ID A0A1M6LU76_9FIRM Unreviewed; 631 AA.
AC A0A1M6LU76;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 28-JAN-2026, entry version 34.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=SAMN02745883_00347 {ECO:0000313|EMBL:SHJ74719.1};
OS Caminicella sporogenes DSM 14501.
OC Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
OC Caminicellaceae; Caminicella.
OX NCBI_TaxID=1121266 {ECO:0000313|EMBL:SHJ74719.1, ECO:0000313|Proteomes:UP000184082};
RN [1] {ECO:0000313|EMBL:SHJ74719.1, ECO:0000313|Proteomes:UP000184082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14501 {ECO:0000313|EMBL:SHJ74719.1,
RC ECO:0000313|Proteomes:UP000184082};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FRAJ01000003; SHJ74719.1; -; Genomic_DNA.
DR RefSeq; WP_072965649.1; NZ_FRAJ01000003.1.
DR AlphaFoldDB; A0A1M6LU76; -.
DR STRING; 1121266.SAMN02745883_00347; -.
DR Proteomes; UP000184082; 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 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; 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; 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:SHJ74719.1};
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:UP000184082}.
FT DOMAIN 1..172
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 631 AA; 72129 MW; 6096133E0F4FA52E CRC64;
MKNIIIGTAG HIDHGKTTLI KALTGIETDR LKEEKKRGIT IDLGFAFFKL PNGRRAGIVD
VPGHERFIKN MLAGASGIDL VLFVIAADEG VMPQTQEHLD ILSYLDVKKG IIVLTKCDLV
DEEWIKLVAE DIKERVKGTF LEDAPIVEVS SINGKGLDKL KSIIMEMTEE VEEKKCNVPC
RLPIDRIFTL SGFGTVVTGT LIEGVIEEKQ IVHIYPKGLE AKVRSIQVHG ESVNKAYAGQ
RVAVNLTGIK KEDIDRGDVL AAPNSMKSSM IIDVKLNLLK TSNRKVENWN RLRLYHGTKE
VLCRVVLLDR DELYPGESCF AQLRLEEEIS SKYGDKFVVR YYSPLETIGG GVILDPNPPK
HKRFREEIIS ELESKSKGNK ENIIEKIILK FSDKYPDIDF ISIQSGISKN EIENIIDKLV
KDELVIKFSE NTFVHRDYIN NLEEKLIKLL NDYHSKNPLK PGLSKEEVRS RLFSNIKGKL
FDEIINYYSN LGTVKVVNKY ISLKEFNIEL SESQKALKDK ILKIYLENKF KTPTIDEIFK
MLNIQGKDRD IIDLLINMGF LIKISDNIIL HVDNYNYAKN TLKEFLVKNK EITLGQFRDL
LNTSRKYAIP LLEYFDYIKF TKRVEDKRML Q
//
