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Q481G3 (SYN_COLP3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. 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:CPS_2591
OrganismColwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus) [Complete proteome] [HAMAP]
Taxonomic identifier167879 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesColwelliaceaeColwellia

Protein attributes

Sequence length466 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 – 466466Asparagine--tRNA ligase HAMAP MF_00534
PRO_1000051388

Sequences

Sequence LengthMass (Da)Tools
Q481G3 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: D2D1030A3F062DD7

FASTA46652,401
        10         20         30         40         50         60 
MSVISITDVL AGNFPVNESI TIHGWIRTRR DSKAGISFLA LHDGSCFDAI QAIVPNELDN 

        70         80         90        100        110        120 
YESDVLKLTT GCSVKVTGIL VESPGKGQAF EIQATEVEVL GFVEDPDTYP MAAKRHSIEF 

       130        140        150        160        170        180 
LREQAHLRPR TNIGGAVTRV RNCLAQAVHR FLHSKGYFWI STPLITGSDC EGAGEMFRVS 

       190        200        210        220        230        240 
TLDMENLPRN DEGKVDYNKD FFGKETFLTV SGQLNVETYC NALSKVYTFG PTFRAENSNT 

       250        260        270        280        290        300 
TRHLAEFWMV EPEIAFADLS DAADLAEEML KYVFKAVLEE RPDDMAFFQQ RVDKTVLDRL 

       310        320        330        340        350        360 
NSVINTDFVR LDYTDAITIL ENCGKKFENQ VSWGVDLNSE HERYLAEEHF NGPVVLQNYP 

       370        380        390        400        410        420 
KDIKSFYMRL NDDGKTVAAM DILAPGIGEI IGGSQREERL DVLDSRLEEM GLDIADYGWY 

       430        440        450        460 
RDLRRYGTVP HSGFGLGFER LVAYATGMQN VRDVIPFPRT PNNAAF 

« Hide

References

[1]"The psychrophilic lifestyle as revealed by the genome sequence of Colwellia psychrerythraea 34H through genomic and proteomic analyses."
Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X., Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M., Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A., Zhou L., Davidsen T.M. expand/collapse author list , Wu M., Huston A.L., Lewis M., Weaver B., Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005) [PubMed: 16043709] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 34H / ATCC BAA-681.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000083 Genomic DNA. Translation: AAZ27879.1.
RefSeqYP_269306.1. NC_003910.7.

3D structure databases

HSSPHSSP built from PDB template 1X56 based on UniProtKB O57980.
ProteinModelPortalQ481G3.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ481G3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3522138.
GenomeReviewsGene locus CPS_2591 in contig CP000083_GR.
KEGGcps:CPS_2591.
NMPDRfig|167879.3.peg.2872.
PATRIC21468243. VBIColPsy94388_2355.
TIGRCPS_2591.

Phylogenomic databases

eggNOGCOG0017.
HOGENOMHBG745843.
OMAAIHRFFH.
ProtClustDBPRK03932.

Enzyme and pathway databases

BioCycCPSY167879:CPS_2591-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_COLP3
AccessionPrimary (citable) accession number: Q481G3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 13, 2005
Last modified: January 25, 2012
This is version 50 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