SPCS_DICDI
ID SPCS_DICDI Reviewed; 479 AA.
AC Q54VQ6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 homolog;
GN Name=sepsecs; ORFNames=DDB_G0280197;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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; AAFI02000035; EAL67325.1; -; Genomic_DNA.
DR RefSeq; XP_641299.1; XM_636207.1.
DR AlphaFoldDB; Q54VQ6; -.
DR SMR; Q54VQ6; -.
DR STRING; 44689.DDB0266531; -.
DR PaxDb; Q54VQ6; -.
DR EnsemblProtists; EAL67325; EAL67325; DDB_G0280197.
DR GeneID; 8622432; -.
DR KEGG; ddi:DDB_G0280197; -.
DR dictyBase; DDB_G0280197; sepsecs.
DR eggNOG; KOG3843; Eukaryota.
DR HOGENOM; CLU_022508_0_0_1; -.
DR InParanoid; Q54VQ6; -.
DR OMA; HIINGAY; -.
DR PhylomeDB; Q54VQ6; -.
DR UniPathway; UPA00906; UER00898.
DR PRO; PR:Q54VQ6; -.
DR Proteomes; UP000002195; Chromosome 3.
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 3: Inferred from homology;
KW Cytoplasm; Protein biosynthesis; Pyridoxal phosphate; Reference proteome;
KW RNA-binding; Selenium; Transferase; tRNA-binding.
FT CHAIN 1..479
FT /note="O-phosphoseryl-tRNA(Sec) selenium transferase"
FT /id="PRO_0000328331"
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 316
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HD40"
FT BINDING 414
FT /ligand="tRNA"
FT /ligand_id="ChEBI:CHEBI:17843"
FT /ligand_part="tRNA discriminator base"
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 287
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q9HD40"
SQ SEQUENCE 479 AA; 53253 MW; 79E790B5603ABC78 CRC64;
MNLKNLETCK GLIKGSYIDQ AIQGTSQFNK LLETLLIHKK LPNIGYNDKI IELILNEISL
MDSNNFIENI GVGEREGRIY SGLVEKRHYG FAHGIGRSGD ITEQQPKAAG SSLIQKLTHS
LVLDAMKLAG LEQSSLSNCL LLPMATGMTL ALTMLTLKSI NANNKRYVLW PRIDQKSCLK
SIITAGLIPI VIPNQLDGDM IRTDLVAIED KIKELGVDNI LCVFSTTSCF APRVPDKIIE
ISEICKRYNI GHIINNAYGL QCSKILHNIS QACKLGRVDA FIQSTDKNFM VPVGGAIISG
PNSEFIDQIS RNYPGRANSS PILDVFITLL SMGKQGWLNL LKERKELLIY FNEQLSKFAL
ENNEKLLNTI NENKISFALT LSSNNFNNNE EIISNNNNNN NNTFSMIGSK LFSRSCSGSR
VIDLKSNKKL LIGGLEFNNY GSHIDNYSTS YLTVACAIGI TKLEIDTFIQ RLSKLFNKK
