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Database: UniProt
Entry: A0A3E0AFL5_9CHLR
LinkDB: A0A3E0AFL5_9CHLR
Original site: A0A3E0AFL5_9CHLR 
ID   A0A3E0AFL5_9CHLR        Unreviewed;       628 AA.
AC   A0A3E0AFL5;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   28-JAN-2026, entry version 28.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   ORFNames=DFR64_0320 {ECO:0000313|EMBL:REG10462.1};
OS   Pelolinea submarina.
OC   Bacteria; Bacillati; Chloroflexota; Anaerolineae; Anaerolineales;
OC   Anaerolineaceae; Pelolinea.
OX   NCBI_TaxID=913107 {ECO:0000313|EMBL:REG10462.1, ECO:0000313|Proteomes:UP000256388};
RN   [1] {ECO:0000313|EMBL:REG10462.1, ECO:0000313|Proteomes:UP000256388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23923 {ECO:0000313|EMBL:REG10462.1,
RC   ECO:0000313|Proteomes:UP000256388};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (AUG-2018) 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:REG10462.1}.
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DR   EMBL; QUMS01000001; REG10462.1; -; Genomic_DNA.
DR   RefSeq; WP_116223644.1; NZ_AP018437.1.
DR   AlphaFoldDB; A0A3E0AFL5; -.
DR   OrthoDB; 9804504at2; -.
DR   Proteomes; UP000256388; 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   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; 2.
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; 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; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Elongation factor {ECO:0000313|EMBL:REG10462.1};
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:UP000256388}.
FT   DOMAIN          1..173
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   628 AA;  70170 MW;  0B1F977C4C3E8BEE CRC64;
     MYVLGTAGHV DHGKSTLVKA LTGIDPDRLK EEKDRQMTID LGFAWYGLPS GNEVGIVDVP
     GHRDFIDNML AGVGGIDAVL LIIAADEGVM PQTREHLAIL KLLKIQYGII VLTKIDLVDD
     PEWLELVEAD IRGLIKGSFL EQAKIMRVSA YTKEGLDELS CEIESILLQC PPKRNSGKPR
     LPIDRVFSLK GFGTVVTGTL LNGEFHSGES VEILPGKRTS RIRSIQSHKR KVDTALPGNR
     TAINLIGVEK EDIKRGQVVV LPGNYSTSRR IDAKVEMLAE ANSSINHNDF LKCFINTAQS
     IARVRVIGKK EIRPGEDGWV QLEFEDEIVV EKGDSFILRR PSPAETIAGG IVLNTHSVKR
     YKRFSDDSLK KMALMDSGSD EDILLSNLDK CGVVSRQEFL KASGFEPGKA NELIDVLVPD
     EIVIIEAAGI RDTLLVSRTN WAILKEKITG IFTDFYQKRP LREGMPRKSL WELLKIPQRS
     FNLILEKLIQ EGLLAEKNGE VGLANYQVHF SEEQEASIQT ILAEFSSNEF QPPSVRAERE
     KYGDDLISAM IDKGYLISLE EDIAILPQTY QQLQAKTIAY FETEKEITLG QFRDLFQTSR
     KYALAFLEYL DKQEVTVRDG DVRKLSAG
//
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