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Reviewed, UniProtKB/Swiss-Prot B2TI01 (SYN_CLOBB)

Last modified November 3, 2009. Version 11. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Asparaginyl-tRNA synthetase
    EC=6.1.1.22
Alternative name(s):
    Asparagine--tRNA ligase
      Short name=AsnRS
Gene names
Name: asnS
Ordered Locus Names: CLL_A0142
OrganismClostridium botulinum (strain Eklund 17B / Type B) [Complete proteome] [HAMAP]
Taxonomic identifier508765 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 464464Asparaginyl-tRNA synthetase HAMAP MF_00534
PRO_1000128205

Sequences

Sequence LengthMass (Da)Tools
B2TI01-1 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: F5595D1D0155E01A

FASTA46453,342
        10         20         30         40         50         60 
MKNTVLIKKI YRETDQFLSK EVMISGWIRT LRASNAFGFI EINDGSFFKN IQVVFDDKLG 

        70         80         90        100        110        120 
NFKEISKLPI SSSISVVGTL VATPDAKQPF EIQAKEIVIE GMSNSDYPLQ KKRHTFEYLR 

       130        140        150        160        170        180 
SIAHLRPRSN AFSATFRVRS VAAFAIHKFF QEQGFVYTHT PIITGSDCEG AGEMFRVTTL 

       190        200        210        220        230        240 
DPKAPELTKE GDIDYTKDFF GKETNLTVSG QLNAECFALA FRNIYTFGPT FRAENSNTTR 

       250        260        270        280        290        300 
HAAEFWMIEP EIAFADLQDD MELAEAMLKY VIKYVMDECP EELQFFNSFV DKGLLERLNH 

       310        320        330        340        350        360 
VVSSDFAKVT YTEAVEILEK CDKEFDYDVS WGIDLQTEHE RYLTEEHFKK PLFVTDYPKE 

       370        380        390        400        410        420 
IKAFYMRMNE DNKTVAATDL LVPGIGEIIG GSQREERLDV LEARMAELGL KKEDYWWYLE 

       430        440        450        460 
LRKYGETKHA GFGLGFERLI MYITGMTNIR DVIPFPRTPG TSEF 

« Hide

References

[1]"Complete sequence of Clostridium botulinum strain Eklund."
Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP001056 Genomic DNA. Translation: ACD23255.1.
RefSeqYP_001884396.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6292907.
GenomeReviewsGene locus CLL_A0142 in contig CP001056_GR.
KEGGcbk:CLL_A0142.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMALQKKRHS.

Family and domain databases

HAMAPMF_00534.
[Tree]
InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR004522. Asn-tRNA-synth_IIb.
IPR002312. Asp-tRNA-synth_IIb.
IPR012340. NA-bd_OB-fold.
IPR004365. NA_bd_OB_tRNA-helicase.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
PANTHERPTHR22594. aa-tRNA-synt_II. 1 hit.
PfamPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
PRINTSPR01042. TRNASYNTHASP.
TIGRFAMsTIGR00457. asnS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYN_CLOBB
AccessionPrimary (citable) accession number: B2TI01
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 1, 2008
Last modified: November 3, 2009
This is version 11 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents