ID D6Z6S6_DESAT Unreviewed; 637 AA.
AC D6Z6S6;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 28-JAN-2026, entry version 79.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN OrderedLocusNames=DaAHT2_0324 {ECO:0000313|EMBL:ADH85035.1};
OS Desulfurivibrio alkaliphilus (strain DSM 19089 / UNIQEM U267 / AHT2).
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia;
OC Desulfobulbales; Desulfobulbaceae; Desulfurivibrio.
OX NCBI_TaxID=589865 {ECO:0000313|EMBL:ADH85035.1, ECO:0000313|Proteomes:UP000001508};
RN [1] {ECO:0000313|Proteomes:UP000001508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19089 / UNIQEM U267 / AHT2
RC {ECO:0000313|Proteomes:UP000001508};
RG US DOE Joint Genome Institute;
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Sorokin D.Y., Muyzer G.,
RA Woyke T.;
RT "Complete sequence of Desulfurivibrio alkaliphilus AHT2.";
RL Submitted (FEB-2010) 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; CP001940; ADH85035.1; -; Genomic_DNA.
DR RefSeq; WP_013162566.1; NC_014216.1.
DR AlphaFoldDB; D6Z6S6; -.
DR FunCoup; D6Z6S6; 106.
DR STRING; 589865.DaAHT2_0324; -.
DR KEGG; dak:DaAHT2_0324; -.
DR eggNOG; COG3276; Bacteria.
DR HOGENOM; CLU_023030_3_0_7; -.
DR InParanoid; D6Z6S6; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000001508; 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; 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; 3.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:ADH85035.1};
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:UP000001508}.
FT DOMAIN 1..172
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 637 AA; 70904 MW; A15EA2E83A73437D CRC64;
MREIVLGTAG HVDHGKTSLV KALTGTDTDR LKEEKARGIT IELGFAFLDL PCGHRLGIVD
VPGHERFVRN MVAGAAGIDL VALVVAADEG IMPQTREHFE ICRLLGVERG MIVITKKDMV
EAEWLELVQE EVRDFVQGSF LAEAPMLAVS SISGEGIAAV RETLDQLVAA SDFSEAHGPF
RLPVDRVFTM KGFGAVVTGT SQAGRIALGD DVLFYPRRVP GKIRGIQVHG REQNEVEAGY
RTAINVQGVD KEEIRRGDVL ATPGCLEPAF VFDAEFLYLS NNEKKLKHRR RVRVHLGTAE
VMGRVSLLED EDLAPGGEAA VQLLLEEPVS VWPGDHYVVR SYSPVYTIGG GVIRNCAAAK
RRRFKEANRE IFELYRSGSQ EELALFHLRE SGSTGLTLQE LSVRLGVFGK KTQKLLEKNI
SARKIIIIEP DKQRMIAGET LTALGAKAEK LLTDFHRENP LKSGLPSEEL RRRLARDLSP
RLFQILLTEL LKQKRVVQEE SLIRLASHQV SLAGDAETLR RELGQFYHRA GLSAPTIKET
LEAHGKYPAE LVRELLAVMV REEELVKVSE DLYYDARALA QLKEKLVAFL QAEGEIDAPR
FKNLTGLTRK FSIPLLEYFD RTKVTLRIGD TRKLRSG
//
