ID A0A1J5N166_9BACT Unreviewed; 635 AA.
AC A0A1J5N166;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 28-JAN-2026, entry version 37.
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:OIQ52010.1};
GN ORFNames=BerOc1_00480 {ECO:0000313|EMBL:OIQ52010.1};
OS Pseudodesulfovibrio hydrargyri.
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia;
OC Desulfovibrionales; Desulfovibrionaceae.
OX NCBI_TaxID=2125990 {ECO:0000313|EMBL:OIQ52010.1, ECO:0000313|Proteomes:UP000181901};
RN [1] {ECO:0000313|EMBL:OIQ52010.1, ECO:0000313|Proteomes:UP000181901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BerOc1 {ECO:0000313|EMBL:OIQ52010.1,
RC ECO:0000313|Proteomes:UP000181901};
RA Goni Urriza M., Gassie C., Bouchez O., Klopp C., Ranchou-Peyruse A.,
RA Remy G.;
RT "Genome of Desulfovibrio dechloracetivorans BerOc1, a mercury methylating
RT strain isolated from highly hydrocarbons and metals contaminated coastal
RT sediments.";
RL Submitted (SEP-2015) 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:OIQ52010.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LKAQ01000001; OIQ52010.1; -; Genomic_DNA.
DR RefSeq; WP_071544113.1; NZ_LKAQ01000001.1.
DR AlphaFoldDB; A0A1J5N166; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000181901; 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 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; 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; 3.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:OIQ52010.1};
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:UP000181901}.
FT DOMAIN 1..173
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 635 AA; 69936 MW; 61FC8FC7236522AF CRC64;
MPVIMGTAGH IDHGKTTLIK ALTGIDCDRL SEEKKRGITI ELGFAFLDLG EENRLGIVDV
PGHEKFVKNM VAGAAGVDFV VLAIAADEGI MPQTREHLEI CQLLGVTTGL VALTKTDMVD
AEWLEMVKEE VAAYLEPTFL GGAPVLPVSA HTGQGLDELK EALRKLVAEF KPRRRSDLFR
LPVDRVFTMK GHGTVVTGTM ISGDLSVGED VILYPGTATS KVRGLQSHGK TVETAQAGRR
TAVNLAGLEV DEVRRGDVLA RPGSLFPSDV WDIELTVLES SRLPLKHRKE IHFHHGAREV
LARIHLLDRD ELAPGETAVC QARFTEPMAG VWGDRIVLRS FSPLRAFAGG RLIGPSGHRV
KRFSKDVERL GRLASDRPEE VAAAQLELAG PKGVNFAELL TMTNLETKGL EKTLGVLGGQ
QRAVLFDKET RRYAGGETAE RLSSELLEFL AAYHRRESMK PGVQRGELAS SWGRDLPPKL
LHFLLERLLK KGDVVAEQEV VRLKDHKVSL ASDQEKVRET ILSAYTEGGA MPPNLKDVLE
PLGMDAKQAG PVLRLMQDQG ELTRVKDDMY YHAPALAGIR DAVVGFFDGR DEMSAPDFKE
LTGLSRKYLI PVLEYFDKEK LTVRVGDVRR LRKRS
//
