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

Q8TXK0 (SPCS_METKA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
O-phosphoseryl-tRNA(Sec) selenium transferase

EC=2.9.1.2
Alternative name(s):
Selenocysteine synthase
Short name=Sec synthase
Selenocysteinyl-tRNA(Sec) synthase
Sep-tRNA:Sec-tRNA synthase
Short name=SepSecS
Gene names
Name:spcS
Ordered Locus Names:MK0672
OrganismMethanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) [Reference proteome] [HAMAP]
Taxonomic identifier190192 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus

Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis By similarity.

Catalytic activity

O-phospho-L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (archaeal/eukaryal route): step 2/2.

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the SepSecS family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 431431O-phosphoseryl-tRNA(Sec) selenium transferase
PRO_0000219882

Regions

Region1 – 3636Tetramerization By similarity
Region88 – 9811Phosphate loop (P-loop) By similarity

Sites

Binding site671PLP By similarity
Binding site891Substrate By similarity
Binding site901Substrate By similarity
Binding site971Substrate By similarity
Binding site2981Substrate By similarity
Site661May act as a substrate filter by repelling compounds with a negatively charged alpha-carboxylate By similarity

Amino acid modifications

Modified residue2691N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8TXK0 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 4557FD9AF640CA03

FASTA43147,589
        10         20         30         40         50         60 
MRGLIPDHML ERGRTVLDSY REPVERLLSE RRMPEEGWPD DVIATFLWEL SRMDTDKDPK 

        70         80         90        100        110        120 
AARIGEREAR VASRLAEESV FGFCHGVGRS GTLVDPQPKA PGASIMYALT NRLVTDFLRR 

       130        140        150        160        170        180 
LGFRIEGAFV VPGATGLSIA LCLSALGEGE EVIYPYAAHK SPIKAVRLAG FGMRVVDTEI 

       190        200        210        220        230        240 
EGDRIVVDPG DVEEALERSE SPAAVLSTLT FFPPRSSDPL PEIAELCEEY GVPHVVNAAY 

       250        260        270        280        290        300 
GIQHEQYRDL LNRAIKRGRV DVVVSSTDKN LLTPVGGGIV YAPDEETLRE VSRAYPGRAS 

       310        320        330        340        350        360 
AAPVAHALIS LLSLGMKGYR RLMRRQKECK ALLDELLEDL EARRDDVRVL DVDNPIASAV 

       370        380        390        400        410        420 
AVEGHDPVDL AARLYVRRVT GPRGVRADDP FGTSRLRGYH SNYITINAAI GVREEDVKTA 

       430 
VERLERELEG E 

« Hide

References

[1]"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens."
Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A.
Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009439 Genomic DNA. Translation: AAM01887.1.
RefSeqNP_613957.1. NC_003551.1.

3D structure databases

ProteinModelPortalQ8TXK0.
SMRQ8TXK0. Positions 1-426.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190192.MK0672.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM01887; AAM01887; MK0672.
GeneID1476773.
KEGGmka:MK0672.

Phylogenomic databases

eggNOGCOG0076.
HOGENOMHOG000254245.
KOK03341.
OMAHIINGAY.

Enzyme and pathway databases

UniPathwayUPA00906; UER00898.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
InterProIPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR019872. Sec-tRNA_Se_transferase.
IPR008829. SLA/LP_auto_ag.
[Graphical view]
PANTHERPTHR12944. PTHR12944. 1 hit.
PfamPF05889. SLA_LP_auto_ag. 1 hit.
[Graphical view]
PIRSFPIRSF017689. SepSecS. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR03531. selenium_SpcS. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSPCS_METKA
AccessionPrimary (citable) accession number: Q8TXK0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: June 1, 2002
Last modified: May 14, 2014
This is version 56 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