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Database: UniProt
Entry: G7QD14_9BACT
LinkDB: G7QD14_9BACT
Original site: G7QD14_9BACT 
ID   G7QD14_9BACT            Unreviewed;       639 AA.
AC   G7QD14;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   28-JAN-2026, entry version 69.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   ORFNames=DFW101_0303 {ECO:0000313|EMBL:EHJ46320.1};
OS   Solidesulfovibrio carbinoliphilus subsp. oakridgensis.
OC   Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia;
OC   Desulfovibrionales; Desulfovibrionaceae; Solidesulfovibrio.
OX   NCBI_TaxID=694327 {ECO:0000313|EMBL:EHJ46320.1, ECO:0000313|Proteomes:UP000004662};
RN   [1] {ECO:0000313|Proteomes:UP000004662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FW-101-2B {ECO:0000313|Proteomes:UP000004662};
RX   PubMed=25767232;
RA   Ramsay B.D., Hwang C., Woo H.L., Carroll S.L., Lucas S., Han J.,
RA   Lapidus A.L., Cheng J.F., Goodwin L.A., Pitluck S., Peters L., Chertkov O.,
RA   Held B., Detter J.C., Han C.S., Tapia R., Land M.L., Hauser L.J.,
RA   Kyrpides N.C., Ivanova N.N., Mikhailova N., Pagani I., Woyke T.,
RA   Arkin A.P., Dehal P., Chivian D., Criddle C.S., Wu W., Chakraborty R.,
RA   Hazen T.C., Fields M.W.;
RT   "High-Quality Draft Genome Sequence of Desulfovibrio carbinoliphilus FW-
RT   101-2B, an Organic Acid-Oxidizing Sulfate-Reducing Bacterium Isolated from
RT   Uranium(VI)-Contaminated Groundwater.";
RL   Genome Announc. 3:0-0(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}.
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DR   EMBL; CM001368; EHJ46320.1; -; Genomic_DNA.
DR   RefSeq; WP_009179767.1; NZ_CM001368.1.
DR   AlphaFoldDB; G7QD14; -.
DR   STRING; 694327.DFW101_0303; -.
DR   eggNOG; COG3276; Bacteria.
DR   HOGENOM; CLU_023030_3_0_7; -.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000004662; Chromosome.
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; 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; ELONGATION FACTOR TU-RELATED; 1.
DR   PANTHER; PTHR43721:SF11; SELENOCYSTEINE-SPECIFIC ELONGATION FACTOR; 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:EHJ46320.1};
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:UP000004662}.
FT   DOMAIN          1..173
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   639 AA;  68882 MW;  D5DEA1B917B9952E CRC64;
     MPVIMGTAGH IDHGKTTLIK ALTGIDCDRL AEEKKRGITI ELGFAFMDLP GGTRLGIIDV
     PGHERFVKNM VAGAAGIDFV TLVIAADEGV MPQTREHLDI CTLLGVTTGV VALTKADMVD
     ADWLAMVTED VRGELAGTFL ADAPIFPVSS HTGAGLPELR EALAALAAGF APRRRSDLAR
     LPIDRVFTLK GYGTVVTGTL IAGSFKVGDD VRLFPSEKRS KIRSLQSHGE TVEASPAGRR
     TAVNLAGLEV EDVERGEVLA LPGTLFPDLS WEVELTCLPG APRGIKHRTE VHFHHGTREV
     LARIHLLDRD KLEPGQTAVC QIRFPEPMAG VHGDRVVVRS GAPLRTMAGG RVLSPMARKV
     KRFDEAALAS LAALATAAGP DLIALHLSRA GTDGLGFARL MTLTDLESKA LDKALSGLCD
     KGAAALVDRE GKEGRHFVHG TVIADLAASL LDAVAAFHKR EPLKLGLSRS ELASTWGKGL
     SPKLFHFVVE RQLRAGKLAT DQDVLRLAGH KVSLASDQAK LRATLLDAYQ KGGLTPPNVK
     DILEPLSLTF KEAQPVYKVL QDEGRIVKAQ ENMYFDAEAI KGLIEKVQAY YQAGAADMGP
     AEFRELTGLS RKFLIALLEY LDKEKITVRV GDKRQLRKR
//
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