ID A0A923HT37_9FIRM Unreviewed; 629 AA.
AC A0A923HT37;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 15.
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:MBC3888143.1};
GN ORFNames=GH810_07460 {ECO:0000313|EMBL:MBC3888143.1};
OS Acetobacterium paludosum.
OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=52693 {ECO:0000313|EMBL:MBC3888143.1, ECO:0000313|Proteomes:UP000616595};
RN [1] {ECO:0000313|EMBL:MBC3888143.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DER-2019 {ECO:0000313|EMBL:MBC3888143.1};
RA Ross D.E., Gulliver D.;
RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBC3888143.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DER-2019 {ECO:0000313|EMBL:MBC3888143.1};
RA Marshall C., May H., Norman S.;
RT "Comparative genomics of the Acetobacterium genus.";
RL Submitted (OCT-2020) 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:MBC3888143.1}.
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DR EMBL; WJBD01000007; MBC3888143.1; -; Genomic_DNA.
DR RefSeq; WP_148567482.1; NZ_RXYA01000010.1.
DR AlphaFoldDB; A0A923HT37; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000616595; 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:MBC3888143.1};
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:UP000616595}.
FT DOMAIN 1..171
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 629 AA; 70439 MW; 11659D7B5763C076 CRC64;
MNLILGTAGH IDHGKTSLVK ALTGIDTDRL KEEKKRGITI ELGFAYLDLS CGNRIGIVDV
PGHEKFINNM LAGAGGIDLA MMVIAADEGI MPQTIEHFGI LSLLEIQHGV VVITKTDLVD
ADWIEMVKDE IREKFKGSFL ENAPIIPVSA YTGAGIEELK QALSQIVSQV KAKKLSTPFR
LPIDRVFSVD GFGTVATGTL IEGRVKVGEN IMLYPTLETA RVRSLQVHGT AVEKAVAGQR
VAVNLTGIKK QQVMRGDTIA PATSMENSMM VDVKLNILKS SNRSVKNASR VHFYHGTKEI
LAKVILLAKD ELEAGESAYV QFRFEEELAL KVGDHFVIRF YSPLETIGGG VVLDANPVKH
RRNQAAVISA MKIKENGTRK DKVLLAIFEQ SKNLRDIDYI RDHIGNESIT KELDELVEEK
KIVQLSEGLY LSKEYLASLK NKLLKILREY HKTYPLKEGA NREEVRGKLI PRASVAAIDS
IINYFIDKKI VKWESEFISL PDFKVVYKEA DTELLNEVEK LYKNGEFAPP SLDDLAKYYG
KNKQYTGAIT MLKKSGTIIA LDLKYCIHKD YYQKALDLMN NYLKENDEIA LGIYRDILGV
SRKYAVALLE EFDKKRITKK VGEARRLYK
//
