ID A0A1T4WC05_9GAMM Unreviewed; 643 AA.
AC A0A1T4WC05;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 28-JAN-2026, entry version 31.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=SAMN02745130_01424 {ECO:0000313|EMBL:SKA74832.1};
OS Thiothrix eikelboomii.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Thiotrichales; Thiotrichaceae; Thiothrix.
OX NCBI_TaxID=92487 {ECO:0000313|EMBL:SKA74832.1, ECO:0000313|Proteomes:UP000190460};
RN [1] {ECO:0000313|EMBL:SKA74832.1, ECO:0000313|Proteomes:UP000190460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49788 {ECO:0000313|EMBL:SKA74832.1,
RC ECO:0000313|Proteomes:UP000190460};
RA Peterson S.W.;
RL Submitted (FEB-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}.
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DR EMBL; FUYB01000005; SKA74832.1; -; Genomic_DNA.
DR RefSeq; WP_078921902.1; NZ_FUYB01000005.1.
DR AlphaFoldDB; A0A1T4WC05; -.
DR STRING; 92487.SAMN02745130_01424; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000190460; 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 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:SKA74832.1};
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:UP000190460}.
FT DOMAIN 1..169
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 643 AA; 71013 MW; F102C47E5EDAD998 CRC64;
MIIGTAGHID HGKTTLIHAL TGVDTDRLPE EKRRGITIEL GFAYLPSSDG RVLGFVDVPG
HEKFVSTMTA GASGIEQAVL VIAADDGIMP QTREHLGILS FMAVKGLTIA LTKIDRVEPE
LITARCLEIQ AWLAQTAYAK AAIFPVAAMT GSGIPALRQH LLALPESITT AASQGVRFAF
DRCFILTGQG VTVSGLLHTG QLQVGDLLKL SPLGLTVRIR SIHAQNRAVQ TTSAGSRCGL
VLVGVEKDQI ERGQWLLANH LPAPCERFDA LLTLAQDTAH RWREGLQVMV HHGAARCPAR
LILLEDTAWQ PGTSGLVQCN LSEPLPIFWH DRIVLRDMSG QHTLAGGLVL DVMPPLRGRK
KPERQAILQA LTAAQPEQAL LQLLRLATLP LSLQAWALQM NYPLAHLLAE LQAQTPDIQI
MDQHGQAWCL LPELAVQLHE QLQAHLDYFH QQQADEPGIS CERLRRMALP NASPDLFSCL
VEYWLQQGIL VQTGSFLHAP GHVLSLTLTE QQLWEQLLPI LQAGRFDPPW VRELAEQLQQ
PESLIRQVLC KQTRRGEVHQ IVHDLFYAPI AIQALAAIVC AQAQPLLNVV NFRNQIGIGR
KRAIQILEFF DRVGLTRRIV GEGAQGKRRD ERLLRNPQLF SNN
//
