Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q73FJ3 (SYS_BACC1)

Last modified November 3, 2009. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Seryl-tRNA synthetase
    EC=6.1.1.11
Alternative name(s):
    Seryl-tRNA(Ser/Sec) synthetase
    Serine--tRNA ligase
      Short name=SerRS
Gene names
Name: serS
Ordered Locus Names: BCE_0013
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]
Taxonomic identifier222523 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length424 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

Domain

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

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 processselenocysteine biosynthetic process

Inferred from electronic annotation. Source: HAMAP

seryl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

serine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 424424Seryl-tRNA synthetase HAMAP MF_00176
PRO_0000121998

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

Sequences

Sequence LengthMass (Da)Tools
Q73FJ3-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 34904276F4E801F0

FASTA42448,770
        10         20         30         40         50         60 
MLDIKFLRTN FEEVKAKLQH RGEDLTDFGR FEELDTRRRE LLVQTEELKS KRNEVSQQIS 

        70         80         90        100        110        120 
VLKREKKDAE SLILEMREVG EKVKDLDNEL RTVEEDLERL MLSIPNIPHE SAPVGETEDD 

       130        140        150        160        170        180 
NVVARTWGEV KEFAFEPKPH WDLATDLGIL DFERAGKVTG SRFVFYKGAG ARLERALISF 

       190        200        210        220        230        240 
MLDLHTDEHG YEEVLPPYMV NRASMTGTGQ LPKFEEDAFR IESEDYFLIP TAEVPVTNMH 

       250        260        270        280        290        300 
RDEILNKEQL PIRYAAFSSC FRSEAGSAGR DTRGLIRQHQ FNKVELVKFV KPEDSYEELE 

       310        320        330        340        350        360 
KLXNDAERVL QLLELPYRVM SMCTGDLGFT AAKKYDIEVW IPSYGTYREI SSCSNFEAFQ 

       370        380        390        400        410        420 
ARRANIRFRR EPNGKPEHVH TLNGSGLAIG RTVAAILENY QQEDGTIIIP EVLRPYMGGK 


TVIK 

« Hide

References

[1]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE017194 Genomic DNA. Translation: AAS38949.1.
RefSeqNP_976341.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ73FJ3.

Genome annotation databases

GeneID2751256.
GenomeReviewsGene locus BCE_0013 in contig AE017194_GR.
KEGGbca:BCE_0013.
NMPDRfig|222523.1.peg.13.
TIGRBCE_0013.

Phylogenomic databases

HOGENOMQ73FJ3.
OMALKPYMGG.

Family and domain databases

HAMAPMF_00176.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-reg.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR002317. Ser-tRNA-synth_IIa.
IPR018156. Ser-tRNA-synth_IIa_C.
IPR015866. Ser-tRNA-synth_IIa_N.
[Graphical view]
Gene3DG3DSA:1.10.287.40. Ser-tRNA-synth_IIa_N. 1 hit.
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.
TIGRFAMsTIGR00414. serS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYS_BACC1
AccessionPrimary (citable) accession number: Q73FJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: November 3, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents