ID A0A833HRC6_9FIRM Unreviewed; 630 AA.
AC A0A833HRC6;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 19.
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:KAB3533105.1};
GN ORFNames=F8153_00720 {ECO:0000313|EMBL:KAB3533105.1};
OS Alkaliphilus serpentinus.
OC Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
OC Natronincolaceae; Alkaliphilus.
OX NCBI_TaxID=1482731 {ECO:0000313|EMBL:KAB3533105.1, ECO:0000313|Proteomes:UP000465601};
RN [1] {ECO:0000313|EMBL:KAB3533105.1, ECO:0000313|Proteomes:UP000465601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LacT {ECO:0000313|EMBL:KAB3533105.1,
RC ECO:0000313|Proteomes:UP000465601};
RA Postec A.;
RT "Alkaliphilus serpentinus sp. nov. and Alkaliphilus pronyensis sp. nov.,
RT two novel anaerobic alkaliphilic species isolated from the serpentinized-
RT hosted hydrothermal field of the Prony Bay (New Caledonia).";
RL Submitted (OCT-2019) 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:KAB3533105.1}.
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DR EMBL; WBZB01000004; KAB3533105.1; -; Genomic_DNA.
DR RefSeq; WP_151864430.1; NZ_WBZB01000004.1.
DR AlphaFoldDB; A0A833HRC6; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000465601; 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; 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:KAB3533105.1};
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:UP000465601}.
FT DOMAIN 1..174
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 630 AA; 71303 MW; B8331F06EF966FF1 CRC64;
MKNIVIGTAG HIDHGKTTLI KALTGRDTDR LKEEKKRGIS IDLGFTHFDL PSGKRAGIID
VPGHEKFIRN MLAGVGGMDI VMLVVAADEG VMPQTKEHLD ILNMINIKKG IIVVTKIGLV
DEEWLQLIQE DIRSKVQDTF LEDSEMILVD SVKGIGVDKL IALIDNLADE TESRDINSPV
RMPIDRVFSI TGFGTVVTGT LMEGKITVED TLEILPEEVK VRVRNIQVHG KSVETAYAGQ
RVAINLANIK KEDIERGQVL AQINSMENTL MMDGRINVLR DYERILSNRD RVRLYYGSTE
VLARVVLLNK EEVKAGETAL IQLRLEETAA VKKGDRIIMI HYSPMETIGG FIVIDGNPKK
HKAFDEKVIK ELELKEKASP EDILEKQIER YSKDYPDISF LAKALSQQPE EILLLIEELA
NKKKVVRLDN NFVIHIKSFE KLKEDATKLL KDYHSKNPLK TGIQKEEFKN KIFPKGKGKV
VDSIMELMDG DFIEIKEKFV SLKGFEVILN DSQQLIKSKL EEIYLSNPFS PPKLEDALKT
LKYNSKDIQQ VVEAMLGNEL IRLNQEVLIH KKVLIDAKEK LISFIENKGS ITLADYRDVL
DTSRKYAVAL LEYFDSNKVT KRAGDERILY
//
