ID A0A3S4Z359_9FIRM Unreviewed; 630 AA.
AC A0A3S4Z359;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-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:VEJ34837.1};
GN ORFNames=NCTC13079_00349 {ECO:0000313|EMBL:VEJ34837.1};
OS Aedoeadaptatus ivorii.
OC Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
OC Peptoniphilaceae; Aedoeadaptatus.
OX NCBI_TaxID=54006 {ECO:0000313|EMBL:VEJ34837.1, ECO:0000313|Proteomes:UP000269544};
RN [1] {ECO:0000313|EMBL:VEJ34837.1, ECO:0000313|Proteomes:UP000269544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13079 {ECO:0000313|EMBL:VEJ34837.1,
RC ECO:0000313|Proteomes:UP000269544};
RG Pathogen Informatics;
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LR134523; VEJ34837.1; -; Genomic_DNA.
DR RefSeq; WP_126464809.1; NZ_JAUSWF010000002.1.
DR AlphaFoldDB; A0A3S4Z359; -.
DR KEGG; piv:NCTC13079_00349; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000269544; Chromosome.
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:InterPro.
DR GO; GO:0001514; P:selenocysteine incorporation; IEA:InterPro.
DR CDD; cd04171; SelB; 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; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000269544}.
FT DOMAIN 1..176
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 630 AA; 70468 MW; 900E49353C2A9B3E CRC64;
MKNVIIGTAG HVDHGKTTLL KALTGVDLDT LQEEQKRGIT INPGYSTMEN DRGLDIGIID
VPGHEKFVHN MLTGIGGVDL VLLLISAEEG IMPQTREHFE IVKALGIDTG ILVLTKVDLV
DREWIPILEE EAREMVQGSF LEDAPLVPVS AYTGENIETL RNLMLDMAEA AEETPRTPEL
TRLPVDRIFS VAGHGTVVTG TLVEGAIRKG DTLRLYPKED LAAVRGIQVH GKEVEEAFGG
QRVALNISVK KDRLEVGDVL APPHSLPLTK QIDVAIHMFA STERTMKNSS RVHVNYGSGE
ALARVILFGE DELLPAMSAY GQLRFEAPIP IRKDDPFVLR FFSPVESIAG GRVLEVHPKR
HKRKDERVVE RLSQKDTGDD ATIFALALEE NRYRYADERE LGAALGFSEE KRHALRKELT
EAGTTVELPG GLLVHAHTAE GVLENARAIL ARYHEEFPLE TGMPKQAFRH QLQEAEHFDD
EKIPEAFLAH FYQKHLLEDH GKRIEDSHFT ATLTPEQEKQ WQRAEAIAKE KGFEGADDSD
FVPVGKKREH VLRFMEESGT LIALETRTLH RDVWDEAVSI ALAMIDETGK MKLADFRNAI
DTSRKYAVEI LDEMDRRGFT KFHDGVRVRA
//