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Q8DRV9 (SYD2_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. 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:
Aspartate--tRNA ligase 2

EC=6.1.1.12
Alternative name(s):
Aspartyl-tRNA synthetase 2
Short name=AspRS 2
Gene names
Name:aspS2
Ordered Locus Names:SMU_2101
OrganismStreptococcus mutans [Complete proteome] [HAMAP]
Taxonomic identifier1309 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length589 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp). HAMAP MF_00044_B

Subunit structure

Homodimer By similarity. HAMAP MF_00044_B

Subcellular location

Cytoplasm HAMAP MF_00044_B.

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 processtRNA aminoacylation for protein translation

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

aspartate-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 – 589589Aspartate--tRNA ligase 2 HAMAP MF_00044_B
PRO_0000110954

Sequences

Sequence LengthMass (Da)Tools
Q8DRV9 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 0EDDDC6426881A4A

FASTA58966,967
        10         20         30         40         50         60 
MKRSMYAGAV RSEHIGQELT LKGWVARRRD LGGLIFIDLR DREGIVQLVI NPKTASNTVV 

        70         80         90        100        110        120 
KSAESLRSEY VIEVTGMIVE RDQANDNLPT GCVEMQVTQL TILNASQTPP FEIKDKIEAN 

       130        140        150        160        170        180 
DDTRLRYRYL DLRRPEMLKN FKLRAKVTHV IRNYLDDLDF IDVETPMLAK STPEGARDYL 

       190        200        210        220        230        240 
VPSRMSRGHF YALPQSPQIT KQLLMNAGFD RYYQIVKCFR DEDLRGDRQP EFTQVDLETS 

       250        260        270        280        290        300 
FLSEQEIQEI TERLIACVMK EVKGIELQLP LPQISYDTAM NNYGSDKPDT RFEMTLQDLT 

       310        320        330        340        350        360 
DLVKNIDFKV FSQAPAVKAI VAKNAANSYS RKAIDKLTDI VKPFGAKGLA WVKYNDGKIG 

       370        380        390        400        410        420 
GPIAKFLTTI EDELIERLQL EANDLVFFVA DDLEIANGSL GALRNHLAKE LNLIDHSKFN 

       430        440        450        460        470        480 
FLWVVDWPMF EWSEEENRYT SAHHPFTLPQ EDTVAELEGD LSKVRAVAYD IVLNGYELGG 

       490        500        510        520        530        540 
GSLRINQRET QERMFKALGF TKESAQKQFG FLLEAMDYGF PPHGGLALGL DRFVMLLAGK 

       550        560        570        580 
ENIREVIAFP KNNKASDPMT QAPSLVSDKQ LDELYLQVNK NAVKNNEQE 

« Hide

References

[1]"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen."
Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.
Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed: 12397186] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159 / Serotype c.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014133 Genomic DNA. Translation: AAN59695.1.
RefSeqNP_722389.1. NC_004350.2.

3D structure databases

ProteinModelPortalQ8DRV9.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTRT00000012865; EBSTRP00000012347; EBSTRG00000012865.
GeneID1029277.
GenomeReviewsGene locus SMU_2101 in contig AE014133_GR.
KEGGsmu:SMU_2101.
NMPDRfig|210007.1.peg.1902.
PATRIC19666147. VBIStrMut61772_1871.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000027607.
HOGENOMHBG396032.
OMAAFPKTQQ.
ProtClustDBPRK00476.

Enzyme and pathway databases

BioCycSMUT210007:SMU_2101-MONOMER.

Family and domain databases

HAMAPMF_00044_B. Asp_tRNA_synth_B.
[Tree]
InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004524. Asp-tRNA-synth_IIb_bac/mt.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR004115. GAD_dom.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR004365. NA-bd_OB_tRNA-helicase.
[Graphical view]
Gene3DG3DSA:3.30.1360.30. GAD_dom. 1 hit.
G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KOK01876.
PANTHERPTHR22594. aa-tRNA-synt_II. 1 hit.
PTHR22594:SF5. AspS_bac. 1 hit.
PfamPF02938. GAD. 1 hit.
PF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
PRINTSPR01042. TRNASYNTHASP.
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
SSF55261. SSF55261. 1 hit.
TIGRFAMsTIGR00459. AspS_bact. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYD2_STRMU
AccessionPrimary (citable) accession number: Q8DRV9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 69 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