ID A0A564ZLW5_9BACT Unreviewed; 650 AA.
AC A0A564ZLW5;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN Name=tuf_1 {ECO:0000313|EMBL:VUZ85558.1};
GN ORFNames=MELA_01943 {ECO:0000313|EMBL:VUZ85558.1};
OS Candidatus Methylomirabilis lanthanidiphila.
OC Bacteria; Candidatus Methylomirabilota; Candidatus Methylomirabilia;
OC Candidatus Methylomirabilales; Candidatus Methylomirabilaceae;
OC Candidatus Methylomirabilis.
OX NCBI_TaxID=2211376 {ECO:0000313|EMBL:VUZ85558.1, ECO:0000313|Proteomes:UP000334340};
RN [1] {ECO:0000313|EMBL:VUZ85558.1, ECO:0000313|Proteomes:UP000334340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Cremers G.;
RL Submitted (JUL-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}.
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DR EMBL; CABIKM010000029; VUZ85558.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A564ZLW5; -.
DR Proteomes; UP000334340; 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; 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; 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 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:VUZ85558.1};
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:UP000334340}.
FT DOMAIN 16..189
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 650 AA; 71732 MW; C8A85866A6537C39 CRC64;
MLRLGRMCYH GAVTAIKHII IGTAGHIDHG KTALVKALTG IDTDRLKEEK ERGISIELGF
ADLTLSDDLQ LGIIDVPGHE RFVKTMLAGV GGIDLVVLVI GADEGVMPQT REHLHICELL
QIKRGVVVLT KVDLVEPDWL EMIRADLKGF LAGTFLEGAP VVPVSAVTGQ GLPQLRSVLR
EAAETIGPKR HDGIVRLPID RVFTIKGFGT VVTGTLWSGT LRAGDEVVVL PLELRSRVRR
LQVHGRTVEQ AWAGQRIAVN LPGLEVDQLN RGDLLSVPDA LEPSMTFDVS LALLKDAPRA
LRNRARVRFH LGTSEILARV VLLDGEDLNP GDETFAHVRL EGPAAALAGD RYVIRSYSPA
QTIGGGSILD PNPPMRRRAK GPLLEHLKVL QTGTAGQQVE RLLAQAGPTP IALDALRVSA
SLDDTTLQRE LRRLVESGMA LALGANGALG YVHRLNYDRL ATEIVARLED FHRQEPLKDG
LPKEELRSKL HQVGPVLFAH LLQSLVETQQ IVIDREKVRH FLHRPTLSAP EQAVKDRLAA
IYQQAGLQPP DLEAALTQAG SARKTGMTIF RCLVDEGTVI KIKDNLYLHR DHYSRAKEML
LNHFRFHAVI TVQQFKELLG VSRKFAIPFL EHFDSAKLTR RQNDERVLYV
//
