ID A0A1W2D2I5_9FIRM Unreviewed; 626 AA.
AC A0A1W2D2I5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 28-JAN-2026, entry version 32.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=SAMN04488500_11348 {ECO:0000313|EMBL:SMC91680.1};
OS Sporomusa malonica.
OC Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
OC Sporomusaceae; Sporomusa.
OX NCBI_TaxID=112901 {ECO:0000313|EMBL:SMC91680.1, ECO:0000313|Proteomes:UP000192738};
RN [1] {ECO:0000313|EMBL:SMC91680.1, ECO:0000313|Proteomes:UP000192738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5090 {ECO:0000313|EMBL:SMC91680.1,
RC ECO:0000313|Proteomes:UP000192738};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FWXI01000013; SMC91680.1; -; Genomic_DNA.
DR RefSeq; WP_084576697.1; NZ_CP155572.1.
DR AlphaFoldDB; A0A1W2D2I5; -.
DR STRING; 112901.SAMN04488500_11348; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000192738; 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 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:SMC91680.1};
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:UP000192738}.
FT DOMAIN 1..173
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 626 AA; 69357 MW; 4946016F888E2D0A CRC64;
MKYIIIGTAG HVDHGKSAII KALTGTDTDR LKEEKLRGIS IDLGFASLPL GEQLVAGIVD
VPGHERFLKN MLAGTGGIDL AMLVIAADEG VMPQTREHLA MLELYGIKHG LVIINKIDKA
DDEWLELVEG EIREFVSHTF LKDAPFCRVS AQTGAGIEEL RKTMKELADT LPVRDSNAPF
RLWIDRVFTI KGYGIVVTGS VLSGQIKVGD TCRLQPAGTI VRVRGLEWHG DKVNEVIAGQ
RAAINLAGLE MEEISRGMAL SAVCRGEVSQ IWDVVADWQQ EIDSGVRVRL HLGTGEFLGR
MYAFKEASHQ TMRLILEQPL AAGAGDRGII RLYSPQHLLG GITLIAPGRA TRRLTSDRKG
LAEAFTKSDQ SAALYHRVAE SRKLLTREEI RQQSGYLPEK TVDRMVNKLT TDKKLQCLDG
VYLATVMFEK LTLTIKGMLK DYHKAQPERS GLSKEIARQK LALDEKSFEI ILAEWLAGGV
LITNGGELAL KSHADKHGGW KQDIVDKASI ALEDVGLASV DLTLLSQKLN LPPDKAKVTH
DALVRAGVLV KVSDIFVYSK TIQYIVQLIH RYFKENETLT VAELRDILNT SRKIALPLME
YLDMHKYTVR DGDVRRPTRK VLDLSE
//