ID A0A0N5CQW9_THECL Unreviewed; 475 AA.
AC A0A0N5CQW9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 08-NOV-2023, entry version 34.
DE RecName: Full=O-phosphoseryl-tRNA(Sec) selenium transferase {ECO:0000256|ARBA:ARBA00021963, ECO:0000256|PIRNR:PIRNR017689};
DE EC=2.9.1.2 {ECO:0000256|ARBA:ARBA00012464, ECO:0000256|PIRNR:PIRNR017689};
DE AltName: Full=Selenocysteine synthase {ECO:0000256|ARBA:ARBA00030669, ECO:0000256|PIRNR:PIRNR017689};
DE AltName: Full=Selenocysteinyl-tRNA(Sec) synthase {ECO:0000256|ARBA:ARBA00032048, ECO:0000256|PIRNR:PIRNR017689};
DE AltName: Full=Sep-tRNA:Sec-tRNA synthase {ECO:0000256|ARBA:ARBA00032693, ECO:0000256|PIRNR:PIRNR017689};
GN ORFNames=TCLT_LOCUS2620 {ECO:0000313|EMBL:VDM98682.1};
OS Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000261901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TCLT_0000261901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM98682.1, ECO:0000313|Proteomes:UP000276776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-
CC tRNA(Sec) required for selenoprotein biosynthesis.
CC {ECO:0000256|ARBA:ARBA00002552, ECO:0000256|PIRNR:PIRNR017689}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-tRNA(Sec) + selenophosphate = L-
CC selenocysteinyl-tRNA(Sec) + 2 phosphate; Xref=Rhea:RHEA:25041,
CC Rhea:RHEA-COMP:9743, Rhea:RHEA-COMP:9947, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16144, ChEBI:CHEBI:43474, ChEBI:CHEBI:78551,
CC ChEBI:CHEBI:78573; EC=2.9.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001746,
CC ECO:0000256|PIRNR:PIRNR017689};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRNR:PIRNR017689, ECO:0000256|PIRSR:PIRSR017689-50};
CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec)
CC (archaeal/eukaryal route): step 2/2. {ECO:0000256|ARBA:ARBA00004822,
CC ECO:0000256|PIRNR:PIRNR017689}.
CC -!- SUBUNIT: Homotetramer formed by a catalytic dimer and a non-catalytic
CC dimer serving as a binding platform that orients tRNASec for catalysis.
CC Each tetramer binds the CCA ends of two tRNAs which point to the active
CC sites of the catalytic dimer. {ECO:0000256|ARBA:ARBA00026053}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR017689}.
CC -!- SIMILARITY: Belongs to the SepSecS family.
CC {ECO:0000256|ARBA:ARBA00007037, ECO:0000256|PIRNR:PIRNR017689}.
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DR EMBL; UYYF01000592; VDM98682.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N5CQW9; -.
DR STRING; 103827.A0A0N5CQW9; -.
DR WBParaSite; TCLT_0000261901-mRNA-1; TCLT_0000261901-mRNA-1; TCLT_0000261901.
DR OMA; MSHANDY; -.
DR UniPathway; UPA00906; UER00898.
DR Proteomes; UP000046394; Unplaced.
DR Proteomes; UP000276776; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098621; F:O-phosphoseryl-tRNA(Sec) selenium transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0001717; P:conversion of seryl-tRNAsec to selenocys-tRNAsec; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR019872; Sec-tRNA_Se_transferase.
DR InterPro; IPR008829; SepSecS/SepCysS.
DR NCBIfam; TIGR03531; selenium_SpcS; 1.
DR PANTHER; PTHR12944:SF2; O-PHOSPHOSERYL-TRNA(SEC) SELENIUM TRANSFERASE; 1.
DR PANTHER; PTHR12944; SOLUBLE LIVER ANTIGEN/LIVER PANCREAS ANTIGEN; 1.
DR Pfam; PF05889; SepSecS; 1.
DR PIRSF; PIRSF017689; SepSecS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR017689};
KW Protein biosynthesis {ECO:0000256|PIRNR:PIRNR017689};
KW Pyridoxal phosphate {ECO:0000256|PIRNR:PIRNR017689,
KW ECO:0000256|PIRSR:PIRSR017689-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000276776};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PIRNR:PIRNR017689};
KW Selenium {ECO:0000256|PIRNR:PIRNR017689};
KW Transferase {ECO:0000256|PIRNR:PIRNR017689};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555,
KW ECO:0000256|PIRNR:PIRNR017689}.
FT BINDING 64
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 304
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 386
FT /ligand="tRNA"
FT /ligand_id="ChEBI:CHEBI:17843"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT SITE 63
FT /note="May act as a substrate filter by repelling compounds
FT with a negatively charged alpha-carboxylate"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-50"
FT MOD_RES 275
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-50"
SQ SEQUENCE 475 AA; 51823 MW; 57DEFD71C63688E6 CRC64;
MKAVEETINR SERCFDRLQR TLLCDGCIPR KGLSVQVIEG FLIRLASLDS NNRFGGISVG
AGEREGRVIS SLVEKLHYGF AHGIGRSGNL TEGQPKAVGS TILSTIANNL ALDAIKFLGI
PSTKAAMVVP VATGMSLSVC LGSWRHYKPH AKFVVFLRID QKSCLKSIFT AGYEPIIIDS
VPGTETSDSL TTDLINLRTV LEKQNHEIIA VLSATSGFAP REPDNLIAVG ELCKRYGVKH
LVNNAYGLQS PECRKRIEEA GSSGYIDAFV QSTDKNFLVP VGGSVVATFS KKALDNIANF
YPGRASMVPS RDLLITLLQI GKTGLKHLYE VQQNNFEILS TAMQDYAESI GQKVLEAKSN
RISIAVTLQG WPKNDQSAFG ARLFSRGITG ARVIQKGLIK KIDGYEFASF GSHSSLGNYD
YINVACAIGM TTEEIDQLIM VLKSETPKWA FTSLKNIDNG NLSIIQYDLA KKLIF
//
