ID A0A0B0I918_9BACI Unreviewed; 637 AA.
AC A0A0B0I918;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 28-JAN-2026, entry version 44.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=LQ50_25530 {ECO:0000313|EMBL:KHF37760.1};
OS Halalkalibacter okhensis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Halalkalibacter.
OX NCBI_TaxID=333138 {ECO:0000313|EMBL:KHF37760.1, ECO:0000313|Proteomes:UP000030832};
RN [1] {ECO:0000313|EMBL:KHF37760.1, ECO:0000313|Proteomes:UP000030832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kh10-101T {ECO:0000313|Proteomes:UP000030832};
RA Prakash J.S.;
RT "Genome sequencing and annotation of Bacillus Okhensis strain Kh10-101T.";
RL Submitted (SEP-2014) 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:KHF37760.1}.
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DR EMBL; JRJU01000075; KHF37760.1; -; Genomic_DNA.
DR RefSeq; WP_034634210.1; NZ_JRJU01000075.1.
DR AlphaFoldDB; A0A0B0I918; -.
DR STRING; 333138.LQ50_25530; -.
DR eggNOG; COG3276; Bacteria.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000030832; 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; 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; 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; 2.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:KHF37760.1};
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:UP000030832}.
FT DOMAIN 1..173
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 637 AA; 72664 MW; BD4228BF694596A1 CRC64;
MNHYTVGMAG HIDHGKTTLT KALTNIETDR LKEEKERSIS IELGYAPLKL TDEMEVSLID
VPGHERFIRQ MIAGVAGIDL VMLVVAADEG VMPQTREHID ILRLLGIENG IIVVTKMTRV
DDEMREIVEL DIREAIEGTF LEKSRLYFVD SLSSMGIDDL KKGIASELQG RPSRDAGGAF
RLPIDQVFTI HGQGTVVRGT VYEGVVNEGD VLDLLPKRIP VRARQLQVHH QSRMNVRAGQ
RVAINVGGVA KEEIKRGDVL VASGHYETTQ TIDVGLMTVE NLLFPLKQRS AIKLHIGTAE
VYGKIVFFDR NELIDGNERI VCQIRLDEPI VTRRGDRFIL RRPTPMETIG GGIVIDPHGE
KYRFGEQTIE MLEQKMDATP IERLQQLLLD HKSLSLKDAS KELNMTEVEM KELVNEGEQT
YQLPTGEITS EKVVRSLKES FQMELERYHK DYPFRIGIKK AEMVQSYTHT YPKRLLEWLL
VEGHKQGWFV ISGPFAALPS HIPHAPKQWE KRVEHVLTSI KNEGLQVTPI AQHLAAQQLP
IVLHEEVNHY LYQQELLYQI DEKLSIHREP FREAVTKLKA ETEEVFTLKE AKDSTGLSRK
YLVPFLEKLD KLGLTIRQEQ ERKWRVDEVE NWLGNKS
//
