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B6db families: 2.9.1.2

2.9.1.2
Activity 2.9.1.2
Description O-phospho-L-seryl-tRNA(Sec):L-selenocysteinyl-tRNA synthase
Notes Rather compact family, composed of eukaryotic and archaeal (methanogens) enzymes.
PDB 3BC8;3BCB;
PLP Fold Type I
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type I

Number of sequences
18
Sequences in seed alignment
ArchaeaSPCS_METKA (Methanopyrus kandleri); SPCS_METJA (Methanocaldococcus jannaschii); SPCS_METMP (Methanococcus maripaludis);
MetazoaEAT44258 (Aedes aegypti); NP_001093359 (Xenopus laevis); BAC28410 (Mus musculus); XP_625123 (Apis mellifera); XP_001362538 (Monodelphis domestica); SPCS_CAEEL (Caenorhabditis elegans); XP_781218 (Strongylocentrotus purpuratus); NP_058651 (Homo sapiens); NP_956448 (Danio rerio);
Other_EukaryaXP_001032036 (Tetrahymena thermophila); EAN80252 (Trypanosoma brucei); XP_641299 (Dictyostelium discoideum AX4); XP_001463557 (Leishmania infantum); XP_001350460 (Plasmodium falciparum); XP_001455539 (Paramecium tetraurelia);

DISPLAY: Fasta format, alignment, hmm, hmm_local


Reference sequence BAC28410
Domain interval 61-459
Catalytic site 284 K
 
References
 Palioura S, Sherrer RL, Steitz TA, Söll D, Simonovic M. (2009) The human SepSecS-tRNASec complex reveals the mechanism of selenocysteine formation Science 325 321-5.

 Ganichkin OM, Xu XM, Carlson BA, Mix H, Hatfield DL, Gladyshev VN, Wahl MC. (2008) Structure and catalytic mechanism of eukaryotic selenocysteine synthase J Biol Chem 5849-65.

 Xu, X.M.; Carlson, B.A.; Mix, H.; Zhang, Y.; Saira K.; Glass, R.S.; Berry, M.J.; Gladyshev, V.N.; Hatfield, D.L. (2007) Biosynthesis of selenocysteine on its tRNA in eukaryotes PLoS Biol. e4.

 Yuan J, Palioura S, Salazar JC, Su D, O'Donoghue P, Hohn MJ, Cardoso AM, Whitman WB, Söll D. (2006) RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea Proc Natl Acad Sci U S A 103 18923-7.

Articles on 2.9.1.2
last changed 2010/01/12 13:16

B6db families