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A0PY64 (SYN_CLONN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. 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:NT01CX_1233
OrganismClostridium novyi (strain NT) [Complete proteome] [HAMAP]
Taxonomic identifier386415 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

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_1000051386

Sequences

Sequence LengthMass (Da)Tools
A0PY64 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 928A023A4390A264

FASTA46353,332
        10         20         30         40         50         60 
METVLVKQLY RETEKFAGKE VKISGWIRTL RASNKFGFIE VNDGSFFKNI QVVFGAELEN 

        70         80         90        100        110        120 
FKEISKYAIS SSISVEGEVV ITEGAKQPFE IHAKKVVLEG KSDADYPLQK KRHTFEYLRS 

       130        140        150        160        170        180 
IAHLRPRSNA FSAVFRVRSL AAYAIHKFFQ DQGFVYVHTP IITGSDCEGA GEMFRVTTLD 

       190        200        210        220        230        240 
MENPPKDEKG NVDYKEDFFG KQANLTVSGQ LEAEIYALAF RNVYTFGPTF RAENSNTARH 

       250        260        270        280        290        300 
ASEFWMIEPE MAFAELKDYM DVAEQMVKYI INYVRENAPE EMEFFNKFID KGLLERLDNV 

       310        320        330        340        350        360 
VNSDFARISY TEAVEILQKS GAEFEYPVEW GIDLQTEHER YLTEQIYKKP VFVTDYPKDI 

       370        380        390        400        410        420 
KAFYMRMNDD NKTVAAADLL VPGIGEIIGG SQREERLDIL EARMAELGLE KEDYWWYLEL 

       430        440        450        460 
RKYGETKHAG YGLGFERMIM YLTGMGNIRD VIPFPRTPGV SEF 

« Hide

References

[1]"The genome and transcriptomes of the anti-tumor agent Clostridium novyi-NT."
Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X., Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B., Zhou S.
Nat. Biotechnol. 24:1573-1580(2006) [PubMed: 17115055] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000382 Genomic DNA. Translation: ABK61604.1.
RefSeqYP_877316.1. NC_008593.1.

3D structure databases

ProteinModelPortalA0PY64.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0PY64.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4540039.
GenomeReviewsGene locus NT01CX_1233 in contig CP000382_GR.
KEGGcno:NT01CX_1233.
PATRIC19478128. VBICloNov112828_0343.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0017.
HOGENOMHBG745843.
OMAAIHRFFH.
ProtClustDBPRK03932.

Enzyme and pathway databases

BioCycCNOV386415:NT01CX_1233-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_CLONN
AccessionPrimary (citable) accession number: A0PY64
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 9, 2007
Last modified: January 25, 2012
This is version 41 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