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B2RK42 (SYN_PORG3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. 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:PGN_1218
OrganismPorphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / JCM 12257) [Complete proteome] [HAMAP]
Taxonomic identifier431947 [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 By similarity 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_1000211906

Sequences

Sequence LengthMass (Da)Tools
B2RK42 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: EE951D983068EEDF

FASTA46953,101
        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 TNTFGVIYRI 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]"Determination of the genome sequence of Porphyromonas gingivalis strain ATCC 33277 and genomic comparison with strain W83 revealed extensive genome rearrangements in P. gingivalis."
Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H., Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T., Nakayama K.
DNA Res. 15:215-225(2008) [PubMed: 18524787] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33277 / DSM 20709 / JCM 12257.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009380 Genomic DNA. Translation: BAG33737.1.
RefSeqYP_001929334.1. NC_010729.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB2RK42.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6329201.
GenomeReviewsGene locus PGN_1218 in contig AP009380_GR.
KEGGpgn:PGN_1218.
PATRIC22975408. VBIPorGin26334_1212.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG745843.
OMAAIHRFFH.
ProtClustDBPRK03932.

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_PORG3
AccessionPrimary (citable) accession number: B2RK42
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 1, 2008
Last modified: January 25, 2012
This is version 33 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