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Database: UniProt
Entry: G2LEF0_CHLTF
LinkDB: G2LEF0_CHLTF
Original site: G2LEF0_CHLTF 
ID   G2LEF0_CHLTF            Unreviewed;       629 AA.
AC   G2LEF0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   28-JAN-2026, entry version 75.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   OrderedLocusNames=Cabther_A0856 {ECO:0000313|EMBL:AEP11613.1};
OS   Chloracidobacterium thermophilum (strain B).
OC   Bacteria; Pseudomonadati; Acidobacteriota; Terriglobia; Terriglobales;
OC   Acidobacteriaceae; Chloracidobacterium.
OX   NCBI_TaxID=981222 {ECO:0000313|EMBL:AEP11613.1, ECO:0000313|Proteomes:UP000006791};
RN   [1] {ECO:0000313|EMBL:AEP11613.1, ECO:0000313|Proteomes:UP000006791}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B {ECO:0000313|EMBL:AEP11613.1,
RC   ECO:0000313|Proteomes:UP000006791};
RX   PubMed=21951563; DOI=10.1111/j.1462-2920.2011.02592.x;
RA   Garcia Costas A.M., Liu Z., Tomsho L.P., Schuster S.C., Ward D.M.,
RA   Bryant D.A.;
RT   "Complete genome of Candidatus Chloracidobacterium thermophilum, a
RT   chlorophyll-based photoheterotroph belonging to the phylum Acidobacteria.";
RL   Environ. Microbiol. 14:177-190(2012).
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; CP002514; AEP11613.1; -; Genomic_DNA.
DR   RefSeq; WP_014099351.1; NC_016024.1.
DR   AlphaFoldDB; G2LEF0; -.
DR   STRING; 981222.Cabther_A0856; -.
DR   KEGG; ctm:Cabther_A0856; -.
DR   HOGENOM; CLU_023030_3_0_0; -.
DR   OrthoDB; 9804504at2; -.
DR   Proteomes; UP000006791; Chromosome 1.
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; 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   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:AEP11613.1};
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:UP000006791}.
FT   DOMAIN          2..174
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   629 AA;  69110 MW;  7177C4CF10397F37 CRC64;
     MERSVIIGTA GHIDHGKTSL VQALTGTNPD RLPEEQRRGM TIDLGFAHLN YRDWRFAFVD
     VPGHERFIKN MLAGAHGIDL VLLVIAADEG VMPQTVEHLS ICQLLGLSHG VIALTKCDLV
     EPDWLALIRD DVARFTQGTF LAGKPVVAVS AHTGAGCEAL LQALAGEAAA VRPHAVACPP
     RLPIDRIFTR PGFGTVVTGT LISGTFAVGE EVSIEPGGIV TRIRGLEVHG VARKEVHAGE
     RVALNLTSLE VGDLRRGDVV TPLHRFHPTS RLDVQLELLA DAPGPLTDNT RVRLHHGTSE
     VMARVTLLDG RHELPPGNVC FAQLRLEAPL LALPDDRFIL RRYSPATTIG GGKILDVHPP
     RRRGRSRQTD DVLKQLAAGG DQRRMAFVRR TGATGLTLAE LASLTGDSDA ELEAFARRTP
     ECVFLGPARR LVAQTALDQL CQNITTTLET LHRERPRQPD LPREEIRQRT AHNLPTEVFQ
     HAVTRLVHEQ RIVADAHAMR LASHQVQLSA SDTAQKQTVE QLCRQAGWHM PTLPDLCRLT
     NRPATQVLAD VQLLIIEGRL VRVGDFFLHA EAASELLARL RQAKTKGETL DVGAFKVLFD
     LPRKYAIPLL EWLDQTGVTR RYGNIRLMA
//
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