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A5FXC2 (SYA_ACICJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 36. 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:Acry_1038
OrganismAcidiphilium cryptum (strain JF-5) [Complete proteome] [HAMAP]
Taxonomic identifier349163 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcidiphilium

Protein attributes

Sequence length878 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 – 878878Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347468

Sites

Metal binding5641Zinc Potential
Metal binding5681Zinc Potential
Metal binding6731Zinc Potential
Metal binding6771Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
A5FXC2 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 1FC00F031C6DB515

FASTA87894,424
        10         20         30         40         50         60 
MTSSNDIRAT FLDFFARNGH EVVPSAPLVP RNDPTLMFVN AGMVPFKNVF TGHEHRPYVR 

        70         80         90        100        110        120 
AASSQKCVRA GGKHNDLDNV GYTARHHTFF EMLGNFSFGD YFKDVAIENA WTLLTRDFGL 

       130        140        150        160        170        180 
PKEKLLVTVY HEDDEAASLW KRIAGLPDEK IIRIATDDNF WRMGDTGPCG PCSEIFYDHG 

       190        200        210        220        230        240 
PSIPGGPPGS PDEDGDRFIE IWNLVFMQFL EEPAGVRNPL PRPSIDTGMG LERFAAILQG 

       250        260        270        280        290        300 
KHDNYDTDTL RALILASAEV SHTDPDGAHK VSHRVIADHL RATSFLIADG VLPSNEGRGY 

       310        320        330        340        350        360 
VLRRIMRRAM RHAHRLGMRE PFIYRLVPAL TRQMGVAFPE LPRAEALIVE TLKLEEQKFA 

       370        380        390        400        410        420 
VMLERGLSLL EDEVQKLGSG EKLPGAVAFK LYDTYGFPLD LTEDALREQH RGLDHEGFTA 

       430        440        450        460        470        480 
SMAEQKARAR AAWAGSGDAA TETVWLDLRD RLGGTEFLGY STEESDASIL AVVVNGAPAG 

       490        500        510        520        530        540 
RAEAGQEVAL ILNQTPFYAE SGGQVGDTGT LTAPGVTIRV TDTQKKAGDL FVHYGTIEEG 

       550        560        570        580        590        600 
EIAPGNSVHA EVDHARRGAI RAHHSATHLL HEALRRALGP HVTQKGSLNA PDRLRFDISQ 

       610        620        630        640        650        660 
PRPVTGAELR AVEREVNARI RENAAVETRL MTPDEAVKRG AMALFGEKYG DEVRVVSMGA 

       670        680        690        700        710        720 
GDAGRSAYSI ELCGGTHVAR TGDIGAFRIL AESGVAAGIR RIEAVTGEAA LAATEAETDL 

       730        740        750        760        770        780 
LEEAAAALKV APAELPARIA ALLEEKKRFE RQVAELQRKL ATGGAAAEIE EVAGIKFAAR 

       790        800        810        820        830        840 
NLGEVSPRDL KSLADSILKS MGSGIAALVS TAESKASIVV AVSPDLTSAN NAVTLVQAAS 

       850        860        870 
GVVGGKGGGG RPDMAQAGGP DASKADEALA AVRALIKP 

« Hide

References

[1]"Complete sequence of chromosome of Acidiphilium cryptum JF-5."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JF-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000697 Genomic DNA. Translation: ABQ30254.1.
RefSeqYP_001234173.1. NC_009484.1.

3D structure databases

ProteinModelPortalA5FXC2.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5FXC2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5160168.
GenomeReviewsGene locus Acry_1038 in contig CP000697_GR.
KEGGacr:Acry_1038.
PATRIC20647076. VBIAciCry6074_1530.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAGESKTDQ.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycACRY349163:ACRY_1038-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.
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_ACICJ
AccessionPrimary (citable) accession number: A5FXC2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: June 12, 2007
Last modified: January 25, 2012
This is version 36 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