ID A0A1P8FAK0_9CHLR Unreviewed; 626 AA.
AC A0A1P8FAK0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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 ORFNames=Dform_02180 {ECO:0000313|EMBL:APV45483.1};
OS Dehalogenimonas formicexedens.
OC Bacteria; Bacillati; Chloroflexota; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalogenimonas.
OX NCBI_TaxID=1839801 {ECO:0000313|EMBL:APV45483.1, ECO:0000313|Proteomes:UP000185934};
RN [1] {ECO:0000313|Proteomes:UP000185934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSZ-14 {ECO:0000313|Proteomes:UP000185934};
RA Key T.A., Bowman K.S., Lee I., Chun J., Albuquerque L., da Costa M.S.,
RA Rainey F.A., Moe W.M.;
RT "Dehalogenimonas formicexedens sp. nov., a chlorinated alkane respiring
RT bacterium isolated from contaminated groundwater.";
RL Submitted (NOV-2016) 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; CP018258; APV45483.1; -; Genomic_DNA.
DR RefSeq; WP_076004973.1; NZ_CP018258.1.
DR AlphaFoldDB; A0A1P8FAK0; -.
DR STRING; 1839801.Dform_02180; -.
DR KEGG; dfo:Dform_02180; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000185934; 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 CDD; cd03696; SelB_II; 1.
DR CDD; cd15491; selB_III; 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; 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 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:APV45483.1};
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:UP000185934}.
FT DOMAIN 1..172
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 626 AA; 68399 MW; 7F835C3056162809 CRC64;
MLTLGTAGHI DHGKSSIVKA LTSIDPDRLP EEKERGMTID LGFAWFALPS GERVGLVDVP
GHQHFVRNVI PGLTGIDAVM LIVAADDGWM PQTEEHRQII DLLGINRGLV VLNKIDIAEA
DWREMVRADI VAHLAGTSLN NVPIIEVSAK TGAGIDSLKA AIEKLAAEVR QEDIKKPRLP
IDRVFNIKGT GTVITGTLHH GSLSVGDEIT ILPENLTSHV RAIESYKQHL TQAMPGSRVA
LNLSGIKKDE LERGDLIVKK GQETPVSRYL DAELKILPSV KQPLKTGAEV SLFFETAELP
ARVIALGGKE LNQGGPSMVQ LRLDREVSTL IGERFILRKS SPAETIGGGR ILDPTAERYQ
LKNAAQKLEI LNIRRNLDID SAVITELSKT QFASRQGFLR ETAFSDTAIG KSIEGLAKKG
SLAARGLWLI DRKYWSDTQL RFLGILAAAH QAEPLNKGLA QAEAAAKLAL PPELFAALVD
ELIGQKKIIR SEDVVALSSH KPMLSGGQSE MENRIIATIE KNPQAPPTRT ELLQSMNGAA
TVLRYLLEQG KVVELPEGIL LSAAQYRSTR QKIIDILKSK GQIAIQDMAA ITGFSRKYSI
PFLTRLDQEG LTKRQDNVRI PARKLE
//
