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Database: UniProt
Entry: A0A1J5NTJ4_MOOTH
LinkDB: A0A1J5NTJ4_MOOTH
Original site: A0A1J5NTJ4_MOOTH 
ID   A0A1J5NTJ4_NEOTH        Unreviewed;       634 AA.
AC   A0A1J5NTJ4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   28-JAN-2026, entry version 34.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   Name=selB {ECO:0000313|EMBL:OIQ59103.1};
GN   ORFNames=MOTE_15200 {ECO:0000313|EMBL:OIQ59103.1};
OS   Neomoorella thermoacetica (Clostridium thermoaceticum).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Neomoorellales;
OC   Neomoorellaceae; Neomoorella.
OX   NCBI_TaxID=1525 {ECO:0000313|EMBL:OIQ59103.1, ECO:0000313|Proteomes:UP000182811};
RN   [1] {ECO:0000313|EMBL:OIQ59103.1, ECO:0000313|Proteomes:UP000182811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21394 {ECO:0000313|EMBL:OIQ59103.1,
RC   ECO:0000313|Proteomes:UP000182811};
RA   Poehlein A., Bengelsdorf F.R., Esser C., Duerre P., Daniel R.;
RT   "Genome-based comparison of Moorella thermoacetic strains.";
RL   Submitted (AUG-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OIQ59103.1}.
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DR   EMBL; MDDC01000010; OIQ59103.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J5NTJ4; -.
DR   OrthoDB; 9804504at2; -.
DR   Proteomes; UP000182811; Unassembled WGS sequence.
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; 2.
DR   InterPro; IPR057335; Beta-barrel_SelB.
DR   InterPro; IPR050055; EF-Tu_GTPase.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR015189; Elong_fac_SelB-wing-hlx_typ-1.
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; PF09105; WHD_1st_SelB; 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; 4.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Elongation factor {ECO:0000313|EMBL:OIQ59103.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          1..173
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   634 AA;  70757 MW;  98B6C2DE15F63FDE CRC64;
     MDYIIVGTAG HVDHGKTVLV KALTGVDTDR LKEEKERGIS IELGFAPLTL PSGRQLGLVD
     VPGHERFIRQ MLAGVGGMDL VMLVVAADEG VMPQTREHLA IIDLLQIKKG IVVVTKIDLV
     EADWLELVRE EVRQAVNGTV LEDAPLVEVS ALTGEGIAEL REQLDALAAV TPPRPAAGRV
     RLPVDRVFSV TGFGTVVTGT LWSGTIKVGD ELEVQPEGLK TRARNLQVHG RTVKEARAGQ
     RVAVNLAGIE TEAVHRGSSL LEPGFLSPTY RLDASFKLLD GARPLANRHR VHFYLGTTEA
     LGRVILLDRD ELNGGEEALV QLLMEKPVVA SREDRFILRS YSPMETIGGG IIIDPAPPRH
     RRFRPEVLDS LRRRLEGSPE KILAQVIQEH REGLDWHEAA SRASLSLEET RKLLQAMAAD
     GQVTLLRVEN DLYAISTGLY QAWWQVVARA LEEFHRHYPL RPGLAREELR SRYFSRLPAR
     VYQALLEEWA REGRLQLAAN TIALAGFTPS FNETQKKLLK ELEEKYRASR WQPPSFKEVA
     ASFNLDQVEL EELLHYLVRE GALVKINDEF YWHRQALGEA REVIKNLAST GPFGLAEARD
     ALGSSRKYVL PLLEYLDKVK FTRRLGDKRV VVGN
//
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