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Q0SNT6 (SYS_BORAP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:BAPKO_0234, BafPKo_0228
OrganismBorrelia afzelii (strain PKo) [Complete proteome] [HAMAP]
Taxonomic identifier390236 [NCBI]
Taxonomic lineageBacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group ›

Protein attributes

Sequence length425 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-Rule MF_00176

Catalytic activity

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

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

Pathway

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

Subunit structure

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

Subcellular location

Cytoplasm By similarity.

Domain

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

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 425425Serine--tRNA ligase HAMAP-Rule MF_00176
PRO_1000019622

Regions

Nucleotide binding259 – 2613ATP By similarity
Nucleotide binding349 – 3524ATP By similarity
Region229 – 2313Serine binding By similarity

Sites

Binding site2751ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site2821Serine By similarity
Binding site3841Serine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0SNT6 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: E81030BB2695B8A0

FASTA42548,948
        10         20         30         40         50         60 
MLDLKFIRDN LDLVKRSIKA RGLVLDIDKL IYLDDKRKKI ITKIGELNAK RNENSSKMRE 

        70         80         90        100        110        120 
NLDKVLKISL IETGKILKKQ LIDLEEELER VSFDFDLENK RVPNILSPDV PIGNSEEDNF 

       130        140        150        160        170        180 
EIKKVGIIPR FDFKPKDHLE LGRDLDLLDF DRAREVSGSK FYYLKNEAVF LEIALINFSL 

       190        200        210        220        230        240 
NKLREKGFNV FITPDVAREF IVDGIGFNPR GNESNIYKIE DTDKYLVGTS EITLGGYYYN 

       250        260        270        280        290        300 
KIIDLTLPIK MAGFSHCFRK EAGAYGQLSK GLYRVHQFSK VEMFCFCKAE ESSIIHDEFL 

       310        320        330        340        350        360 
SIQEQIFTEL EIPYRVLNIC SFDLGSPAYK KYDIEAWMPG RDGKGGYGEI TSTSNCTDYQ 

       370        380        390        400        410        420 
SRRLKIRYKD QDGQNKFAHM VNGTAIATTR VIISILENFQ DEKGGVKIPK SLVKYTGFDY 


IPFKN

« Hide

References

[1]"Comparative genome analysis: selection pressure on the Borrelia vls cassettes is essential for infectivity."
Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J., Wilske B., Platzer M.
BMC Genomics 7:211-211(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PKo.
[2]"Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii Lyme disease agent isolates."
Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J., Fraser-Liggett C.M., Schutzer S.E.
J. Bacteriol. 193:6995-6996(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PKo.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000395 Genomic DNA. Translation: ABH01492.1.
CP002933 Genomic DNA. Translation: AEL69455.1.
RefSeqYP_005592445.1. NC_017238.1.
YP_709668.1. NC_008277.1.

3D structure databases

ProteinModelPortalQ0SNT6.
ModBaseSearch...

Protein-protein interaction databases

STRING390236.BAPKO_0234.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABH01492; ABH01492; BAPKO_0234.
AEL69455; AEL69455; BafPKo_0228.
GeneID12159182.
4227844.
KEGGbaf:BAPKO_0234.
bafz:BafPKo_0228.
PATRIC37188756. VBIBorAfz3878_0291.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0172.
HOGENOMHOG000035937.
KOK01875.
OMANENANAM.
ProtClustDBPRK05431.

Enzyme and pathway databases

UniPathwayUPA00906; UER00895.

Family and domain databases

Gene3D1.10.287.40. 1 hit.
HAMAPMF_00176. Ser_tRNA_synth_type1.
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR002317. Ser-tRNA-ligase_type_1.
IPR015866. Ser-tRNA-synth_1_N.
IPR010978. tRNA-bd_arm.
[Graphical view]
PANTHERPTHR11778. PTHR11778. 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_BORAP
AccessionPrimary (citable) accession number: Q0SNT6
Secondary accession number(s): G0IR69
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 5, 2006
Last modified: May 1, 2013
This is version 58 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

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