ID A4J6J7_DESRM Unreviewed; 635 AA.
AC A4J6J7;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 28-JAN-2026, entry version 103.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN OrderedLocusNames=Dred_2185 {ECO:0000313|EMBL:ABO50700.1};
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO50700.1, ECO:0000313|Proteomes:UP000001556};
RN [1] {ECO:0000313|EMBL:ABO50700.1, ECO:0000313|Proteomes:UP000001556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI-1 {ECO:0000313|EMBL:ABO50700.1,
RC ECO:0000313|Proteomes:UP000001556};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) 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; CP000612; ABO50700.1; -; Genomic_DNA.
DR RefSeq; WP_011878502.1; NC_009253.1.
DR AlphaFoldDB; A4J6J7; -.
DR STRING; 349161.Dred_2185; -.
DR KEGG; drm:Dred_2185; -.
DR eggNOG; COG3276; Bacteria.
DR HOGENOM; CLU_023030_3_0_9; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000001556; 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; IPR003029; S1_domain.
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.
DR PROSITE; PS50126; S1; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:ABO50700.1};
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:UP000001556}.
FT DOMAIN 1..176
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT DOMAIN 194..264
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 635 AA; 71692 MW; 4EF9B0E1544248ED CRC64;
MKHIIIGTAG HVDHGKTLLI KTLTGMDTDR LKEEKERGIS IELGFAQLKL PSGKQAGIVD
VPGHEKFIKN MLAGVGGIDL VLLVIAADEG VMPQTKEHVD IIQLLQVKKG IVVLTKIDMV
DEEWLSLVTE EIREYLKDTV LSEAPVVPVS STTKQGIPQL LDLIDQFVDD TEERNSSGKL
RLPIDRVFSV TGFGTVVTGT LLSGRVSTGD TVEIMPLGTV SRVRSIQVHG KKVEQARAGQ
RTAVNIIGVE VEEVKRGSVL VTPNSVEPSH RMDVKFLLLE SAEKPLKNRA RVRLYLGTDE
ILGRVRLLDR EEIEPNQEAY VQLELEERGI AGKGDRFVIR SYSPMRTIGG GVVIEPNAPK
HKRYRSEVLE GLATKEKGTP EELVNQLLAG KQGLFSPEEI IEATGLAGDD LKISIEKLQS
EQQVKCIPVD KKSLYIAQFT YNKWRQEIKS MVINYHREYP LREGYPKEEL RSRKFPFINN
KHFQYLLQAM EIDGLLKLHD KTLALAEFTG ELSGSQQKLV QDMICAIQEG NFQPPSWVEV
VKKFRLKDAE SQEYLQYFLR TGQLVKLSDD ELYYTADRYQ QAKTKIVEYL KENKEISVAQ
TRDLLKTSRK FTLPLLETMD RERLTRRVGD NRVLV
//
