Skip Header

Contribute Send feedback
Read comments (?) or add your own

O51244 (SYS_BORBU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. 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
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:BB_0226
OrganismBorrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680) [Reference proteome] [HAMAP]
Taxonomic identifier224326 [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_0000122011

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
O51244 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 9AE5CEBB420D5A3B

FASTA42548,787
        10         20         30         40         50         60 
MLDLKFIRDN LDLVKRSIKA RGLVLDIDKL IYLDDKRKKL ITKIGELNAK RNENSSKMQE 

        70         80         90        100        110        120 
NLDKVLKISL IETGKILKKQ LIDLEEELER VSVDFDLENK KVPNILSPDV PIGSSEEDNF 

       130        140        150        160        170        180 
EIKRVGVVPQ FDFKPKDHLE LGRDLDLLDF DRAREISGSK FYYLKNEAVF LEIALINFSL 

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

       250        260        270        280        290        300 
KIIDLTLPIR MAGFSHCFRK EAGAYGQLSK GLYRVHQFSK VEMFCFCKAE ESGVIHDEFL 

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

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


IPFKN

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000783 Genomic DNA. Translation: AAC66622.1.
PIRB70128.
RefSeqNP_212360.1. NC_001318.1.

3D structure databases

ProteinModelPortalO51244.
ModBaseSearch...

Protein-protein interaction databases

STRING224326.BB0226.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC66622; AAC66622; BB_0226.
GeneID1195063.
KEGGbbu:BB_0226.
PATRIC20557066. VBIBorBur75917_0624.

Phylogenomic databases

eggNOGCOG0172.
KOK01875.
OMANENANAM.
ProtClustDBPRK05431.

Enzyme and pathway databases

BioCycBBUR224326:BB_0226-MONOMER.
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_BORBU
AccessionPrimary (citable) accession number: O51244
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: May 1, 2013
This is version 91 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents