ID A0A4R3VGY6_9BURK Unreviewed; 648 AA.
AC A0A4R3VGY6;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 28-JAN-2026, entry version 26.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=EV686_101440 {ECO:0000313|EMBL:TCV02979.1};
OS Paracandidimonas soli.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Alcaligenaceae; Paracandidimonas.
OX NCBI_TaxID=1917182 {ECO:0000313|EMBL:TCV02979.1, ECO:0000313|Proteomes:UP000294692};
RN [1] {ECO:0000313|EMBL:TCV02979.1, ECO:0000313|Proteomes:UP000294692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100048 {ECO:0000313|EMBL:TCV02979.1,
RC ECO:0000313|Proteomes:UP000294692};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) 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:TCV02979.1}.
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DR EMBL; SMBX01000001; TCV02979.1; -; Genomic_DNA.
DR RefSeq; WP_132472989.1; NZ_JBHRVM010000001.1.
DR AlphaFoldDB; A0A4R3VGY6; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000294692; 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; cd04171; SelB; 1.
DR CDD; cd15491; selB_III; 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; 3.
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; 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 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; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:TCV02979.1};
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:UP000294692}.
FT DOMAIN 1..169
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 648 AA; 69601 MW; 74C4A18608AA94C8 CRC64;
MIVGTAGHID HGKTALVRAL TGVDGDRLAE EKARGITIEL GFAYADLGGG GITGFVDVPG
HERLIHTMLA GAGGIDMALL VVAADDGIMP QTREHLAILD LLGIRRAIVA LTKADLAGPE
RRAEVVEEIR DALAGTNLGD APVMAVSSVT GEGIDDLRAA LAACEAEAAA RDASGLFRFA
VDRSFVLQGV GTVVTGTVLA GRVGLDDSVM ISPMGLSARV RGIHAQNRKA AEGVAGQRCA
LNLAGDGVTK EAIHRGDLLL APALHAPTAR IDAELTLLAS EPKPLGIWFP ARLYSHAFET
GVRIVPLQGP LSPGGRGLVQ LVLEHPVAAT VGDTFILRDT SASRTIGGGR FLDLRPPARK
RSTPERLAWL EASRIEGPEA ALSALVADPA GGMDGRDEMP AAVTVDLPAF LRDRGLPYRS
LSQMPACIGV AAIGDLVLSS SALDRLRADL LAQLQTFHEE NPDLSGIGRE KLRLSLTPRL
PKDSFLRFLG EEAGAGRVAL DGAFVRLPGH MVKLSPEDEA LFSRIHPQLL GEGRFRPPRV
RDFANAFEID EREIRRMMRL TQKLGWTDQI AHDHFFAREV TREMVAIILD VAEQSEDGWF
TAPAFRDRVQ NGRKVAIEIL DFFDRLGLTL RRGDLRRINP HRVDLFGD
//
