Skip Header

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

A1TRL4 (SYA_ACIAC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. 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:Aave_3035
OrganismAcidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli) [Complete proteome] [HAMAP]
Taxonomic identifier397945 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length948 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.

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 – 948948Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347471

Sites

Metal binding6381Zinc Potential
Metal binding6421Zinc Potential
Metal binding7391Zinc Potential
Metal binding7431Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
A1TRL4 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 15942A7F6D276DE1

FASTA948102,424
        10         20         30         40         50         60 
MTKPTPPSSV ADIRKSFLDF FASKGHTVVP SSPLVPGNDP TLMFTNSGMV QFKDVFLGTD 

        70         80         90        100        110        120 
KRPYVRATSV QACLRAGGKH NDLENVGYTA RHHTFFEMLG NWSFGDYFKR DSLKWAWELL 

       130        140        150        160        170        180 
TEVYGLPKER LLATVYAEDD EAYDIWTKEI GLPPERVIRI GDNKGGRYKS DNFWMMADTG 

       190        200        210        220        230        240 
PCGPCSEIFY DHGPHIPGGP PGSPDEDGDR FIEIWNNVFM QFDMAEDGSV TPLPAPCVDT 

       250        260        270        280        290        300 
GMGLERLAAI LQHVHSNYEI DLFAALIQAA ARETGTADLA NPSLKVIADH IRATAFLVSD 

       310        320        330        340        350        360 
GVIPSNEGRG YVQRRIVRRA IRHGYKLGRK TPFFHSLVKD LVAQMGDAYP KLREQEQRIT 

       370        380        390        400        410        420 
EVLKAEEERF FETLANGMDL LDSALDIQLA SKALQNKTLR WFASEGREEK LVSFKDDVQV 

       430        440        450        460        470        480 
AEAVLISDEL RSTEYMQRLK ETVPGLNEVK TLHSVIRDWS GLTLPGDLAF KLHDTYGFPL 

       490        500        510        520        530        540 
DLTNDVCRER GVTVDEDGFK AAMDRQKAQA RAAGKFKMDK ALEYGGEANR FSGYDGLTES 

       550        560        570        580        590        600 
AKIVAIYVDG TSAQALEAGQ NGVVVLDNTP FYAESGGQVG DQGVIHAGGA RFAVDDTLKI 

       610        620        630        640        650        660 
RADVYGHHGR LESGTLRVGD AVQAEVDAAL RAATMRNHSV THIMHKALRE VLGSHVQQKG 

       670        680        690        700        710        720 
SLVNAERTRF DFAHNAPVTD AQIREIERRV NEEILANTPT GARVMDIESA QKTGAMMLFG 

       730        740        750        760        770        780 
EKYGETVRVL DIGTSRELCG GTHVARTGDI GLFKVVGESG VAAGVRRIEA VTGAGALAYL 

       790        800        810        820        830        840 
QQLEDTVAKA AGALRAPAAE ITGRIGQALE QVKALEREVA ALKGKLASSQ GDELAGQAVD 

       850        860        870        880        890        900 
VKGLKVLAAT LPGADAKTLR DTMDKLKDKL KSAAIVLAAV DGAKVQIAAG VTPDAMAKVK 

       910        920        930        940 
AGELVNFVAS QVGGKGGGKP DMAMAGGTDA AALPAALASV AAWVGERA 

« Hide

References

[1]"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AAC00-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000512 Genomic DNA. Translation: ABM33602.1.
RefSeqYP_971376.1. NC_008752.1.

3D structure databases

ProteinModelPortalA1TRL4.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1TRL4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4666376.
GenomeReviewsGene locus Aave_3035 in contig CP000512_GR.
KEGGaav:Aave_3035.
NMPDRfig|397945.5.peg.2584.
PATRIC20681225. VBIAciCit38535_3088.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAMFTNSGM.
PhylomeDBA1TRL4.

Enzyme and pathway databases

BioCycAAVE397945:AAVE_3035-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. 2 hits.
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. 2 hits.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYA_ACIAC
AccessionPrimary (citable) accession number: A1TRL4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: February 6, 2007
Last modified: January 25, 2012
This is version 45 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