ID A0A443IKJ3_9BACI Unreviewed; 630 AA.
AC A0A443IKJ3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JAN-2026, entry version 28.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN Name=selB {ECO:0000313|EMBL:RWR05425.1};
GN ORFNames=D4N35_015525 {ECO:0000313|EMBL:RWR05425.1};
OS Siminovitchia fortis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Siminovitchia.
OX NCBI_TaxID=254758 {ECO:0000313|EMBL:RWR05425.1, ECO:0000313|Proteomes:UP000273811};
RN [1] {ECO:0000313|EMBL:RWR05425.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16012 {ECO:0000313|EMBL:RWR05425.1};
RA Sun L., Chen Z.;
RL Submitted (DEC-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWR05425.1}.
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DR EMBL; QYTU02000044; RWR05425.1; -; Genomic_DNA.
DR RefSeq; WP_120075321.1; NZ_CP126113.1.
DR AlphaFoldDB; A0A443IKJ3; -.
DR GeneID; 56391943; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000273811; 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; 2.40.30.10:FF:000020; Translation elongation factor EF-1; 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:RWR05425.1};
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:UP000273811}.
FT DOMAIN 2..178
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 630 AA; 71866 MW; 1B7934E67EB81298 CRC64;
MNRFFTIGMA GHIDHGKTTL TKALTGVNTD RLKEEKERNI SIELGFAPLI NEDQLQVSIV
DVPGHERFIR QMIAGVAGID MVILVIAADE GIMPQTQEHL DILSLLGIHN GLAVITKIDQ
TDEELLEIVI EDVKETLEKT FLNNAPIFLV DSLSQKGIPE LKVAIRDKVM QIEKRENKAP
FRLPIDQVFT LKGQGTVVRG TIYDGEVRQG ERLMLLPVNK EVRVRQIQVH RKQAEIAVAG
QRTAINLGGI SYDSVSRGDV LAADGFYSVS DRIDVVFYPL KDMNSRIKQR QPVKLYVGTS
EVMGKIIFFD RNEVNNTEDG EILCQVQLNE KVVVTRGDRF ILRNPSPVET IGGGWIIEPN
GRKYRFGKKT IDQLMMKKEG TALDRIRSLM EEKHVLTYDE LLKGASVTEK ELDEAEKVLL
KMEGGLFSLH SIFERVKNKV TDLIESFHKR YPMRVGMDKA EIISEMKKHF PAPLLEFAVK
TLLEEKVIKI ENQYVSLTDA APTLPVKWKT KLEAVEKELN DQGIEVEKFN TVLKKYEIPP
DLQKEFYHYL IHTKRAHILD DDMLIAKEAV EQARLQLEAD THLEEFTLQM ARESLPVSRK
YLVPLLELFD RLGYTKRMDN TRKWVQKNSG
//
