ID A0A1M5NH41_9FIRM Unreviewed; 626 AA.
AC A0A1M5NH41;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 28-JAN-2026, entry version 36.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=SAMN02744040_00038 {ECO:0000313|EMBL:SHG88830.1};
OS Tepidibacter thalassicus DSM 15285.
OC Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
OC Peptostreptococcaceae; Tepidibacter.
OX NCBI_TaxID=1123350 {ECO:0000313|EMBL:SHG88830.1, ECO:0000313|Proteomes:UP000242520};
RN [1] {ECO:0000313|Proteomes:UP000242520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15285 {ECO:0000313|Proteomes:UP000242520};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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; FQXH01000005; SHG88830.1; -; Genomic_DNA.
DR RefSeq; WP_072722863.1; NZ_FQXH01000005.1.
DR AlphaFoldDB; A0A1M5NH41; -.
DR STRING; 1123350.SAMN02744040_00038; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000242520; 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; 2.
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:SHG88830.1};
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:UP000242520}.
FT DOMAIN 1..172
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 626 AA; 71717 MW; 910EEEC7114066B3 CRC64;
MKNVIIGTAG HIDHGKTTLI KALTGRETDR LKEEKKRGIS IDLGFTYFDL PSGKRAGIVD
VPGHEKFIKN MLAGASGMDM VLLVVAADEG VMPQTIEHLD ILNFLNVKNG IIVITKSDLV
EDDFLELVKE DIKEQVKDTF LKDALIIEVD SVTKRGINDL IEAIDRISEE VKNKNLDSLP
RLNIDRVFSV KGFGTVVTGT LIEGKINIDD NMFIYPKGIE TKVRSIQVHG NSVKTAYAGQ
RVAINLSNVK VEDIQRGDVL AYPDSLIESM MIDVKISLVK HSLRKIEYWD RIRLYHGTRE
ILGRIVPLDK EYLNPGDTGY CQIRLEESIV AKNRDTFVIR FYSPMKTVGG GVILDSNPKK
HKRFDKEVLQ YLKLKERGDT KEVLEEIIKK HSREYPSLKD ISVYIGEKEE IIQDKVNSLC
ADKKVVSINN MYIHRYFYEE LMEKTLNLLL DFHNKYPLKK GVLKEELRSK VEKNLKNKDF
DKLLNLFIEE QKIKVVQNLV SIYDFEVVFS ESQIKIKQEI ESKLKNDGLT PRNISEIIQG
RQEYKEVLEA LISDTLVKVT DELVYHKEYY QKALSIVKRY IKENGSLTLG DFRDLIGASR
KYAMALLEDF DKNKITKRVG DKRVLI
//
