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Q9Y9X3 (SYA_AERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 74. 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:APE_2166
OrganismAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) [Complete proteome] [HAMAP]
Taxonomic identifier272557 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Aeropyrum

Protein attributes

Sequence length900 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 – 900900Alanine--tRNA ligase HAMAP MF_00036_A
PRO_0000075259

Sites

Metal binding5871Zinc By similarity
Metal binding5911Zinc By similarity
Metal binding6911Zinc By similarity
Metal binding6951Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Y9X3 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 4602BC9B249C4C04

FASTA900102,333
        10         20         30         40         50         60 
MGFVRKEGAR CREAFWTLNP EFSEPQDTPC VEYWFDKVKS VSGMSVGEAR EAFLSFFEKH 

        70         80         90        100        110        120 
GHTRVPPRPV VARWREDLYL TIASIVVFQP HVTSGLVPPP ANPLVISQPS IRLEDIDNVG 

       130        140        150        160        170        180 
ITIGRHLTSF EMAAHHAFNY PDRQVYWKEE TVRLAFEFFT QVLGIPPELI VFKESWWEGG 

       190        200        210        220        230        240 
GNAGPSFEVA VGGLELATLV FMKYRVVDGR YEEIPLKIVD TGYGVERLAW FTQKTPTAFH 

       250        260        270        280        290        300 
AIYGSLVDDF RRMLGVEKPD ENVMWAAFRV AGFLDPEDPE SLRNYYQTVA SLAGGDVETV 

       310        320        330        340        350        360 
RSILTREARL YSVLDHTKTI ALMLGDGIVP SNSGEGYLAR LVVRRALRQL SLLNAEVPLV 

       370        380        390        400        410        420 
DLVERQARFW MRDFPQLKEN LDYILDAVSL EEERFRDVLR KARSIVEREL KRKKRLGVDD 

       430        440        450        460        470        480 
LIRLYDSMGV PPEIAAEIAA SRGAPVEVPH NFYSLVAARH RGPEKIRGYG FDETGLPRDV 

       490        500        510        520        530        540 
EEWARRFGET RRVFHEDPYA KAWKARVLGV KGRYLVADST IFYPTGGGQI HDTGVIRVNN 

       550        560        570        580        590        600 
QQYRIIDVQK VGDAIVHVAE REIAAEPGDE VWMEIDWERR YSIMRHHTVT HVLIAAARRV 

       610        620        630        640        650        660 
LGRHAWQAGA EKTEEKGRLD ITHHRPLTRD DIEKLENVVN QVIRERRRVW EDMVDKNEAE 

       670        680        690        700        710        720 
EKYGFTIYQG GVPMEKRLRL VFVEDWDVEA CFGTHVRNTG EIGGFKIISY SRIQDGVVRL 

       730        740        750        760        770        780 
EYVAGDRVAI YARELEERLA RIGDAVKAPR GQEEARVKGL IASLEQARED LKRYRDYWVK 

       790        800        810        820        830        840 
TIEEAYISRA RRVNGVKVLA VESLEKDRRT VQEILRKLTS RHEDLIAALV VENEGNTQVE 

       850        860        870        880        890        900 
IAAGPKAAEK VDLGALVKIV IKKVGGRGGG RGSYASLRVE GRLSADKVEE LLADALENVL

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000002 Genomic DNA. Translation: BAA81177.1.
PIRA72524.
RefSeqNP_148431.1. NC_000854.2.

3D structure databases

ProteinModelPortalQ9Y9X3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1445236.
GenomeReviewsGene locus APE_2166 in contig BA000002_GR.
KEGGape:APE_2166.
NMPDRfig|272557.1.peg.1539.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG392147.
OMAMFTNSGM.
PhylomeDBQ9Y9X3.
ProtClustDBPRK13902.

Enzyme and pathway databases

BioCycAPER272557:APE2166-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_AERPE
AccessionPrimary (citable) accession number: Q9Y9X3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: January 25, 2012
This is version 74 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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