870 
KILGGKGGGR PDFAQAGINN MATTSKISIE VNSLLHNIL

« Hide

References

[1]"Genome sequence of Blochmannia pennsylvanicus indicates parallel evolutionary trends among bacterial mutualists of insects."
Degnan P.H., Lazarus A.B., Wernegreen J.J.
Genome Res. 15:1023-1033(2005) [PubMed: 16077009] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BPEN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000016 Genomic DNA. Translation: AAZ40814.1.
RefSeqYP_277687.1. NC_007292.1.

3D structure databases

ProteinModelPortalQ493M6.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ493M6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3562669.
GenomeReviewsGene locus BPEN_174 in contig CP000016_GR.
KEGGbpn:BPEN_174.
PATRIC31965243. VBICanBlo110049_0171.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAVILEMES.
PhylomeDBQ493M6.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycCBLO291272:BPEN_174-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_BLOPB
AccessionPrimary (citable) accession number: Q493M6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: September 13, 2005
Last modified: January 25, 2012
This is version 44 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

SIMILARITY comments

Index of protein domains and families

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