ID A0A7U4TI42_DESA2 Unreviewed; 634 AA.
AC A0A7U4TI42;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=HS1_001825 {ECO:0000313|EMBL:AMM41619.1};
OS Desulfofervidus auxilii.
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota;
OC Candidatus Desulfofervidia; Candidatus Desulfofervidales;
OC Candidatus Desulfofervidaceae; Candidatus Desulfofervidus.
OX NCBI_TaxID=1621989 {ECO:0000313|EMBL:AMM41619.1, ECO:0000313|Proteomes:UP000070560};
RN [1] {ECO:0000313|EMBL:AMM41619.1, ECO:0000313|Proteomes:UP000070560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS1 {ECO:0000313|EMBL:AMM41619.1,
RC ECO:0000313|Proteomes:UP000070560};
RA Krukenberg V., Richter M., Wegener G.;
RT "Candidatus Desulfofervidus auxilii, a hydrogenotrophic sulfate-reducing
RT bacterium involved in the thermophilic anaerobic oxidation of methane.";
RL Submitted (OCT-2015) 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; CP013015; AMM41619.1; -; Genomic_DNA.
DR RefSeq; WP_066064307.1; NZ_CP013015.1.
DR AlphaFoldDB; A0A7U4TI42; -.
DR KEGG; daw:HS1_001825; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000070560; 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; 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; 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; 3.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:AMM41619.1};
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:UP000070560}.
FT DOMAIN 1..174
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 634 AA; 71668 MW; 554F2429A67ACD26 CRC64;
MKPIILGTAG HIDHGKTALI RALTGIDTDR LKEEKERGIT IELGFAFLTL PSGQLVGIVD
VPGHERFVHH MVAGAGGMDL VALVIAADEG VMPQTREHLD ICSLLKVRHG LVVITKIDLV
DTEWLELVEE DIKGFLKGTF LEKSPIIKVS SVTKEGIPEL ITALEKLVTQ VEPKSTASLF
RLPIDRVFTI KGFGTVVTGT TIGGSVKIGD SLVVYPQKKK TRVRNLQVHH QTVTTAFAGQ
RTAVNLQGLE KEEIQRGNVL APSDSLLPTF MLDGTLEILS SVSKPLKNRT LVRLHLHTAE
ILAYAILLDK EEIKPGETGY VQFRLRQPTV ALPGDRFVIR SYSPIFTLGG GAILHPAPVK
HKRFRPQVIE DLKALETGNL EKAILCHLNQ AGYKGISRQT IRIFTNNFSE TLDHTLETLQ
KKQRIYLINK DTHHYIHRRY IEEISKKMVS FLNTFHATHP LLLGISKDEL KSKLLPFIRD
ELFGFVLHYL EGKHIIVIEQ NLVRLSSHTI RLNKEEQILK EKIYHVLHTA QYSPPSPQEL
AKMLKTNPEK IMHLLRLLTE EGKIIRIKED FYFDTTLLNT LKEKLTTYLK THQGITPAEF
KNLTHASRKY NIPLLEYFDH IKLTLRVGDK RVLR
//
