Skip Header

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

A1R709 (SYA_ARTAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. 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:AAur_2281
OrganismArthrobacter aurescens (strain TC1) [Complete proteome] [HAMAP]
Taxonomic identifier290340 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Protein attributes

Sequence length892 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 By similarity 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.

Sequence caution

The sequence ABM07701.1 differs from that shown. Reason: Erroneous initiation.

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 – 892892Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347492

Sites

Metal binding5771Zinc Potential
Metal binding5811Zinc Potential
Metal binding6801Zinc Potential
Metal binding6841Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
A1R709 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: 94F591DEFFE5B4A3

FASTA89295,822
        10         20         30         40         50         60 
MKSQEITKRW VDFFVNKGHT AVPSASLVSS DPSLLFTVAG MVPFIPYLTA REEPPYSRAT 

        70         80         90        100        110        120 
SVQKCIRTGD IEEVGKTARH GTFFQMCGNF SFGDYFKEDA IKFAFELLTT SVDDGGYGLP 

       130        140        150        160        170        180 
AERLWVTVYE EDDEAKELWL KNTGIPAERI QRMGKADNYW STGQPGPAGP CSEIYYDRGP 

       190        200        210        220        230        240 
AYGIEGGPLA DETRYIEIWN LVFMQYQIEN VRSKVDFDIV GELPQKNIDT GLGMERLAMI 

       250        260        270        280        290        300 
LQGVENMYET DQVRPVIDKA AELSGREYTS AESPEDPHHT DDVRMRVVGD HIRSALMLIA 

       310        320        330        340        350        360 
DGVAPSNEGR GYVLRRLIRR AVRAMRLLGV EKACLPDLLP ASRDAMKGVY PVVETDFARI 

       370        380        390        400        410        420 
SRIAYAEEKA FLRTIASGTA RLEDAVAESK AAGVPLSGAD AFALHDTYGF PIDLTLEMAE 

       430        440        450        460        470        480 
EAGLQVDEAG FRALMLEQRQ RAQADAKGKK GGHADLSAYQ ELLGKGETVF TGYDELEGEA 

       490        500        510        520        530        540 
KVRGIVSGGR AVAHASTGDE IELVLNETPF YAEAGGQSAD TGLITGDGFV VEVLDVQRPI 

       550        560        570        580        590        600 
KGLSVHKAIV REGEIGSDAL VRAAVDRERR HAAEQAHTGT HIVHAALHQI LGPEATQRGS 

       610        620        630        640        650        660 
YNKAGYLRFD FAWGEGLSTA TRSEIEEVSN IAIRNNFRVD TKVMGLAEAK ALGAMALFGE 

       670        680        690        700        710        720 
NYGSEVRVVE IDGAWSRELC GGTHVSNTSL IGSLSLLGEQ SVGSGNRRVE AFVGLDAFRH 

       730        740        750        760        770        780 
LAAERALVSE LTELLKVPSG QLADRISSTL NKLKATEKEL DRLRKEQLAA AAANLVGTAK 

       790        800        810        820        830        840 
DAAGVRVVAH DAGQVGGADD LRNLALDLRN RLGSEASTVA VAGVSNDRPV ILIATNEAAR 

       850        860        870        880        890 
EAGVKAGALV RLAAGILGGG GGGKDDVAQG GGTDAGKVSE ALTAVVDAIA KR 

« Hide

References

[1]"Secrets of soil survival revealed by the genome sequence of Arthrobacter aurescens TC1."
Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B., Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V., Khouri H.M., Wackett L.P., Nelson K.E., Sadowsky M.J.
PLoS Genet. 2:2094-2106(2006) [PubMed: 17194220] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TC1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000474 Genomic DNA. Translation: ABM07701.1. Different initiation.
RefSeqYP_948021.1. NC_008711.1.

3D structure databases

ProteinModelPortalA1R709.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1R709.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4639186.
GenomeReviewsGene locus AAur_2281 in contig CP000474_GR.
KEGGaau:AAur_2281.
PATRIC20979984. VBIArtAur67810_2316.
TIGRAAur_2281.

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycAAUR290340:AAUR_2281-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_ARTAT
AccessionPrimary (citable) accession number: A1R709
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: January 25, 2012
This is version 42 of the entry and version 2 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