ID A0A1U8D3U3_ALLSI Unreviewed; 492 AA.
AC A0A1U8D3U3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 2.
DT 27-MAR-2024, 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 Name=SEPSECS {ECO:0000313|RefSeq:XP_014375952.2};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_014375952.2};
RN [1] {ECO:0000313|RefSeq:XP_014375952.2}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_014375952.2; XM_014520466.2.
DR STRING; 38654.A0A1U8D3U3; -.
DR KEGG; asn:102371649; -.
DR InParanoid; A0A1U8D3U3; -.
DR OrthoDB; 121300at2759; -.
DR UniPathway; UPA00906; UER00898.
DR Proteomes; UP000189705; Unplaced.
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:UP000189705};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PIRNR:PIRNR017689};
KW Selenium {ECO:0000256|PIRNR:PIRNR017689};
KW Transferase {ECO:0000256|PIRNR:PIRNR017689,
KW ECO:0000313|RefSeq:XP_014375952.2};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555,
KW ECO:0000256|PIRNR:PIRNR017689}.
FT REGION 468..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 271
FT /ligand="tRNA"
FT /ligand_id="ChEBI:CHEBI:17843"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 398
FT /ligand="tRNA"
FT /ligand_id="ChEBI:CHEBI:17843"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT BINDING 463
FT /ligand="tRNA"
FT /ligand_id="ChEBI:CHEBI:17843"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT SITE 74
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 284
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017689-50"
SQ SEQUENCE 492 AA; 54401 MW; B43952067F8CB9A5 CRC64;
MNGENFGASE RLVAAAYVRQ GAQGRRAHDF ITLLFILXGK CPDDGWDEST IELFLHELAI
MDSNNFLGNC GVGEREGRVA SGLVARRHYR LIHGIGRSGD ISAVQPKAAG SSLLNKLTNL
IVLDIIKLAG VRTVTSCFVV PMATGMSLTL CFLTLRHKRP KAKYIIWPRI DQKSCFKSMI
TAGFEPVVIE NVLENDELRT DLQGVEAKIQ ELGAENVLCV HSTTSCFAPR VPDRLEELAV
ICANYDIPHI VNNAYGVQSS KCMHLIQQGA RVGRIDAFIQ SLDKNFMVPV GGAIIAGFND
SFIKEISKMY PGRASASPSL DVFITLLSLG ANGYRQLLKQ RKEMFSYLTS ELKKLAEIHN
ERLLDTPHNP ISLAMSLKNL DEHSDTAVTQ LGSMLFTRQV SGARVVPRNF QQTVNNYTFK
GFMSHAISYP CAYLNAASAI GMKKQDVDMF LKRLDKCLKT FGKETNKGKD VPKTNDCHAD
LVEGEPEEPN KM
//
