ID A0A0B5FUJ0_9BACT Unreviewed; 638 AA.
AC A0A0B5FUJ0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 28-JAN-2026, entry version 46.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=GSUB_12890 {ECO:0000313|EMBL:AJF07276.1};
OS Geoalkalibacter subterraneus.
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfuromonadia;
OC Desulfuromonadales; Geoalkalibacteraceae; Geoalkalibacter.
OX NCBI_TaxID=483547 {ECO:0000313|EMBL:AJF07276.1, ECO:0000313|Proteomes:UP000035036};
RN [1] {ECO:0000313|EMBL:AJF07276.1, ECO:0000313|Proteomes:UP000035036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red1 {ECO:0000313|EMBL:AJF07276.1,
RC ECO:0000313|Proteomes:UP000035036};
RX PubMed=25767222;
RA Badalamenti J.P., Krajmalnik-Brown R., Torres C.I., Bond D.R.;
RT "Genomes of Geoalkalibacter ferrihydriticus Z-0531T and Geoalkalibacter
RT subterraneus Red1T, Two Haloalkaliphilic Metal-Reducing
RT Deltaproteobacteria.";
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; CP010311; AJF07276.1; -; Genomic_DNA.
DR RefSeq; WP_040201142.1; NZ_CP010311.1.
DR AlphaFoldDB; A0A0B5FUJ0; -.
DR STRING; 483547.GSUB_12890; -.
DR KEGG; gsb:GSUB_12890; -.
DR HOGENOM; CLU_023030_3_0_7; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000035036; 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 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; 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:AJF07276.1};
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:UP000035036}.
FT DOMAIN 5..181
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 638 AA; 71105 MW; 65F80331BC1098DD CRC64;
MSKTEHHVII GTAGHVDHGK TALIGALTGV ETDRLTEEKK RGISIDLGFA PFRLPGGMIA
GVVDVPGHEK FISNMLTGIG GIDLVLLVVD VNEGVMPQTR EHLQILDLLQ IPQGIIVLTK
CDLAEEDWID IVEEEVREEV SGTFLEKAPV ARVSAITGDG LDGLASLIET KARTLPIKDA
DGPMRLPIDR HFTLSGFGTV ITGTLLSGRV RAGDMVEVLP PGDTVRVREV QVHGKQVEEA
SAGQRVALNL AGLDRERIRR GAVVGTPKVF EQTTCIDARL TLLADAPRPL KFRDPVHLYL
GTARVVGLVA LLDRDLMEPG ESAIVQIHLD RPLVAHREDR FIVRSYSPMT TIGGGRVLDP
RPVKHRRFRT EIMEALKDLE SGEKSFLLQK LSDQQSTTVK NLELLSGLGR ERVEKNLRQL
EEEGLAWQLV DQWAASDALA SWRHRLRDAT TRFHSENPLQ PGIPHATLKG ALPDKVSSKA
FQKLLTMIID DGQLVRKGEW IALSDWTPQP TRQQAEDLEK IEAAYQRGGA LVKNRNEMIE
RLNLTPEQAD TYFTFLFAEG RLVKLTEETY LHAETYQNAV QLLRDHFAQN ETLTLAQFRD
LFGSARKQVQ ALLEHFDSLK YTRRVGDERV AWKLPEKD
//
