ID A0A157S874_9BORD Unreviewed; 645 AA.
AC A0A157S874;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 28-JAN-2026, entry version 35.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN Name=SelB(TCA) {ECO:0000313|EMBL:SAI66116.1};
GN ORFNames=SAMEA3906486_00789 {ECO:0000313|EMBL:SAI66116.1};
OS Bordetella ansorpii.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Alcaligenaceae; Bordetella.
OX NCBI_TaxID=288768 {ECO:0000313|EMBL:SAI66116.1, ECO:0000313|Proteomes:UP000076848};
RN [1] {ECO:0000313|EMBL:SAI66116.1, ECO:0000313|Proteomes:UP000076848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H050680373 {ECO:0000313|EMBL:SAI66116.1,
RC ECO:0000313|Proteomes:UP000076848};
RG Pathogen Informatics;
RL Submitted (APR-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; FKIF01000002; SAI66116.1; -; Genomic_DNA.
DR RefSeq; WP_066123954.1; NZ_FKIF01000002.1.
DR AlphaFoldDB; A0A157S874; -.
DR STRING; 288768.SAMEA3906486_00789; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000076848; 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; 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:SAI66116.1};
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:UP000076848}.
FT DOMAIN 1..172
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 645 AA; 69279 MW; 690CCD59D3CB91E4 CRC64;
MIVGTAGHID HGKTTLVRAL TGVDTDRLKE EKARGISIEL GYAYTPLPNG DVLGFIDVPG
HEKLVHTMAA GATGIDFGLL VVAADDGVMP QTREHLAILV LLGVARGAVA LTKADRADAQ
RLRGVLDEIA QLAAGTFLAG APVFPTRAAE PGDAGTAALK SHLDDAAQAL PARGAQGLFR
LAVDRAFTLA GHGTVVTGTA HAGRVRVGDE TADLRLMPAG TPVRVRSIHA QNRAGAEGVA
GQRCALNLPG MDKDAIARGD WIADARCFRP SRHVDVELDW LESADGPLRA WAPLHIHIGA
AHHMAHAVPL APEQLVPGQR GRVQLVFDTP VCAMPGDRYI ARNAQASRTV GGGRVLDPNA
PDRKRRTPQR LAWLDAVAAL LDGQGLAAVL REAPLGLDEA QLQRLTGMPA QSLAVPDDAR
WAAARAPRAA RTLLLAEHWE ALCERAVTAL DGFHEHSPDE PGLDAGRLRR IAAPTASEPL
WQAVLERLLA QGRLARNGAW LHRPQHAATL GEAEAALADR LLPLIRDGLY DPPWVRDLAR
SQNEPEDRVR QLLRKLLRRG VVAQVVKDLY YHRDHVAALA VLVAELCERD GSAHAAAFRD
ATGLGRKRAI QILEFFDRVG YTRRLRDNHV LRTDTALFSR ATGAS
//
