ID A0A1H3NFK6_9FIRM Unreviewed; 633 AA.
AC A0A1H3NFK6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 28-JAN-2026, entry version 29.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=SAMN05192546_10569 {ECO:0000313|EMBL:SDY86959.1};
OS Tindallia californiensis.
OC Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
OC Tindalliaceae; Tindallia.
OX NCBI_TaxID=159292 {ECO:0000313|EMBL:SDY86959.1, ECO:0000313|Proteomes:UP000199230};
RN [1] {ECO:0000313|EMBL:SDY86959.1, ECO:0000313|Proteomes:UP000199230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APO {ECO:0000313|EMBL:SDY86959.1,
RC ECO:0000313|Proteomes:UP000199230};
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; FNPV01000005; SDY86959.1; -; Genomic_DNA.
DR RefSeq; WP_093313081.1; NZ_FNPV01000005.1.
DR AlphaFoldDB; A0A1H3NFK6; -.
DR STRING; 159292.SAMN05192546_10569; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000199230; 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 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; 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; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:SDY86959.1};
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:UP000199230}.
FT DOMAIN 1..174
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 633 AA; 71676 MW; ADCCF60B89FA3500 CRC64;
MKHLVIGTAG HIDHGKTTLI QALTGRNTDR LKEEMKRGIS IELGFTHFDL PGGIRAGIID
VPGHERFIRH MLAGVGGVDL VMLVIAADEG VMAQTKEHLD ILQMLSIKKG IVVLTKADIV
EPEWLEMVKE DVRESLQETF LESAPIIAVD SVSKRGINEL IEKLTDHYQE VDSRDEKAPF
RMPIDRVFTI TGFGTVVTGT LMEGSLNIEE TVQLYPGEET LRIRNIQVHG ETVKKAYAGQ
RVALNLSGIK KELIQRGDYL AKPGSLKSTM MVDGRLTLLK NAPRSLKQRD RVRIYHGASE
ILARIVILEK DVIEPGESTL VQFRLEENAV FKKGDNIIIR FYSPMETLGG AVIIEPSPEK
HKSMQQDIID KLMLKESGGI EADLEQALQK ISDTFPDKSI LAESIGCDES DIKEVIGYLQ
DQNLIYSIED KYYIHRDYYE SIIDEISMNL INYHKKNPLR QGMLKEELKS RVFSNPKNRA
ADLFLELISQ EKIICIEGKF VSAQGFSIKL TPEQKEILNQ IETIYLESLY SPPRLEEVKK
GIKGKEKTIQ QVIEMMMGDK LLRLQNDLVL HQKAYEGAKE KIKEHFINCE TLSVAEFRDL
LGTSRKYAVG ILEYLDQEKF TKREGDNRTL GKK
//
