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Q6MEC9 (SYN_PARUW) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. 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:pc0346
OrganismProtochlamydia amoebophila (strain UWE25) [Complete proteome] [HAMAP]
Taxonomic identifier264201 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesParachlamydiaceaeCandidatus Protochlamydia

Protein attributes

Sequence length467 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 – 467467Asparagine--tRNA ligase HAMAP MF_00534
PRO_0000176437

Sequences

Sequence LengthMass (Da)Tools
Q6MEC9 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 88C897627C8BC543

FASTA46753,285
        10         20         30         40         50         60 
MRTKIKSLRG TTPEVRALIG HDITLKGWVR TVRNQKTFTF IEINDGSTLS NFQIIATPDI 

        70         80         90        100        110        120 
AGYDQLINQL STGVSVSAIG TIVESPGKEQ NLEMQATAIT IIGKCDPEVY LLQKKRHTFE 

       130        140        150        160        170        180 
FLRSIAHLRP RTNTIGAVTR VRNALAFATH QFFQKRGFLY IHTPIITGSD CEGAGKMFQV 

       190        200        210        220        230        240 
TTLDQNNPAR TPEGRVDYTQ DFFGKPTYLT VSGQLNGEIY ACALSDVYTF GPTFRAENSN 

       250        260        270        280        290        300 
TSRHLAEFWM IEPEMAFADL NDNMDCAEDY LKYILKYVLD NCQEDMEFFN KHVATDLISR 

       310        320        330        340        350        360 
LEHVINTSFE RASYTYAVRI LEKADKKFEY PVKWGLDLQS EHERFLAEEF FGKPVILTDY 

       370        380        390        400        410        420 
PKDIKAFYMR TNEDNKTVAA MDVLVPKVGE IIGGSQREER LSVLESKLKE FNLPAEEYWW 

       430        440        450        460 
YLELRKFGSV PHSGFGAGFE RLVQFTTGME NIRDVIPFPR HPGKADF 

« Hide

References

[1]"Illuminating the evolutionary history of chlamydiae."
Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U., Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T., Mewes H.-W., Wagner M.
Science 304:728-730(2004) [PubMed: 15073324] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UWE25.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX908798 Genomic DNA. Translation: CAF23070.1.
RefSeqYP_007345.1. NC_005861.1.

3D structure databases

ProteinModelPortalQ6MEC9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6MEC9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2779793.
GenomeReviewsGene locus pc0346 in contig BX908798_GR.
KEGGpcu:pc0346.
NMPDRfig|264201.1.peg.346.
PATRIC31995994. VBICanPro72727_0352.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0017.
HOGENOMHBG745843.
OMAAIHRFFH.
PhylomeDBQ6MEC9.
ProtClustDBPRK03932.

Enzyme and pathway databases

BioCycCPRO264201:PC0346-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_PARUW
AccessionPrimary (citable) accession number: Q6MEC9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 56 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