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B1W3I1 (SYA_STRGG) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. 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:SGR_6034
OrganismStreptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350) [Complete proteome] [HAMAP]
Taxonomic identifier455632 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length889 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 – 889889Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347831

Sites

Metal binding5731Zinc Potential
Metal binding5771Zinc Potential
Metal binding6751Zinc Potential
Metal binding6791Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
B1W3I1 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 4C7FE94F80C9944F

FASTA88995,304
        10         20         30         40         50         60 
MESAEIRRRW LSFFEERGHT AVPSASLIAD DPTLLLVPAG MVPFKPYFLG EVKPPAPRVT 

        70         80         90        100        110        120 
SVQKCVRTPD IEEVGKTTRH GTFFQMCGNF SFGDYFKEGA IQLAWEALTN SVEDGGYGLD 

       130        140        150        160        170        180 
PEKLWITVYL DDDEAEQIWR DKIGVPAERI QRLGKKDNFW SMGVPGPCGP CSEINYDRGP 

       190        200        210        220        230        240 
EFGVEGGPAV NDERYVEIWN LVFMQYERGA GDGKEDFPIL GDLPSKNIDT GLGLERLAMI 

       250        260        270        280        290        300 
LQGVQNMYET DTLRVVMDKA TELTGVRYGA ENSTDVSLRV VADHIRTSVM LIGDGVTPGN 

       310        320        330        340        350        360 
EGRGYVLRRI MRRAIRNMRL LGATGTVVKD LIDVVIDTMG QQYPELITDR KRIETVALAE 

       370        380        390        400        410        420 
EAAFLKALKG GTNILETAVT ETKAAGGQVL AGDKAFLLHD TWGFPIDLTL EMAAEQGLSV 

       430        440        450        460        470        480 
DEDGFRRLMQ EQRDKAKADA RAKKTGHADL SAYREVADTA GATEFTGYAS LAGESTIVGL 

       490        500        510        520        530        540 
LVDGVPSPAA TEGDEVEVVL DRTPFYAEGG GQLADTGRIR LDTGAVIEVR DVQKPVPGVH 

       550        560        570        580        590        600 
VHKGVVQVGE VTVGAPVFAS IDATRRRAIA RAHSATHLTH QALRDALGPT AAQAGSENSP 

       610        620        630        640        650        660 
GRFRFDFGSP AAVPGTVLTD VEQRINEVLS RELDVQAEVM SIDEAKKQGA IAEFGEKYGE 

       670        680        690        700        710        720 
RVRVVTIGDF SKELCGGTHV GNTAQLGLVK LLGESSIGSG VRRIEALVGV DAYNFLAKEH 

       730        740        750        760        770        780 
TVVAQLQELV KGRPEELPEK IAGMLGKLKD AEKEIEKFRA EKVLAAAAGL VESAKDVRGT 

       790        800        810        820        830        840 
ALVTGQVPDG TSADDLRKLV LDVRGRIQGG RPAVVALFTT ANGRPLTVIA TNEAARERGL 

       850        860        870        880 
KAGDLVRTAA KTLGGGGGGK PDVAQGGGTN PAAIGDAVAA VERLVTETA

« Hide

References

[1]"Genome sequence of the streptomycin-producing microorganism Streptomyces griseus IFO 13350."
Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H., Yamashita A., Hattori M., Horinouchi S.
J. Bacteriol. 190:4050-4060(2008) [PubMed: 18375553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 4626 / NBRC 13350.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP009493 Genomic DNA. Translation: BAG22863.1.
RefSeqYP_001827546.1. NC_010572.1.

3D structure databases

ProteinModelPortalB1W3I1.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1W3I1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6209909.
GenomeReviewsGene locus SGR_6034 in contig AP009493_GR.
KEGGsgr:SGR_6034.
PATRIC23758909. VBIStrGri32265_6186.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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_STRGG
AccessionPrimary (citable) accession number: B1W3I1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 28 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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