ID A0A1I7JS69_9BURK Unreviewed; 640 AA.
AC A0A1I7JS69;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JAN-2026, entry version 34.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=SAMN04489707_103012 {ECO:0000313|EMBL:SFU88043.1};
OS Paenacidovorax caeni.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Comamonadaceae; Paenacidovorax.
OX NCBI_TaxID=343013 {ECO:0000313|EMBL:SFU88043.1, ECO:0000313|Proteomes:UP000183656};
RN [1] {ECO:0000313|EMBL:SFU88043.1, ECO:0000313|Proteomes:UP000183656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-24608 {ECO:0000313|EMBL:SFU88043.1,
RC ECO:0000313|Proteomes:UP000183656};
RA de Groot N.N.;
RL Submitted (OCT-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; FPBX01000030; SFU88043.1; -; Genomic_DNA.
DR RefSeq; WP_054256775.1; NZ_CYIG01000024.1.
DR AlphaFoldDB; A0A1I7JS69; -.
DR STRING; 343013.SAMN04489707_103012; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000183656; 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; 1.10.10.2770; -; 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; 1.
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 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:SFU88043.1};
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:UP000183656}.
FT DOMAIN 1..176
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 640 AA; 67733 MW; 3566B2041A761705 CRC64;
MIIGTAGHID HGKTSLVRAL TGVETDRLPE EKRRGISIEL GYAYLHPPGG PSLGFVDVPG
HERLLHTMLA GATGIAHALL IVAADDGVMP QTREHLAVVA LLGVTQGSVA ITKIDRLDPA
TRATRLAEVQ AEVRALLAPT ALAQAPMFPV SAITGEGVEA LRQHLLACAA TCGSASSHDS
ARAFRMPADR VFTLTGVGTV VTGSVTSGVA PVGAELCIAP HGTGARLRGV HAQNQPASEA
RTGQRCALAL AGVAKEDVHR GDWVCAPSIA LATTRIDVQC QLWPDEPKAL RSGTPVHVHL
GTSDVTGSIV LLDSDTLAPG ATALAQLVLH GTVAAWHGDR GVLRDASATR TLAGVRVLDP
FAPQRYRKTA ERLAQLAAQA LPDRATRVAA LLAHAPLGLD LAHTARAEAL PGPGDLPLPP
DAIRLAGEGL AIAPAALQAL QALVLERLRA FHAASPEEIG PDARRLRRLA APRASDALWQ
HVVEDMVAHQ LVVRSSHWLH LPEHAARMNA TEEALAQRIR PLLLAGAFDP PWVRTLAQDL
GAAEALVRQT LASMARRGEA FQVVKDLYYP LPTLERLAAL ARQCMDASDA VQAAAFRDAT
GLGRKRAIQL LEFFDRVGFT RRVKDAHLLR PGTPLFTAQD
//
