ID A0AA35G8D1_9FIRM Unreviewed; 632 AA.
AC A0AA35G8D1;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=caldi_02390 {ECO:0000313|EMBL:BDG59149.1};
OS Caldinitratiruptor microaerophilus.
OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
OC Symbiobacteriaceae; Caldinitratiruptor.
OX NCBI_TaxID=671077 {ECO:0000313|EMBL:BDG59149.1, ECO:0000313|Proteomes:UP001163687};
RN [1] {ECO:0000313|EMBL:BDG59149.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 16183 {ECO:0000313|EMBL:BDG59149.1};
RA Mukaiyama R., Nishiyama T., Ueda K.;
RT "Complete genome sequence of Caldinitratiruptor microaerophilus.";
RL Submitted (MAR-2022) 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; AP025628; BDG59149.1; -; Genomic_DNA.
DR RefSeq; WP_264843264.1; NZ_AP025628.1.
DR AlphaFoldDB; A0AA35G8D1; -.
DR KEGG; cmic:caldi_02390; -.
DR Proteomes; UP001163687; Chromosome.
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 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; IPR031157; G_TR_CS.
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; 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; 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:BDG59149.1};
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:UP001163687}.
FT DOMAIN 1..174
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 632 AA; 69084 MW; 5E81FB5C728FE639 CRC64;
MKHLIIGTAG HVDHGKTALI RALTGQDTDR LPEEKARGIS IDLGFAQFRL PSGRRASIID
VPGHERFIRN MLAGITGIDL VLLVVAADEG VMPQTREHLD ILQLLGIKQG VVVLTKVDLV
DAELLDLVRE DVAAAVKGTF LEGAPVVPVS SVTGEGLDRL VQIVDGLLEV TEPKDVTSFA
RMPVDQAFVR PGFGTVVRGT LVSGRIRTGD RLELLPQGLE VRVRGLQVHG EKVEVAEAGQ
RVGVNLSGVE RAEVRRGDVL AEPGVLRPTD TFAGRLHLLA SVPRPLRHGA RVHLHTGASE
VTGRVLLLDR DELEPGDSAF IQFRSEAPLV VGRGDRFIIR SYSPVHTIGG GGVIEPHARY
RRHHAPHLEE LRAKETGGRT GVIAETLARR GPVPLAEAEL ARLIGAPADV LAPDLRALEE
AGEILALEGG YWVHRRGYAA FVEAARSALE AFYRQWPLRP GLPKEELRRK AVPQADARAF
AAVLGRAVAA GELVLDRDRV LLPGREVRLT PAQESLARSL EAAVRAAGFS PPSVAELRDR
FPDALTEELI LHLQEEGRVV RLPGDLILHA DHLREARERT RQFLRTHPTL TVADFRDLLG
TTRKYALPIL DHFDTQRWTR RTGDERVAGP LL
//
