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P61698 (SYA_BDEBA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Bd0501
OrganismBdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100) [Complete proteome] [HAMAP]
Taxonomic identifier264462 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Bdellovibrionales › Bdellovibrionaceae › Bdellovibrio

Protein attributes

Sequence length907 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 – 907907Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000075065

Sites

Metal binding5811Zinc Potential
Metal binding5851Zinc Potential
Metal binding6831Zinc Potential
Metal binding6871Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
P61698 [UniParc].

Last modified June 7, 2004. Version 1.
Checksum: 2B391C58F24BFDAB

FASTA90799,514
        10         20         30         40         50         60 
MKSSEIRNAF IKYFEKNGHK VVPSSSLIPE NDPTLLFANA GMNQFKNTFL GLEKRDYSRA 

        70         80         90        100        110        120 
VTAQKCVRAG GKHNDLENVG FTARHHTFFE MVGNFSFGDY FKKDAIHFAW EFLTKELAIP 

       130        140        150        160        170        180 
KEKLYVTVHI SDDEAADIWH NQEGVPRERI FRFDKDNFWK MGDTGPCGPC TEIFYDHGPK 

       190        200        210        220        230        240 
AGTISDPFKG IEAGEDRFVE IWNLVFMQYF ENPPGTLTPL PKPSVDTGGG LERMSAAMQG 

       250        260        270        280        290        300 
VFNNYDTDLF QPMIQLACKI GNIEYISDKE VLAKNPAAAE VTSALRVLAD HCRSTSFLIA 

       310        320        330        340        350        360 
DGALPSNEGR GYVLRRIMRR AIRYGRKLSA DKSFLPGMAE ALIESMGSVY PELKTRRDHI 

       370        380        390        400        410        420 
LNTIRDEEDR FIATLDKGTA ILEDELKKAK SKGIKELSGE VVFRMYDTYG FPADLTRVIA 

       430        440        450        460        470        480 
NEQGIEVNEA AFEKEMEDNR AKSKASWKGK SMGADEAHMI KFAKDYLQSG KSVTFLGYEG 

       490        500        510        520        530        540 
TIGDGKVMGL SNGQAEVQEL KTGDTGLMIL NATTFYGEGG GQSGDVGYIM HDTNRARVIN 

       550        560        570        580        590        600 
TTKIDDIVLH HVEIEHGSFK VGTAVVTGVD PVERRNTAAN HSATHLLHAA LRKVLGTHVT 

       610        620        630        640        650        660 
QAGSLVDSQK TRFDFTHNKP VSSEEIKKIE DLVNEQIARC NPVQTEMMSH KAALEKGAMA 

       670        680        690        700        710        720 
LFGEKYASDV RVLTMGDFSC ELCGGTHVKN TSEIRLFKIV SEAGVSSGVR RIEAITADNA 

       730        740        750        760        770        780 
LQYMMSAVTH LDDALAAAGF QKSPHYIKHL ETTGETATLA NRVESLKDQV KQLEKEMKKL 

       790        800        810        820        830        840 
QGGQVNVDDL AANALTFKTK AGASAKLVLA DVPLDDRQVL AEVTDHLKNK IQSGIVVVVG 

       850        860        870        880        890        900 
QGDGSHPIIV SVSKEISGET KAGDLLKEVA GVMGGKGGGR PDFAQGAAPN RAQLNEAFSK 


VKSMLGL

« Hide

References

[1]"A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a genomic perspective."
Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C., Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E., Schuster S.C.
Science 303:689-692(2004) [PubMed: 14752164] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15356 / DSM 50701 / NCIB 9529 / HD100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842647 Genomic DNA. Translation: CAE78480.1.
RefSeqNP_967487.1. NC_005363.1.

3D structure databases

ProteinModelPortalP61698.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2733324.
GenomeReviewsGene locus Bd0501 in contig BX842601_GR.
KEGGbba:Bd0501.
NMPDRfig|264462.1.peg.457.
PATRIC21075738. VBIBdeBac73187_0458.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG354397.
OMAGESKTDQ.
PhylomeDBP61698.

Enzyme and pathway databases

BioCycBBAC264462:BD0501-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_BDEBA
AccessionPrimary (citable) accession number: P61698
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: January 25, 2012
This is version 51 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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