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O66647 (SYS_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine--tRNA ligase
EC=6.1.1.11
Alternative name(s):
Seryl-tRNA synthetase
Short name=SerRS
Seryl-tRNA(Ser/Sec) synthetase
Gene names
Name:serS
Ordered Locus Names:aq_298
OrganismAquifex aeolicus (strain VF5)
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) By similarity. HAMAP MF_00176

Catalytic activity

ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). HAMAP MF_00176

ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). HAMAP MF_00176

Pathway

Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. HAMAP MF_00176

Subunit structure

Homodimer. The tRNA molecule binds across the dimer By similarity.

Subcellular location

Cytoplasm By similarity HAMAP MF_00176.

Domain

Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding By similarity. HAMAP MF_00176

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processseryl-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

serine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 425425Serine--tRNA ligase HAMAP MF_00176
PRO_0000121995

Regions

Nucleotide binding262 – 2643ATP By similarity
Nucleotide binding349 – 3524ATP By similarity
Region231 – 2333Serine binding By similarity

Sites

Binding site2851Serine By similarity
Binding site3851Serine By similarity

Secondary structure

1 ................................................................................ 425
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O66647 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 30173C92567DC784

FASTA42549,433
        10         20         30         40         50         60 
MIDINLIREK PDYVKERLAT RDKELVSLVD KVLELDKRRR EIIKRLEALR SERNKLSKEI 

        70         80         90        100        110        120 
GKLKREGKDT TEIQNRVKEL KEEIDRLEEE LRKVEEELKN TLLWIPNLPH PSVPVGEDEK 

       130        140        150        160        170        180 
DNVEVRRWGE PRKFDFEPKP HWEIGERLGI LDFKRGAKLS GSRFTVIAGW GARLERALIN 

       190        200        210        220        230        240 
FMLDLHTKKG YKEICPPHLV KPEILIGTGQ LPKFEEDLYK CERDNLYLIP TAEVPLTNLY 

       250        260        270        280        290        300 
REEILKEENL PIYLTAYTPC YRREAGAYGK DIRGIIRQHQ FDKVELVKIV HPDTSYDELE 

       310        320        330        340        350        360 
KLVKDAEEVL QLLGLPYRVV ELCTGDLGFS AAKTYDIEVW FPSQNKYREI SSCSNCEDFQ 

       370        380        390        400        410        420 
ARRMNTRFKD SKTGKNRFVH TLNGSGLAVG RTLAAILENY QQEDGSVVVP EVLRDYVGTD 


VIRPE

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000657 Genomic DNA. Translation: AAC06595.1.
PIRC70327.
RefSeqNP_213207.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DQ3X-ray3.00A/B1-425[»]
ProteinModelPortalO66647.
SMRO66647. Positions 1-425.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1192881.
GenomeReviewsGene locus aq_298 in contig AE000657_GR.
KEGGaae:aq_298.
NMPDRfig|224324.1.peg.222.
PATRIC20958212. VBIAquAeo85532_0245.

Phylogenomic databases

HOGENOMHBG629391.
OMAHTKPLEE.
PhylomeDBO66647.
ProtClustDBPRK05431.

Enzyme and pathway databases

BioCycAAEO224324:AQ_298-MONOMER.

Family and domain databases

HAMAPMF_00176. Ser_tRNA_synth_type1.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR002317. Ser-tRNA-synth_IIa.
IPR015866. Ser-tRNA-synth_IIa_N.
IPR010978. tRNA-bd_arm.
[Graphical view]
Gene3DG3DSA:1.10.287.40. Ser-tRNA-synth_IIa_N. 1 hit.
KOK01875.
PANTHERPTHR11778. tRNA-synt_ser. 1 hit.
PfamPF02403. Seryl_tRNA_N. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PIRSFPIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
PRINTSPR00981. TRNASYNTHSER.
SUPFAMSSF46589. tRNA_binding_arm. 1 hit.
TIGRFAMsTIGR00414. SerS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYS_AQUAE
AccessionPrimary (citable) accession number: O66647
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: January 25, 2012
This is version 76 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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