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Database: UniProt
Entry: A0A0S8HNQ5_9DELT
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ID   A0A0S8HNQ5_9DELT        Unreviewed;       635 AA.
AC   A0A0S8HNQ5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, 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=AMJ94_17645 {ECO:0000313|EMBL:KPK86910.1};
OS   Deltaproteobacteria bacterium SM23_61.
OC   Bacteria; Deltaproteobacteria.
OX   NCBI_TaxID=1703399 {ECO:0000313|EMBL:KPK86910.1, ECO:0000313|Proteomes:UP000051218};
RN   [1] {ECO:0000313|EMBL:KPK86910.1, ECO:0000313|Proteomes:UP000051218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_61 {ECO:0000313|EMBL:KPK86910.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPK86910.1}.
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DR   EMBL; LJUR01000217; KPK86910.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8HNQ5; -.
DR   STRING; 1703399.AMJ94_17645; -.
DR   PATRIC; fig|1703399.3.peg.3392; -.
DR   Proteomes; UP000051218; 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; 2.
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; 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; 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; 3.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Elongation factor {ECO:0000313|EMBL:KPK86910.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:KPK86910.1}.
FT   DOMAIN          1..172
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   635 AA;  70540 MW;  87B0D645D9C59C65 CRC64;
     MKRVVLGTAG HIDHGKTTLI KALTGVDCDR LKEEKERGIT IELGFTSMVL PSGLRISIVD
     VPGHEKFVRH MVAGATGMDL VVLIIAADEG IMPQTREHLD ICKLLRVKKG LVALTKIDLA
     EGDWLDLVKE EIREFVKGTF LEGAAILPVS STTGAGIPDL VSELDRLAQA VEERSSEGLF
     RLPIDRVFTM KGFGTVITGT IIAGKISVGD SVEVIPKGLE SKVRGIQAHG EAVESATAGL
     RVGINLQGLE KAVIDRGNVI VRAQSLKPTS LLDVILHLLP SAAKPLKNRA RVRVHVGTVE
     VLGRAILLDQ EEIKPGQEAY LQLRLEEPVT ALPGDRFVIR SYSPVFTIGG GEILDAFPSR
     HKRLSPQIKE EMAVLEKGSE EEKVKLRLLM AGAGGLSWTD LVMRSNQLPS RLKPLVDSLV
     SQGGILRFDG DRLRYLHPRV MADLKRFTLD YLKEFHQKNP LQGGAGKEEL KSKLPHQVDP
     RLFNHLLSIL TEEKKIALEK ETVRLASHTI SLKEEEKDLR KKIVVLFSRT RLQPPTVKET
     LAELGVSENE LKPVLQLLTK EKVLVKVKED LYFHRQALEE LEGKVVDFLK QNKEMTPPQF
     KDLSQVSRKF AIPLLEHFDG KKLTMRIGDK RVLRK
//
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