ID F2NFH0_DESAR Unreviewed; 634 AA.
AC F2NFH0;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 28-JAN-2026, entry version 74.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN OrderedLocusNames=Desac_2265 {ECO:0000313|EMBL:AEB10089.1};
OS Desulfobacca acetoxidans (strain ATCC 700848 / DSM 11109 / ASRB2).
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobaccia;
OC Desulfobaccales; Desulfobaccaceae; Desulfobacca.
OX NCBI_TaxID=880072 {ECO:0000313|EMBL:AEB10089.1, ECO:0000313|Proteomes:UP000000483};
RN [1] {ECO:0000313|EMBL:AEB10089.1, ECO:0000313|Proteomes:UP000000483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700848 / DSM 11109 / ASRB2
RC {ECO:0000313|Proteomes:UP000000483};
RX PubMed=21886866;
RA Goker M., Teshima H., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Huntemann M., Liolios K., Ivanova N., Pagani I., Mavromatis K.,
RA Ovchinikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Brambilla E.M., Rohde M., Spring S., Detter J.C., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of the acetate-degrading sulfate reducer
RT Desulfobacca acetoxidans type strain (ASRB2).";
RL Stand. Genomic Sci. 4:393-401(2011).
RN [2] {ECO:0000313|Proteomes:UP000000483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700848 / DSM 11109 / ASRB2
RC {ECO:0000313|Proteomes:UP000000483};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA Teshima H., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schueler E.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Desulfobacca acetoxidans DSM 11109.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002629; AEB10089.1; -; Genomic_DNA.
DR RefSeq; WP_013707198.1; NC_015388.1.
DR AlphaFoldDB; F2NFH0; -.
DR STRING; 880072.Desac_2265; -.
DR KEGG; dao:Desac_2265; -.
DR eggNOG; COG3276; Bacteria.
DR HOGENOM; CLU_023030_3_0_7; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000000483; 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 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; 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:AEB10089.1};
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:UP000000483}.
FT DOMAIN 1..174
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 634 AA; 70646 MW; FC04DE0950329FCF CRC64;
MHPIILGTAG HIDHGKTSLI KALTGVDTDR LKEEKLRGIT IELGFASLTL PNGQRLGIVD
VPGHERFVRH MLAGATGMDL VALIIAADEG VMPQTREHLE ICQLLKVKRG LVVLTKIDLV
EEEWLELVEE DVRNFLSNTF LEGAPIIRFS AVSGQGTSEL LQTLMALGAV VPPKPVSGIF
RLPIDRVFTI KGFGTVVTGT AISGQLRVSD LVTIYPPQYK AKVRNIQVHD EYVEETLAGF
RTAINLQGID KFELERGMVA ATPDSLRCSL RLDARLEILP STPRPLKNRR EVRLHTGASE
QLATVILLSQ EELAPGESGL VQFRLSKPLA LKPFDRFVIR EVSPVITVGG GHVIHINPPV
HRRLQKDIIK KLELLESCPE AERIASHLEE SAAAGLSRQE LVQLLTLSAA ELTPILEQLQ
KDGRIIAYDT ENNRYALKTV VAALQSQAVQ RLQKFHQTQP LKLGLSKEEL RRRLPENLEV
RLFNYLLVDL EQQKQVAVEK ELVRLAGHQV VLAGEQEELA NRLEVLYEKS GLTPPTLKEA
GTAVQARGSQ LNEIIKLLTG KGLLVKVKED LFFHQSVIAA LKTKLVHYLK EHQEISVPQF
KDLTQTSRKF SIPLMEYFDA ARVTVRVGEN RRLR
//
