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A6VKD6 (SYA_ACTSZ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. 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:Asuc_0052
OrganismActinobacillus succinogenes (strain ATCC 55618 / 130Z) [Complete proteome] [HAMAP]
Taxonomic identifier339671 [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_0000347479

Sites

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

Sequences

Sequence LengthMass (Da)Tools
A6VKD6 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: BD1EF118813B3295

FASTA87496,045
        10         20         30         40         50         60 
MKTTAEIRQS FLDFFHSKGH QVVESSSLVP ENDPTLLFTN AGMNQFKDVF LGMDKRPYSR 

        70         80         90        100        110        120 
ATTAQRCVRA GGKHNDLENV GYTARHHTFF EMMGNFSFGD YFKYDAINFA WEFLTSPKWL 

       130        140        150        160        170        180 
ALPKEKLYVT VYETDDEAYD IWNKEVGVPQ EHIIRIGDNK GAPYASDNFW AMGDTGPCGP 

       190        200        210        220        230        240 
CTEIFYDHGD HIWGGLPGTP EEDGDRYIEI WNIVFMQFNR LADGTMEKLP KPSVDTGMGL 

       250        260        270        280        290        300 
ERMTAVLQHV NSNYEIDIFQ TLIKKVAEIV GTTDLGNKSL RVIADHIRSC AYLIADGVIP 

       310        320        330        340        350        360 
SNEGRGYVLR RIIRRAVRHG HLLGAKETFF YKLVPTLIEV MAEAGKQVKE KQANVEKLLR 

       370        380        390        400        410        420 
LEEEQFARTL ERGLILLDAE LANVKNGVLS GEVAFKLYDT YGFPLDLTAD VCRERNIAVD 

       430        440        450        460        470        480 
ENGFDKEMEA QRLRAQSASN FGMDYTSIIR VDGETKFEGY TNVESLAKVT ALFRDGKAVE 

       490        500        510        520        530        540 
SVSAGQSAVV ILENTPFYAE MGGQIGDSGM LTANGLHFDV KDTQKYGQVF GHIGELTQGT 

       550        560        570        580        590        600 
LSVGQIVNAQ VDAQRRQYTK LNHSATHLLH AALRQVLGEH VAQKGSLVSD VGLRFDFVQP 

       610        620        630        640        650        660 
EAVTKEQIME IERLVNFHIR ANHPVLTEEM GVAEAKSKGA IALFGEKYGE TVRVVTMSPF 

       670        680        690        700        710        720 
SIELCGGLHV ERTGEIGLLK IISEGAVAAG IRRVEAVTGE EAINWLFNQQ TILAQSADLL 

       730        740        750        760        770        780 
KSDIPSLPEK IIQLQDKVKK TEKELQQLKE KAAMQAGSDL AKSAVKINGV SVVTHQLDGA 

       790        800        810        820        830        840 
DAKVLRVMVD DLKNQLGSAV IALGSASGGK VNLIAGVTAD LTAKVKAGEL VNVMAQQVGG 

       850        860        870 
KGGGRPDMAM AGGSQPENLS AALIVASDWL KTMI

« Hide

References

[1]"Complete sequence of Actinobacillus succinogenes 130Z."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Vieille C., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 55618 / 130Z.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000746 Genomic DNA. Translation: ABR73433.1.
RefSeqYP_001343368.1. NC_009655.1.

3D structure databases

ProteinModelPortalA6VKD6.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6VKD6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5348995.
GenomeReviewsGene locus Asuc_0052 in contig CP000746_GR.
KEGGasu:Asuc_0052.
PATRIC20758248. VBIActSuc117883_0058.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAGESKTDQ.
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_ACTSZ
AccessionPrimary (citable) accession number: A6VKD6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: August 21, 2007
Last modified: January 25, 2012
This is version 37 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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