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A4SS99 (SYA_AERS4) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:ASA_3811
OrganismAeromonas salmonicida (strain A449) [Complete proteome] [HAMAP]
Taxonomic identifier382245 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Aeromonadales › Aeromonadaceae › Aeromonas

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_0000347481

Sites

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

Sequences

Sequence LengthMass (Da)Tools
A4SS99 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: D25D68EE224BA3F1

FASTA87495,779
        10         20         30         40         50         60 
MYMSTSEIRA AFLEYFRSQG HQVVSSSSLV PHNDPTLLFT NAGMNQFKDV FLGADKRAYN 

        70         80         90        100        110        120 
RATTSQRCVR AGGKHNDLEN VGYTARHHTF FEMLGNFSFG DYFKQDAIRF AWEFLTGTLK 

       130        140        150        160        170        180 
LPKERLLVTV YETDDEAFNI WANEVGVPVE RIVRIGDNKG AAFASDNFWQ MSDTGPCGPC 

       190        200        210        220        230        240 
TEIFYDHGDH IWGGPPGSPE EDGDRFIEIW NVVFMQFNRQ ADGTMEPLPR PSVDTGMGLE 

       250        260        270        280        290        300 
RISAIMQGVH SNYEIDIFQA LIKKAAEIVG TTDLSNQSLR VIADHIRSCA FLIADGVMPS 

       310        320        330        340        350        360 
NEGRGYVLRR IIRRAVRHGR KLGATDVFFY KLAAELAVQM KDVGAELIAQ LPLVKRVLRI 

       370        380        390        400        410        420 
EEEQFVRTLD RGLLLLEDVL ANLGDAKVIP GEVVFKLYDT YGFPADLTAD VVREREIGID 

       430        440        450        460        470        480 
EEGFNAEMEK QRARAKEASS FGVNYNEVLK LDFETPFTGY KQLSQKTSVV GIYKDGVEVN 

       490        500        510        520        530        540 
GLIAGEEAVV VLAETPFYAE SGGQVGDCGV LKVDDGIFAV TDTQKAGKAI IHKGYLELGT 

       550        560        570        580        590        600 
LEKGALVEAV VDGERRQAVA LNHSVTHLLH AALRQALGDH VTQKGSLVGA ERMRFDFSHF 

       610        620        630        640        650        660 
EGLTMATIRR VEELVNAQIR ANHDIATQVM DLEAAKSAGA MALFGEKYED DVRVVRMGDY 

       670        680        690        700        710        720 
STELCGGTHA KRTGDIGFFK IIAESGIAAG VRRIEAVTGK GAIDFMHQMG EQIEEAAALV 

       730        740        750        760        770        780 
KGDQFSIADK VRQILDKSKM MERELEQLKA KLAAQAGSDL LSQVIEINGQ KVLIAALEGA 

       790        800        810        820        830        840 
DPKSLRGMLD ELKNRMKSGV VLLATSSDDK VNLIAGVTSD LTGKVKAGEL VNLVAQQVGG 

       850        860        870 
KGGGRPDMAQ AGGTQPEAVP AALQSVHSWL EERL

« Hide

References

[1]"The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into the evolution of a fish pathogen."
Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C., Brown L.L.
BMC Genomics 9:427-427(2008) [PubMed: 18801193] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A449.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000644 Genomic DNA. Translation: ABO91771.1.
RefSeqYP_001143519.1. NC_009348.1.

3D structure databases

ProteinModelPortalA4SS99.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4SS99.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4997680.
GenomeReviewsGene locus ASA_3811 in contig CP000644_GR.
KEGGasa:ASA_3811.
PATRIC20794064. VBIAerSal2987_3787.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAGESKTDQ.
PhylomeDBA4SS99.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycASAL382245:ASA_3811-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_AERS4
AccessionPrimary (citable) accession number: A4SS99
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: May 15, 2007
Last modified: January 25, 2012
This is version 41 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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