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Database: UniProt
Entry: A0A931H0N7_9BURK
LinkDB: A0A931H0N7_9BURK
Original site: A0A931H0N7_9BURK 
ID   A0A931H0N7_9BURK        Unreviewed;       591 AA.
AC   A0A931H0N7;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   28-JAN-2026, entry version 16.
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:MBG9386413.1};
GN   ORFNames=I5803_00120 {ECO:0000313|EMBL:MBG9386413.1};
OS   Caenimonas aquaedulcis.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Comamonadaceae; Caenimonas.
OX   NCBI_TaxID=2793270 {ECO:0000313|EMBL:MBG9386413.1, ECO:0000313|Proteomes:UP000651050};
RN   [1] {ECO:0000313|EMBL:MBG9386413.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DR4.4 {ECO:0000313|EMBL:MBG9386413.1};
RA   Le V., Ko S.-R., Ahn C.-Y., Oh H.-M.;
RT   "Bacterial whole genome sequence for Caenimonas sp. DR4.4.";
RL   Submitted (NOV-2020) 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:MBG9386413.1}.
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DR   EMBL; JADWYS010000001; MBG9386413.1; -; Genomic_DNA.
DR   RefSeq; WP_196984403.1; NZ_JADWYS010000001.1.
DR   AlphaFoldDB; A0A931H0N7; -.
DR   Proteomes; UP000651050; 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   FunFam; 3.40.50.300:FF:001064; Selenocysteine-specific translation elongation factor; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
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; 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; 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; 1.
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:MBG9386413.1};
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:UP000651050}.
FT   DOMAIN          1..172
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          571..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..584
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   591 AA;  63295 MW;  70F1146EA5B8951D CRC64;
     MIVATAGHID HGKTTLVKAL TGVDTDRLPQ EKARGISIDI GFAYWQTPGG AVVGFVDVPG
     HERFVRNMLA GVCGIDYAMV VVAADDGVMP QTREHLNILD LLGIRFGVAV ITKADRVDSA
     RLREVADETR GLLQGTSLQD VRVLPVSSVT GAGVDALRDA LAQAAAGFTR NASEGRRMRF
     AVDRAFTVAG SGTVVTGTVF DGAVRLGDRL LLSPGGREVR VRGIQKDGVK AERAQAGERC
     ALNLAGVELS QVQRGDWVLH ADLHAPTSRL DVELQVLPGE AHALAHRTPV HLHLGTRDVT
     ARVTLSHGSS VEPGRRAFAR LIVDQPIAAA RGDRFILRDQ SAQRTLGGGW VLDASPSQRR
     LPQEMRVRQM QALAQPTPVD ALRALVACSP GGVDATALTR NFNLAPEAFT QLLKEAGLAA
     VGTGAQTLVL TPAAADAKLL RKPVQALPEN PEHVRLWQLA EPVLRRAGFA GVTVAQLSEA
     LRAKEFVLRD MLHRKAQAGD TVRVNDDRFY ARATIDEFIR VARTVAQHAP DGRFTAGKFR
     DDAGIGRALA VQVLEALDRI GATQRVADVR VMRSPARSPS SESPLQGART P
//
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