ID A0A235FCR6_9BACL Unreviewed; 629 AA.
AC A0A235FCR6;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 28-JAN-2026, entry version 29.
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:OYD58747.1};
GN ORFNames=CGZ90_02275 {ECO:0000313|EMBL:OYD58747.1};
OS Fictibacillus aquaticus.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Fictibacillaceae;
OC Fictibacillus.
OX NCBI_TaxID=2021314 {ECO:0000313|EMBL:OYD58747.1, ECO:0000313|Proteomes:UP000215059};
RN [1] {ECO:0000313|EMBL:OYD58747.1, ECO:0000313|Proteomes:UP000215059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GDSW-R2A3 {ECO:0000313|EMBL:OYD58747.1,
RC ECO:0000313|Proteomes:UP000215059};
RA Mayilraj S.;
RT "Fictibacillus sp. nov. GDSW-R2A3 Genome sequencing and assembly.";
RL Submitted (JUL-2017) 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:OYD58747.1}.
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DR EMBL; NOII01000001; OYD58747.1; -; Genomic_DNA.
DR RefSeq; WP_094250708.1; NZ_JBHLXL010000001.1.
DR AlphaFoldDB; A0A235FCR6; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000215059; Unassembled WGS sequence.
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; cd03696; SelB_II; 1.
DR CDD; cd15491; selB_III; 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 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 PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:OYD58747.1};
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:UP000215059}.
FT DOMAIN 3..176
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 629 AA; 71080 MW; C0081FA3115013A5 CRC64;
MKLRHFTIGM AGHIDHGKTT LTKALTGVST DTLKEEIKRS ITIEPGFAPF SLSQNIHSSI
VDVPGHEKLI RQMIAGVAGI DLVLLVIAAD EGIMPQTKEH FEILSFLNIQ NGIIVFTKSD
QIDEELKLYL LEELEELVSG TVFAEFPALF VDSISTNGIS ELIKEIEKQL LTVEPRDASG
PFRMPIDHVF TVKGQGTVVR GTIFEGRADV GDILVLAPGY EKVKVRQIQV HKDPKETAYA
GQRAAINLAG AEREAIKRGH VLIREGSFTE TQTIDIALYT PKELLHPVKQ RTAIKFYSGT
TETMGTLVFF DRNELDDSSN TEPVYCQVRL EQPAVIQRGD RFIIRRPSPE ETIGGGSVID
PNGKKYKFGS STSNMLKEKA EGTPQDRITR VLESKKMLNL QQIERETGLS GDELRSAIES
MGNRLIASGN DYFLRSEVER TCDLFYEEVL RFHEKHPLKP GIQKASLFSI FDNYPLKLLQ
FSLSIMTDIK RLAFHNQYVA DIHFSAHYPS RWSKRMENAV KKLEEDGLTP EPFLHYTESE
QIPAELGADL KHYLLREKRA IEMNDDHLIA SSAYESSLLE MKRLLTSPFT VQDAKSVTGL
SRKYLIPFVE LLDKERETKR NEDNTREWL
//