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Database: UniProt
Entry: S0FY25_9BACT
LinkDB: S0FY25_9BACT
Original site: S0FY25_9BACT 
ID   S0FY25_9BACT            Unreviewed;       637 AA.
AC   S0FY25;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   28-JAN-2026, entry version 49.
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:EMS79610.1};
GN   ORFNames=Dpo_4c01610 {ECO:0000313|EMBL:EMS79610.1};
OS   Desulfotignum phosphitoxidans DSM 13687.
OC   Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
OC   Desulfobacterales; Desulfobacteraceae; Desulfotignum.
OX   NCBI_TaxID=1286635 {ECO:0000313|EMBL:EMS79610.1, ECO:0000313|Proteomes:UP000014216};
RN   [1] {ECO:0000313|EMBL:EMS79610.1, ECO:0000313|Proteomes:UP000014216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13687 {ECO:0000313|EMBL:EMS79610.1,
RC   ECO:0000313|Proteomes:UP000014216};
RX   PubMed=23704177;
RA   Poehlein A., Daniel R., Simeonova D.D.;
RT   "Draft Genome Sequence of Desulfotignum phosphitoxidans DSM 13687 Strain
RT   FiPS-3.";
RL   Genome Announc. 1:E00227-13(2013).
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:EMS79610.1}.
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DR   EMBL; APJX01000004; EMS79610.1; -; Genomic_DNA.
DR   RefSeq; WP_006965853.1; NZ_APJX01000004.1.
DR   AlphaFoldDB; S0FY25; -.
DR   PATRIC; fig|1286635.3.peg.2196; -.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000014216; 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; 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   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:EMS79610.1};
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:UP000014216}.
FT   DOMAIN          1..173
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   637 AA;  71492 MW;  47CF8C6D8439138E CRC64;
     MENIILGTAG HIDHGKTSLV KALTGIETDR LKEEKQRGIT IELGFAFLDL PGGTHIGIVD
     MPGHEKFVKN MVAGSSGIDV VTMVIAADEG VMPQTREHME ICHLMGIEHG LIALTKTDLV
     DEDLLELALE DIHDFVDGTF LEDQPVIPVS SATGQGLDDF VAALEKICRQ LPERRFSSIF
     RLPVDRVFSM KGFGTVITGT LTSGQIRVGE DIMVYPKRIV SKVRGIQVHS SSMNEAGPGT
     RTAINFQGLD KESVDRGDIL STPDTLIESY MVDAGFHYLK SNAKPAKVRT RVRFHSGTSE
     ILGYMVLLDR DELLPGEDAL VQFRLESPVC CIKDDRYVIR SYSPVKTIGG GAILNPVARK
     YRHMDAAVIQ GLTGLAADDP EQTILFFLSL NGYKGLSFND LRVMTNLSDK KLSTTLQKLL
     AQQAVIQTDK EKQTFVSGAF FDDFKKKVLE KIQHYHTANP LKEGMPTQEL KSKFRYIKDP
     RFFNILFSRL EKENAVIQDK NLVKLTDFKV ALQVDQHQIK EDILRIYRSA GLTPPFFRTV
     CLDLDLDKKT AMDVLQMLID EKQIIKTKDD LYFDAQAMAR LEAELVTFLK NNESITTPEF
     KDMTGISRKF VIPLIEYFDA IHLTIRVGDT RQLRRKS
//
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