ID A0A370NEN3_9BURK Unreviewed; 640 AA.
AC A0A370NEN3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, 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 Name=selB {ECO:0000313|EMBL:RDK04035.1};
GN ORFNames=DLM46_03370 {ECO:0000313|EMBL:RDK04035.1};
OS Paraburkholderia lacunae.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=2211104 {ECO:0000313|EMBL:RDK04035.1, ECO:0000313|Proteomes:UP000254875};
RN [1] {ECO:0000313|Proteomes:UP000254875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S27 {ECO:0000313|Proteomes:UP000254875};
RA Feng T.;
RL Submitted (MAY-2018) 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:RDK04035.1}.
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DR EMBL; QHKS01000002; RDK04035.1; -; Genomic_DNA.
DR RefSeq; WP_115099375.1; NZ_QHKS01000002.1.
DR AlphaFoldDB; A0A370NEN3; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000254875; 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; 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; 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; ELONGATION FACTOR TU-RELATED; 1.
DR PANTHER; PTHR43721:SF9; GTP-BINDING PROTEIN 1; 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 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:RDK04035.1};
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:UP000254875}.
FT DOMAIN 1..173
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 640 AA; 70220 MW; E5DEBE7B1E68FCA9 CRC64;
MIIGTAGHID HGKTTLVHAL TGVDTDRLKE EKARGISIEL GYAYRPLDNG DVLGFIDVPG
HEQLVHTMVA GACGIDFALI AIAADDGVMP QTREHLAILQ LLGITRGAIA LTKIDRVERA
RVGQARDEIR TWLAPTMLAD APVFETQALQ AGDAGVAALD AHLREAALAW RARRDDGLFR
LAVDRVFTLA GAGTIVTGTA FAGRVSVGDT VWLTPRAEPV RVRSVHVQNR PAQTGRAGER
CALNLAGIPK ERIARGDWIV DRRLVAASER LDVELTMLPD AEMTLQHWKP LHVHLATMHR
VAHGTLLEGE TLAAGQAARV QLVFDAPVCA LPGDRFIVRN AQATRTVGGG RVLDPFGPAR
KRRTPERHAW LDALTAWLET GRIEPLLEQS PRGMLRSTLE RLTGRALDDS TLPAEALVVP
LRGSHEGEAC IVLRAHWACM RANVVDALRT FHERSPDEQG PDTARARRIA APLLSDALWR
ELVEVMVADG EITRSGPWLH LPSHSVSFDA SEERLAAQLL PLVAAGRYDP PWVRDLASAV
EVPEEQVRQL LRKLARKGEV YQVVRDLFYR RDTVRELARL IAQLAGERGE GLAAASFRDA
TGLGRKRAIQ LLEFFDRVGY TRFLHEVHVL RGDGPLLEAL
//
