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Q72ZI3 (SYN_BACC1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. 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:BCE_4685
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]
Taxonomic identifier222523 [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
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_0000176386

Sequences

Sequence LengthMass (Da)Tools
Q72ZI3 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 84CA5776AA7AB268

FASTA46352,954
        10         20         30         40         50         60 
MENTLVKSLY RDTDKYAGQT VQVSGWIRNL RDSKAFGFIE LNDGSFFKSV QIVFDTELDN 

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

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

       190        200        210        220        230        240 
LNNVPKGEDG QVDESKDFFG 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 
KAFYMRLNDD GKTVAATDLL VPGIGELIGG SQREERMDVL VDRIKELGMN EEDYWWYLEL 

       430        440        450        460 
RKYGGTKHAG FGLGFERFLM YITGMANIRD VIPFPRTPGS SEF 

« Hide

References

[1]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10987.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017194 Genomic DNA. Translation: AAS43586.1.
RefSeqNP_980978.1. NC_003909.8.

3D structure databases

ProteinModelPortalQ72ZI3.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ72ZI3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000027873; EBBACP00000027223; EBBACG00000027864.
GeneID2749571.
GenomeReviewsGene locus BCE_4685 in contig AE017194_GR.
KEGGbca:BCE_4685.
NMPDRfig|222523.1.peg.4650.
PATRIC18857986. VBIBacCer118379_4488.
TIGRBCE_4685.

Phylogenomic databases

eggNOGCOG0017.
GeneTreeEBGT00050000000858.
HOGENOMHBG745843.
OMAAIHRFFH.
ProtClustDBPRK03932.

Enzyme and pathway databases

BioCycBCER405917:BCE_4685-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_BACC1
AccessionPrimary (citable) accession number: Q72ZI3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 59 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