ID A0A023X4T3_9ACTN Unreviewed; 486 AA. AC A0A023X4T3; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 17-JUN-2020, entry version 37. DE RecName: Full=L-seryl-tRNA(Sec) selenium transferase {ECO:0000256|HAMAP-Rule:MF_00423}; DE EC=2.9.1.1 {ECO:0000256|HAMAP-Rule:MF_00423}; DE AltName: Full=Selenocysteine synthase {ECO:0000256|HAMAP-Rule:MF_00423}; DE Short=Sec synthase {ECO:0000256|HAMAP-Rule:MF_00423}; DE AltName: Full=Selenocysteinyl-tRNA(Sec) synthase {ECO:0000256|HAMAP-Rule:MF_00423}; GN Name=selA {ECO:0000256|HAMAP-Rule:MF_00423}; GN ORFNames=RradSPS_1761 {ECO:0000313|EMBL:AHY47044.1}; OS Rubrobacter radiotolerans. OC Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales; Rubrobacteraceae; OC Rubrobacter. OX NCBI_TaxID=42256 {ECO:0000313|EMBL:AHY47044.1, ECO:0000313|Proteomes:UP000025229}; RN [1] {ECO:0000313|EMBL:AHY47044.1, ECO:0000313|Proteomes:UP000025229} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RSPS-4 {ECO:0000313|EMBL:AHY47044.1, RC ECO:0000313|Proteomes:UP000025229}; RA Egas C.C., Barroso C.C., Froufe H.J.C., Pacheco J.J., Albuquerque L.L., RA da Costa M.M.S.; RT "Complete genome sequence of the Radio-Resistant Rubrobacter radiotolerans RT RSPS-4."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) CC required for selenoprotein biosynthesis. {ECO:0000256|HAMAP- CC Rule:MF_00423, ECO:0000256|SAAS:SAAS00546321}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + L-seryl-tRNA(Sec) + selenophosphate = L- CC selenocysteinyl-tRNA(Sec) + phosphate; Xref=Rhea:RHEA:22728, CC Rhea:RHEA-COMP:9742, Rhea:RHEA-COMP:9743, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16144, ChEBI:CHEBI:43474, ChEBI:CHEBI:78533, CC ChEBI:CHEBI:78573; EC=2.9.1.1; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00423, ECO:0000256|SAAS:SAAS01169763}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00423, CC ECO:0000256|PIRSR:PIRSR618319-50, ECO:0000256|SAAS:SAAS00352468}; CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) CC biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) CC (bacterial route): step 1/1. {ECO:0000256|HAMAP-Rule:MF_00423, CC ECO:0000256|SAAS:SAAS00029255}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00423, CC ECO:0000256|SAAS:SAAS00352483}. CC -!- SIMILARITY: Belongs to the SelA family. {ECO:0000256|HAMAP- CC Rule:MF_00423, ECO:0000256|SAAS:SAAS00571347}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP007514; AHY47044.1; -; Genomic_DNA. DR STRING; 42256.RradSPS_1761; -. DR EnsemblBacteria; AHY47044; AHY47044; RradSPS_1761. DR KEGG; rrd:RradSPS_1761; -. DR PATRIC; fig|42256.3.peg.1785; -. DR HOGENOM; CLU_038142_1_0_11; -. DR UniPathway; UPA00906; UER00896. DR Proteomes; UP000025229; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004125; F:L-seryl-tRNASec selenium transferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0001514; P:selenocysteine incorporation; IEA:UniProtKB-UniRule. DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.640.10; -; 1. DR HAMAP; MF_00423; SelA; 1. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR018319; SelA-like. DR InterPro; IPR004534; SelA_trans. DR InterPro; IPR025862; SelA_trans_N_dom. DR Pfam; PF12390; Se-cys_synth_N; 1. DR Pfam; PF03841; SelA; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR00474; selA; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00423, ECO:0000256|SAAS:SAAS00430028}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00423, KW ECO:0000256|SAAS:SAAS00029246}; KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00423, KW ECO:0000256|PIRSR:PIRSR618319-50, ECO:0000256|SAAS:SAAS00430041}; KW Reference proteome {ECO:0000313|Proteomes:UP000025229}; KW Selenium {ECO:0000256|HAMAP-Rule:MF_00423, ECO:0000256|SAAS:SAAS00430051}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00423, KW ECO:0000256|SAAS:SAAS00430034, ECO:0000313|EMBL:AHY47044.1}. FT DOMAIN 24..63 FT /note="Se-cys_synth_N" FT /evidence="ECO:0000259|Pfam:PF12390" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 308 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00423, FT ECO:0000256|PIRSR:PIRSR618319-50" SQ SEQUENCE 486 AA; 51225 MW; 314BCB4EA6F64C3D CRC64; MNRRENSHET PAKTTPDAGL RGRLRALPAV DSVLGYAPVA DHVKRYGATV VTEAVRETLE DLRRRILLGD EPDASEAAVT AGVEVRLRER EARGLRRVVN ATGVVLHTNL GRSVLSGRAV AAAVEAASGY SNLEYDLGEG RRGSRYEHAV PLLRELAGAE DALVVNNCAG ATLLALAAVV GGGPDAEPGG EVVVSRGQLI EIGGGFRIPE VLEVSGATLR EVGTTNRTRL EDYRRAINER TRAVLWVHPS NFEVVGFTES VGVGELASLG PPVIADVGSG ALLPFAHEPR VPEAVRAGAA VVIFSGDKLL GGPQAGIVVG KRELVGRMRS HPLTRALRAD KLCLAALEAT LKAYLDGRAD EELPTRRMLD ADPETVRERA ESLAGALADS LAGVVPQDVR FGVVPTVARS GGGTLPTYEI PSFAVRVAGA EANTLAARLR DAGPEGTPVV GRVHEGALLL DARTLLDGDE ERIVAAFRRC FRGADG //