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Q1LTE8 (SYS_BAUCH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. 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:BCI_0318
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia

Protein attributes

Sequence length430 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 – 430430Serine--tRNA ligase HAMAP MF_00176
PRO_1000019618

Regions

Nucleotide binding268 – 2703ATP By similarity
Nucleotide binding355 – 3584ATP By similarity
Region237 – 2393Serine binding By similarity

Sites

Binding site2911Serine By similarity
Binding site3911Serine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1LTE8 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 90A8E0735E80F9E5

FASTA43049,484
        10         20         30         40         50         60 
MLDPYLLRHD IKIVAKKLAS KNFLLAVDKV NQQEALRKQL QIKKEHLQFI RKSKSRIVNL 

        70         80         90        100        110        120 
AKANGENITI LCQEINQINE QLKQTKSELS SLKQLINDYM LLLPNIPADD VPYGSDKKDN 

       130        140        150        160        170        180 
IEIKRWGEPR KYNFPIKDHV NLGYITGNID FTAGVKLAGT RFVVIRGQIA RLYRALSQFM 

       190        200        210        220        230        240 
LDLHTQQHGY EEYYLPYLVN RTSLYGTGHL PKFYEDLFHI QSINKENISN IYTLIPTAEV 

       250        260        270        280        290        300 
PLINLLRDKI FDENILPLKM TANTPCFRAE AGSYGRDTHG LIRMHQFDKV EMVQAIKPEH 

       310        320        330        340        350        360 
SMIALEEMTK HAEKVLQLLN LHYRKVLLCT GDTGFASSKT YDLEVWLPSQ NIYCEVSSCS 

       370        380        390        400        410        420 
NTSDFQTRRV LARYRNKKDK QLRFLHTING SGLAIGRTLI AILENYQLAD GRIEVPKSLR 

       430 
SYMQGLTILG 

« Hide

References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000238 Genomic DNA. Translation: ABF14125.1.
RefSeqYP_588766.1. NC_007984.1.

3D structure databases

ProteinModelPortalQ1LTE8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1LTE8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4056311.
GenomeReviewsGene locus BCI_0318 in contig CP000238_GR.
KEGGbci:BCI_0318.
PATRIC21074143. VBIBauCic75062_0305.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0172.
HOGENOMHBG629391.
OMAHTKPLEE.
PhylomeDBQ1LTE8.

Enzyme and pathway databases

BioCycBCIC186490:BCI_0318-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_BAUCH
AccessionPrimary (citable) accession number: Q1LTE8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 30, 2006
Last modified: January 25, 2012
This is version 45 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