ID A0A1B7XH90_9BACT Unreviewed; 641 AA.
AC A0A1B7XH90;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 28-JAN-2026, entry version 35.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=SP90_05275 {ECO:0000313|EMBL:OBQ54890.1};
OS Halodesulfovibrio spirochaetisodalis.
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia;
OC Desulfovibrionales; Desulfovibrionaceae; Halodesulfovibrio.
OX NCBI_TaxID=1560234 {ECO:0000313|EMBL:OBQ54890.1, ECO:0000313|Proteomes:UP000091979};
RN [1] {ECO:0000313|EMBL:OBQ54890.1, ECO:0000313|Proteomes:UP000091979}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC271 {ECO:0000313|EMBL:OBQ54890.1,
RC ECO:0000313|Proteomes:UP000091979};
RA Shivani Y., Subhash Y., Sasikala C., Ramana C.V.;
RT "Desulfovibrio sp. JC271 draft genome sequence.";
RL Submitted (JAN-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:OBQ54890.1}.
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DR EMBL; JXMS01000006; OBQ54890.1; -; Genomic_DNA.
DR RefSeq; WP_066853314.1; NZ_JXMS01000006.1.
DR AlphaFoldDB; A0A1B7XH90; -.
DR STRING; 1560234.SP90_05275; -.
DR PATRIC; fig|1560234.3.peg.3021; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000091979; 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; 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; 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:OBQ54890.1};
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:UP000091979}.
FT DOMAIN 1..173
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 641 AA; 71111 MW; D925FE77044BF693 CRC64;
MPVVMGTAGH IDHGKTTLVK TLTGIDCDRL EEEKKRGITI ELGFAFFDLP DGGKMGIVDV
PGHEKFVKNM VAGASGIDFV MLVIAADEGV MPQTREHLEI CSLLGIPTGF VALTKTDMVD
EEWLELVQED VKAFLQGSFL EDAPIFPVSS HTGEGLDTVR AHIAKLEKEL TPQRRSDLFR
MPVDRSFTMK GHGTVVTGTM VSGSLNVGDE VRFYPHDMTG KVRGLQSHGS AVEQAPAGKR
TAINIAGVEV AEVHRGDVLA RPETLFPSDT WHIELTCLSS SPSPLKNRTE IHFHHGARDV
LARLYFPDRD KLMPGDTAIC EVRFTEPMVG VANDRCVIRS FSPLRTVAGG KLLHPEAERL
RKKNPHYDVI WNSLQELPKA EPEDRVRLHL AMAAEKGLSF ARLCIFTDIE TKKLDKILNL
FGGKQEALCF DKEERLYIAG NILTELSESC IEFMAAFHKN EPMKAGLSRG MLASGWGKEL
SPKLVHFLVE RLIKAKSIVI DGDVLRLPAH KVSMAADQEG LRKVILEAYE KGGITPPNLK
EVLEPLEVEV KEAVPVLKLM EDAGEMVKVK DTLYYHAPSL EKVKDMVREY LSSHDDMGPA
ELRDLTGLSR KYAIPLLEYF DRVRLTMRIG DKRQLRGSGG A
//
