ID A0A940SXC8_9ENTE Unreviewed; 637 AA.
AC A0A940SXC8;
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:MBP1044190.1};
GN ORFNames=I6N95_24580 {ECO:0000313|EMBL:MBP1044190.1};
OS Vagococcus allomyrinae.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Vagococcus.
OX NCBI_TaxID=2794353 {ECO:0000313|EMBL:MBP1044190.1, ECO:0000313|Proteomes:UP000674938};
RN [1] {ECO:0000313|EMBL:MBP1044190.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BWB3-3 {ECO:0000313|EMBL:MBP1044190.1};
RA Lee S.D.;
RT "Vagococcus allomyrinae sp. nov. and Enterococcus lavae sp. nov., isolated
RT from the larvae of Allomyrina dichotoma.";
RL Submitted (DEC-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:MBP1044190.1}.
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DR EMBL; JAEEGA010000023; MBP1044190.1; -; Genomic_DNA.
DR RefSeq; WP_209532457.1; NZ_JAEEGA010000023.1.
DR AlphaFoldDB; A0A940SXC8; -.
DR Proteomes; UP000674938; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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:MBP1044190.1};
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:UP000674938}.
FT DOMAIN 3..174
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 637 AA; 70321 MW; 1280A657D45119F3 CRC64;
MSNQHIVIGT AGHIDHGKTT LIKGLTGIET DTTAEEKRRG VSINLGFAYL DLPDGQRIGI
VDVPGHERFV KNMLAGVAGI NLVLLVIDAN EGIMPQTREH LDILQLLGVK DFIVVLTKVG
TVEEDLRQLV VEDIRETLSH TALADAPLIE TDAVLGIGMA ALKSEIYRRV TSIEKSLNES
EPRLNIDRVF SVKGHGTIVT GTLIDGSLKV GADLVVYPSA KKTKIRSIQV HESAQEEAFA
GQRTALNLTK LSLGDLKRGD VITVKNNVTP TWMIDVKLRA LPSAERPLGL WNRVHIHLGT
KEVLGRVVPL GAADIPPGGE GYVQLRLEEQ VAVKQGDHLI LRSYSPTVTI AGGIVLEANA
EKHRRYNQDI LESLHVKESG DFNLVLLDYL NKQAGFVTAK TMADYLNTSS LKINQSLETL
LAKKKVVQVN QTFISSCQLK EISSAIYELL QDYHQKFPLR SGMSLEEVRS RFELRQREVE
AILLLLEGQG VVKRSQGSIK LASFSVIFSA EQQAIKKRIE TTLLEAGLAP PSLAELLAND
PAATAVLETL VGDSVYYLNQ ETVIHMTVYH SALAQVQSFL AAHGTMTLGE FRDMMHTSRK
YSKMFLEHLD ELNVTKRLED SRVLVEYEGL SMRKVME
//
