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A4X5Z0 (SYA_SALTO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:Strop_1828
OrganismSalinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440) [Complete proteome] [HAMAP]
Taxonomic identifier369723 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicromonosporineaeMicromonosporaceaeSalinispora

Protein attributes

Sequence length892 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 – 892892Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347776

Sites

Metal binding5801Zinc Potential
Metal binding5841Zinc Potential
Metal binding6821Zinc Potential
Metal binding6861Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
A4X5Z0 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 9A52DEBDA6EC954B

FASTA89296,214
        10         20         30         40         50         60 
MKTAEIRRRY LAHFEANGHA VVPSAPLPAI SDPNLLFVAA GMMQFVPYFL GQQTAPYKRA 

        70         80         90        100        110        120 
VSVQKCLRTP DIDEVGKTSR HGTFFQMNGN FSFGDYFKDE AIPLAWELST KPVDAGGLGL 

       130        140        150        160        170        180 
DPDRIWPTVY LDDDEAFQIW RSVGVPADRI VRRGKADNFW SMGIPGPCGP CSELFYDRGP 

       190        200        210        220        230        240 
EYGREGGPEV DEDRYLEFWN LVFMQFERGP GTGKEDYPIL GDLPAKNIDT GMGLERMASI 

       250        260        270        280        290        300 
LQGVDNLYEI DEVRPILAKA AELTGKRYGA HSGQVASESH PDDVRLRVVA DHVRTALMLI 

       310        320        330        340        350        360 
GDGVIPSNEG RGYVLRRIMR RAIRSIRLLG WQERAMPELL PVARDCMSAS YPELATDFGR 

       370        380        390        400        410        420 
IADYAYAEED AFLSTLRAGT TILDTAIAET RTAGRRAISG AKAFQLHDTY GFPIDLTLEI 

       430        440        450        460        470        480 
ASEQGLQVDA EGFRRLMADQ RARAKADAQA RKTGHVDLSA YRTVLDEGGP VTFTGYQEVS 

       490        500        510        520        530        540 
RESTVRAVLG AASPHAAAVE GETVELVLDT TPFYAEGGGQ QPDLGVITVG GGQVEVLDVQ 

       550        560        570        580        590        600 
QPVPGLIVHR ARVLRGEVRV GETGFAEIDT DRRRAISRSH TATHLVHQTM RNFLGESATQ 

       610        620        630        640        650        660 
AGSLNAPGRL RFDFNTPTGV APSVLRDVEQ QVNEALLADL EVRAFVTSLA EARRIGAMAL 

       670        680        690        700        710        720 
FGEKYGEQVR VVEVGDYARE LCGGTHVGRS GQLGLVKILS ESSIGSGVRR VEALVGIDAF 

       730        740        750        760        770        780 
NFLAREHLLV ARLAELYRVP SDQVAERVEQ TVTQLRDAEK ELEKLRAQLV LGGAAALAAQ 

       790        800        810        820        830        840 
ASEVRGVAYV GTEAPEGAAG NDVRTLAQEI RSRIDPARPA VVAVAARANG KASLVVAVNP 

       850        860        870        880        890 
AARSQGLSAA DLVKVAFAGR GGGSPELAQG GGLPAAEAPG LLRTVENAIA GA 

« Hide

References

[1]"Complete sequence of Salinispora tropica CNB-440."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sun H., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Jensen P.R., Moore B.S., Udwary D.W., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-916 / DSM 44818 / CNB-440.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000667 Genomic DNA. Translation: ABP54290.1.
RefSeqYP_001158668.1. NC_009380.1.

3D structure databases

ProteinModelPortalA4X5Z0.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4X5Z0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5058287.
GenomeReviewsGene locus Strop_1828 in contig CP000667_GR.
KEGGstp:Strop_1828.
PATRIC23442660. VBISalTro43511_1876.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAGESKTDQ.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycSTRO369723:STROP_1828-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.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
KOK01872.
PANTHERPTHR11777:SF6. PTHR11777:SF6. 1 hit.
PfamPF01411. 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_SALTO
AccessionPrimary (citable) accession number: A4X5Z0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: May 29, 2007
Last modified: January 25, 2012
This is version 38 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