ID M1ZFZ2_9FIRM Unreviewed; 638 AA.
AC M1ZFZ2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 28-JAN-2026, entry version 53.
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:SHD77920.1};
GN ORFNames=CUESP1_2576 {ECO:0000313|EMBL:SHD77920.1};
OS [Clostridium] ultunense Esp.
OC Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
OC Tepidimicrobiaceae; Schnuerera.
OX NCBI_TaxID=1288971 {ECO:0000313|EMBL:SHD77920.1, ECO:0000313|Proteomes:UP000245423};
RN [1] {ECO:0000313|EMBL:SHD77920.1, ECO:0000313|Proteomes:UP000245423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Clostridium ultunense strain Esp {ECO:0000313|EMBL:SHD77920.1};
RA Manzoor S.;
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; LT669839; SHD77920.1; -; Genomic_DNA.
DR RefSeq; WP_005582146.1; NZ_LT669839.1.
DR AlphaFoldDB; M1ZFZ2; -.
DR HOGENOM; CLU_023030_3_0_9; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000245423; Chromosome 1.
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; 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; 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; 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:SHD77920.1};
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:UP000245423}.
FT DOMAIN 1..174
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 638 AA; 72794 MW; EC09014DF1CDCC1D CRC64;
MKHIIVGTAG HIDHGKTTLI RALTGRNTDR LKEERDRGIS IELGFTYFDL PSGKRAGIID
VPGHERFVKN MLAGVMGMDI VLLVIAADEG VMPQTSEHLA ILDLLGIEKG FIVLTKSDLA
ESEWLELVKE DIKEQVKGTF LEDSPIIPVS STKKTGIDKV IGLIDELTLE IEDRETDDMP
RLPVDRVFTM AGFGTVVTGT LLSGTLNVGD EIQAFPGNKL ARIRTLQVHD QDTKTAFAGQ
RVAINMAGIK KDEVHRGDVI APKDSMKETL MLDVKVKLIK AMDRSVKNRT RLRLYIGTKE
LLCRIVLLDK EILNPGEEAY AQLRLEEKVV AKRGDRFIIR FYSPMFTIGG GEILEPNPTK
KQPFDEEAIK ELEIKEKGQS IDIIEKIILD KSKYFPTIKE ISTTTAMLEE KVKKDINSLT
ESKKVILFSL TKDFHVIHID YFNKLSERII GELESFHKKY PLRIGMPKEE IRSRFLNNAP
ARVGERFIDL LIEKEFIEQK MESVHRKGFK IEYNDIQLKI KEDIIKILKK KKFIPPKKEE
LIEMTGYDSS QVDEVINSLV NSGEIIKLNE EIYLYKTLYE EGLRLLKGYV QEYKSITVAQ
FRDILNTNRK VALALLEYFD QFKITKRDGD KRLLVEDK
//
