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H6R6F6 (H6R6F6_NOCCG) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 10. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Serine--tRNA ligase HAMAP-Rule MF_00176
EC=6.1.1.11 HAMAP-Rule MF_00176
Alternative name(s):
Seryl-tRNA synthetase HAMAP-Rule MF_00176
Seryl-tRNA(Ser/Sec) synthetase HAMAP-Rule MF_00176
Gene names
Name:serS HAMAP-Rule MF_00176 EMBL CCF60929.1
Ordered Locus Names:NOCYR_0105 EMBL CCF60929.1
OrganismNocardia cyriacigeorgica (strain GUH-2) [Complete proteome] [HAMAP] EMBL CCF60929.1
Taxonomic identifier1127134 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Nocardia ›

Protein attributes

Sequence length420 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(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). HAMAP-Rule MF_00176

ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). 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. HAMAP-Rule MF_00176

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. HAMAP-Rule MF_00176

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding258 – 2603ATP By similarity HAMAP-Rule MF_00176
Nucleotide binding345 – 3484ATP By similarity HAMAP-Rule MF_00176
Region227 – 2293Serine binding By similarity HAMAP-Rule MF_00176

Sites

Binding site2741ATP; via amide nitrogen and carbonyl oxygen By similarity HAMAP-Rule MF_00176
Binding site2811Serine By similarity HAMAP-Rule MF_00176
Binding site3801Serine By similarity HAMAP-Rule MF_00176

Sequences

Sequence LengthMass (Da)Tools
H6R6F6 [UniParc].

Last modified April 18, 2012. Version 1.
Checksum: AC287C841C7308C8

FASTA42045,797
        10         20         30         40         50         60 
MIDLRFLREH PDVVRASQRA RGEDPALVDA LLEADAARRA AVATADNLRA EHKAMGKKIG 

        70         80         90        100        110        120 
KASKEERPAL LAEASEMSAK VKEAEAAQHA ADADLDAAQR AISNVVQEGA PAGGEDDYIL 

       130        140        150        160        170        180 
LDTIGTPPEF DFTPKDHLEL GESLGLIDME RGAKVSGARF YFLTGYGALL QLGLLQLAAQ 

       190        200        210        220        230        240 
RAVANGFTMM IPPVLVRPEI MAGTGFLGQH SAEVYHLADD DLYLVGTSEV PLAGYHSDEI 

       250        260        270        280        290        300 
LDLSGGAKRY AGWSSCFRRE AGSYGKDTRG IIRVHQFDKV EMFVYCKPED ADAEHQRLLA 

       310        320        330        340        350        360 
WEREMLAAIE VPYRIIDVAA GDLGSSAARK FDCEAWVPSQ RTYRELTSTS NCTTFQARRL 

       370        380        390        400        410        420 
SVRYRDENGK PQIAATLNGT LATTRWIVAL LENHQQADGS VRVPEALVPF VGTDVLTAPK

« Hide

References

[1]"Genome sequence of the human- and animal-pathogenic strain Nocardia cyriacigeorgica GUH-2."
Zoropogui A., Pujic P., Normand P., Barbe V., Beaman B., Beaman L., Boiron P., Colinon C., Deredjian A., Graindorge A., Mangenot S., Nazaret S., Neto M., Petit S., Roche D., Vallenet D., Rodriguez-Nava V., Richard Y., Cournoyer B., Blaha D.
J. Bacteriol. 194:2098-2099(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GUH-2 EMBL CCF60929.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FO082843 Genomic DNA. Translation: CCF60929.1.
RefSeqYP_005261573.1. NC_016887.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCF60929; CCF60929; NOCYR_0105.
GeneID11925001.
KEGGncy:NOCYR_0105.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01875.

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. tRNA_binding_arm. 1 hit.
TIGRFAMsTIGR00414. serS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameH6R6F6_NOCCG
AccessionPrimary (citable) accession number: H6R6F6
Entry history
Integrated into UniProtKB/TrEMBL: April 18, 2012
Last sequence update: April 18, 2012
Last modified: April 3, 2013
This is version 10 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info