Skip Header

Contribute Send feedback
Read comments (?) or add your own

A6UUN3 (SYA_META3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. 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:Maeo_0621
OrganismMethanococcus aeolicus (strain Nankai-3 / ATCC BAA-1280) [Complete proteome] [HAMAP]
Taxonomic identifier419665 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

Protein attributes

Sequence length910 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_A

Catalytic activity

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036_A

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00036_A

Subcellular location

Cytoplasm By similarity HAMAP MF_00036_A.

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_A

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 – 910910Alanine--tRNA ligase HAMAP MF_00036_A
PRO_1000074505

Sites

Metal binding6141Zinc By similarity
Metal binding6181Zinc By similarity
Metal binding7181Zinc By similarity
Metal binding7221Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
A6UUN3 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: FC63B7FF19AB9408

FASTA910102,722
        10         20         30         40         50         60 
MEIKHDYNVQ LFKEKGFIRK QCKECNQYFW TLDPKRETCG DSPCDEYSFI GSSITNKEYT 

        70         80         90        100        110        120 
YNEMVKEFLN FFDKNGHTPI KRYPVSARRW RDDILLTIAS IAVFQPWVTK GIVKPVANPL 

       130        140        150        160        170        180 
VIAQPCIRLN DIDNVGRTGR HMTCFTMGGH HAFNTDEDFK YWTDRTVELC YNFFTNLGID 

       190        200        210        220        230        240 
GSSITFIESW WEGGGNAGPC YEVITHGVEL ATLVFMQYEK TEQGDYIEMP LKIVDTGYGL 

       250        260        270        280        290        300 
ERFVWASKGT PTVYEAVFGD IIGKLMDDAN INMNDIGPKI LAESATLAGL MDIENVGDLR 

       310        320        330        340        350        360 
ILRQKVAEKL NLDVNELDSI LSPIENIYAI ADHTRCLAFM LGDGIVPSNV KDGYLARLLV 

       370        380        390        400        410        420 
RKTLRYIKNV GLSLSLKDIV AMQLENLKEI YPELMDMKEY IMDVLEEEEN KYIQTITKGK 

       430        440        450        460        470        480 
GAVERIAKSK DEITLDDLIE LYDSKGLPPE VVRDIVEEIN KKGSKNNKGN KTIKITVPDN 

       490        500        510        520        530        540 
FYTIVAERHE EKKEDSKSEK GENTAEKSTI SINLDDIPET ELLFYSNPYQ KEVEAKILKI 

       550        560        570        580        590        600 
IGNVVILDKT VFYPEGGGQK YDIGLIGNKK IISVQKNNNG IVCHTVENTD GLNEEDTIIA 

       610        620        630        640        650        660 
KLNWENRLNL MRNHTATHII NAAASKVLGK HIWQTGSNVE SNKARLDITH YKRITREEIK 

       670        680        690        700        710        720 
EIEKIANQIV LDAIPVKSTV MGRNEAEQKY GFKIYQGGVV PGNILRILDI EGVDVEACGG 

       730        740        750        760        770        780 
THCQNTSEVG YIKILKTERI QDGVERLEYT SGINSVNEVS LMEDILLNAS SIVGVPCENL 

       790        800        810        820        830        840 
PKTVNRFFEE WKEQKKIIEE LHKKIGELEK GNLNDKFEKV GKYDLLVEKV EGAPKELMSI 

       850        860        870        880        890        900 
ADNLVNEKDN SIVILLNNSG YILCKCGEKV EIKMGELLRK IAKGGGKDKM AQGKCADDIE 

       910 
TLKSKVVGEL 

« Hide

References

[1]"Complete sequence of Methanococcus aeolicus Nankai-3."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A. expand/collapse author list , Sieprawska-Lupa M., Whitman W.B., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Nankai-3 / ATCC BAA-1280.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000743 Genomic DNA. Translation: ABR56205.1.
RefSeqYP_001324817.1. NC_009635.1.

3D structure databases

ProteinModelPortalA6UUN3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6UUN3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5327332.
GenomeReviewsGene locus Maeo_0621 in contig CP000743_GR.
KEGGmae:Maeo_0621.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04130.
HOGENOMHBG392147.
OMAMFTNSGM.
ProtClustDBPRK13902.

Enzyme and pathway databases

BioCycMAEO419665:MAEO_0621-MONOMER.

Family and domain databases

HAMAPMF_00036_A. Ala_tRNA_synth_A.
[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.
IPR022429. Ala-tRNA_synth_arc.
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.
TIGRFAMsTIGR03683. A-tRNA_syn_arch. 1 hit.
TIGR00344. AlaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_META3
AccessionPrimary (citable) accession number: A6UUN3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 21, 2007
Last modified: January 25, 2012
This is version 35 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