ID A0A6V8LLI5_9BACT Unreviewed; 635 AA.
AC A0A6V8LLI5;
DT 10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 1.
DT 28-JAN-2026, entry version 24.
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:GFK93522.1};
GN ORFNames=NNJEOMEG_01356 {ECO:0000313|EMBL:GFK93522.1};
OS Fundidesulfovibrio magnetotacticus.
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia;
OC Desulfovibrionales; Desulfovibrionaceae; Fundidesulfovibrio.
OX NCBI_TaxID=2730080 {ECO:0000313|EMBL:GFK93522.1, ECO:0000313|Proteomes:UP000494245};
RN [1] {ECO:0000313|EMBL:GFK93522.1, ECO:0000313|Proteomes:UP000494245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SIID29052-01 {ECO:0000313|EMBL:GFK93522.1,
RC ECO:0000313|Proteomes:UP000494245};
RG Desulfovibrio sp. FSS-1 genome sequencing consortium;
RA Shimoshige H., Kobayashi H., Maekawa T.;
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GFK93522.1, ECO:0000313|Proteomes:UP000494245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SIID29052-01 {ECO:0000313|EMBL:GFK93522.1,
RC ECO:0000313|Proteomes:UP000494245};
RA Shimoshige H., Kobayashi H., Maekawa T.;
RT "Draft genome sequence of Desulfovibrio sp. strainFSS-1.";
RL Submitted (MAY-2020) 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:GFK93522.1}.
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DR EMBL; BLTE01000005; GFK93522.1; -; Genomic_DNA.
DR RefSeq; WP_173082637.1; NZ_BLTE01000005.1.
DR AlphaFoldDB; A0A6V8LLI5; -.
DR Proteomes; UP000494245; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 FunFam; 3.40.50.300:FF:001064; Selenocysteine-specific translation elongation factor; 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 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; 3.
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:GFK93522.1};
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:UP000494245}.
FT DOMAIN 1..171
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 635 AA; 69226 MW; 9B4C0B1348DAF3BC CRC64;
MALILGTAGH IDHGKTTLVK ALTGTDCDRL AEEKKRGITI ELGFAFLELP GVRLGVVDVP
GHERFVKNMV AGAAGIDFVV LVIAADEGVM PQTREHLEIC TLLGIRHGVV ALTKVDMVDE
DWLGLVTEDV RAFLAGSFLA EAPMVPVSAH TGQGLDELRA ELARLAAEFP GKRRSDLARL
PIDRVFTMKG HGTVVTGTLI SGRLRTGDDV LLYPSMRPTK VRSLQVHGLP AEEGQAGQRT
AVNVMGLEVD DVERGEVLAH PGTLFPSLAW NLEVTCLASS PRALKHRGEV HFHHGTREVM
ARLYFLDRDK LEPGQTALCQ ARFESPLAGV SGDRCVMRSF SPLRTVAGAT ILSPLGGRIK
RNGPELADLA ALPEASAEEL TRLHLKLRGR EGASFPALMT LTGLESRELE RVLQAFSGKG
QACLYDREAR MWLSGEVLES LAAGLLEHVA AYHRREPLKQ GVSRGELASA WGRELPPKLV
HFLVERLLKA GKLSQDQESL RLPGHSVSLG AGQADLRERL LALYEAGGIT PPNYKDVLET
LGASAKEALP VYKLLSEQNL VRRINEDLYF AVSALDGLKA KVAEYFATHA DLGPQDFREL
TGLTRKFAIP LLEFLDKEKV TVRVGDKRLP RVRQG
//
