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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//