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Q5NXU8 (SYS_AROAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
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:AZOSEA39910
ORF Names:ebA7034
OrganismAromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAromatoleum

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 termComplete 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 – 427427Serine--tRNA ligase HAMAP MF_00176
PRO_0000121996

Regions

Nucleotide binding263 – 2653ATP By similarity
Nucleotide binding350 – 3534ATP By similarity
Region232 – 2343Serine binding By similarity

Sites

Binding site2861Serine By similarity
Binding site3851Serine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5NXU8 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 96423CFB1657143F

FASTA42747,052
        10         20         30         40         50         60 
MLDIQLLRTQ IDAVAAALAA RGANFDAAAF QSMENERKTL QTRTQDLQAR RNTLSKQIGV 

        70         80         90        100        110        120 
LKSRGEDASA AMAEVGGIGD ELKANEQALA TLLERINAFV AGLPNLPHDS VPPGRDESAN 

       130        140        150        160        170        180 
VEIARWGTPR EFDFEVSDHV DIGSGLGGLD FETAAKISGS RFALMRDGLA RLHRALAQFM 

       190        200        210        220        230        240 
LDVHTREHGY TEVHVPYLVN PDSMFGTGQL PKFEAELFSV MKDDGRFYLI PTAEVPITNI 

       250        260        270        280        290        300 
VRNELLAHDV LPLKFVGHTP CFRSEAGSYG RDTRGMIRQH QFDKVELVRI EHPDASWAAL 

       310        320        330        340        350        360 
EELTGHAEAI LRKLELPYRK VVLCTGDMGF SAAKTYDLEV WLPAQKTYRE ISSCSCTGAF 

       370        380        390        400        410        420 
QARRMQARFR NTQGKNELVH TLNGSGLAVG RTLVAVLENY QQADGSVVVP KVLVPWMGGI 


EVLEPRG 

« Hide

References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed: 15551059] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EbN1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR555306 Genomic DNA. Translation: CAI10116.1.
RefSeqYP_161017.1. NC_006513.1.

3D structure databases

ProteinModelPortalQ5NXU8.
SMRQ5NXU8. Positions 1-426.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5NXU8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3182502.
GenomeReviewsGene locus AZOSEA39910 in contig CR555306_GR.
KEGGeba:ebA7034.
NMPDRfig|76114.4.peg.4007.
PATRIC20974215. VBIAroAro98752_4021.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0172.
HOGENOMHBG629391.
OMAPKFADDM.
ProtClustDBPRK05431.

Enzyme and pathway databases

BioCycASP76114:EBA7034-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_AROAE
AccessionPrimary (citable) accession number: Q5NXU8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 4, 2005
Last modified: January 25, 2012
This is version 51 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

SIMILARITY comments

Index of protein domains and families