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Q82F68 (SYD_STRAW) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 66. 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

EC=6.1.1.12
Alternative name(s):
Aspartyl-tRNA synthetase
Short name=AspRS
Gene names
Name:aspS
Ordered Locus Names:SAV_4395
OrganismStreptomyces avermitilis [Complete proteome] [HAMAP]
Taxonomic identifier33903 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length587 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 – 587587Aspartate--tRNA ligase HAMAP MF_00044_B
PRO_0000110951

Sequences

Sequence LengthMass (Da)Tools
Q82F68 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 377A27DAF9EC9823

FASTA58765,725
        10         20         30         40         50         60 
MHRYRSHTCG ELRASDVGSD VRLSGWLHNR RDLGGILFID LRDHYGITQL VARPGTPAYE 

        70         80         90        100        110        120 
ALDKVSKEST VRVDGKVVSR GTENVNPDLP TGEIEVEVSE VELLGAAAPL PFTINAEDGV 

       130        140        150        160        170        180 
NEERRLEYRF LDLRRERMHR NILLRTAVIS AIRHKMTALG FNEMATPILS ATSPEGARDF 

       190        200        210        220        230        240 
VVPSRLHPGK FYALPQAPQQ FKQLLMISGF DRYFQIAPCF RDEDARADRS PGEFYQLDVE 

       250        260        270        280        290        300 
MSFVEQEDVF QPIEKLMTEL FEEFGGGRHV TSPFPRIPFR EAMLKYGSDK PDLRAQLELV 

       310        320        330        340        350        360 
DITDIFEGSE FKAFAGKHVR ALPVPDVSGQ TRKFFDGLGD YAVEQGAKGL AWVRVGEDGS 

       370        380        390        400        410        420 
LTGPIAKFLT EENVAELTKR LSLAPGHAVF FGAGEFDEVS KIMGAVRVEA AKRSGNFEEN 

       430        440        450        460        470        480 
VFRFCWIVDF PMYEKDEDTG KIDFSHNPFS MPQGGLEALE TQDPLDILGW QYDIVCNGVE 

       490        500        510        520        530        540 
LSSGAIRNHE PEIMLKAFEI AGYDRDTVEE QFAGMLRAFR FGAPPHGGIA PGVDRIVMLL 

       550        560        570        580 
ADEPNIRETI AFPLNGNAQD LMMGAPTELD ETRLRELHLS VRKPQPK 

« Hide

References

[1]"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed: 11572948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.
[2]"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
Nat. Biotechnol. 21:526-531(2003) [PubMed: 12692562] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000030 Genomic DNA. Translation: BAC72107.1.
RefSeqNP_825572.1. NC_003155.4.

3D structure databases

ProteinModelPortalQ82F68.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1210986.
GenomeReviewsGene locus SAV_4395 in contig BA000030_GR.
KEGGsma:SAV_4395.
NMPDRfig|227882.1.peg.4398.
PATRIC23722595. VBIStrAve112782_4679.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG396032.
OMAYQLDVEM.
ProtClustDBPRK00476.

Enzyme and pathway databases

BioCycSAVE227882:SAV4395-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 nameSYD_STRAW
AccessionPrimary (citable) accession number: Q82F68
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 66 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