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Database: UniProt
Entry: A0A1Q8R313_9FIRM
LinkDB: A0A1Q8R313_9FIRM
Original site: A0A1Q8R313_9FIRM 
ID   A0A1Q8R313_9FIRM        Unreviewed;       631 AA.
AC   A0A1Q8R313;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   28-JAN-2026, entry version 33.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   ORFNames=DSOL_0193 {ECO:0000313|EMBL:OLN34015.1};
OS   Desulfosporosinus metallidurans.
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
OC   Desulfitobacteriaceae; Desulfosporosinus.
OX   NCBI_TaxID=1888891 {ECO:0000313|EMBL:OLN34015.1, ECO:0000313|Proteomes:UP000186102};
RN   [1] {ECO:0000313|EMBL:OLN34015.1, ECO:0000313|Proteomes:UP000186102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OL {ECO:0000313|EMBL:OLN34015.1,
RC   ECO:0000313|Proteomes:UP000186102};
RA   Mardanov A., Beletsky A., Panova A., Karnachuk O., Ravin N.;
RT   "Complete genome of Desulfosporosinus sp. OL.";
RL   Submitted (SEP-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}.
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:OLN34015.1}.
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DR   EMBL; MLBF01000001; OLN34015.1; -; Genomic_DNA.
DR   RefSeq; WP_075363028.1; NZ_MLBF01000001.1.
DR   AlphaFoldDB; A0A1Q8R313; -.
DR   STRING; 1888891.DSOL_0193; -.
DR   OrthoDB; 9804504at2; -.
DR   Proteomes; UP000186102; 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; 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; 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; 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; 1.
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:OLN34015.1};
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:UP000186102}.
FT   DOMAIN          3..176
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   631 AA;  70638 MW;  83B7930A2F993898 CRC64;
     MDERHYLVGT AGHVDHGKTE LIRALSGMET DRLKEEKQRG ISIELGFAHM KLPSGRQVGI
     VDVPGHERFV RQMLAGASGM DVVLLVIAAD EGIMPQTQEH LDILTLLGIP RGIIVINKKD
     LVDEEWLEFM EEEVREKLRE TVFHEAPICK VSALTGEGIP LLRQTIDELL SDVESKNSTG
     PVRMPLDRVF SIQGFGTVVT GTLNSGEVKL GQELAIEPAH ILTKVRSLQV YKNKVNSAEA
     GQRVAVNLAG VDVTEVKQGS VLVMPNVFKV GKILDIKVLN LSSTEKPLTQ RQRVRFHLGT
     TEILGRIHLL DHEELAPGQE GFAQILLEEP VVAAPGDRFV LRFYSPTHTI AGGKVLSVAE
     FKQKRFRENV LAQLRIKDQG DPLDLIEREI TEPLSGPDLA ARMHVSLAEL EDSLSSLEKS
     ERLEIWKEDE TPLYWGKAMA EAWRLKLITV VRAYEDLNPL RGGINREELK TRLGITWTHR
     RWQTILELGS NRGFYRISGS KVQTNEGAEI PSGVLKRLDA LRSHWHNVGL MPPELGTIAE
     ACGIPKADVQ EYAGYLCDQE EWVSVSGSYY QINDIQKAKS VLVDALKLHG EVGVAEVREL
     WGTSRKYAVP LLEYFDQQRV TRRQGDKRTL F
//
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