ID A0A160SXX0_9CHLR Unreviewed; 626 AA.
AC A0A160SXX0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 2.
DT 28-JAN-2026, entry version 38.
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:CUS02221.2};
GN ORFNames=CFX0092_A0340 {ECO:0000313|EMBL:CUS02221.2};
OS Candidatus Promineifilum breve.
OC Bacteria; Bacillati; Chloroflexota; Ardenticatenia;
OC Candidatus Promineifilales; Candidatus Promineifilaceae;
OC Candidatus Promineifilum.
OX NCBI_TaxID=1806508 {ECO:0000313|EMBL:CUS02221.2, ECO:0000313|Proteomes:UP000215027};
RN [1] {ECO:0000313|EMBL:CUS02221.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Cfx-K {ECO:0000313|EMBL:CUS02221.2};
RA Mcilroy J.S., Karst M S., Albertsen M.;
RL Submitted (JAN-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; LN890655; CUS02221.2; -; Genomic_DNA.
DR RefSeq; WP_095041863.1; NZ_LN890655.1.
DR AlphaFoldDB; A0A160SXX0; -.
DR KEGG; pbf:CFX0092_A0340; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000215027; Chromosome I.
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:0035368; F:selenocysteine insertion sequence binding; IEA:TreeGrafter.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:TreeGrafter.
DR GO; GO:0001514; P:selenocysteine incorporation; IEA:InterPro.
DR GO; GO:0016259; P:selenocysteine metabolic process; IEA:TreeGrafter.
DR CDD; cd04171; SelB; 1.
DR CDD; cd03696; SelB_II; 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; IPR004161; EFTu-like_2.
DR InterPro; IPR050543; eIF2G.
DR InterPro; IPR015190; Elong_fac_SelB-wing-hlx_typ-2.
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; PTHR42854; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3 FAMILY MEMBER; 1.
DR PANTHER; PTHR42854:SF3; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3-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; 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; 2.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:CUS02221.2};
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:UP000215027}.
FT DOMAIN 1..172
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 626 AA; 68027 MW; 6B5361B8FEFF3CBC CRC64;
MHVIGTAGHV DHGKSTLVQA LTGIDPDRLA EEKAREMTID LGFAWLSLAG EEVGIVDVPG
HRDFIENMLA GIGGIDLVLF VIAADEGIMP QTREHLAIVD LLQIEHGIVA LTKCDLVDDP
DWLDLVTLEI GDALQGTVLA GAPIVPVSAR IGRGLDQLRQ TLAQTLSQLE PKTDRGQARL
PIDRVFTMPG FGTIVTGTLI DGRLRVGDEI EAQPGGLTGR VRGLQTHKVK REVAHPGSRV
AVNLTNISRE ELRRGQVIAP RGFLRPSRLL DVAYRHLPDA DAPLAHNAEV KVFIGAAEVT
AHARLIGQEA LPPGQSGWVQ LALAEPLAVL RGDRFILRRA SPGSTLGGGR VLDANPGRRH
RRFRADVVER FRALEEDAPA ELLLAALLRW GPLPPATLIE KSGLPPAAGR SALQDLIAAG
QVIDLGKTVI AATSWRGLIE RAPQELAEYH RQYPLRLGME REELRARLQV PAVVYVSLCE
IMVGNGEIVE AGAVLRRPDH RITFTPGQQD AITRLMTFLD SRGIMAPSVK ECQAIVDPAT
FLALSDLGRV KAITADVVYA TDLYDQLIDR LTTFLHQQGS ITVAEARDLL GASRKYAIAL
LEHMDERRIT RRASDVRTPA RPLPAP
//