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A2BN65 (SYA_HYPBU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 34. 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:Hbut_1607
OrganismHyperthermus butylicus (strain DSM 5456 / JCM 9403)
Taxonomic identifier415426 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Pyrodictiaceae › Hyperthermus

Protein attributes

Sequence length921 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
Reference 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 – 921921Alanine--tRNA ligase HAMAP MF_00036_A
PRO_0000347880

Sites

Metal binding6021Zinc By similarity
Metal binding6061Zinc By similarity
Metal binding7061Zinc By similarity
Metal binding7101Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
A2BN65 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: BB7F569DDD503717

FASTA921104,001
        10         20         30         40         50         60 
MKLDPKVYQL EFFREKGFTR KQCRVCGEYF WTLNPDQEHC NDAPCVEYYF WELPRVRGLS 

        70         80         90        100        110        120 
VRDARRKFIE FFKRHGHEYV EPRPVVARWR EDLYLTIASI VAFQPHVTSG IVPPPANPLV 

       130        140        150        160        170        180 
IVQPCIRLED IDFVGLTIGR HLTSFEMGGH HAFNYPDKTV YWKEETVRFA FEFFTKELGI 

       190        200        210        220        230        240 
PEDMVTFKES WWEGGGNAGP SFEVTVGGLE LATLVFMQYR VVDGKYEPMD IRVVDTGYGI 

       250        260        270        280        290        300 
ERIAWFSQDV PTAFHAIYGE LLDEFRKLLG VAEPPRELLW GAARAAGRLD PEDPESVERY 

       310        320        330        340        350        360 
YQVVAERAGL SIREARELLG REAALYTLLD HTKTIALMLG DGIVPSNTGE GYLARLVIRR 

       370        380        390        400        410        420 
ALRTLRRLGA DIELAVLVER QARYWGADYY PRLLSHLDYI LRVVRLEEER YSKTLERGLR 

       430        440        450        460        470        480 
EVTKLLKRKK KLSIDDLITL YDSHGVPPDM VAEAASKLGV NVDVPHNFYA LVAKKHGASG 

       490        500        510        520        530        540 
AVAREVEEKP KLPRDIEEWA RGFPATRRLF HENPYAREFT ANLLGVRGSH VILDATLFYP 

       550        560        570        580        590        600 
TGGGQLHDTG VLRLCGEEYR VLRVEKVGDV VVHVLDREPS CSSGEAWGRI DWDRRYRLMR 

       610        620        630        640        650        660 
HHTAVHVLLG AARRVLGDHV WQAGAEKTPE KARLDITHYE LPSREEIRKI EELANSAILA 

       670        680        690        700        710        720 
RIHVDIEEID RNTAEKLYGF RIYQGGVPMT PRLRIVRIGD WDVEACFGTH VANTAEIGAI 

       730        740        750        760        770        780 
KIVNVEKLQD GVVRFEIVAG SEVARYAASL EDKLDTIASI VGGGRGEAVK RVEKLAEELK 

       790        800        810        820        830        840 
EAKRQVSRLR SFLADMLVKS VKATAKSIDG VKVYVMTEEL PDENIYREVM LKLSREEPDS 

       850        860        870        880        890        900 
ITIAVIRRGE DLLMEIGAGS KAAKRVDLRA VAKQLASKGL RGGGKPSHIT LYGRGLAEKA 

       910        920 
SKVASEVVEV IASLVSRAGT A

« Hide

References

[1]"The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C."
Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M., She Q., Garrett R.A., Klenk H.-P.
Archaea 2:127-135(2007) [PubMed: 17350933] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 5456 / JCM 9403.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000493 Genomic DNA. Translation: ABM81426.1.
RefSeqYP_001013771.1. NC_008818.1.

3D structure databases

ProteinModelPortalA2BN65.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2BN65.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4781445.
GenomeReviewsGene locus Hbut_1607 in contig CP000493_GR.
KEGGhbu:Hbut_1607.

Phylogenomic databases

eggNOGarNOG04130.
HOGENOMHBG392147.
OMAMFTNSGM.
PhylomeDBA2BN65.
ProtClustDBPRK13902.

Enzyme and pathway databases

BioCycHBUT415426:HBUT_1607-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.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR012947. tRNA_SAD.
[Graphical view]
KOK01872.
PANTHERPTHR11777:SF6. PTHR11777:SF6. 1 hit.
PfamPF01411. 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_HYPBU
AccessionPrimary (citable) accession number: A2BN65
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: February 20, 2007
Last modified: January 25, 2012
This is version 34 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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