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Database: UniProt
Entry: A0A1M7SFL0_9BACT
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Original site: A0A1M7SFL0_9BACT 
ID   A0A1M7SFL0_9BACT        Unreviewed;       640 AA.
AC   A0A1M7SFL0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   28-JAN-2026, entry version 36.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   ORFNames=SAMN02745728_00891 {ECO:0000313|EMBL:SHN57308.1};
OS   Desulfovibrio litoralis DSM 11393.
OC   Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia;
OC   Desulfovibrionales; Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=1121455 {ECO:0000313|EMBL:SHN57308.1, ECO:0000313|Proteomes:UP000186469};
RN   [1] {ECO:0000313|EMBL:SHN57308.1, ECO:0000313|Proteomes:UP000186469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11393 {ECO:0000313|EMBL:SHN57308.1,
RC   ECO:0000313|Proteomes:UP000186469};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) 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}.
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DR   EMBL; FRDI01000003; SHN57308.1; -; Genomic_DNA.
DR   RefSeq; WP_072696568.1; NZ_FRDI01000003.1.
DR   AlphaFoldDB; A0A1M7SFL0; -.
DR   STRING; 1121455.SAMN02745728_00891; -.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000186469; 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; 3.
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:SHN57308.1};
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:UP000186469}.
FT   DOMAIN          1..171
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   640 AA;  72189 MW;  506665580F1A87E9 CRC64;
     MPVILGTAGH IDHGKTSLIN ALTDINCDRL IEEKKRGITI ELGFAFLNND DGERLSIIDV
     PGHERFVKNM VAGASGIDLV LLVIAADEGI MPQTKEHLEI CSLLGIKQGL IALTKTDLVE
     QEWLDLVQEE IKDFLKGSFL ENADIFPVSV QTGSGLESLK KELLTREKNL RNKKRSDLFR
     LPIDRIFSLK GHGTVVTGTM IAGQVKNGEE LTVYPKEKNT KVRSLHSHDK NVEIAEAGGR
     TAINLSNLEV SDIQKGEVLA RPDSLFPSLH WDIKLTCLSS TPTAIKHRTE IHFHHGTKET
     LARLYFFDRD KLNPGETALC QVRFTEPMVG VFGDRCVIRA YSPLRTIAGA ELLNPLSLEL
     KKKDPLFQEK TEKLLQLGNA EAKDLILMRL ELAEKQGLNY NELLAFTNLN SKTLEKELAL
     LNGKQELSCF DKEEKRYIAQ SIVQALENSA LSFINEFHKQ NPAKNGLGKN EFYSGWGASL
     YPKLLHFLLE RLSKKKLLHV EGDLVRIPSH QAKLETNQQD IKTALLNIYK ESDKTPLNIK
     EILESLALNQ KEALPLLKNL QDSGELVKIS DEIYYYRPVL DKIWEAVTAW FESNDDLNLA
     VLKDLTSLSR KYLIALLEYF DREKLTVRVG DKRLLRGSKK
//
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