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Q817I8 (SYN_BACCR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 61. 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:BC_4559
OrganismBacillus cereus (strain ATCC 14579 / DSM 31)
Taxonomic identifier226900 [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 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
Reference 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_0000176387

Sequences

Sequence LengthMass (Da)Tools
Q817I8 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: AA56A17402CD1F60

FASTA46353,040
        10         20         30         40         50         60 
MENTLVKSLY RDTEKYADQT VQVSGWIRNL RDSKAFGFIE LNDGSFFKSV QIVFDTELEN 

        70         80         90        100        110        120 
FKEIAKLPLS SSVKVEGKVI ATPGAKQPFE IKAEKIDIEG LSDSDYPLQK KRHTFEYLRT 

       130        140        150        160        170        180 
IAHLRPRTNA FSATFRVRSI AAFAIHQFFQ ERGFVHVHTP IITGSDTEGA GEMFRVTTQD 

       190        200        210        220        230        240 
LNNLPKGEDG KVDESKDFFG KETNLTVSGQ LNAEAYALAF RDVYTFGPTF RAENSNTTRH 

       250        260        270        280        290        300 
AAEFWMVEPE IAFAELGDVM NLTEDMLKYA MKYVLEHAPE EMEFFNSFVD KTVLERMNNV 

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

       370        380        390        400        410        420 
KAFYMRLNED GKTVAATDLL VPGIGELIGG SQREERMDVL VDRIKELGMN EEDYWWYLEL 

       430        440        450        460 
RKYGGTKHAG FGLGFERFLM YITGMANIRD VIPFPRTPGS SEF 

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed: 12721630] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016877 Genomic DNA. Translation: AAP11466.1.
RefSeqNP_834265.1. NC_004722.1.

3D structure databases

ProteinModelPortalQ817I8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ817I8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000032503; EBBACP00000031709; EBBACG00000032494.
GeneID1206904.
GenomeReviewsGene locus BC_4559 in contig AE016877_GR.
KEGGbce:BC4559.
PATRIC32605241. VBIBacCer54481_4719.

Phylogenomic databases

eggNOGCOG0017.
GeneTreeEBGT00050000000858.
HOGENOMHBG745843.
OMAAIHRFFH.
PhylomeDBQ817I8.
ProtClustDBPRK03932.

Enzyme and pathway databases

BioCycBCER226900:BC_4559-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_BACCR
AccessionPrimary (citable) accession number: Q817I8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 61 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