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A7GTK8 (SYN_BACCN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 38. 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:
Asparagine--tRNA ligase

EC=6.1.1.22
Alternative name(s):
Asparaginyl-tRNA synthetase
Short name=AsnRS
Gene names
Name:asnS
Ordered Locus Names:Bcer98_3247
OrganismBacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]
Taxonomic identifier315749 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn). HAMAP MF_00534

Subunit structure

Homodimer By similarity. HAMAP MF_00534

Subcellular location

Cytoplasm By similarity HAMAP MF_00534.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processasparaginyl-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

asparagine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 463463Asparagine--tRNA ligase HAMAP MF_00534
PRO_1000081844

Sequences

Sequence LengthMass (Da)Tools
A7GTK8 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: D6CAE7361F8F1514

FASTA46353,415
        10         20         30         40         50         60 
MENTLVKSLY RETDKYVDQK VQVSGWIRNL RDSKVFGFIE LNDGSFFKSV QIVFDTELDN 

        70         80         90        100        110        120 
FKEITKLPLS SSIRVEGKFI ATPTAKQPFE IKAEKIEIEG LSDSDYPLQK KRHTFEYLRT 

       130        140        150        160        170        180 
IAHLRPRTNA FSATFRVRSI AAYAIHKFFQ ERGFVHVHTP IITGSDTEGA GEMFRVTTHD 

       190        200        210        220        230        240 
MNNLPKGEDG QVDDSKDFFG RETNLTVSGQ LPAEAYALAF RDVYTFGPTF RAENSNTTRH 

       250        260        270        280        290        300 
AAEFWMVEPE IAFAELEDVM DLTEDMLKYA MKYVLEHAPE EMEFFNKFVD KTVLERMNNV 

       310        320        330        340        350        360 
INSDFGRITY TEAIKVLQES GADFKYPVEW GIDLQTEHER YLSEQVFKRP VFVTDYPKDI 

       370        380        390        400        410        420 
KAFYMRMNDD GKTVAATDLL VPGIGELIGG SQREERMDVL VDRIKELGMK EEDYWWYLEL 

       430        440        450        460 
RKYGGTKHAG FGLGFERFLM YITGMGNIRD VIPFPRTPGS AEF 

« Hide

References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NVH 391-98.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000764 Genomic DNA. Translation: ABS23466.1.
RefSeqYP_001376461.1. NC_009674.1.

3D structure databases

ProteinModelPortalA7GTK8.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7GTK8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000038716; EBBACP00000037767; EBBACG00000038707.
GeneID5343770.
GenomeReviewsGene locus Bcer98_3247 in contig CP000764_GR.
KEGGbcy:Bcer98_3247.
PATRIC18935136. VBIBacCyt128034_3409.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0017.
GeneTreeEBGT00050000000858.
HOGENOMHBG745843.
OMAAIHRFFH.
ProtClustDBPRK03932.

Enzyme and pathway databases

BioCycBCER315749:BCER98_3247-MONOMER.

Family and domain databases

HAMAPMF_00534. Asn_tRNA_synth.
[Tree]
InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004522. Asn-tRNA-synth_IIb.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR004365. NA-bd_OB_tRNA-helicase.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KOK01893.
PANTHERPTHR22594. aa-tRNA-synt_II. 1 hit.
PTHR22594:SF6. PTHR22594:SF6. 1 hit.
PfamPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
PRINTSPR01042. TRNASYNTHASP.
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
TIGRFAMsTIGR00457. AsnS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYN_BACCN
AccessionPrimary (citable) accession number: A7GTK8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: September 11, 2007
Last modified: January 25, 2012
This is version 38 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