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Reviewed, UniProtKB/Swiss-Prot B0BYR8 (SYS_ACAM1)

Last modified November 3, 2009. Version 11. 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: AM1_2069
OrganismAcaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]
Taxonomic identifier329726 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaAcaryochloris

Protein attributes

Sequence length424 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 – 424424Seryl-tRNA synthetase HAMAP MF_00176
PRO_1000077183

Regions

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

Sites

Binding site2871Serine By similarity
Binding site3871Serine By similarity

Sequences

Sequence LengthMass (Da)Tools
B0BYR8-1 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 5956B09FC385E842

FASTA42447,218
        10         20         30         40         50         60 
MIDLKQLREN PEAFAECLSR RGDYDLQAIL DLDQKQRELE TERSQLQARS NQIGKTIGER 

        70         80         90        100        110        120 
MKGGANPKDP EIQNLRQEGS TVKATLSDLE PKERDLKAEI GELLLTIPNL PSDDTPVGKD 

       130        140        150        160        170        180 
ETANVEVSRW GDEYIPKNAK LAHWEIGENL GILNFERSVK VAQSRFATLV GAGAALERAL 

       190        200        210        220        230        240 
IQFMLDQQVE AGYVEVLPPV LVNSDSLTAT GQLPKFAEES FKCAEDDLWL SPTAEVPVTN 

       250        260        270        280        290        300 
LYRDEIINAD DLPIFHCAYT PCFRREAGSY GRDTRGLIRL HQFNKVELVK LVHPSTSAAE 

       310        320        330        340        350        360 
HEALVKNAAA ILEALKLPYR VLQLCTGDLG FSAAKCYDLE VWLPSADCYR EISSCSNFLD 

       370        380        390        400        410        420 
FQARRGNIRF KESGQKGTQF VHTLNGSGLA VGRTMAAVLE NYQQPDGSVQ VPDVLQPYLK 


RKVL 

« Hide

References

Cross-references

Sequence databases

CP000828 Genomic DNA. Translation: ABW27084.1.
RefSeqYP_001516398.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5680883.
GenomeReviewsGene locus AM1_2069 in contig CP000828_GR.
KEGGamr:AM1_2069.

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_ACAM1
AccessionPrimary (citable) accession number: B0BYR8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 26, 2008
Last modified: November 3, 2009
This is version 11 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