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B3H177 (SYA_ACTP7) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. 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:APP7_0694
OrganismActinobacillus pleuropneumoniae serotype 7 (strain AP76) [Complete proteome] [HAMAP]
Taxonomic identifier537457 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

Protein attributes

Sequence length874 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 By similarity 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 – 874874Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347478

Sites

Metal binding5631Zinc Potential
Metal binding5671Zinc Potential
Metal binding6651Zinc Potential
Metal binding6691Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
B3H177 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: 0A1F064F99F7738B

FASTA87496,230
        10         20         30         40         50         60 
MKTTSEIRQS FLDFFHSKGH TVVPSSSLVP ENDPTLLFTN AGMNQFKDVF LGLEKRPYTR 

        70         80         90        100        110        120 
ATTAQRCVRA GGKHNDLENV GYTARHHTFF EMMGNFSFGD YFKHDAIQFG WEYLTSPQWL 

       130        140        150        160        170        180 
GLPKEKLYVT VYETDDEAYD IWNKIVGVPT DHIIRIGDNK GAPYASDNFW AMGDTGPCGP 

       190        200        210        220        230        240 
CTEIFYDHGE TFWGGLPGSP EEDGDRYIEV WNIVFMQFNR LADGTMEKLP KPSVDTGMGL 

       250        260        270        280        290        300 
ERMTAVMQHV NSNYETDIFQ TLIKEVAGLL NVTDLDNKSL RVVADHIRAC SYLIADGVVP 

       310        320        330        340        350        360 
SNEGRGYVLR RIIRRAVRHG NLLGAKEAFF YKLVPTLATV MGHAGEVLTQ KQAHIQKTLK 

       370        380        390        400        410        420 
AEEEQFARTL ERGLALLEDA LTKVENNTLS GEVAFKLYDT YGFPLDLTAD VCREREITID 

       430        440        450        460        470        480 
EAGFEAEMTA QRERAKASSN FGADYNNVIK VEGQTDFIGY DNLAAQATIV GLFSNGKAVD 

       490        500        510        520        530        540 
TIQSGESAVI ILDQTPFYAE MGGQVGDSGL ISTEICNFAV NDTQKYGQVF GHIGQLTSGS 

       550        560        570        580        590        600 
LSIGDKVTAT VDATRRVAIT ANHSATHLLH SALREVLGDH VAQKGSLVSE NILRFDFSQP 

       610        620        630        640        650        660 
EAISKSQLEE IERIVNRKIR ENIQVTIETM DIESAKKKGA MALFGEKYGD VVRVVGMTEF 

       670        680        690        700        710        720 
SIELCGGTHV QRTGDIGLFK LVSEGAVAAG IRRVEAVTAE TAIEWLHNQQ KVLQQSAEFL 

       730        740        750        760        770        780 
KADSNSLVEK IQQLQDKAKR TEKELQQLKD KLAAQAGSEL VKQANKINGV NVVVQKLENV 

       790        800        810        820        830        840 
EVKSLRTMVD DLKNQLESAI VVFGTVADEK VNLIVGVTKD LSSKVNAGEL VGAMAQQVGG 

       850        860        870 
KGGGRADMAM AGGSEPQNLD NALKFAEEWI QAKL

« Hide

References

[1]"Genome and proteome analysis of A. pleuropneumoniae serotype 7."
Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N., Tegetmeyer H., Singh M., Gerlach G.F.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AP76.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001091 Genomic DNA. Translation: ACE61346.1.
RefSeqYP_001968488.1. NC_010939.1.

3D structure databases

ProteinModelPortalB3H177.
ModBaseSearch...

Protein-protein interaction databases

STRINGB3H177.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6396276.
GenomeReviewsGene locus APP7_0694 in contig CP001091_GR.
KEGGapa:APP7_0694.
PATRIC20755007. VBIActPle116979_0714.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG354397.
OMAMFTNSGM.
ProtClustDBPRK00252.

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_ACTP7
AccessionPrimary (citable) accession number: B3H177
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: July 22, 2008
Last modified: January 25, 2012
This is version 27 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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