ID M3X7Z6_FELCA Unreviewed; 504 AA.
AC M3X7Z6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 61.
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|Ensembl:ENSFCAP00000022748.1,
GN ECO:0000313|VGNC:VGNC:80003};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000022748.1, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000022748.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000022748.1,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000022748.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000022748.1,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000022748.1}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000022748.1};
RG Ensembl;
RL Submitted (SEP-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 EMBL; AANG04001605; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003985533.2; XM_003985484.4.
DR AlphaFoldDB; M3X7Z6; -.
DR STRING; 9685.ENSFCAP00000022748; -.
DR PaxDb; 9685-ENSFCAP00000022748; -.
DR Ensembl; ENSFCAT00000032548.4; ENSFCAP00000022748.1; ENSFCAG00000023094.4.
DR GeneID; 101081043; -.
DR KEGG; fca:101081043; -.
DR CTD; 51091; -.
DR VGNC; VGNC:80003; SEPSECS.
DR eggNOG; KOG3843; Eukaryota.
DR GeneTree; ENSGT00390000007332; -.
DR HOGENOM; CLU_022508_0_0_1; -.
DR InParanoid; M3X7Z6; -.
DR OMA; MSHANDY; -.
DR OrthoDB; 121300at2759; -.
DR UniPathway; UPA00906; UER00898.
DR Proteomes; UP000011712; Chromosome B1.
DR Bgee; ENSFCAG00000023094; Expressed in liver and 10 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
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:UniProtKB-UniRule.
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; 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 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.
DR PROSITE; PS00435; PEROXIDASE_1; 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:UP000011712};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PIRNR:PIRNR017689};
KW Selenium {ECO:0000256|PIRNR:PIRNR017689};
KW Transferase {ECO:0000256|PIRNR:PIRNR017689};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555,
KW ECO:0000256|PIRNR:PIRNR017689}.
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 504 AA; 55829 MW; D3C929D17735AFEF CRC64;
MNRESFAAGE RLVSPAYVRQ GCEARRSHEH LVRLLLEKGK CPEDGWDEST LELFLHELAI
MDSNNFLGNC GVGEREGRVA SALVARRHYR FIHGIGRSGD ISAVQPKAAG SSLLNKITNS
LVLDIIKLAG VHTVTNCFVV PMATGMSLTL CFLTLRHRRP KAKYIIWPRI DQKSCFKSMI
TAGFEPVVIE NVLEGDELRT DLEAVEAKVR ELGPDHILCV HSTTSCFAPR VPDRLEELAV
ICADYGIPHV VNNAYGVQSS KCMHLIQQGA RVGRIDAFVQ SLDKNFMVPV GGAIIAGFND
SFIQEISKMY PGRASASPSL DVLITLLSLG SNGYKKLLKE RKEMFSYLSS QLKKLSETYN
ERLLHTPHNP ISLAMTLKTL GEDEDKAVTQ LGSMLFTRQV SGARVVPLGS VQTVSGYTFQ
GFMSHTNNYP CAYLNAAAAI GMKTQDVDLF IKRLDKCLKA VRKEQNKESH VSGVDNYDRT
ENVDIEEMAL KLDNVLLDTY QNSS
//
