ID A0A511W202_9BACI Unreviewed; 626 AA.
AC A0A511W202;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=AHA02nite_07930 {ECO:0000313|EMBL:GEN45017.1};
OS Alkalibacillus haloalkaliphilus.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Alkalibacillus.
OX NCBI_TaxID=94136 {ECO:0000313|EMBL:GEN45017.1, ECO:0000313|Proteomes:UP000321440};
RN [1] {ECO:0000313|EMBL:GEN45017.1, ECO:0000313|Proteomes:UP000321440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 103110 {ECO:0000313|EMBL:GEN45017.1,
RC ECO:0000313|Proteomes:UP000321440};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Alkalibacillus haloalkaliphilus NBRC
RT 103110.";
RL Submitted (JUL-2019) 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:GEN45017.1}.
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DR EMBL; BJYA01000002; GEN45017.1; -; Genomic_DNA.
DR RefSeq; WP_170235963.1; NZ_BJYA01000002.1.
DR AlphaFoldDB; A0A511W202; -.
DR Proteomes; UP000321440; 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; 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:GEN45017.1};
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:UP000321440}.
FT DOMAIN 3..175
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 626 AA; 71306 MW; 9A3242279BECD240 CRC64;
MTKSNYTIGM AGHIDHGKSE LTKALTGVET DRLKEEQERK ISIELGYAPL YADQEYSLSI
IDVPGHEKFI RQMIAGVSGV DHTLLIIAAD EGVMPQTVEH IEILNYLEIN RAYIVITKVD
LVEEELLQLV KDDINHHIKN TIFENVPIYC VDSISGNGID LLKTDLITAL KRMPEKDHSG
FFRMPVDQAF HVHGIGTVVR GTIVEGSISE REQIAVKPQD INTEAKSLQQ FGQTVSEARA
GTRTAIALKG VDYHSVKRGD VLTTNSHEAS NRIDLKLHIS PNLNKAIKQR SPIKFHTGTS
EVHGRIILFD RNEIESANEE VYAQVELDHT VYATRHDFFI LRRATPMETI GGGRIINAPA
KRHRFGTNTV KLLKQQSELT IDEAIIEYIE GNGVVKKKEV VNELAIDPTE GHERLNTLYE
LDKIYFINDL IMTRNWLNQY VQLLNTELTN YHNHFSLRQG YPKAEFVQLL PIKAKTGKVI
VDHLVEEGHF RQINNNIALP SFSPFIDDAL KQDVELGLTK LQQDALHVEK FSNYFPTIGQ
DTILDLQHYL TNTNQIVQLS EELIVSHETF HNALDQLRKE TTDQFTLKEA KDVLSLSRKY
LIPLLEKLDE FEYTKRLDNA RQWNNQ
//
