ID A0A2S0MGP4_9BURK Unreviewed; 639 AA.
AC A0A2S0MGP4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 28-JAN-2026, entry version 29.
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:AVO35065.1};
GN ORFNames=C6570_13095 {ECO:0000313|EMBL:AVO35065.1};
OS Ottowia oryzae.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Comamonadaceae; Ottowia.
OX NCBI_TaxID=2109914 {ECO:0000313|EMBL:AVO35065.1, ECO:0000313|Proteomes:UP000239709};
RN [1] {ECO:0000313|EMBL:AVO35065.1, ECO:0000313|Proteomes:UP000239709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KADR8-3 {ECO:0000313|EMBL:AVO35065.1,
RC ECO:0000313|Proteomes:UP000239709};
RA Kim S.-J., Heo J., Kwon S.-W.;
RT "Genome sequencing of Ottowia sp.";
RL Submitted (MAR-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}.
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DR EMBL; CP027666; AVO35065.1; -; Genomic_DNA.
DR RefSeq; WP_106703614.1; NZ_CP027666.1.
DR AlphaFoldDB; A0A2S0MGP4; -.
DR KEGG; otk:C6570_13095; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000239709; Chromosome.
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; 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 InterPro; IPR048931; WHD_2nd_SelB_bact.
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; 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:AVO35065.1};
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:UP000239709}.
FT DOMAIN 1..169
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 639 AA; 66987 MW; C4C3232F2474E4F1 CRC64;
MIIGTAGHID HGKSTLVRAL TGVDTDRLPE EKKRGISIEL GYAFLDVEGS DARVGFIDVP
GHERLVHTMV AGASGIDMAL LLVAADDGPM PQTLEHLAVL SLLGIRRGVV AITKADRASP
ERIAEVRAEM AALLAPTPLS GAPILAVSAQ TGEGVDALKA IILEAARADA AGAEGGFDHK
AFRLAIDRSF TLAGTGTVVT GTIHAGQVRV GDELAVLPTP SGQPVLTRAR SLHAQNRAVE
AAQAGQRCAV ALPGIAKNDV ERGQWLCDPA IALQTHRIDV QLTLWHGEAK AMKSGARVLV
HIGAAHVAAS VALLDVDVLA PGESALAQLV LHAPVGAWHG ERVLLRDAAA SRTVAGGTVL
DPFAPTRYRR TPQRLAELRA LTLPTAPERL AGLLAVAPYG VDVARFAAAQ GLASLTPDSV
PNKALAQAGL ALGATQTEAF EQAALAALAA FHDKQPDELG PDTARLRRLA APRLPAPLWQ
TLLARLAADG RLGLRGAVAH LPSHGAQLTA QETRIAQKVA PGLAAAGFEG AWVRDLAKGA
GESEALVRIT LARLARQGDL HQTVKDLYYA PATMARLAAI AREVGSEHDG DVLAAQFRDA
TGLGRKRAIQ ILEYFDRIGL TRRVGDLHKL RAESTLFIE
//
