Skip Header

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

A7Z735 (SYA_BACA2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. 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:RBAM_024510
OrganismBacillus amyloliquefaciens (strain FZB42) [Complete proteome] [HAMAP]
Taxonomic identifier326423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length878 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 – 878878Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000347497

Sites

Metal binding5661Zinc Potential
Metal binding5701Zinc Potential
Metal binding6681Zinc Potential
Metal binding6721Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
A7Z735 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 07F9E7B93214AB3D

FASTA87896,918
        10         20         30         40         50         60 
MKHLTSAEVR QMFLDFFKEK GHAVEPSASL VPHEDPSLLW INSGVATLKK YFDGRVVPEN 

        70         80         90        100        110        120 
PRIVNAQKSI RTNDIENVGK TARHHTFFEM LGNFSIGDYF KEEAITWAWE FLTSEKWIGF 

       130        140        150        160        170        180 
DPELLSVTVH PEDEEAYTLW AEKIGVPEER IIRLEGNFWD IGEGPSGPNT EIFYDRGEKY 

       190        200        210        220        230        240 
GNDPSDSELY PGGENDRYLE VWNLVFSEFN HNPDGTYTPL PKKNIDTGMG LERMVSVIQD 

       250        260        270        280        290        300 
VSTNFDTDLF MPIIEATERI SGDAYGKDAV KDTAFKVIAD HIRTVAFAVS DGALPSNEGR 

       310        320        330        340        350        360 
GYVLRRLLRR AVRYAKTLGI SRPFMYELVP TVAGIMDAFY PEVKEKQEFI AKVIKTEEER 

       370        380        390        400        410        420 
FHETLNEGLA ILSDVIKKEK EKGSGIISGK DVFKLYDTYG FPVELTEEYA EDEQMTVDHK 

       430        440        450        460        470        480 
GFEAEMEKQR ERARNARQDV GSMQVQGGAL RDITAESTFV GYSAVKAEAK VIELLHDGQL 

       490        500        510        520        530        540 
ISEAHEGDTV QILLDKTPFY AESGGQIGDR GVLRSEQAVV TIKDVKKAPN GQHVHEGTVD 

       550        560        570        580        590        600 
SGTIQKGASV TAEVEDQMRS GVVKNHTATH LLHQALKDVL GTHVNQAGSL VTENRLRFDF 

       610        620        630        640        650        660 
SHFGQVTKEE LERIEGIVNE KIWESIPVAI DLKPINEAKE MGAMALFGEK YGDIVRVVQV 

       670        680        690        700        710        720 
GDYSLELCGG CHVTNTAEIG LFKIVSESGI GAGTRRIEAV TGKGAYQEMN SQLSLLQHAA 

       730        740        750        760        770        780 
DELKSNVKDV PKRIQSLQAE LKEAQRENES LLSKLGNVEA GAILSKVKDI GGVKVLAEKV 

       790        800        810        820        830        840 
NAKDMNHLRT MVDDLKAKLG SAVIILGAVQ NEKVNLSAGV TKDLIEKGLH AGKMVKQAAE 

       850        860        870 
VCGGGGGGRP DMAQAGGKHP EKLEEALASA VDWIKSVL 

« Hide

References

[1]"Comparative analysis of the complete genome sequence of the plant growth-promoting bacterium Bacillus amyloliquefaciens FZB42."
Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., Strittmatter A., Gottschalk G., Borriss R.
Nat. Biotechnol. 25:1007-1014(2007) [PubMed: 17704766] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FZB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000560 Genomic DNA. Translation: ABS74811.1.
RefSeqYP_001422042.1. NC_009725.1.

3D structure databases

ProteinModelPortalA7Z735.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7Z735.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000006772; EBBACP00000006650; EBBACG00000006764.
GeneID5461310.
GenomeReviewsGene locus RBAM_024510 in contig CP000560_GR.
KEGGbay:RBAM_024510.
PATRIC18750012. VBIBacAmy31356_2481.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
GeneTreeEBGT00050000001776.
HOGENOMHBG354397.
OMAMFTNSGM.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycBAMY326423:RBAM_024510-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_BACA2
AccessionPrimary (citable) accession number: A7Z735
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: October 23, 2007
Last modified: January 25, 2012
This is version 33 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