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Q7MVE5 (SYN_PORGI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. 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:PG_1121
OrganismPorphyromonas gingivalis (strain ATCC BAA-308 / W83) [Complete proteome] [HAMAP]
Taxonomic identifier242619 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas

Protein attributes

Sequence length469 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 – 469469Asparagine--tRNA ligase HAMAP MF_00534
PRO_0000176441

Sequences

Sequence LengthMass (Da)Tools
Q7MVE5 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: B6DA3CC719A4E175

FASTA46953,073
        10         20         30         40         50         60 
MDKKMKRTRI ADALHGGLVG QEINIKGWVR TKRGNKAVNF IALNDGSTIH NMQIVADLAS 

        70         80         90        100        110        120 
FDAAQMSQIT TGACIGVIGT LVESQGAGQS VEVQASAIEI YGTADPATYP LQKKGHTLEF 

       130        140        150        160        170        180 
LREIAHLRPR TNTFGAIYRI RHHMAIAIHT FFHNKGYYYF HAPLITASDC EGAGQMFQVT 

       190        200        210        220        230        240 
TLNPDSLPRT EEGQVDYRKD FFGRHTSLTV SGQLEGEMAA MALGGIYTFG PTFRAENSNT 

       250        260        270        280        290        300 
PRHLAEFWMI EPEVAFLEIE DNMDLAEEFI KYCVQWALDN CMDDISFLSE HFDKELIDRL 

       310        320        330        340        350        360 
KFVLEKPFVR LAYTEGIRIL EEAVKNGVKF EFPIYWGADL ASEHERYLVE VHFKTPVIMT 

       370        380        390        400        410        420 
DYPKEIKSFY MKLNDDGKTV RGMDVLFPKI GEIIGGSERE ADYDKLVARA NEMGVPEKDI 

       430        440        450        460 
WWYLDSRRYG TAPHSGFGLG FERLLLFVTG MSNIRDVIPF PRTPNNAEF 

« Hide

References

[1]"Complete genome sequence of the oral pathogenic bacterium Porphyromonas gingivalis strain W83."
Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E., Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J., Granger D., Tettelin H. expand/collapse author list , Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E., Fraser C.M.
J. Bacteriol. 185:5591-5601(2003) [PubMed: 12949112] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-308 / W83.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015924 Genomic DNA. Translation: AAQ66230.1.
RefSeqNP_905331.1. NC_002950.2.

3D structure databases

ProteinModelPortalQ7MVE5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2553310.
GenomeReviewsGene locus PG_1121 in contig AE015924_GR.
KEGGpgi:PG1121.
NMPDRfig|242619.1.peg.972.
PATRIC22979292. VBIPorGin134034_1039.
TIGRPG_1121.

Phylogenomic databases

HOGENOMHBG745843.
OMAAIHRFFH.
PhylomeDBQ7MVE5.
ProtClustDBPRK03932.

Enzyme and pathway databases

BioCycPGIN242619:PG_1121-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_PORGI
AccessionPrimary (citable) accession number: Q7MVE5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: December 15, 2003
Last modified: January 25, 2012
This is version 63 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