ID A0A7I8DCM3_9BACL Unreviewed; 642 AA.
AC A0A7I8DCM3;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=skT53_29280 {ECO:0000313|EMBL:BCJ87943.1};
OS Effusibacillus dendaii.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Effusibacillus.
OX NCBI_TaxID=2743772 {ECO:0000313|EMBL:BCJ87943.1, ECO:0000313|Proteomes:UP000593802};
RN [1] {ECO:0000313|EMBL:BCJ87943.1, ECO:0000313|Proteomes:UP000593802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=skT53 {ECO:0000313|Proteomes:UP000593802};
RA Konishi T., Kawasaki H.;
RT "Complete Genome Sequence of Effusibacillus dendaii Strain skT53, Isolated
RT from Farmland soil.";
RL Submitted (AUG-2020) 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; AP023366; BCJ87943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7I8DCM3; -.
DR KEGG; eff:skT53_29280; -.
DR Proteomes; UP000593802; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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; ELONGATION FACTOR TU-RELATED; 1.
DR PANTHER; PTHR43721:SF11; SELENOCYSTEINE-SPECIFIC ELONGATION FACTOR; 1.
DR Pfam; PF25461; Beta-barrel_SelB; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 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; 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:BCJ87943.1};
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:UP000593802}.
FT DOMAIN 10..183
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 642 AA; 71929 MW; C25D7B2642EEB18D CRC64;
MKGENAVTQD HFIIVGTAGH IDHGKTTLVR ALTGLDTDTH KEEKERGISI DIGFAPLTLP
DGRRIGVIDV PGHERFIKNM LAGAAGIDLI LLVIDANEGI MPQTKEHLHI VELLHVQKGI
VVLTKIDTVD EEWRSLVTEE IREGLAGTIL QDAPIVPVSA YTGEGIDVLR EQISELAKDI
QPREVSAPFR MPIDRVFSLP GFGTVVTGTI LAGQVKVGDA LEVLPGGEPV RVRSIQVHGE
TTERAQAGQR TALNLVGVER TELGRGDVVA KPKLFKPSEL LDVRFRLLSD SPWTLKNRMR
IRLYIGTSEV LGRVVLLEGD ELLPGQEGFL QLDLESPIVC ETKDHFILRT YSPMLTIGGG
VVIDPHPARL YRRNRQYVIE ELESKEKGGP QERILQLLDE EIGLTAAELS TRLKATVEQT
QTWLTELMER EGICEIPGTN GFISFKSLNR VLNEIELKIQ AHYERERFHT FVAKAQVMSQ
LTKKLKPKIY DGILELGERA ERIEVRQDRI KLAGYEVPLN PKEEQLLQEI VGRFQSDLYQ
PPTLQELLTL YKGQEKTVQG IITLLKERET LVEVEEGLLF SRQAIEQAPT ILSEIGTEAG
FTVAEFRDRV GTSRKFALGL LEYLDRTKVT KRVEDRRVLL KK
//
