SPCS_PONAB
ID SPCS_PONAB Reviewed; 501 AA.
AC Q5RAK7;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=UGA suppressor tRNA-associated protein;
GN Name=SEPSECS;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR859008; CAH91203.1; -; mRNA.
DR RefSeq; NP_001125707.1; NM_001132235.1.
DR AlphaFoldDB; Q5RAK7; -.
DR SMR; Q5RAK7; -.
DR STRING; 9601.ENSPPYP00000016363; -.
DR GeneID; 100172631; -.
DR KEGG; pon:100172631; -.
DR CTD; 51091; -.
DR eggNOG; KOG3843; Eukaryota.
DR InParanoid; Q5RAK7; -.
DR OrthoDB; 680116at2759; -.
DR UniPathway; UPA00906; UER00898.
DR Proteomes; UP000001595; 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; IEA:UniProtKB-KW.
DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
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; Phosphoprotein; Protein biosynthesis; Pyridoxal phosphate;
KW Reference proteome; RNA-binding; Selenium; Transferase; tRNA-binding.
FT CHAIN 1..501
FT /note="O-phosphoseryl-tRNA(Sec) selenium transferase"
FT /id="PRO_0000219877"
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 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 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HD40"
FT MOD_RES 284
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q9HD40"
SQ SEQUENCE 501 AA; 55589 MW; 686D97429DA61BF2 CRC64;
MNRESFAAGE RLVSPAYVRQ GCEARRSHEH LIRLLLEKGK CPENGWDEST LELFLHELAI
MDSNNFLGNC GVGEREGRVA SALVARRHYR FIHGIGRSGD ISAVQPKAAG SSLLNKIANS
LVLDIIKLAG VHTVANCFVV PMATGMSLTL CFLTLRHKRP KAKYIIWPRI DQKSCFKSMI
TAGFEPVVIE NVLEGDELRT DLKAVEAKVQ ELGPDYILCI HSTTSCFAPR VPDRLEELAV
ICANYGIPHI VNNAYGVQSS KCMHLIQQGA RVGRIDAFVQ SLDKNFMVPV GGAIIAGFND
SFIQEIGKMY PGRASASPSL DVLITLLSLG SNGYRKLLKE RKEMFSYLSN QIKKLSEAYN
ERLLHTPHNP ISLAMTLKTL DEHHDKAVTQ LGSMLFTRQV SGARVVPLGS VQTVSGYTFR
GFMSHTNNYP CAYLNAASAI GMKMQDVDLF IKRLDKCLKA VRKEQSKESD DNYDKTEDVD
IEEMALKLDN VLLDTYQDAS S
