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B1WYQ5 (SYA_CYAA5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 29. 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:cce_1722
OrganismCyanothece sp. (strain ATCC 51142) [Complete proteome] [HAMAP]
Taxonomic identifier43989 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Chroococcales › Cyanothece

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

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 – 879879Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347578

Sites

Metal binding5641Zinc Potential
Metal binding5681Zinc Potential
Metal binding6661Zinc Potential
Metal binding6701Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
B1WYQ5 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: D478C2DD4499FB14

FASTA87997,796
        10         20         30         40         50         60 
MTTTAPFLTG NQIRDRFLQF YAQHNHQILP SASLVPEDPT VLLTIAGMLP FKPIFLGQKQ 

        70         80         90        100        110        120 
PDFPRATTSQ KCIRTNDIEN VGRTARHHTF FEMLGNFSFG DYFKEQAIKW AWELSTKVYR 

       130        140        150        160        170        180 
LPPENIVVSV FEKDDEAFKL WEEMIGIPPQ RIKRMGEKDN FWKAGPTGPC GPCSELYYDF 

       190        200        210        220        230        240 
HPELGEDNID LEDDSRFIEF YNLVFMEYNR DAEGNLAPLQ NKNIDTGMGL ERMAQILQKV 

       250        260        270        280        290        300 
PNNYETDLIF PIIETAANIA NIDYQKATEK TKVSLKVIGD HVRSVVHMIA DGITASNTDR 

       310        320        330        340        350        360 
GYVLRRLIRR VVRHGRLIGI EGQFIKQVAE TAIELSENAY PQVRERESFI KGELEREETA 

       370        380        390        400        410        420 
FLKTLERGEK LLAEIIEKTE TQGQISGVDA FTLYDTYGFP LELTQEIAEE SNLTVNIEEF 

       430        440        450        460        470        480 
EAEMRQQQER SKAAHETIDL TVQGSLDKLA EHIHPTAFLG YTDLQLTAKV EAVLIQGKTV 

       490        500        510        520        530        540 
DTAEAGSEVQ IVLDQTPFYG ESGGQIGDRG FLTGENLVIR VEDVQKESGI FVHFGRVERG 

       550        560        570        580        590        600 
SVSVNDQVTA TIDRACRRQV QANHTATHLL QAALKKVVDK SISQAGSLVA FDRLRFDFNC 

       610        620        630        640        650        660 
PRAVTSEELQ EIEDLINTWI AEAHETEIAV MPIETAKEKG AIAMFGEKYG SEVRVIDVPG 

       670        680        690        700        710        720 
VSMELCGGTH VKNTAEIGLF KIMSESGISS GVRRIEAVAG PAVLEYLKVR ETVVKDLCDR 

       730        740        750        760        770        780 
FKIKPEEISD RITTLQSELK TTQKELEAVK QDLAVAKSDQ LLTEAESIGE FKLLVSDMGE 

       790        800        810        820        830        840 
MDAKALQTAA ERLQQKLGEG AVILGSIPSE GKVSLVAAFS KKVNQEKQLQ AGKFIGQIAK 

       850        860        870 
ICGGGGGGRP NLAQAGGREP SKLSEALLTA KEQLTESLK

« Hide

References

[1]"The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium important in the marine nitrogen cycle."
Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C., Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., Ghosh B.K., Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.
Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008) [PubMed: 18812508] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51142.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000806 Genomic DNA. Translation: ACB51072.1.
RefSeqYP_001803138.1. NC_010546.1.

3D structure databases

ProteinModelPortalB1WYQ5.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1WYQ5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6168771.
GenomeReviewsGene locus cce_1722 in contig CP000806_GR.
KEGGcyt:cce_1722.
PATRIC21541903. VBICyaSp130209_1781.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG354397.
OMAGESKTDQ.
PhylomeDBB1WYQ5.
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_CYAA5
AccessionPrimary (citable) accession number: B1WYQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 29 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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