SPCS_DANRE
ID SPCS_DANRE Reviewed; 490 AA.
AC Q803A7;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=O-phosphoseryl-tRNA(Sec) selenium transferase;
DE EC=2.9.1.2 {ECO:0000250|UniProtKB:Q9HD40};
DE AltName: Full=Selenocysteine synthase;
DE Short=Sec synthase;
DE AltName: Full=Selenocysteinyl-tRNA(Sec) synthase;
DE AltName: Full=Sep-tRNA:Sec-tRNA synthase;
DE Short=SepSecS;
DE AltName: Full=Soluble liver antigen/liver pancreas antigen-like;
DE AltName: Full=UGA suppressor tRNA-associated protein homolog;
GN Name=sepsecs; Synonyms=sla/lpl; ORFNames=zgc:55980;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-
CC tRNA(Sec) required for selenoprotein biosynthesis.
CC {ECO:0000250|UniProtKB:Q9HD40}.
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:0000250|UniProtKB:Q9HD40};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q9HD40};
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:0000250|UniProtKB:Q9HD40}.
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:0000250|UniProtKB:Q9HD40}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9HD40}.
CC -!- SIMILARITY: Belongs to the SepSecS family. {ECO:0000305}.
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DR EMBL; BC044561; AAH44561.1; -; mRNA.
DR RefSeq; NP_956448.1; NM_200154.1.
DR AlphaFoldDB; Q803A7; -.
DR SMR; Q803A7; -.
DR STRING; 7955.ENSDARP00000042491; -.
DR PaxDb; Q803A7; -.
DR GeneID; 393123; -.
DR KEGG; dre:393123; -.
DR CTD; 51091; -.
DR ZFIN; ZDB-GENE-040426-859; sepsecs.
DR eggNOG; KOG3843; Eukaryota.
DR InParanoid; Q803A7; -.
DR OrthoDB; 680116at2759; -.
DR PhylomeDB; Q803A7; -.
DR UniPathway; UPA00906; UER00898.
DR PRO; PR:Q803A7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098621; F:phosphoseryl-selenocysteinyl-tRNA selenium transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0001514; P:selenocysteine incorporation; IBA:GO_Central.
DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 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; PTHR12944; 1.
DR Pfam; PF05889; SepSecS; 1.
DR PIRSF; PIRSF017689; SepSecS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR03531; selenium_SpcS; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Protein biosynthesis; Pyridoxal phosphate; Reference proteome;
KW RNA-binding; Selenium; Transferase; tRNA-binding.
FT CHAIN 1..490
FT /note="O-phosphoseryl-tRNA(Sec) selenium transferase"
FT /id="PRO_0000219878"
FT REGION 1..44
FT /note="Tetramerization"
FT /evidence="ECO:0000250|UniProtKB:Q9HD40"
FT REGION 96..106
FT /note="Phosphate loop (P-loop)"
FT /evidence="ECO:0000250|UniProtKB:Q9HD40"
FT REGION 466..490
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:0000250|UniProtKB:Q9HD40"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HD40"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HD40"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HD40"
FT BINDING 271
FT /ligand="tRNA"
FT /ligand_id="ChEBI:CHEBI:17843"
FT /ligand_part="tRNA variable arm"
FT /evidence="ECO:0000250|UniProtKB:Q9HD40"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HD40"
FT BINDING 398
FT /ligand="tRNA"
FT /ligand_id="ChEBI:CHEBI:17843"
FT /ligand_part="tRNA discriminator base"
FT /evidence="ECO:0000250|UniProtKB:Q9HD40"
FT BINDING 463
FT /ligand="tRNA"
FT /ligand_id="ChEBI:CHEBI:17843"
FT /ligand_part="tRNA acceptor arm"
FT /evidence="ECO:0000250|UniProtKB:Q9HD40"
FT SITE 74
FT /note="May act as a substrate filter by repelling compounds
FT with a negatively charged alpha-carboxylate"
FT /evidence="ECO:0000250|UniProtKB:Q6P6M7"
FT MOD_RES 284
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q9HD40"
SQ SEQUENCE 490 AA; 53730 MW; 3B3D68CDC3E70AA7 CRC64;
MNSENFRLSE KLVSASYVRQ GLDARRGHEQ LIRRLLDQGK CPEEGWSEST IELFLNELAV
MDSNNFLGNC GVGEREGRVA SSLVARRHYR LIHGIGRSGD IAAVQPKAAG SSLLNKITNS
VVLDVLKLTG VRSVSSCFVV PMATGMSLTL CFLTLRHRRP KARYILWPRI DQKSCFKSMV
TAGFEPVVIE NVLEGDELRT NLEEVERKIE EFGAENTLCV HSTTSCFAPR VPDRLEELSV
LCAKHDIPHI VNNAYGVQPS KCMHLIQQGA RVGRIDAFVQ SLDKNFVVPV GGAIIAGFDE
NFIQEISKIY PGRASASPSL DVLITLLTLG ANGYKKLLAD RKELYGHLAQ ELSALAARHG
ERLLKTPHNP ISLAMSLNHL EAHSSSAVTQ LGSMLFTRQV SGARVVPLGV QQTVSGHTFS
GFMSHSEAYP CPYLNAASAI GITKGDVTVC MKRLGKCLKI LKKEKSDPAD LEAEDGELEE
SPQRSTELRV
