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Database: UniProt
Entry: B8C339_THAPS
LinkDB: B8C339_THAPS
Original site: B8C339_THAPS 
ID   B8C339_THAPS            Unreviewed;       476 AA.
AC   B8C339;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 66.
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};
DE   Flags: Fragment;
GN   ORFNames=THAPSDRAFT_262555 {ECO:0000313|EMBL:EED92493.1};
OS   Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC   Thalassiosiraceae; Thalassiosira.
OX   NCBI_TaxID=35128 {ECO:0000313|EMBL:EED92493.1, ECO:0000313|Proteomes:UP000001449};
RN   [1] {ECO:0000313|EMBL:EED92493.1, ECO:0000313|Proteomes:UP000001449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 {ECO:0000313|EMBL:EED92493.1};
RX   PubMed=15459382; DOI=10.1126/science.1101156;
RA   Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D.,
RA   Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M., Brzezinski M.A.,
RA   Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S., Detter J.C.,
RA   Glavina T., Goodstein D., Hadi M.Z., Hellsten U., Hildebrand M.,
RA   Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N., Lau W.W., Lane T.W.,
RA   Larimer F.W., Lippmeier J.C., Lucas S., Medina M., Montsant A., Obornik M.,
RA   Parker M.S., Palenik B., Pazour G.J., Richardson P.M., Rynearson T.A.,
RA   Saito M.A., Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A.,
RA   Wilkerson F.P., Rokhsar D.S.;
RT   "The genome of the diatom Thalassiosira pseudonana: ecology, evolution, and
RT   metabolism.";
RL   Science 306:79-86(2004).
RN   [2] {ECO:0000313|EMBL:EED92493.1, ECO:0000313|Proteomes:UP000001449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 {ECO:0000313|EMBL:EED92493.1};
RX   PubMed=18923393; DOI=10.1038/nature07410;
RA   Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA   Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA   Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA   Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA   Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA   Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA   Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA   La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA   Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA   Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA   Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA   Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA   Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA   Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "The Phaeodactylum genome reveals the evolutionary history of diatom
RT   genomes.";
RL   Nature 456:239-244(2008).
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         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   -!- SIMILARITY: Belongs to the SepSecS family.
CC       {ECO:0000256|ARBA:ARBA00007037}.
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DR   EMBL; CM000642; EED92493.1; -; Genomic_DNA.
DR   RefSeq; XP_002290741.1; XM_002290705.1.
DR   AlphaFoldDB; B8C339; -.
DR   STRING; 35128.B8C339; -.
DR   PaxDb; 35128-Thaps262555; -.
DR   EnsemblProtists; EED92493; EED92493; THAPSDRAFT_262555.
DR   GeneID; 7450104; -.
DR   KEGG; tps:THAPSDRAFT_262555; -.
DR   eggNOG; KOG3843; Eukaryota.
DR   HOGENOM; CLU_022508_0_0_1; -.
DR   InParanoid; B8C339; -.
DR   OMA; MSHANDY; -.
DR   UniPathway; UPA00906; UER00898.
DR   Proteomes; UP000001449; Chromosome 5.
DR   GO; GO:0098621; F:O-phosphoseryl-tRNA(Sec) selenium transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR   GO; GO:0001717; P:conversion of seryl-tRNAsec to selenocys-tRNAsec; IEA:InterPro.
DR   GO; GO:0001514; P:selenocysteine incorporation; IBA:GO_Central.
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   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR017689-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001449};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PIRSR:PIRSR017689-
KW   50};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PIRSR:PIRSR017689-
KW   50}.
FT   BINDING         51
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT   BINDING         316
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT   BINDING         407
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT   BINDING         472
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017689-1"
FT   SITE            50
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         287
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017689-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EED92493.1"
FT   NON_TER         476
FT                   /evidence="ECO:0000313|EMBL:EED92493.1"
SQ   SEQUENCE   476 AA;  51829 MW;  D85B9F02D906E6FD CRC64;
     ASNSQTKALF HHKRLPDHGW TDVQIQRLLL ELSVLDTNCE ESVKWTGAGE REGRIYAPLV
     SQRHFGFGHG IGRSGDVMEA QPKAVGSSAL LRLTLRLTLD AVRRGAGLNG TLGKGDSRNG
     PASFGTLLPV CTGMSMALVL SGLRDRARTL DSASIGTEHV NTERNIVLWS RIDQKSCYKS
     ILSAGLKCVV LPTKKHPDTD EVSTDLEALK EALDSFGNSI LAVLTTTSCF CPRVPDEVDQ
     VAKMIMSAGV SHVVNHAYGL QCQTTNKLLN RACIIGRVDA IICSTDKNFL VPVGGALILS
     PDSNVIETIS KNYPGRASSS PMVDLFITLL SMGLNGYKGI LEERKRLTEL FGQSLQRVAT
     VFGETVLNCP RNTISFGMTL DNLATINGSD DELNSLITKF GSMLFTRCIS GTRVVPRGST
     KTISGHTFEG FGSSNDDYPY AYMTSACAVG MGEEEMNEFF VRLEKSWIDY RKKLEQ
//
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