ID A0A975BIN0_9BACT Unreviewed; 636 AA.
AC A0A975BIN0;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 16.
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:QTA86043.1};
GN ORFNames=dnm_020610 {ECO:0000313|EMBL:QTA86043.1};
OS Desulfonema magnum.
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
OC Desulfobacterales; Desulfococcaceae; Desulfonema.
OX NCBI_TaxID=45655 {ECO:0000313|EMBL:QTA86043.1, ECO:0000313|Proteomes:UP000663722};
RN [1] {ECO:0000313|EMBL:QTA86043.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=4be13 {ECO:0000313|EMBL:QTA86043.1};
RX PubMed=33611323; DOI=10.1159/000513383;
RA Schnaars V., Wohlbrand L., Scheve S., Hinrichs C., Reinhardt R., Rabus R.;
RT "Proteogenomic Insights into the Physiology of Marine, Sulfate-Reducing,
RT Filamentous Desulfonema limicola and Desulfonema magnum.";
RL Microb. Physiol. 0:1-20(2021).
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 ---------------------------------------------------------------------------
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; CP061800; QTA86043.1; -; Genomic_DNA.
DR RefSeq; WP_207681848.1; NZ_CP061800.1.
DR AlphaFoldDB; A0A975BIN0; -.
DR KEGG; dmm:dnm_020610; -.
DR Proteomes; UP000663722; 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 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; 4.
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; IPR031157; G_TR_CS.
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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:QTA86043.1};
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:UP000663722}.
FT DOMAIN 1..173
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 636 AA; 70773 MW; A122A52FF60695D9 CRC64;
MKQIILGTAG HIDHGKTSLI KAVTGTNTDR LKEEQQRGIT IELGFASLDL PGGQHLGIVD
VPGHEKFVKN MVAGASGIDL VAMVIAADEG VMPQTREHME ICNLLGVKHG LVVLTKTDLV
DEEWLELVQE DISSFVEGTF LEDKPVVPVS SATGEGISEF VNILDDMSAM IPTRSSTGLF
RLPVDRVFTM KGFGTVITGT LISGRVRVGD TIMIYPSCIT SKVRGLQVHN QSVNEAEAGM
RTAINFQGLE KTAVTRGEVL SNPDALIPSY MLDMSLHFLP SNKKAIKNRT RVRFHAGTSE
VLGNLILIDR EELEPGETLV AQLRLDTPVA VVKDDKFVIR SYSPVRTIGG GHIINPIPPK
HKRFRPEVIE GLQQLVDSPP EEIIAYHIDH SGYKGVSFSE LKIMTNLPEK QLDKTLQELL
SKRTVIRTDK EKQICIHHNS FEKLKKEIHN YLDGYHKTNP LKVGMSKEEL KSKFPAVVGP
KLLNLMLNQM IKDKEIVPEE DIIRLSTHEV SLGVDQADVK EKILEAYVKG GLTPPYFKEL
GKTLSLDAVR AKDVLMILVG EGKIIKAKED LYFHTDAINE LKTKVTDFFL AHEEMTTPDF
KTIASVSRKY LIPLLEYFDS KNITIRVGDV RKLRSR
//
