Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8DG51 (SYN_THEEB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 58. 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
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:tlr2473
OrganismThermosynechococcus elongatus (strain BP-1)
Taxonomic identifier197221 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Chroococcales › Thermosynechococcus

Protein attributes

Sequence length462 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 – 462462Asparagine--tRNA ligase HAMAP MF_00534
PRO_0000176467

Sequences

Sequence LengthMass (Da)Tools
Q8DG51 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 5D94717A3A8FDFED

FASTA46252,373
        10         20         30         40         50         60 
MQQRIKDILH QGQVGDRITV KGWVRTKREL KECTFVNLND GSTLAGLQVV IPNTVAAATP 

        70         80         90        100        110        120 
TMKDLTTGAA AEFTGELVRS PGKNQAIELH AEEIHLWGTA DPETYPLQKK RHSFEFLRTI 

       130        140        150        160        170        180 
AHLRPRTNTL GAVMRVRNAC ATAIHQFFQE RGFLWVHTPI ITASDCEGAG ELFTVTTLDL 

       190        200        210        220        230        240 
TQPPKTPEGK IDFSQDFFGR RAYLTVSGQL EAEIMATAFT NVYTFGPTFR AENSNTSRHL 

       250        260        270        280        290        300 
AEFWMVEPEM AFCDLRGDME LAEAFLQFVF RYVLDHCPED MAFFQERIDH SVMATAEQMA 

       310        320        330        340        350        360 
TQPFAHLSYS EAIQVLEKSG RAFEFPVAWG LDLQSEHERY LAEEYCQRPV IVYDYPAAIK 

       370        380        390        400        410        420 
AFYMRLNDDG KTVAAMDILA PKIGEIIGGS QREERFDVLQ ERIVTQGLDP APYWWYLDLR 

       430        440        450        460 
RYGSVPHAGF GLGFERLVQF MTGMDNIRDV IPFPRTPGNA EF

« Hide

References

[1]"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1."
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takeuchi C., Yamada M., Tabata S.
DNA Res. 9:123-130(2002) [PubMed: 12240834] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BP-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000039 Genomic DNA. Translation: BAC10024.1.
RefSeqNP_683262.1. NC_004113.1.

3D structure databases

ProteinModelPortalQ8DG51.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8DG51.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1010585.
GenomeReviewsGene locus tlr2473 in contig BA000039_GR.
KEGGtel:tlr2473.
NMPDRfig|197221.1.peg.2471.
PATRIC23930442. VBITheElo119873_2598.

Phylogenomic databases

eggNOGNOG146472.
HOGENOMHBG745843.
OMAAIHRFFH.
ProtClustDBPRK03932.

Enzyme and pathway databases

BioCycTELO197221:TLR2473-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_THEEB
AccessionPrimary (citable) accession number: Q8DG51
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 58 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents