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Database: UniProt
Entry: D2Z4M7_9BACT
LinkDB: D2Z4M7_9BACT
Original site: D2Z4M7_9BACT 
ID   D2Z4M7_9BACT            Unreviewed;       637 AA.
AC   D2Z4M7;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   28-JAN-2026, entry version 68.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   ORFNames=Dpep_2349 {ECO:0000313|EMBL:EFC92371.1};
OS   Dethiosulfovibrio peptidovorans DSM 11002.
OC   Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
OC   Dethiosulfovibrionaceae; Dethiosulfovibrio.
OX   NCBI_TaxID=469381 {ECO:0000313|EMBL:EFC92371.1, ECO:0000313|Proteomes:UP000006427};
RN   [1] {ECO:0000313|EMBL:EFC92371.1, ECO:0000313|Proteomes:UP000006427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11002 {ECO:0000313|EMBL:EFC92371.1,
RC   ECO:0000313|Proteomes:UP000006427};
RX   PubMed=21304695;
RA   Labutti K., Mayilraj S., Clum A., Lucas S., Glavina Del Rio T., Nolan M.,
RA   Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Goodwin L., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Spring S., Goker M.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Permanent draft genome sequence of Dethiosulfovibrio peptidovorans type
RT   strain (SEBR 4207).";
RL   Stand. Genomic Sci. 3:85-92(2010).
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:EFC92371.1}.
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DR   EMBL; ABTR02000001; EFC92371.1; -; Genomic_DNA.
DR   RefSeq; WP_005662384.1; NZ_ABTR02000001.1.
DR   AlphaFoldDB; D2Z4M7; -.
DR   STRING; 469381.Dpep_2349; -.
DR   PaxDb; 469381-Dpep_2349; -.
DR   eggNOG; COG3276; Bacteria.
DR   OrthoDB; 9804504at2; -.
DR   Proteomes; UP000006427; 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; 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   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:EFC92371.1};
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:UP000006427}.
FT   DOMAIN          4..177
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   637 AA;  69401 MW;  76832B01688EAF69 CRC64;
     MTEEMSLVIG TAGHIDHGKT HLVKALTGVD CDRLSEERKR GITIELGFAP LELPSGRVVS
     VIDVPGHEKF IRQMVAGASG LDAVLLVVAA DEGVMPQTRE HLDIIELLGV REGFVVLTKA
     DLVDEEMLEL ATDDVQDLVK GTFLQDKPIL AVSSVTGDNL GAVMDEMDKL VDEVVPRDRE
     GAFFMPIDRS FPVAGFGTVV TGTAYRGRVS QGDDMEILPA ELDTRVRSLQ VHGSSVDSAE
     AGQRVAMSLN GLSVDQLNRG DVVCASGVFR ASSCLDVGLK VLPGAIEGIS HWQRLRVHLG
     TSDVLARVAF LDRKELLPGE EAVAQLVLEE PVVASICQRF VVRFYSPLRT IGGGEVLSPY
     GKKARGRRAR EETVARLEAL MASDSREDRI AALVDFHGRI PFDDLIVQTQ ETRKGLAEIL
     KDRLKSRGVS VIPVGNGIII SDGERARLEG SILKRLESFH EEHPHQEGEA ADRLVNGLFA
     DEDRKFGRAF VGWMVEGGVL ISKESLLSLP GFEKEDDQAF QAKVDVLKGL CDDAGFHPPV
     LTDCPKALGM DEKEFSRFLT DVRRMGLFSV VDGTFLISSD VERRLLSALR EVDGGITIAS
     VRDITGSSRK FVLPLLEYLD GKGVTRRVGD RRIILGG
//
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