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Database: UniProt
Entry: A0A4R2P7L2_9BACL
LinkDB: A0A4R2P7L2_9BACL
Original site: A0A4R2P7L2_9BACL 
ID   A0A4R2P7L2_9BACL        Unreviewed;       637 AA.
AC   A0A4R2P7L2;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   28-JAN-2026, entry version 26.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   ORFNames=EV207_1067 {ECO:0000313|EMBL:TCP30184.1};
OS   Scopulibacillus darangshiensis.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Sporolactobacillaceae;
OC   Scopulibacillus.
OX   NCBI_TaxID=442528 {ECO:0000313|EMBL:TCP30184.1, ECO:0000313|Proteomes:UP000295416};
RN   [1] {ECO:0000313|EMBL:TCP30184.1, ECO:0000313|Proteomes:UP000295416}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19377 {ECO:0000313|EMBL:TCP30184.1,
RC   ECO:0000313|Proteomes:UP000295416};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAR-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:TCP30184.1}.
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DR   EMBL; SLXK01000006; TCP30184.1; -; Genomic_DNA.
DR   RefSeq; WP_132744709.1; NZ_SLXK01000006.1.
DR   AlphaFoldDB; A0A4R2P7L2; -.
DR   OrthoDB; 9804504at2; -.
DR   Proteomes; UP000295416; 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; 2.
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:TCP30184.1};
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:UP000295416}.
FT   DOMAIN          12..185
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   637 AA;  71360 MW;  881E926102A1CC87 CRC64;
     MANTIGEIDM LKHDMTIGLA GHIDHGKTSL TKALTDIETD RLKEEQTRNI SIENGFAYLD
     LEDQRRAAII DVPGHERFIR QMIAGVAGID LVILVIAADE GVMPQTEEHI DILTLLGIKQ
     ALIVLTKIGV VDDEWLAMVE EDVSSYLKKT SFADAPIYKV DSVSGKGIAL LKDAINAASH
     EIRAKNPNEP FRMPIDDVFT LHGLGTIVRG TIFNGQVHKD DNLMLLPKGQ KVKVKSLQIH
     HKDTSIASSG QRAAMNIGGL SRDDVKRGDV LVSDGTIYMP SSRLDVQLKI LNNIDRPFKQ
     RSPVICHLGT AAVMGKLIMF DRNKCEAGDD LYCQIELAAP LTAKKGDRFI VRRPTPAETI
     GGGQVIDVEA VKHRFGEGTI KLLERKAQGA PADLVYQYLV EFEEATERDL LRSTGLPNDL
     LIQILNDTLE RRVIARLSHN TYVLNDRLNQ AQGLLLENLK AYHQDYPMRQ GLSKADLLRS
     LPFGEALQSK VYERLKESNE LESHDHMVKL SDFTPHFPDQ WARRMTGVVN DLAKQGLKPV
     SWSELADESG IPAGLQKDLK DYLLSVGKTM LLEEDLLMHH QAFCDAVKRL RQKSNEAFTI
     QDAKAVLDLS RKYLIPFLEC CDREGYTVRE NNKRRWK
//
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