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Database: UniProt
Entry: A0A1G0QJY3_9BACT
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ID   A0A1G0QJY3_9BACT        Unreviewed;       665 AA.
AC   A0A1G0QJY3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, 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   ORFNames=A2080_15985 {ECO:0000313|EMBL:OGU48179.1};
OS   Ignavibacteria bacterium GWC2_36_12.
OC   Bacteria; Ignavibacteriota; Ignavibacteria.
OX   NCBI_TaxID=1798427 {ECO:0000313|EMBL:OGU48179.1, ECO:0000313|Proteomes:UP000178676};
RN   [1] {ECO:0000313|EMBL:OGU48179.1, ECO:0000313|Proteomes:UP000178676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGU48179.1}.
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DR   EMBL; MGZZ01000189; OGU48179.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G0QJY3; -.
DR   STRING; 1798427.A2080_15985; -.
DR   Proteomes; UP000178676; 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   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; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015191; SelB_WHD4.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
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; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF09107; SelB-wing_3; 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; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Elongation factor {ECO:0000313|EMBL:OGU48179.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:OGU48179.1}.
FT   DOMAIN          7..178
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   665 AA;  74954 MW;  5931516301A52BD4 CRC64;
     MKDEKIKTHF ILGTAGHVDH GKTALIKALS GIDCDTHPEE KIRGITINLG FAHIDFPSGI
     SIGIVDVPGH KDFINTMISG ACGIDFVMLV IAADSGVMPQ TLEHLHIMQM FGIKSGIVVV
     TKADLADEEM LMIVEEDINE LLKNTFLQDC PVFKVSSKTG EGIGELRDYL SQLNLAGTGG
     SEDGAFRMFI DRIFSVSGFG TVVTGSVLSG SLKVEDKIYL QPGEKELRVK RLEKHGKEVQ
     EVSAGNRAAI NLSGLKKEEF RRGMVLCDRI INPTQMIDAR IKIISNSKKI NLWSNVIFLS
     GTYESQARVH LIDADNLKCG ESALAQIHLD QLFIARAGDK FIIRNSSGDM TLGGGEIIDP
     HPLHHRRRTE KLVSQLKSIS GGRLTEVIAA EVRKNRLPVT LECIVLNLNI PLSEITDFFA
     GTLPDDITYY NSQEDDTVYL MSSDLVNRVK QRIIKSIENY HKRNPLDEEG KTFEELMGVF
     GVNRNPSVEG FMKCLLDNMI KDDMLKKSAD TWIVKTHTVK LTDEDKKHIK FVEVFHKNYA
     MNTPLMSELI PKAYKFGITE EKLNQIILYL VRQGRLYNID NNYLCKDIVD NCRKILLEFL
     IDDNGITVAQ FRDLVKGNRK ICLLLLAQYD REGIIFRDGD LRFLTDKGRN WYKQRYEEFV
     TKSVF
//
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