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Entry: A0A562R543_9BACT
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ID   A0A562R543_9BACT        Unreviewed;       643 AA.
AC   A0A562R543;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   28-JAN-2026, entry version 29.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   ORFNames=LZ24_03165 {ECO:0000313|EMBL:TWI64179.1};
OS   Desulfobotulus alkaliphilus.
OC   Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
OC   Desulfobacterales; Desulfobacteraceae; Desulfobotulus.
OX   NCBI_TaxID=622671 {ECO:0000313|EMBL:TWI64179.1, ECO:0000313|Proteomes:UP000318307};
RN   [1] {ECO:0000313|EMBL:TWI64179.1, ECO:0000313|Proteomes:UP000318307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ASO4-4 {ECO:0000313|EMBL:TWI64179.1,
RC   ECO:0000313|Proteomes:UP000318307};
RA   Muyzer G.;
RT   "Genome sequencing of 100 strains of the haloalkaliphilic
RT   chemolithoautotrophic sulfur-oxidizing bacterium Thioalkalivibrio.";
RL   Submitted (JUL-2019) 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:TWI64179.1}.
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DR   EMBL; VLLC01000043; TWI64179.1; -; Genomic_DNA.
DR   RefSeq; WP_144686646.1; NZ_VLLC01000043.1.
DR   AlphaFoldDB; A0A562R543; -.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000318307; 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   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   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:TWI64179.1};
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:UP000318307}.
FT   DOMAIN          1..173
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   643 AA;  71810 MW;  60E83E95CD5670A4 CRC64;
     MKEIILGTAG HIDHGKTSLV RALTGTDTDR LKEEKKRGIT IELGFAALNL PDGRRLGVVD
     VPGHEKFVKN MVAGASGIDI VAMIIAADEG VMPQTREHLE ICSLLGIRHG LVVLTKSDMV
     DEEWLEMVTD DVRDFLSDSF LADAPLIPVS SHTGKGLDTL IQAISDMASL IPDIRNTTVF
     RLPVDRVFTM KGFGTVITGT LVSGSVSVGD TVMVYPELTQ SRVRGLQVHN DSVQTAVCGQ
     RTAVNFQGLD LSEVQRGDVI APPDALKNTF MVDTDFHYLG SNEKPLKNRT KVRFHTGTSE
     ITALTVLLDR DTLEPGEKAP VQFRFDRPMV CVRDDRYVVR SYSPIRTIGG GAILNPVPRK
     HKRFQDNIIE GLSHLSEAGS EEAAAFHLMQ AGFAGASMSD LRLVTNLSEK QLTAVLQKLL
     SSRSILVTDK DAKTYIHADA FQRLCSFATN YLEKYHASYP LREGLSKEEL KSKFPAYIQP
     RLLNQVLNQL VKDEKLSQEG DLVRLSTHKV ALQVDQEALR LKILENYENT GITPPYFREI
     VRTLDKAQAE AAPDVMKILI RENLMVRVKE DFYFHRQALD SLQEKVVAFL LENEEMNPSQ
     FKDICGGIAR KYVIPLMEYF DGIHLTIRIG DTRKLRKQQP RET
//
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