ID A0A517E0E1_9FIRM Unreviewed; 626 AA.
AC A0A517E0E1;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 28-JAN-2026, entry version 28.
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:QDR83071.1};
GN ORFNames=SPTER_45430 {ECO:0000313|EMBL:QDR83071.1};
OS Sporomusa termitida.
OC Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
OC Sporomusaceae; Sporomusa.
OX NCBI_TaxID=2377 {ECO:0000313|EMBL:QDR83071.1, ECO:0000313|Proteomes:UP000320776};
RN [1] {ECO:0000313|EMBL:QDR83071.1, ECO:0000313|Proteomes:UP000320776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4440 {ECO:0000313|EMBL:QDR83071.1,
RC ECO:0000313|Proteomes:UP000320776};
RA Poehlein A., Daniel R.;
RT "Closed genome of Sporomusa termitida DSM 4440.";
RL Submitted (FEB-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}.
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DR EMBL; CP036259; QDR83071.1; -; Genomic_DNA.
DR RefSeq; WP_144352389.1; NZ_CP036259.1.
DR AlphaFoldDB; A0A517E0E1; -.
DR KEGG; sted:SPTER_45430; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000320776; Chromosome.
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 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; 2.
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:QDR83071.1};
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:UP000320776}.
FT DOMAIN 1..172
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 626 AA; 68619 MW; A841CA6379961F26 CRC64;
MKCVIIGTAG HVDHGKSAVI RALTGTDTDR LKEEKLRGIS IDLGFAALPL RAELVAGIVD
VPGHERFLKN MLAGTGGIDL VLLVIAADEG VMPQTREHLA MLELYGIKQG IIVVNKIDKA
DNEWLELIES DIREFIEPTF LKNAPLCRVS ALTGEGIAEL GEKLAEIAGR LTARDCNAPF
RLWLDRVFSI KGHGLVVTGS VLSGQAQVGD TLRLYPSGQL IRVRGLEWHG AKVNGIVAGQ
RAAVNLAGPE LEQISRGMIL SAVERGEVSQ IWDVAADWLQ AVESGLRVRL HLGTGEFLGR
IYAFKGASHR LMRLILEQPL AAGSGDRGII RLYSPQHLLG GVTLIAPGRA TRRLTASRTA
LAAAVSTADL SAAVYYRLAE SPLLLTRAEI RQQSGYLSDK TVDEIIDKLT AQARIHCLDG
TYIAAEIFDQ QTRAITGILK EYHKTQPERS GLSKEIIRQK LQLAEKSFET LLAVWLRKGM
VAITGGDLAL KSHADKHGDW KQELVGQAAV FLENIGLENV SPALLAQKLL LPADKSKAAH
DILTRAGVLI KVNDIFVYRK TIQYIVQLIH KHFQGHETLT VSELRDILNT SRKIAVPVME
YLDVNKYTVR IGDVRYPSRK ILDLSE
//
