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A7Z0D5 (SYS_BACA2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:RBAM_000160
OrganismBacillus amyloliquefaciens (strain FZB42) [Complete proteome] [HAMAP]
Taxonomic identifier326423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

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 HAMAP-Rule 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-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_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 [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

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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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FZB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000560 Genomic DNA. Translation: ABS72461.1.
RefSeqYP_001419692.1. NC_009725.1.

3D structure databases

ProteinModelPortalA7Z0D5.
SMRA7Z0D5. Positions 1-425.
ModBaseSearch...

Protein-protein interaction databases

STRING326423.RBAM_000160.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS72461; ABS72461; RBAM_000160.
GeneID5460158.
KEGGbay:RBAM_000160.
PATRIC18744923. VBIBacAmy31356_0013.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0172.
HOGENOMHOG000035938.
KOK01875.
OMAEESWEWH.
ProtClustDBPRK05431.

Enzyme and pathway databases

BioCycBAMY326423:GCM4-16-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_BACA2
AccessionPrimary (citable) accession number: A7Z0D5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 23, 2007
Last modified: May 29, 2013
This is version 46 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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