ID A0A8J3IJI2_9CHLR Unreviewed; 672 AA.
AC A0A8J3IJI2;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=KSF_026320 {ECO:0000313|EMBL:GHO92584.1};
OS Reticulibacter mediterranei.
OC Bacteria; Bacillati; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Reticulibacteraceae; Reticulibacter.
OX NCBI_TaxID=2778369 {ECO:0000313|EMBL:GHO92584.1, ECO:0000313|Proteomes:UP000597444};
RN [1] {ECO:0000313|EMBL:GHO92584.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ID150040 {ECO:0000313|EMBL:GHO92584.1};
RA Yabe S., Wang C.M., Zheng Y., Sakai Y., Cavaletti L., Monciardini P.,
RA Donadio S.;
RT "Taxonomic study of unclassified bacteria belonging to the class
RT Ktedonobacteria.";
RL Submitted (OCT-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:GHO92584.1}.
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DR EMBL; BNJK01000001; GHO92584.1; -; Genomic_DNA.
DR RefSeq; WP_220203407.1; NZ_BNJK01000001.1.
DR AlphaFoldDB; A0A8J3IJI2; -.
DR Proteomes; UP000597444; 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:InterPro.
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; 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; 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; IPR015190; Elong_fac_SelB-wing-hlx_typ-2.
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 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; 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; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000597444}.
FT DOMAIN 1..172
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 672 AA; 74091 MW; 829DAE831AE08EAF CRC64;
MACIGTAGHV DHGKSTLVKA LTGIDPDRLT EEKERGMTID LGFAWLTLPG GREVSIVDVP
GHESFIKNML AGVGGIDAAL LVVAADEGVM PQTREHLAIL DLLGVSRGVV ALTKSDLVDE
EWLELVREEV QEQLQGTTLA DATIIPVSVY QDQKRGLPQL LIQLDRILNE AQERQNIGRP
RLPIDRVFTI TGFGTVVTGT LLDGAFSVGR EVEILPQGIT SRIRGLQTHK QQRDTVFPGN
RVAMNLANVA RTELARGNVV ALPGQLRTTV LLDARIQLLK DAGHSLTHNM QVDFYCGSQE
IPARVRLLDT EELIPGESAW VQLRLSRPAV VARRDRFILR IPSPGMTIGG GEIVDVLPRY
HRRFQPVVLE ALERLMQGSP EELVLAALDR RVPGRGEAKA TASRVGSAKV IHGLVGYELA
DIIKQANMAE DVTLQILETL LSEGRVRKVG GFWFAQHTWD MLADEATQQV GEYHRLYPLR
SGLSKEEWRG RLNLSPRMAN EVLVELQNEG RLAMVVAGGE AGGMRSVQEG ALRTGGLLRL
PDFTPRFTPS QQQLVDHLLQ RFRASPYTPP GRGEVEEMVG VEILNALIEQ RQLFKVGEGI
LFLRETYDEA VKKLVAYVRM HGKMTVAEAR DILGATRKYI LPLLEHMDAL RITKRSGDER
VLGSGASLVD SE
//
