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Database: UniProt
Entry: A0A1F8QI03_9CHLR
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ID   A0A1F8QI03_9CHLR        Unreviewed;       645 AA.
AC   A0A1F8QI03;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   ORFNames=A2Z16_11920 {ECO:0000313|EMBL:OGO35030.1};
OS   Chloroflexi bacterium RBG_16_54_18.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797648 {ECO:0000313|EMBL:OGO35030.1, ECO:0000313|Proteomes:UP000177170};
RN   [1] {ECO:0000313|EMBL:OGO35030.1, ECO:0000313|Proteomes:UP000177170}
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:OGO35030.1}.
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DR   EMBL; MGNP01000006; OGO35030.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8QI03; -.
DR   STRING; 1797648.A2Z16_11920; -.
DR   Proteomes; UP000177170; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; IPR015190; Elong_fac_SelB-wing-hlx_typ-2.
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; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF09106; SelB-wing_2; 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; 2.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Elongation factor {ECO:0000313|EMBL:OGO35030.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:OGO35030.1}.
FT   DOMAIN          1..181
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   645 AA;  71569 MW;  FC20B275634EB0CA CRC64;
     MRVIGTAGHV DHGKSTLVQA LTGIHPDRLK EEREREMTID LGFAWLSLPP ADDDSPGEEV
     GIIDVPGHRD FIENMLAGVG GIDAALFVVA ADEGVMPQTR EHLAILDILQ IQGGVVALTK
     VDLLYDPEWL DLVENDLRTV LSGTVLENSP ILRVSSNTMQ GIPELKKALS ASLFTHPLRP
     DLNRPRLPVD RAFSMPGFGT VVTGTLVDGS FQAGDEIEVL PQALRGRIRG LQTHKQKEQI
     AVPGSRTAIN ISGLSLEQIA RGDVVAHPGD YRTTQRLDAV FRLLPASSQP LHHNTEVKLF
     INTSEVLARL RLLGAEEILP GQQGWLQLEM SEPIVCVRGD RYILRRPSPG ETLGGGKIVD
     PHPKRRHKRF SSEVLKRLED LLQGTPEDVL LQALNVSGAA SVKDLVARSN LPSQSAFPAL
     QTLAENGLLI NLDRAAEPDL QEFQPDELLV SKHLWEQLSS QVTQELSAYH IRYPLRTGLP
     REELKSRLKE MLRPSPRLFN AAMRRLEGEG LVRESGPAVS LPGHTLRFTP AQEAQVDRLL
     RRFTDAPYAP PTLKECQLEV GEEVVSALVE QGRLVAVPPD LLFRQEDYDQ MLTELRGLFS
     QHKELTVAQV RDHFNTSRRY ILTWLEYLDS QGITVRSGDA RRLKG
//
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