ID A0A9Q7AB62_9BACT Unreviewed; 634 AA.
AC A0A9Q7AB62;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 13.
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:QTX33660.1};
GN ORFNames=KAR29_03295 {ECO:0000313|EMBL:QTX33660.1};
OS Aminithiophilus ramosus.
OC Bacteria; Thermotogati; Synergistota; Synergistia; Synergistales;
OC Aminithiophilaceae; Aminithiophilus.
OX NCBI_TaxID=3029084 {ECO:0000313|EMBL:QTX33660.1, ECO:0000313|Proteomes:UP000671879};
RN [1] {ECO:0000313|Proteomes:UP000671879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J.5.4.2-T.3.5.2 {ECO:0000313|Proteomes:UP000671879};
RA Bunk B., Sproer C., Spring S., Pester M.;
RT "A novel Synergistetes isolate from a pyrite-forming mixed culture.";
RL Submitted (APR-2021) 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; CP072943; QTX33660.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9Q7AB62; -.
DR KEGG; aram:KAR29_03295; -.
DR Proteomes; UP000671879; Chromosome.
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; 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; 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 NCBIfam; TIGR00475; selB; 1.
DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR PANTHER; PTHR43721:SF11; SELENOCYSTEINE-SPECIFIC ELONGATION FACTOR; 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; 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:QTX33660.1};
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:UP000671879}.
FT DOMAIN 3..176
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 634 AA; 69880 MW; 26A49F1227E56074 CRC64;
MRELSLVLGT AGHIDHGKTS LVKALTGIDC DRLSEEKRRG ITIELGFASL ELADGRVVSL
VDVPGHERFI RQMVAGAAGI DAVLFVVAAD EGVMPQTREH LEILSLLGLR RGIVALTKID
VVDDDLLELA RMDVEALLKG TFLEAAPLVP LSSVDGRGID VLKEEIGRLV DQLRPRRSEG
LFFLPIDRAF PISGFGTVVT GTAYSGSIGV GDEVAILPSD VRGKVRGLQV HGKAVDVAGA
GQRVAVNVSG VSVDSFEKGD VLSLSGAFEV TSCLDVRFRL LPSANEPLRH WQRVRLHLGT
CDLLARLSLL DRGEILPGEE AVAQIVTESP LLALSGQPFV VRFYSPLRTV GGGRVLNVYG
HKPRGARARR ERLIWLTELN LRLERNESLL EPFVDRGGFL PFRELLRLLQ VPAAPLIEEI
EGNEEVHLLR AGSDYVLSEK WLKALEAKVG AALKAFHDEE PLLDGMAQDR FFRLLLPGGD
LRPAKALAER LLHRGTVVSG DGLFRLPSFV PGRNDLLAER SEALLRFCRE REIQFPDIAE
ARERLALDEK DFKSLLAALR QKGRLFILAE SFLLSDEVDL RLQARARTIE GDVTLAAVRD
LMGSTRRFVL PLLEFWDSRG VTRRVGDKRV FLKK
//
