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Q9UY36 (SYA_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 77. 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:PYRAB16720
ORF Names:PAB1245
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length914 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 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 – 914914Alanine--tRNA ligase HAMAP MF_00036_A
PRO_0000075271

Sites

Metal binding6131Zinc By similarity
Metal binding6171Zinc By similarity
Metal binding7171Zinc By similarity
Metal binding7211Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9UY36 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: C4B449FE9E03B4E1

FASTA914104,858
        10         20         30         40         50         60 
MEFIMKTRMF EEEGWIRKKC KVCGKPFWTL DPDRETCGDP PCDEYQFIGK PGIPKKYTLD 

        70         80         90        100        110        120 
EMREKFLKFF EKHEVYPHGR VKRYPVLPRW RDDVLLVGAS IMDFQPWVIS GEADPPANPL 

       130        140        150        160        170        180 
VISQPSIRFT DIDNVGITGR HFTIFEMMAH HAFNYPGKPI YWIDETVELA FEFFTKELKM 

       190        200        210        220        230        240 
KPEDITFKEN PWAGGGNAGP AFEVLYRGLE VATLVFMQYK KAPENAPEDQ VVIIKGDRYV 

       250        260        270        280        290        300 
PMETKVVDTG YGLERLVWMS QGTPTAYDAV LGYVVEPLKR MAGVEKIDER ILMENSRLAG 

       310        320        330        340        350        360 
MFDIEDMGDL KLLRKKVAEK VGISVEELEK AIRPYELIYA IADHTKALTF MLADGVIPSN 

       370        380        390        400        410        420 
VKAGYLARLL IRKSIRHLKE LGLEVPLSEI VALHIKELHK TFPEFKEMED VILEIIDLEE 

       430        440        450        460        470        480 
KKYSETLKRG SDLVRREIAK LKKKGMSEIP LEKLITFYES HGLTPELVKE IAEKEGIKVH 

       490        500        510        520        530        540 
VPDNFYSIVA KEAEKEKEEK EEEVVDFELV KDLPETRTLY YEDPFMKEFE ARVLRVIGDW 

       550        560        570        580        590        600 
IVLDQTAFYP EGGGQPYDTG VLFVNGSEVK VTNVQKVGKV IVHKVENPGL FKEGMEVRGR 

       610        620        630        640        650        660 
IDWDRRIQHM RHHTGTHVLM GALVRVLGKH VWQAGSQLTT DWARLDISHY KRISDEELRE 

       670        680        690        700        710        720 
IERLANRIVM EDRKVTWEWL PRTEAEQRYG FRLYQGGVVP GRVIRVVKIE DWDVQACGGT 

       730        740        750        760        770        780 
HLPSTGLVGP IKILRTERIQ DGVERIIFAC GEAAIKEWQK EREILKKASQ VLRVPPEKLP 

       790        800        810        820        830        840 
ETAERFFNEW KEARKEVEKL KKELAKLLVY ELEAKVQKVK EYEFIGEIVE GSMDDLREAV 

       850        860        870        880        890        900 
ERLKKPNRIV VLVSKEGYFA ISVGDNVNLN ANDLAKKLTS IAGGGGGGRK DVAQGRIKDV 

       910 
SKAKEAIESI VKLL 

« Hide

References

[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed: 12622808] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ248288 Genomic DNA. Translation: CAB50576.1.
PIRB75017.
RefSeqNP_127346.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9UY36.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBPYRT00000003041; EBPYRP00000002972; EBPYRG00000003041.
GeneID1495969.
GenomeReviewsGene locus PYRAB16720 in contig AL096836_GR.
KEGGpab:PAB1245.
NMPDRfig|272844.1.peg.1779.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000022658.
HOGENOMHBG392147.
OMAMFTNSGM.
PhylomeDBQ9UY36.
ProtClustDBPRK13902.

Enzyme and pathway databases

BioCycPABY272844:PAB1245-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_PYRAB
AccessionPrimary (citable) accession number: Q9UY36
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: January 25, 2012
This is version 77 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