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Q67P26 (SYN_SYMTH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. 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:STH1582
OrganismSymbiobacterium thermophilum [Complete proteome] [HAMAP]
Taxonomic identifier2734 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiales Family XVIII. Incertae SedisSymbiobacterium

Protein attributes

Sequence length437 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 – 437437Asparagine--tRNA ligase HAMAP MF_00534
PRO_0000176466

Sequences

Sequence LengthMass (Da)Tools
Q67P26 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 22A2A82F8C1F30D0

FASTA43750,445
        10         20         30         40         50         60 
MKWVTVDRLP QYEGQTVELR GWVQNYRSSG KIQFIIFRDG TGVCQAVLFI KDVPPEVFEA 

        70         80         90        100        110        120 
GKRLTQESSI IIRGSVRKDD RAPGGYEIGV QDLEIVQIAE EYPITKKEHG TEFLMDHRHL 

       130        140        150        160        170        180 
WIRSNRQVAI LRIRNEITMA IHQFLQENGF VLTESPILMG TAAEGGATLF ETTYVNDEPA 

       190        200        210        220        230        240 
YLSQSGQLHV EATAMALGRV YTFGPTFRAE KSKTRRHLIE FWMVEPEAAY FTHEDNMRLQ 

       250        260        270        280        290        300 
EEMVTYVVRR VLERRSKELQ LIGRDTTLLE KVEPPFPRIT YTEAVEMLKK LHKPGDEWEP 

       310        320        330        340        350        360 
IEWGEDFGAP HETVLTQQFE KPVFVEKFPV KVKAFYMQPD PENPDVVLGA DLLAPEGYGE 

       370        380        390        400        410        420 
IIGGSQRIHD PELLKRRFEE HGLDMNTYGW YYDLRRFGSV PHSGFGLGIE RTVAWICGLE 

       430 
HVRETIPFPR LLNRLHP 

« Hide

References

[1]"Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium that depends on microbial commensalism."
Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K., Ikeda H., Hattori M., Beppu T.
Nucleic Acids Res. 32:4937-4944(2004) [PubMed: 15383646] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: T / IAM 14863.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006840 Genomic DNA. Translation: BAD40567.1.
RefSeqYP_075411.1. NC_006177.1.

3D structure databases

ProteinModelPortalQ67P26.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2980353.
GenomeReviewsGene locus STH1582 in contig AP006840_GR.
KEGGsth:STH1582.
NMPDRfig|292459.1.peg.1522.
PATRIC23781323. VBISymThe116959_1582.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG745843.
OMADHLPQET.

Enzyme and pathway databases

BioCycSTHE292459:STH1582-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_SYMTH
AccessionPrimary (citable) accession number: Q67P26
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: October 11, 2004
Last modified: January 25, 2012
This is version 52 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