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Database: UniProt
Entry: A0A1D8GPG3_9FIRM
LinkDB: A0A1D8GPG3_9FIRM
Original site: A0A1D8GPG3_9FIRM 
ID   A0A1D8GPG3_9FIRM        Unreviewed;       631 AA.
AC   A0A1D8GPG3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   28-JAN-2026, entry version 38.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   ORFNames=Gferi_26445 {ECO:0000313|EMBL:AOT72785.1};
OS   Geosporobacter ferrireducens.
OC   Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
OC   Thermotaleaceae; Geosporobacter.
OX   NCBI_TaxID=1424294 {ECO:0000313|EMBL:AOT72785.1, ECO:0000313|Proteomes:UP000095743};
RN   [1] {ECO:0000313|EMBL:AOT72785.1, ECO:0000313|Proteomes:UP000095743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRF9 {ECO:0000313|EMBL:AOT72785.1,
RC   ECO:0000313|Proteomes:UP000095743};
RA   Kim S.-J.;
RT   "Genomic analysis reveals versatility of anaerobic energy metabolism of
RT   Geosporobacter ferrireducens IRF9 of phylum Firmicutes.";
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}.
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DR   EMBL; CP017269; AOT72785.1; -; Genomic_DNA.
DR   RefSeq; WP_069981094.1; NZ_CP017269.1.
DR   AlphaFoldDB; A0A1D8GPG3; -.
DR   STRING; 1424294.Gferi_26445; -.
DR   KEGG; gfe:Gferi_26445; -.
DR   OrthoDB; 9804504at2; -.
DR   Proteomes; UP000095743; Chromosome.
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; 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; 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:AOT72785.1};
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:UP000095743}.
FT   DOMAIN          1..172
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   631 AA;  72114 MW;  F213DDC1949A6B87 CRC64;
     MKNVIVGTAG HIDHGKTTLI KALTGTDTDR LLEEKKRGIT IDLGFTHFDL PSGRRAGIID
     VPGHEKFIKN MLAGVGGIDI VLLVIAADEG FMPQTQEHLD ILTILEVKKG IIVLTKVDLV
     DPEWLSLVQE EIREKVKDTF LRDAPMLAVS STQGQGLKEL VERIDFYTEE TEEKNTSIPF
     RLPVDRVFTM SGFGTVITGT LIEGSVHEGD QMTIYPQELT AKVRNLHVHG KKVESAYAGQ
     RVAINLSGVK KEDILRGNVA AEQNSMKETM MLDVKLNMLK HAERIIDNRD RLRLYHGTAE
     VLCRVVLLDR EEIKPGESCY AQLRLEESIV AKRGDHFVIR FYSPMETLGG GVILEPNPIK
     HKRFKADTLE ELKVKEEGSP EQILEKVILR FNDAFANIGF YATQTGLSEN TILAIVDKLT
     EKGIIRKFSG TVPVHIDYLT KLEDSIIKVL QNYHNSNPLK IGMGKEELRN KLKIKIKGKL
     YDELLEHFEN NQIIRLHNNF TALADFEVKY SPEQLVILEE IDRLYLEREF QTPAPEDFLN
     SKKNEQKYRE VLEALIEKKQ LIKINEDILL HVENYEKAKE MLKQFIKENG QITLSEFRDL
     IHTTRKYALP LIENFDQNKI TKRIDEKRVL Y
//
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