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O67140 (SELA_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. 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:
L-seryl-tRNA(Sec) selenium transferase

EC=2.9.1.1
Alternative name(s):
Selenocysteine synthase
Short name=Sec synthase
Selenocysteinyl-tRNA(Sec) synthase
Gene names
Name:selA
Ordered Locus Names:aq_1031
OrganismAquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis By similarity. HAMAP-Rule MF_00423

Catalytic activity

L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate. HAMAP-Rule MF_00423

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00423

Pathway

Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (bacterial route): step 1/1. HAMAP-Rule MF_00423

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00423.

Sequence similarities

Belongs to the SelA family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
Selenium
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processselenocysteine incorporation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

selenocysteinyl-tRNA(Sec) biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionL-seryl-tRNASec selenium transferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 452452L-seryl-tRNA(Sec) selenium transferase HAMAP-Rule MF_00423
PRO_0000189594

Amino acid modifications

Modified residue2851N6-(pyridoxal phosphate)lysine By similarity

Secondary structure

....................................................................................... 452
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O67140 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: E511326E17E9F015

FASTA45250,848
        10         20         30         40         50         60 
MKSLLRQIPQ ISKVVEIFKK KYPEIYVVKA AREVAEKYRK EIIEGKRKDL NGFLEDVERK 

        70         80         90        100        110        120 
IKSLMKPNIK RVINATGVVI NTNLGRAPLS KDVINFISEI ANGYSNLEYN LEEGKRGSRI 

       130        140        150        160        170        180 
AHIEKYLNEL TGAESSFVVN NNAGAVFLVL NTLAEGKEVI ISRGELVEIG GSFRIPDIMK 

       190        200        210        220        230        240 
KSGAILREVG TTNKTKVSDY EGAINQNTAL LMKVHKSNFY MEGFVEEVKL EDLVKLGHKY 

       250        260        270        280        290        300 
GIPTYYDAGS GLLINLKEFG ISVDEPNFRD CISLGIDLVS GSGDKLLGGP QAGIIVGKKN 

       310        320        330        340        350        360 
LIEKIKKNPI ARALRIDKLT LSGLEMTLKL YFEKRYEDIP VIRMLTQDEK ALRQKAKRLE 

       370        380        390        400        410        420 
KLLKDIPGLK ISVIKDKAKP GGGSLPELEL PTYCVAIRHD RLSSQELSRR LRLAEPPIVC 

       430        440        450 
RIREDQLLFD MRTVFHEDLK TIKKTLQELL SI 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC07094.1.
PIRA70389.
RefSeqNP_213703.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3W1HX-ray3.89A/B/C/D/E1-452[»]
3W1IX-ray3.19A/B/C/D/E/F/G/H/I/J62-452[»]
3W1JX-ray3.25A/B/C/D/E/F/G/H/I/J62-452[»]
3W1KX-ray7.50A/B/C/D/E1-452[»]
3WCNX-ray3.35A/B1-452[»]
3WCOX-ray2.40A/B62-452[»]
ProteinModelPortalO67140.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224324.aq_1031.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC07094; AAC07094; aq_1031.
GeneID1193774.
KEGGaae:aq_1031.
PATRIC20959366. VBIAquAeo85532_0805.

Phylogenomic databases

eggNOGCOG1921.
HOGENOMHOG000163726.
KOK01042.
OMANRTHARD.
OrthoDBEOG69WFGN.
ProtClustDBPRK04311.

Enzyme and pathway databases

BioCycAAEO224324:GJBH-736-MONOMER.
UniPathwayUPA00906; UER00896.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
HAMAPMF_00423. SelA.
InterProIPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR018319. SelA-like.
IPR004534. SelA_trans.
[Graphical view]
PfamPF03841. SelA. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR00474. selA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSELA_AQUAE
AccessionPrimary (citable) accession number: O67140
Entry history
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 86 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways