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A1A198 (SYA_BIFAA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:BAD_0700
OrganismBifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) [Complete proteome] [HAMAP]
Taxonomic identifier367928 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium

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.

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_0000347507

Sites

Metal binding5731Zinc Potential
Metal binding5771Zinc Potential
Metal binding6771Zinc Potential
Metal binding6811Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
A1A198 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 302D8579893EFF45

FASTA89297,576
        10         20         30         40         50         60 
MRTSEIAKRF LDYFEQHDHL VVPSASLISP NPTTLFTIAG MVPFIPYLMG EQTPPKHRMA 

        70         80         90        100        110        120 
SNQKCVRTLD IDEVGKTTRH GTFFQMLGNF SFGDYFKEEA IHYAYELLTT PQDKGGYGFD 

       130        140        150        160        170        180 
PEKLWMTTFT DDEEARSMWK NEGVDPEHIQ IMGMEDNFWT TGGPGPGGPC SEIYVDRGPK 

       190        200        210        220        230        240 
YGVEGGPIAD ENRYIEIWDL VFENYEVDNV KSKTDLHIVG ELENKNIDTG AGLERLAYLM 

       250        260        270        280        290        300 
QGKQNIYETD EVFPVIEAAQ KLSGRTYGDD EAMDVRFRIV ADHVRSALMI MSDGVRPSNN 

       310        320        330        340        350        360 
GRGYVLRRLL RRTVKAMREL GVTEPVMPTL LPTSKAAMEP SYPELNDTFH DVSEAAYGEE 

       370        380        390        400        410        420 
DAFRRTLESG TEIFDMAVTK AKQGGSDLVS GEDAFKLHDT YGFPIEITLE MAADQGVKVD 

       430        440        450        460        470        480 
EAKFRELMAE QKSRARADAL KKRHNVDLSV YDDFKKTLLQ PIDFLGYTDM SARAKVLGIM 

       490        500        510        520        530        540 
QEGKGSVPAV TGPANIEVIL DRTPFYAQAG GQLADQGEIL SDDGAVLEVD DVQKPIKDLI 

       550        560        570        580        590        600 
VHQCRLTEGT LVVGAEVNAN IDLERRGAIA RSHTATHMVH KALREELGPQ ATQRGSEDAP 

       610        620        630        640        650        660 
NRLRFDFQWS SAPSKDAMNA VEARVNEKLR ENLAVTTQEM KFDDAIALGA MHLFGEKYGD 

       670        680        690        700        710        720 
IVRVVSIGED GWSRELCGGT HIDHVGKIGA INIMSEASIG SGVRRVDAVV GQGAYEFNAR 

       730        740        750        760        770        780 
EHALVSQLSD MVNARPDELA ERVNMLLAKL KESDRRLAAM YESQLAASVP TLVAEAKASS 

       790        800        810        820        830        840 
APVKVAKKNV GHFGSFDALR KTVLDVRGQL GEDAPVVVAL AGMNEDGKPM VAVATNEAAR 

       850        860        870        880        890 
KQGIKAGDLV RGASKVLGGG GGGKPDFAQG GGADATKIDE ALEALAGQAL KG

« Hide

References

[1]"Bifidobacterium adolescentis complete genome sequence."
Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S., Tanaka K., Watanabe K.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15703 / DSM 20083 / NCTC 11814 / E194a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP009256 Genomic DNA. Translation: BAF39481.1.
RefSeqYP_909563.1. NC_008618.1.

3D structure databases

ProteinModelPortalA1A198.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1A198.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4557202.
GenomeReviewsGene locus BAD_0700 in contig AP009256_GR.
KEGGbad:BAD_0700.
NMPDRfig|1680.3.peg.1278.
PATRIC21100763. VBIBifAdo27973_0757.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHBG354397.
OMAGESKTDQ.
ProtClustDBPRK00252.

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_BIFAA
AccessionPrimary (citable) accession number: A1A198
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 44 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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