ID A0A1H6SXZ8_9BURK Unreviewed; 646 AA.
AC A0A1H6SXZ8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 28-JAN-2026, entry version 27.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=SAMN05192539_1003389 {ECO:0000313|EMBL:SEI71796.1};
OS Paraburkholderia diazotrophica.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=667676 {ECO:0000313|EMBL:SEI71796.1, ECO:0000313|Proteomes:UP000198866};
RN [1] {ECO:0000313|Proteomes:UP000198866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 26031 {ECO:0000313|Proteomes:UP000198866};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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}.
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DR EMBL; FNYE01000003; SEI71796.1; -; Genomic_DNA.
DR RefSeq; WP_090864288.1; NZ_FNYE01000003.1.
DR AlphaFoldDB; A0A1H6SXZ8; -.
DR STRING; 667676.SAMN05192539_1003389; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000198866; 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; cd03696; SelB_II; 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; IPR031157; G_TR_CS.
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 InterPro; IPR048931; WHD_2nd_SelB_bact.
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; PF21214; WHD_2nd_SelB_bact; 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; 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:SEI71796.1};
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:UP000198866}.
FT DOMAIN 1..173
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 646 AA; 70303 MW; 6A727DB5370B11B1 CRC64;
MIVGTAGHID HGKTTLVRAL TGVDTDRLKE EKARGISIEL GYAYTPLDNG DVLGMIDVPG
HEKLVHTMAA GACGIDYALL VIAADDGIMP QTREHLAILQ LLGVTRGAIA LTKTDRVDAA
RLTQVRDEIR AWLASTPFSG ASFFETNATA RDDSGVRALS LHLREAAVAW PGRRDDGLFR
LAIDRVFTLA GQGTIVTGTV FAGRVATGDT LMLEPLHRAV RVRSIHAQNR AADAGRAGQR
CALNLAGIDK DAIARGDWIV DARLAKPGER LDVELTLLDD AGITLQHWAP LHVHIGTLHR
VAHVALLDGD TLDAGQTARV QFVFDPPVCA LPGDRFIVRN AQATRTVGGG RVLDPFGPPR
KRRTAERRAW LDALRVWLDD GRIGPLLEEA PRGVSRSMLM QLTGLPAEAL PLPADADEIV
LHGRDAGDAV IVLRSHWARL RSKVLAALDQ YHARLPDELG PDAARLRRIA APLVQDAMWR
ALIDSLVDES AIARSGPWLH LPAHTVSLDA REQVLASALL PLIAQGRYDP PWVRDLATAT
ARDEDAVRQV LRKLARQGDV YQIVRDLFYH RDVVHELARL VAAIAGEGGG ALGASAFRDA
TGLGRKRAIQ ILEFFDRIGY TRFQRDVHWL RPDSQLQEAL ACEPAA
//
