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B7HII5 (SYS_BACC4) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 23. 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:BCB4264_A0016
OrganismBacillus cereus (strain B4264) [Complete proteome] [HAMAP]
Taxonomic identifier405532 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length424 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 – 424424Serine--tRNA ligase HAMAP MF_00176
PRO_1000199465

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
B7HII5 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 2A876A0D7C280B26

FASTA42448,790
        10         20         30         40         50         60 
MLDIKFLRTN FEEVKAKLQH RGEDLTDFGR FEELDTRRRE LLVQTEELKS KRNEVSQQIS 

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

       130        140        150        160        170        180 
NVVARTWGEV KEFTYEPKPH 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 
KLTNDAERVL QLLELPYRVM SMCTGDLGFT AAKKYDIEVW IPSYGTYREI SSCSNFEAFQ 

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


TVIK 

« Hide

References

[1]"Genome sequence of Bacillus cereus B4264."
Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., Ravel J., Sutton G.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B4264.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001176 Genomic DNA. Translation: ACK61623.1.
RefSeqYP_002364867.1. NC_011725.1.

3D structure databases

ProteinModelPortalB7HII5.
SMRB7HII5. Positions 1-424.
ModBaseSearch...

Protein-protein interaction databases

STRINGB7HII5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000111103; EBBACP00000105083; EBBACG00000111096.
GeneID7100703.
GenomeReviewsGene locus BCB4264_A0016 in contig CP001176_GR.
KEGGbcb:BCB4264_A0016.
PATRIC18871991. VBIBacCer117876_0012.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000002086.
HOGENOMHBG629391.
OMAPKFADDM.
ProtClustDBPRK05431.

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_BACC4
AccessionPrimary (citable) accession number: B7HII5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: January 25, 2012
This is version 23 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