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Q8G5W9 (SYA_BIFLO) 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:BL0882
OrganismBifidobacterium longum (strain NCC 2705)
Taxonomic identifier206672 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium

Protein attributes

Sequence length893 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
Reference 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 – 893893Alanine--tRNA ligase HAMAP MF_00036_B
PRO_0000075066

Sites

Metal binding5741Zinc Potential
Metal binding5781Zinc Potential
Metal binding6781Zinc Potential
Metal binding6821Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q8G5W9 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: D10D2CF8AF4AA0D5

FASTA89397,444
        10         20         30         40         50         60 
MRTADIAKRY LDYFAKHDHL IVPSASLISP NPTTLFTIAG MVPFIPYLMG EQTPPKRRMA 

        70         80         90        100        110        120 
SNQKCVRTLD IDEVGKTTRH GTFFQMLGNF SFGDYFKEEA IHYAWELLTT SQDEGGYGFD 

       130        140        150        160        170        180 
PEKLWMTTFT DDDEARSMWI NEGVDPEHIQ KMGMEDNFWT TGGPGPGGPC SEIYVDRGPA 

       190        200        210        220        230        240 
FGKEGGPIAD ENRYIEIWDL VFENYEVDNV KSKTDLHIVG ELENKNIDTG AGLERLAYLL 

       250        260        270        280        290        300 
QGKNNIYETD EVFPVIEAAE QLSGLKYGEN EDADVRFRVV ADHVRSALMI MSDGVRPSNV 

       310        320        330        340        350        360 
GRGYVLRRLL RRTVRSMRML GVTDPVLPTL FPTSKAAMEA SYPELNDTFH EVSESAYGEE 

       370        380        390        400        410        420 
DAFRRTLETG TTILDVAVNK AKSDSAEPVV AGEDAFKLHD TYGFPIELTL EMAAEQGVKV 

       430        440        450        460        470        480 
DEAKFRELMA EQKSRARADA LKKRHNVDLS VYDDFKKTLV SPIDFLGYTD MSARAKVIGI 

       490        500        510        520        530        540 
MQEGKGSVPA VTGPANVEVI LDRTPFYAEA GGQLADQGEI LSDDGAVLEV DDVQKPIKDL 

       550        560        570        580        590        600 
IVHQCRLTEG TLVVGAEVNA NIDLARRGAI ARSHTATHMV HKALREELGP QATQRGSEDA 

       610        620        630        640        650        660 
PNRLRFDFQW SKAPAKSVIS AVEERVNDKL RDNLAVTTKE MKFDDAIALG AMHLFGEKYG 

       670        680        690        700        710        720 
DIVRVVSIGE DGWSRELCGG THVDHVGKIG MVNILSEASI GSGVRRVDAV VGQGAYDFNA 

       730        740        750        760        770        780 
REHALVSQLS DKLNARPDEL AERVNALLAK LKESDRRLAS MYESQLAASV PALVADTKNS 

       790        800        810        820        830        840 
AAPVKVAVKN VGHFGAVDAL RKTVLDVRAQ LGEDAPVVVA LAGVNEDDKP MVAVATNEAA 

       850        860        870        880        890 
RKAGIKAGDL VRGAAKVLGG GGGGKPDFAQ GGGVDASKID EALEALKHEA QKA

« Hide

References

[1]"The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract."
Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.
Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed: 12381787] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCC 2705.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE014295 Genomic DNA. Translation: AAN24695.1.
RefSeqNP_696059.1. NC_004307.2.

3D structure databases

ProteinModelPortalQ8G5W9.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1022383.
GenomeReviewsGene locus BL0882 in contig AE014295_GR.
KEGGblo:BL0882.
PATRIC21118211. VBIBifLon107831_0578.

Phylogenomic databases

HOGENOMHBG354397.
OMAMFTNSGM.
PhylomeDBQ8G5W9.
ProtClustDBPRK00252.

Enzyme and pathway databases

BioCycBLON206672:BL0882-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_BIFLO
AccessionPrimary (citable) accession number: Q8G5W9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: March 1, 2003
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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