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P73851 (SYDND_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. 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(Asp/Asn) ligase

EC=6.1.1.23
Alternative name(s):
Aspartyl-tRNA synthetase
Short name=AspRS
Non-discriminating aspartyl-tRNA synthetase
Short name=ND-AspRS
Gene names
Name:aspS
Ordered Locus Names:slr1720
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis

Protein attributes

Sequence length599 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn) By similarity. HAMAP-Rule MF_00044

Catalytic activity

ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx). HAMAP-Rule MF_00044

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00044

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00044.

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
Reference proteome
Gene Ontology (GO)
   Biological_processaspartyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

aspartate-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

aspartate-tRNA(Asn) ligase activity

Inferred from electronic annotation. Source: UniProtKB-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 – 599599Aspartate--tRNA(Asp/Asn) ligase HAMAP-Rule MF_00044
PRO_0000110967

Regions

Nucleotide binding224 – 2263ATP By similarity
Nucleotide binding540 – 5434ATP By similarity
Region202 – 2054Aspartate By similarity

Sites

Binding site1781Aspartate By similarity
Binding site2241Aspartate By similarity
Binding site2331ATP By similarity
Binding site4581Aspartate By similarity
Binding site4881ATP By similarity
Binding site4951Aspartate By similarity
Site301Important for tRNA non-discrimination By similarity

Sequences

Sequence LengthMass (Da)Tools
P73851 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 2B89C952C82A5246

FASTA59967,209
        10         20         30         40         50         60 
MRTHYCGDLR TTHLGETVTL YGWVDRRRDH GGVIFLDLRD RQGIVQIASS PDQTPASYPV 

        70         80         90        100        110        120 
AEGLRNEYVV QVTGVVSKRP PESLNEKIPT GEIEIYADSI ILLNGVNQQL PFVVSSHEAE 

       130        140        150        160        170        180 
QVREDVRLKY RYLDLRRARL SQNLQLRHQV VKAMRRFLED QENFLEIETP ILTRSTPEGA 

       190        200        210        220        230        240 
RDYLVPSRVN PGEWYALPQS PQLFKQLLMV AGMDRYYQIA RCFRDEDLRA DRQPEFTQLD 

       250        260        270        280        290        300 
MEMSFMGQEE ILDLNEALIC HIFKVVKNID LPRPFPRLTY QESMAKYGND RPDTRFGLEL 

       310        320        330        340        350        360 
VDVSDLLGNT GFKVFSAAVS SGGSIKAIRV PGGNETISNV RIKPGGDLFK EATEAGAKGI 

       370        380        390        400        410        420 
AYIRVRDNGE IDTIGAIKEN LDEAQVKTLL QLTQAEAGDL LLFGAGDTAT VDKSLSRLRL 

       430        440        450        460        470        480 
VLGEQLGLID PDAINLLWIT DFPMFEWNSD EKRFEALHHP FTAPHPDDLG DLKTARAQAY 

       490        500        510        520        530        540 
DLVMNGVEIG GGSLRIYQRE VQEKVFATIG LSPEEAHEKF GFLLDAFEYG TPPHGGIAYG 

       550        560        570        580        590 
LDRLVMLLAK EDSIRDVIAF PKTQQASCLL TEAPAAVDKK QLKELSVAST YVPKVKVDD 

« Hide

References

[1]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 6803 / Kazusa.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000022 Genomic DNA. Translation: BAA17910.1.
PIRS75048.
RefSeqNP_441230.1. NC_000911.1.
YP_005651287.1. NC_017277.1.
YP_007451112.1. NC_020286.1.

3D structure databases

ProteinModelPortalP73851.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP73851. 2 interactions.
STRING1148.slr1720.

Proteomic databases

PaxDbP73851.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA17910; BAA17910; BAA17910.
GeneID954572.
KEGGsyn:slr1720.
syy:SYNGTS_1334.
syz:MYO_113460.
PATRIC23839800. VBISynSp132158_1461.

Phylogenomic databases

eggNOGCOG0173.
HOGENOMHOG000275159.
KOK01876.
OMAIGYEIST.
OrthoDBEOG68Q0NX.
PhylomeDBP73851.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
3.30.1360.30. 1 hit.
HAMAPMF_00044. Asp_tRNA_synth.
InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004524. Asp-tRNA-ligase_IIb_bac/mt.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR004115. GAD-like.
IPR029351. GAD_dom.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PANTHERPTHR22594. PTHR22594. 1 hit.
PTHR22594:SF5. PTHR22594:SF5. 1 hit.
PfamPF02938. GAD. 1 hit.
PF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSPR01042. TRNASYNTHASP.
SUPFAMSSF50249. SSF50249. 1 hit.
SSF55261. SSF55261. 1 hit.
TIGRFAMsTIGR00459. aspS_bact. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYDND_SYNY3
AccessionPrimary (citable) accession number: P73851
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: July 9, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

SIMILARITY comments

Index of protein domains and families