ID A0A4Q0VR21_9BACI Unreviewed; 642 AA.
AC A0A4Q0VR21;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 28-JAN-2026, entry version 26.
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:RXI98708.1};
GN ORFNames=DS745_16145 {ECO:0000313|EMBL:RXI98708.1};
OS Anaerobacillus alkaliphilus.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Anaerobacillus.
OX NCBI_TaxID=1548597 {ECO:0000313|EMBL:RXI98708.1, ECO:0000313|Proteomes:UP000290649};
RN [1] {ECO:0000313|EMBL:RXI98708.1, ECO:0000313|Proteomes:UP000290649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B16-10 {ECO:0000313|EMBL:RXI98708.1,
RC ECO:0000313|Proteomes:UP000290649};
RX PubMed=30672727; DOI=.1099/ijsem.0.003128;
RA Borsodi A.K., Aszalos J.M., Bihari P., Nagy I., Schumann P., Sproer C.,
RA Kovacs A.L., Boka K., Dobosy P., Ovari M., Szili-Kovacs T., Toth E.;
RT "Anaerobacillus alkaliphilus sp. nov., a novel alkaliphilic and moderately
RT halophilic bacterium.";
RL Int. J. Syst. Evol. Microbiol. 69:631-637(2019).
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:RXI98708.1}.
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DR EMBL; QOUX01000046; RXI98708.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q0VR21; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000290649; 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; 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; 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:RXI98708.1};
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:UP000290649}.
FT DOMAIN 3..175
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 642 AA; 73137 MW; EDE37A4CE3F19258 CRC64;
MGDRFYTIGM AGHIDHGKTT LTKALTNIDT DRLKEEKERN ISIELGFAPL KLKSDIQVSV
IDVPGHERFI RQMIAGVAGI DLVMLIVGAD EGVMPQTKEH LDILSLLGIK NGIIVVTKID
RVDEELLELV QEDIAMEVAG TFLEEAPFVF VDSISKKGID QLKDVIEEKL SDVPSRDAKG
AFRLPIDQVF TVHGQGTVVR GTIYEGAINE GDILEILPQG LKVRARQLQV HHEKKERGFA
GQRTAINLGG VSKEEVKRGD VLVSTQQYAT TSTIDVSLQT LKGLDHPLKQ RGHIKLHLGT
AEVYGKIVFF DRNELSGEES ETILCQLRLD EPIVTRRGDR FILRRPTPVE TIGGGFVIDP
NGEKYKFGET TIDMLERKKE GTPLERVTDM LKEEKYVSIV KLQKLVDLPE DIVRNAINEL
LEKNNIIEGE QGDFVLSSIY VEIVELIRRD LEEFHEENSL REGKSKAEVL HSLKQNYPAK
LLEFVLSRSE QENQLAKRGQ FIALAEFQPH FPSKWAKRME QVVTELEKQA LQVENWESIV
TKAGLPTQLQ EDLKHYLVRT NKVIPLDEKH YISRTHIKVA VKKLREKTAD EFELQDAKEV
LQLSRKYLVP FMELLDRLRL TTRTETKRKW QHVEYDKWIA TE
//
