SMART: Pfam domain SepSecS

The domain within your query sequence starts at position 61 and ends at position 459; the E-value for the SepSecS domain shown below is 4e-182.

MDSNNFLGNCGVGEREGRVASALVARRHYRFIHGIGRSGDISAVQPKAAGSSLLNKITNS
LVLNVIKLAGVHSVASCFVVPMATGMSLTLCFLTLRHKRPKAKYIIWPRIDQKSCFKSMV
TAGFEPVVIENVLEGDELRTDLKAVEAKIQELGPEHILCLHSTTACFAPRVPDRLEELAV
ICANYDIPHVVNNAYGLQSSKCMHLIQQGARVGRIDAFVQSLDKNFMVPVGGAIIAGFNE
PFIQDISKMYPGRASASPSLDVLITLLSLGCSGYRKLLKERKEMFVYLSTQLKKLAEAHN
ERLLQTPHNPISLAMTLKTIDGHHDKAVTQLGSMLFTRQVSGARAVPLGNVQTVSGHTFR
GFMSHADNYPCAYLNAAAAIGMKMQDVDLFIKRLDKCLN

SepSecS

PFAM accession number:	PF05889
Interpro abstract (IPR008829):	Early annotation suggested this family, SepSecS, of several eukaryotic and archaeal proteins, was involved in antigen-antibodies responses in the liver and pancreas [ (PUBMED:10801173) (PUBMED:11481605) ]. Structural studies show that the family is O-phosphoseryl-tRNA(Sec) selenium transferase, an enzyme involved in the synthesis of the amino acid selenocysteine (Sec). Sec is the only amino acid whose biosynthesis occurs on its cognate transfer RNA (tRNA). SepSecS catalyses the final step in the formation of the amino acid [ (PUBMED:17194211) (PUBMED:18093968) (PUBMED:18158303) (PUBMED:19608919) ]. The early observation that autoantibodies isolated from patients with type I autoimmune hepatitis targeted a ribonucleoprotein complex containing tRNASec led to the identification and characterisation of the archaeal and the human SepSecS [ (PUBMED:11481605) ]. SepSecS forms its own branch in the family of fold-type I pyridoxal phosphate (PLP) enzymes that goes back to the last universal common ancestor. This entry also includes O-phosphoseryl-tRNA:Cys-tRNA synthase SepCysS. It is found in Methanogenic archaea, which have an alternative pathway for Cys-tRNACys formation [ (PUBMED:17512006) (PUBMED:18559341) ].
GO function:	transferase activity (GO:0016740)

PFAM accession number:

PF05889

Interpro abstract (IPR008829):

Early annotation suggested this family, SepSecS, of several eukaryotic and archaeal proteins, was involved in antigen-antibodies responses in the liver and pancreas [ (PUBMED:10801173) (PUBMED:11481605) ]. Structural studies show that the family is O-phosphoseryl-tRNA(Sec) selenium transferase, an enzyme involved in the synthesis of the amino acid selenocysteine (Sec). Sec is the only amino acid whose biosynthesis occurs on its cognate transfer RNA (tRNA). SepSecS catalyses the final step in the formation of the amino acid [ (PUBMED:17194211) (PUBMED:18093968) (PUBMED:18158303) (PUBMED:19608919) ]. The early observation that autoantibodies isolated from patients with type I autoimmune hepatitis targeted a ribonucleoprotein complex containing tRNASec led to the identification and characterisation of the archaeal and the human SepSecS [ (PUBMED:11481605) ]. SepSecS forms its own branch in the family of fold-type I pyridoxal phosphate (PLP) enzymes that goes back to the last universal common ancestor.

This entry also includes O-phosphoseryl-tRNA:Cys-tRNA synthase SepCysS. It is found in Methanogenic archaea, which have an alternative pathway for Cys-tRNACys formation [ (PUBMED:17512006) (PUBMED:18559341) ].

GO function:

transferase activity (GO:0016740)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry SepSecS