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A5GRE1 (SYS_SYNR3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 49. 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:SynRCC307_0547
OrganismSynechococcus sp. (strain RCC307) [Complete proteome] [HAMAP]
Taxonomic identifier316278 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

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.

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 – 425425Serine--tRNA ligase HAMAP-Rule MF_00176
PRO_1000019850

Regions

Nucleotide binding264 – 2663ATP By similarity
Nucleotide binding351 – 3544ATP By similarity
Region233 – 2353Serine binding By similarity

Sites

Binding site2871Serine By similarity
Binding site3851Serine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5GRE1 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 72BB71DE409ED4EC

FASTA42547,543
        10         20         30         40         50         60 
MLDQRLLRDN PELISQQLGR RGMEVDLTKL QLIAKQERDL EEQRSNLQAE GNRTGKEVGM 

        70         80         90        100        110        120 
LIKGGAAPDS DEVKALREKG NRIKQQVAVL EEEEKGLEAK LREQLLALPN LPSADAPEGK 

       130        140        150        160        170        180 
SEADNVEVKR WGEPRQGKDL EEHWQLADRL GLFETERSVR IAQSRFITLM GDGARLERAL 

       190        200        210        220        230        240 
ISFMLDLHST KGYTEVMPPI LVNSASLTGS GQLPKFAEES FRCADDDLWL TPTAEVPLTS 

       250        260        270        280        290        300 
LHRDEVIAVE QLPLKYAAYT PCFRREAGSY GRDTRGLIRL HQFNKVELYW FCHPEKSAEA 

       310        320        330        340        350        360 
HEQLTLDAEA VLEALELPYR RLELCTGDMG FSAARTYDLE VWLPGAGSYR EISSCSTCGD 

       370        380        390        400        410        420 
FQARRSAIRF KEGKGTQLLH TLNGSGLAIG RTMAALLENG QQPDGSIQLP AALVPYFGRE 


RLTPQ 

« Hide

References

[1]Genoscope
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RCC307.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CT978603 Genomic DNA. Translation: CAK27450.1.
RefSeqYP_001226803.1. NC_009482.1.

3D structure databases

ProteinModelPortalA5GRE1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316278.SynRCC307_0547.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAK27450; CAK27450; SynRCC307_0547.
GeneID5157122.
KEGGsyr:SynRCC307_0547.
PATRIC23821954. VBISynSp108374_0540.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0172.
HOGENOMHOG000035938.
KOK01875.
OMAYRPERHE.
OrthoDBEOG61KBH9.
ProtClustDBPRK05431.

Enzyme and pathway databases

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_SYNR3
AccessionPrimary (citable) accession number: A5GRE1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: February 19, 2014
This is version 49 of the entry and version 1 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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries