ID A0A2T6C9G2_9BACL Unreviewed; 632 AA.
AC A0A2T6C9G2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=C8P63_101162 {ECO:0000313|EMBL:PTX64941.1};
OS Melghirimyces profundicolus.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
OC Thermoactinomycetaceae; Melghirimyces.
OX NCBI_TaxID=1242148 {ECO:0000313|EMBL:PTX64941.1, ECO:0000313|Proteomes:UP000244240};
RN [1] {ECO:0000313|EMBL:PTX64941.1, ECO:0000313|Proteomes:UP000244240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45787 {ECO:0000313|EMBL:PTX64941.1,
RC ECO:0000313|Proteomes:UP000244240};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (APR-2018) 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:PTX64941.1}.
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DR EMBL; QBKR01000001; PTX64941.1; -; Genomic_DNA.
DR RefSeq; WP_108021426.1; NZ_QBKR01000001.1.
DR AlphaFoldDB; A0A2T6C9G2; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000244240; 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 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; 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; 2.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:PTX64941.1};
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:UP000244240}.
FT DOMAIN 3..174
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 632 AA; 70073 MW; FA9D757DB269FCB8 CRC64;
MDEKHYVLGT AGHIDHGKTR LTRALTGVDT DRLQEEKERN ISIEPGFAPL TLPSGRRLSI
VDVPGHERFI RQMVSGVTGI DFVLLVVAAD DGVMPQTREH LSILNLLGIR EGLIVLSKID
RADPELLPII EEDVRDTAKG TFLENAPLIR TSAVTGEGIQ EILDTLDQKL PHLEERKSDA
PFRLPVDRAF TVKGAGAVVT GTVQSGSVTP GTDLLVQPEG FPVKVRQIQV HGQTVPIAQA
GQRAALNLSG IDHRNLARGQ TIIKPEAWNP TWRMDIRAIS LHDLSFSVRQ RSRVKVLIGT
AEVFADLIFY DRKEWKPGEE VYASLILEEP VVAGRGDRFI LRRPTPATTL GGGEVVEPRA
PKRKIRSSAA ETIRQLHFSP LPQRILEMLK HALLLDAVDI ARSAGESVDA VSTELEALNR
EGSALKLGDR YASAEALGVL EKQLKDGLKE YHENHPMYDG IPKAEWASRF LPSLSSKDAN
TLLEHWEEAG WIHLKGDSVA LASFVPSLPK RLKPKAQSLL ERLRREGLSP SEWSLLSAEA
DLDPEEGEDL RGYLIRQKKL VPLTADLLIH RDSFDGAAAA VKRIIHQNGT LTMQQAKKEF
SLSRKYLIPL LERMDQEGIT RRKGNERVLT KS
//
