ID A0A1W2BNC7_9BACT Unreviewed; 639 AA.
AC A0A1W2BNC7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 28-JAN-2026, entry version 32.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=SAMN02746065_1093 {ECO:0000313|EMBL:SMC74449.1};
OS Desulfocicer vacuolatum DSM 3385.
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
OC Desulfobacterales; Desulfobacteraceae; Desulfocicer.
OX NCBI_TaxID=1121400 {ECO:0000313|EMBL:SMC74449.1, ECO:0000313|Proteomes:UP000192418};
RN [1] {ECO:0000313|EMBL:SMC74449.1, ECO:0000313|Proteomes:UP000192418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3385 {ECO:0000313|EMBL:SMC74449.1,
RC ECO:0000313|Proteomes:UP000192418};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FWXY01000009; SMC74449.1; -; Genomic_DNA.
DR RefSeq; WP_084068744.1; NZ_FWXY01000009.1.
DR AlphaFoldDB; A0A1W2BNC7; -.
DR STRING; 1121400.SAMN02746065_1093; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000192418; 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 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; 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 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.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:SMC74449.1};
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:UP000192418}.
FT DOMAIN 1..174
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 639 AA; 71225 MW; 51D2936980B31D80 CRC64;
MDQIILGTAG HIDHGKTSLI RALTGIETDR LKEEKKRGIT IELGFASIPL ESGEVVGIVD
VPGHEKFVKN MVAGASGIDI VSMAIAADEG VMPQTREHME ICTLMGIKHG FIAMTKIDLV
DEDLMELAME DILEFTQGTF LEDAPIIQVS STTGEGLEDF KKTLNELCHK IPPRTPSPIF
RLPVDRVFSM KGFGTVITGT LASGKTNVGD NIMIFPSRIT SKVRGIQVHG NSVDTVTAGS
RTAINFQGLD RETIDRGDIL STPDTLHPSY MVDAEILFLS SNAKPAKPRT RVRFHSGTSE
VFGYMVLLDR AELTPGDTAC VQIRLETPVC LMKGDRFVIR SYSPIKTIGG GQILNPVARK
HKLSDTQAIE GLACLMEEDH EAILSYFAEQ GKFSGVSFAD LRIMTSIPDK KLGNILQKML
ANRRLIQTDK EQRIYVHGAL FDTIAQEVID RLGAYHKDNP LKEGMPSQEL KSKFRAFNDK
DSKLFPLVIA RLTKENKVIQ DKGTIRLSQH EVALQVDEKE VREKILKIYQ KSGLTPPFFR
TICQDLEVDQ KVARDVLQML IDEKSIVKTK DDLYFDAKAI KDIETKLVTF LQKSGEITTP
QFKDMAGVSR KYIIPLIEYF DTINLTIRVG DTRQLRKKS
//
