Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P81434 (SYS_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:BUsg_303
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length427 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.

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: UniProtKB-HAMAP

selenocysteinyl-tRNA(Sec) biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

seryl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

serine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Serine--tRNA ligase HAMAP-Rule MF_00176
PRO_0000122019

Regions

Nucleotide binding264 – 2663ATP By similarity
Nucleotide binding351 – 3544ATP By similarity
Region233 – 2353Serine binding By similarity
Compositional bias371 – 3766Poly-Lys HAMAP-Rule MF_00176

Sites

Binding site2871Serine By similarity
Binding site3871Serine By similarity

Experimental info

Sequence conflict451D → E in AAC05434. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P81434 [UniParc].

Last modified August 30, 2002. Version 2.
Checksum: CC416EFD7C861B87

FASTA42749,238
        10         20         30         40         50         60 
MLNPYLLRNQ IDAISKKLLK KKFKLDISLI SSLEKKRKKL QIKTDNLQYK HNTLSALFKK 

        70         80         90        100        110        120 
EKKIQELDEN LKRTLTKSSK NLSELKIELN LLQEKIHNFS LSIPNIPSDD VPEGNSSENN 

       130        140        150        160        170        180 
KIVKYWGKKR EYSFAVRDHV EIGNKLNQLD WKSSAKISGA RFIVMKGNIA LLHRALSQFM 

       190        200        210        220        230        240 
LDLHTIKHGY TETYVPYLVN HDSLYGTGQL PKFTDDLFHI NSIDKKKYVL IPTAEVPLTN 

       250        260        270        280        290        300 
LFSNQILNET ELPIMLTAHT PCFRSEASSY GRDSKGLIRL HQFDKVELVQ IIQPELSMNA 

       310        320        330        340        350        360 
LELLTHHAEK VLQLLELPYR KVLLCGGEMG FSATKTYDLE VWFPSQKKYR EISSCSNMSD 

       370        380        390        400        410        420 
FQARRMKTRY KKKKEKSNSF VHTLNGSGLA IGRTLAAILE NYQDSDGRVT IPKILQKKYM 


QGIEYIN 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of a DNA fragment from Buchnera aphidicola (Aphid endosymbiont) containing the genes aspS-trxB-serS-serC-aroA-rpsA-himD-tpiA."
Thao M.L., Baumann P.
Curr. Microbiol. 35:68-69(1997)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L43549 Genomic DNA. Translation: AAC05434.1.
AE013218 Genomic DNA. Translation: AAM67857.1.
RefSeqNP_660646.1. NC_004061.1.

3D structure databases

ProteinModelPortalP81434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg303.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67857; AAM67857; BUsg_303.
GeneID1005507.
KEGGbas:BUsg303.
PATRIC21247413. VBIBucAph100086_0316.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0172.
KOK01875.
OMAEQQIDLK.
OrthoDBEOG61KBH9.
ProtClustDBPRK05431.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-317-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. SSF46589. 1 hit.
TIGRFAMsTIGR00414. serS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYS_BUCAP
AccessionPrimary (citable) accession number: P81434
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 30, 2002
Last modified: February 19, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries