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Database: UniProt
Entry: Q72ER9_NITV2
LinkDB: Q72ER9_NITV2
Original site: Q72ER9_NITV2 
ID   Q72ER9_NITV2            Unreviewed;       642 AA.
AC   Q72ER9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   28-JAN-2026, entry version 142.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   Name=selB {ECO:0000313|EMBL:AAS94982.1};
GN   OrderedLocusNames=DVU_0500 {ECO:0000313|EMBL:AAS94982.1};
OS   Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 /
OS   NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris).
OC   Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia;
OC   Desulfovibrionales; Desulfovibrionaceae; Nitratidesulfovibrio.
OX   NCBI_TaxID=882 {ECO:0000313|EMBL:AAS94982.1, ECO:0000313|Proteomes:UP000002194};
RN   [1] {ECO:0000313|EMBL:AAS94982.1, ECO:0000313|Proteomes:UP000002194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough
RC   {ECO:0000313|Proteomes:UP000002194};
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N., Methe B., Brinkac L.M., Daugherty S.C.,
RA   Deboy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C.,
RA   Sullivan S.A., Fouts D., Haft D.H., Selengut J., Peterson J.D.,
RA   Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G., Hance M.,
RA   Tran K., Khouri H., Gill J., Utterback T.R., Feldblyum T.V., Wall J.D.,
RA   Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
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}.
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DR   EMBL; AE017285; AAS94982.1; -; Genomic_DNA.
DR   RefSeq; WP_010937806.1; NC_002937.3.
DR   AlphaFoldDB; Q72ER9; -.
DR   SMR; Q72ER9; -.
DR   STRING; 882.DVU_0500; -.
DR   PaxDb; 882-DVU_0500; -.
DR   EnsemblBacteria; AAS94982; AAS94982; DVU_0500.
DR   KEGG; dvu:DVU_0500; -.
DR   PATRIC; fig|882.5.peg.477; -.
DR   eggNOG; COG3276; Bacteria.
DR   HOGENOM; CLU_023030_3_0_7; -.
DR   OrthoDB; 9803139at2; -.
DR   PhylomeDB; Q72ER9; -.
DR   Proteomes; UP000002194; Chromosome.
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   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; 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   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; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Elongation factor {ECO:0000313|EMBL:AAS94982.1};
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:UP000002194}.
FT   DOMAIN          1..173
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   642 AA;  69951 MW;  D2538A565179385A CRC64;
     MPVIMGTAGH IDHGKTSLVR ALTGIDCDRL DEEKRRGITI ELGFAFCDLP GGGRLGVVDV
     PGHEKFVRNM VAGASGVDFV MLVIAADEGV MPQTREHLEI CSLLGIRHGL VALTKVDMVD
     ADWLELAQDD VAGFLAGTFL EGAPIFPVSA VTGQGLDTLR EHLATLEREL RPERRTDLFR
     LPVDRVFTMR GHGTVVTGTM ISGSLKVGDD VVLYPEGRTS KVRGLQSHGG PVDKALAGRR
     TAVNLQGVDV AEVQRGEVLA LPGTLFPAQR WDVRLTCLSS AARPLRNRTE VHFHHGAREV
     LARLHFHDRD RLNPGETALC QVRFTEPMVG VFGDRCVVRT FSPLRTVAGG VVVNPTGHDL
     RRRDPHFADK VALLASLPEA TEEELVQAHV DLSGNAGAGF VRLSVLTDLE SKRLEKVLQA
     LGARGRLFCF DREERAYVGA DALQALSAGC LDHAGAFHAK EPLKPGMARG VLASGWGRGL
     HPRLIHFVVE RLIKQGALVA EGDVLRLPGH KVSLASDQEG LRGKLLAIYS EAGMTPPNLK
     DVLETLSLEQ KEAAPVLKLL HDGGELVRVK DGLLFHRSAL DELKGRVARW FDDHDDLDPS
     GFKELSGGLS RKYIIPLLEY FDRERVTIRV GDKRQLRGAK AG
//
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