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Q8DSG3 (SYD1_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 68. 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 1

EC=6.1.1.12
Alternative name(s):
Aspartyl-tRNA synthetase 1
Short name=AspRS 1
Gene names
Name:aspS1
Ordered Locus Names:SMU_1822
OrganismStreptococcus mutans [Complete proteome] [HAMAP]
Taxonomic identifier1309 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length583 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 – 583583Aspartate--tRNA ligase 1 HAMAP MF_00044_B
PRO_0000110953

Sequences

Sequence LengthMass (Da)Tools
Q8DSG3 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: C54974E7690F315C

FASTA58366,163
        10         20         30         40         50         60 
MKELFIGNYG LEQVGQKVTA KGWVANIRNH GKLAFIELRD REGLLQVFVD SAVADFDKLH 

        70         80         90        100        110        120 
DLHKESILAV TGEIVARDER FVNPHIKSGQ VELRAETIEI IASSKLLPFE LDNHAHAGED 

       130        140        150        160        170        180 
IRQKYRYLDL RREKMTANLK LRHQVTKAIR DYLNQADFID VETPYLTKST PEGARDFLVP 

       190        200        210        220        230        240 
SRVFKNQFYA LPQSPQMLKQ LLMGAGLERY YQIVRCFRDE DLRGDRQPEF TQVDLEMSFV 

       250        260        270        280        290        300 
SEEDVRNLVE GMLKAVVKAS KGIELTEAFP IISYAQAMRR FGSDKPDTRF AMELKDLTEL 

       310        320        330        340        350        360 
SRGNTSLFLQ KGLKKENGVV MGICAKNAAK AFTNRQMATL KQLVMDFGVA GFATATIEKG 

       370        380        390        400        410        420 
QVTGSLKSTF KDHNTELLEL FEAEDGDMIF FVTGSLKRVQ EALGGLRVRL AKDLELIDND 

       430        440        450        460        470        480 
KLNFLWVVDW PLLEWNEDLN RYQAMHHPFT QGAFEDGSDW KENPEKMMSR AYDIVLNGYE 

       490        500        510        520        530        540 
IGGGSLRIHK RSAQEAMFEL LGMKKEDYER DFGFFLEALE YGFPPHGGLA LGLDRLVMIL 

       550        560        570        580 
AEEGNIREVI AFPKNGQGAD AMLESPSLVA DQQLAELRLA LRD 

« 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: AAN59447.1.
RefSeqNP_722141.1. NC_004350.2.

3D structure databases

ProteinModelPortalQ8DSG3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTRT00000013752; EBSTRP00000013234; EBSTRG00000013752.
GeneID1029036.
GenomeReviewsGene locus SMU_1822 in contig AE014133_GR.
KEGGsmu:SMU_1822.
NMPDRfig|210007.1.peg.1654.
PATRIC19665645. VBIStrMut61772_1627.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000027607.
HOGENOMHBG396032.
OMAVAPKQKV.
ProtClustDBPRK00476.

Enzyme and pathway databases

BioCycSMUT210007:SMU_1822-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 nameSYD1_STRMU
AccessionPrimary (citable) accession number: Q8DSG3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 68 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