ID A0A1H0CDG2_9BACT Unreviewed; 635 AA.
AC A0A1H0CDG2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 28-JAN-2026, entry version 31.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=SAMN04488516_1038 {ECO:0000313|EMBL:SDN55938.1};
OS Desulfonauticus submarinus.
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia;
OC Desulfovibrionales; Desulfonauticaceae; Desulfonauticus.
OX NCBI_TaxID=206665 {ECO:0000313|EMBL:SDN55938.1, ECO:0000313|Proteomes:UP000199602};
RN [1] {ECO:0000313|EMBL:SDN55938.1, ECO:0000313|Proteomes:UP000199602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15269 {ECO:0000313|EMBL:SDN55938.1,
RC ECO:0000313|Proteomes:UP000199602};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Translation factor necessary for the incorporation of
CC selenocysteine into proteins. It probably replaces EF-Tu for the
CC insertion of selenocysteine directed by the UGA codon. SelB binds GTP
CC and GDP. {ECO:0000256|ARBA:ARBA00025526}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; FNIN01000003; SDN55938.1; -; Genomic_DNA.
DR RefSeq; WP_092063997.1; NZ_FNIN01000003.1.
DR AlphaFoldDB; A0A1H0CDG2; -.
DR STRING; 206665.SAMN04488516_1038; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000199602; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0001514; P:selenocysteine incorporation; IEA:InterPro.
DR CDD; cd04171; SelB; 1.
DR CDD; cd03696; SelB_II; 1.
DR CDD; cd15491; selB_III; 1.
DR FunFam; 3.40.50.300:FF:001064; Selenocysteine-specific translation elongation factor; 1.
DR Gene3D; 1.10.10.2770; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR057335; Beta-barrel_SelB.
DR InterPro; IPR050055; EF-Tu_GTPase.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR015190; Elong_fac_SelB-wing-hlx_typ-2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015191; SelB_WHD4.
DR InterPro; IPR005225; Small_GTP-bd.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004535; Transl_elong_SelB.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; TIGR00475; selB; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR Pfam; PF25461; Beta-barrel_SelB; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF09106; WHD_2nd_SelB; 1.
DR Pfam; PF09107; WHD_3rd_SelB; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 3.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:SDN55938.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000199602}.
FT DOMAIN 1..174
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 635 AA; 72206 MW; C82C0B56C8596CF0 CRC64;
MPIVMGTAGH IDHGKTTLIK ALTGIDCDRL AEEKKRGITI ELGFAYLDLP DGTRVSIVDV
PGHEKFVKNM VAGAAGIDFV LLVVAADEGI MPQTEEHLEI CSLLGINRGL VVLTKVDMVD
EEWLTLVKEE VQEYLKNTFL RDAPIVSVSS HTGKGLQELQ QVILEQVQKI RKNRIFDVFR
LPVDRVFTLH GHGTVITGTT ISGKIKTGED IEIYPKGILA KVRSVQVHSE SKEVAQAGER
TALNLQGIEK EKIDRGNVLA RPGTLFPSKV WTIELHCLST AAKPLKHRTE IHFHHGSKEI
LARIYLLDRD ELKPGEKALA QVRFPEPMVG VFQDRFVIRS FSPLRTIGGG IVLDPMSVSL
KRRSPEIKYF KNLVNLNASQ LILNVLNRQG IKGLNFDQLL ILTNLRSKDL QKELQILSSK
QEVFLVEKDI KLYVGKRVVE KLSNSLLDFL TQFHSKNELL EGITRSQLLS SWGKNYSDKL
VNFLIDKLTK ENKIKIENKF IKLFSHKVKV KGEKRDLLER IFKIIETSGF NPPNFKEIKD
KFKLDTKELN EILALLEKEK KIVKINNNFY YAVSIAEKLK QLLLDFFAKQ QEMTLADFKS
ITGLSRKYTI PLLEYFDRQK ITMRIGDKRV LRKKS
//
