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Reviewed, UniProtKB/Swiss-Prot A7Z0D5 (SYS_BACA2)

Last modified November 3, 2009. Version 16. 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: RBAM_000160
OrganismBacillus amyloliquefaciens (strain FZB42) [Complete proteome] [HAMAP]
Taxonomic identifier326423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length425 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 – 425425Seryl-tRNA synthetase HAMAP MF_00176
PRO_1000019615

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
A7Z0D5-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 0C741E2B39F77ED0

FASTA42548,894
        10         20         30         40         50         60 
MIDTKVLRAN FQEVKAKLIP KGEDLSDFDK FEELDEKRRE LIGKVEELKG KRNEVSQQVA 

        70         80         90        100        110        120 
VLKREKKDAD HIIKEMREVG EEIKKLDEEL RTVETTLETI LLSIPNIPHD SVPVGETEDD 

       130        140        150        160        170        180 
NIEIRKWGEA PAFSYEPKPH WDIADHLNIL DFERASKVTG SRFVFYKGLG ARLERALYNF 

       190        200        210        220        230        240 
MLDLHVDEYD YTEVIPPYMV NRTSMTGTGQ LPKFEEDAFK IREEDYFLIP TAEVPITNMH 

       250        260        270        280        290        300 
RDEILSGENL PINYAAFSAC FRSEAGSAGR DTRGLIRQHQ FNKVELVKFV KPEDSYEELE 

       310        320        330        340        350        360 
KLTNQAERVL QLLELPYRVM SMCTGDLGFT AAKKYDIEVW IPSQDTYREI SSCSNFEAFQ 

       370        380        390        400        410        420 
ARRANIRFRR EAKGKPEHVH TLNGSGLAVG RTVAAILENY QQEDGSVIIP KVLRPYMGNK 


EVIKP 

« Hide

References

[1]"Comparative analysis of the complete genome sequence of the plant growth-promoting bacterium Bacillus amyloliquefaciens FZB42."
Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., Strittmatter A., Gottschalk G., Borriss R.
Nat. Biotechnol. 25:1007-1014(2007) [PubMed: 17704766] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000560 Genomic DNA. Translation: ABS72461.1.
RefSeqYP_001419692.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA7Z0D5.

Genome annotation databases

GeneID5460158.
GenomeReviewsGene locus RBAM_000160 in contig CP000560_GR.
KEGGbay:RBAM_000160.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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_BACA2
AccessionPrimary (citable) accession number: A7Z0D5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 23, 2007
Last modified: November 3, 2009
This is version 16 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