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Q6AFA1 (SYA_LEIXX) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. 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:Lxx10910
OrganismLeifsonia xyli subsp. xyli (strain CTCB07) [Complete proteome] [HAMAP]
Taxonomic identifier281090 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrobacteriaceaeLeifsonia

Protein attributes

Sequence length885 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 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 – 885885Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000075135

Sites

Metal binding5721Zinc Potential
Metal binding5761Zinc Potential
Metal binding6751Zinc Potential
Metal binding6791Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q6AFA1 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 9FC15F35FE43F6EA

FASTA88594,580
        10         20         30         40         50         60 
MQTAEIHRRW LDFFARRGHT VVPSASLVSD DPSLLFTVAG MVPFVPYLTG IVPAPFPRAT 

        70         80         90        100        110        120 
SVQKCIRTLD IEEVGKTPRH GTFFQMCGNF SFGDYFKEQA IAFAWDLLTT AETEGGLGFD 

       130        140        150        160        170        180 
PKDLWVTVYE EDDEAREIWR RVSGLAEERI QGLGKDTNYW STGQPGPAGP CSEIFFDRGP 

       190        200        210        220        230        240 
AYGIDGGPAT DDDRYVEIWN LVFMQFLRGE GTGKDDFEIL GDLPKKNIDT GLGLERVAFL 

       250        260        270        280        290        300 
KQGVENMYEI DQVRPVLDRA AELAGKPYGN EAHEDDVRLR VVADHVRSAL MLMTDGVTPS 

       310        320        330        340        350        360 
NEGRGYVLRR LLRRTVRAMW LLGVEAATFP ALFPVSRDAM KAAYPEVETE FARTSQLAYA 

       370        380        390        400        410        420 
EEETFLRTLV AGTSILDTAV ANTQKAGKRE LAGDTAFLLH DTYGFPIDLT LEMAEEAGLS 

       430        440        450        460        470        480 
VDRAAFDTLM ADQRARAKAD AKAKKTALAD LSVYSGLRAL GETVFTGYTE LETESSVLGL 

       490        500        510        520        530        540 
IIDGHSANKA VEGQVAEVIL GATALYAEAG GQDADTGTIV GPGYVLDVLD VQKPVRGLVS 

       550        560        570        580        590        600 
HRVLVRSGEV GVGVPATSLV DADYRRGAKQ AHSGTHIIHA ALRQVLGSNA HQSGSYNKAG 

       610        620        630        640        650        660 
YLRLDFSWNQ ALSPETRSEI EEISNSAIRQ NLEVTTRELP LAEAKALGAM ALFGEKYGDT 

       670        680        690        700        710        720 
VRVVDIGGPW SRELCAGTHV ARSAEIGLIN LVSESSVGST NRRVESLVGL EAFKDLAVER 

       730        740        750        760        770        780 
TIVSQLSSSL KTPREQLPEK IADLMASLKA AEKRIQAFEA RAVLDRVQGL LEAVSRRGAV 

       790        800        810        820        830        840 
QVVAADAGTL STADDLRLLA ITVRDRLGSD PATVALAALA GGKPVVIVAT NQAARDAGVT 

       850        860        870        880 
AGALAKTAAG VLGGGGGGKA DLAQGGGTDA TAIPAALAAV STAIG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016822 Genomic DNA. Translation: AAT88944.1.
RefSeqYP_062049.1. NC_006087.1.

3D structure databases

ProteinModelPortalQ6AFA1.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2938703.
GenomeReviewsGene locus Lxx10910 in contig AE016822_GR.
KEGGlxx:Lxx10910.
NMPDRfig|281090.3.peg.463.
PATRIC22335754. VBILeiXyl11655_1127.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG354397.
OMAGESKTDQ.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycLXYL281090:LXX10910-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_LEIXX
AccessionPrimary (citable) accession number: Q6AFA1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: September 13, 2004
Last modified: January 25, 2012
This is version 49 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