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Database: UniProt
Entry: W2TKN9_NECAM
LinkDB: W2TKN9_NECAM
Original site: W2TKN9_NECAM 
ID   W2TKN9_NECAM            Unreviewed;       207 AA.
AC   W2TKN9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=O-phosphoseryl-tRNA(Sec) selenium transferase {ECO:0000256|ARBA:ARBA00021963};
DE            EC=2.9.1.2 {ECO:0000256|ARBA:ARBA00012464};
DE   AltName: Full=Selenocysteine synthase {ECO:0000256|ARBA:ARBA00030669};
DE   AltName: Full=Selenocysteinyl-tRNA(Sec) synthase {ECO:0000256|ARBA:ARBA00032048};
DE   AltName: Full=Sep-tRNA:Sec-tRNA synthase {ECO:0000256|ARBA:ARBA00032693};
GN   ORFNames=NECAME_08311 {ECO:0000313|EMBL:ETN81726.1};
OS   Necator americanus (Human hookworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae; Bunostominae;
OC   Necator.
OX   NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN81726.1, ECO:0000313|Proteomes:UP000053676};
RN   [1] {ECO:0000313|Proteomes:UP000053676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24441737; DOI=10.1038/ng.2875;
RA   Tang Y.T., Gao X., Rosa B.A., Abubucker S., Hallsworth-Pepin K., Martin J.,
RA   Tyagi R., Heizer E., Zhang X., Bhonagiri-Palsikar V., Minx P., Warren W.C.,
RA   Wang Q., Zhan B., Hotez P.J., Sternberg P.W., Dougall A., Gaze S.T.,
RA   Mulvenna J., Sotillo J., Ranganathan S., Rabelo E.M., Wilson R.K.,
RA   Felgner P.L., Bethony J., Hawdon J.M., Gasser R.B., Loukas A., Mitreva M.;
RT   "Genome of the human hookworm Necator americanus.";
RL   Nat. Genet. 46:261-269(2014).
CC   -!- FUNCTION: Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-
CC       tRNA(Sec) required for selenoprotein biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00002552}.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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   -!- 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   -!- SIMILARITY: Belongs to the SepSecS family.
CC       {ECO:0000256|ARBA:ARBA00007037}.
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DR   EMBL; KI658635; ETN81726.1; -; Genomic_DNA.
DR   RefSeq; XP_013303953.1; XM_013448499.1.
DR   AlphaFoldDB; W2TKN9; -.
DR   STRING; 51031.W2TKN9; -.
DR   EnsemblMetazoa; NECAME_08311; NECAME_08311; NECAME_08311.
DR   GeneID; 25348341; -.
DR   KEGG; nai:NECAME_08311; -.
DR   CTD; 25348341; -.
DR   OrthoDB; 121300at2759; -.
DR   UniPathway; UPA00906; UER00898.
DR   Proteomes; UP000053676; Unassembled WGS sequence.
DR   GO; GO:0098621; F:O-phosphoseryl-tRNA(Sec) selenium transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0001717; P:conversion of seryl-tRNAsec to selenocys-tRNAsec; IEA:InterPro.
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   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   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053676};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Transferase {ECO:0000313|EMBL:ETN81726.1};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
SQ   SEQUENCE   207 AA;  23709 MW;  4149E9BED1EE608F CRC64;
     MALSLCMGSW RKLRPKAKYV LWCRVDQKSC FKAILHAGYE PIIVDPVREG DALMTDVETL
     NRILEQRGEE ILCVLSTTSC FAPRSPDSLE AISGICQHTD MRRVGKEHFY SRRRKCCGEP
     KRYVLDDSLR YYLNNVPDSV GHNIKVPVAA VWILKDAKVQ KRMPYAASAI MELFTWNTNG
     SVEKEPERIS FCKFSTIERG VQSEENE
//
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