ID U5W783_9ACTN Unreviewed; 589 AA.
AC U5W783;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 28-JAN-2026, entry version 58.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=AFR_27945 {ECO:0000313|EMBL:AGZ43850.1};
OS Actinoplanes friuliensis DSM 7358.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ43850.1, ECO:0000313|Proteomes:UP000017746};
RN [1] {ECO:0000313|EMBL:AGZ43850.1, ECO:0000313|Proteomes:UP000017746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ43850.1,
RC ECO:0000313|Proteomes:UP000017746};
RX PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL J. Biotechnol. 178:41-42(2014).
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; CP006272; AGZ43850.1; -; Genomic_DNA.
DR RefSeq; WP_023560187.1; NC_022657.1.
DR AlphaFoldDB; U5W783; -.
DR STRING; 1246995.AFR_27945; -.
DR KEGG; afs:AFR_27945; -.
DR PATRIC; fig|1246995.3.peg.5664; -.
DR eggNOG; COG1510; Bacteria.
DR eggNOG; COG3276; Bacteria.
DR HOGENOM; CLU_023030_1_1_11; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000017746; 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 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; 2.
DR InterPro; IPR057335; Beta-barrel_SelB.
DR InterPro; IPR050055; EF-Tu_GTPase.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015191; SelB_WHD4.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
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 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; PF09107; WHD_3rd_SelB; 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; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:AGZ43850.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000017746}.
FT DOMAIN 1..168
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 589 AA; 61282 MW; D8ED9C72D1783F9D CRC64;
MHVLATAGHV DHGKSTLVRA LTGMEPDRWA EERRRGMTID LGFAWTGLPS GATVAFVDVP
GHERFVPTML AGIGPVPAAM IVVAADEGWR AQSAEHLAAL EAAGVRHGLL VVTRSDLADP
GPATAQARAE IGATPLGDVE AVAVSGVTGA GLDDLRAALD RLVDRLPEPD TGATVRLWID
RSFTIKGAGT VVTGTLGAGT LRPGDELELT GATRPVPVRV RGLQSLGAAT DEVRAVARVA
VNLRGVGKDD AGRGSALLTP GRFRFTDLVD VRVHGDPVAD LPASVTLHVG SAAVPARVRP
LGTDTARLRL GTVLPLRIGD RALIRDPGRH HIAGGVTVLD VVPPGLSRRG AAAARATELA
TMHGVPDAAD ELRRRLLVPR DDLLRMGVDD PGAAVAGRWL ADPGHWRALG ERLSEELAAY
AAENPLEPGA PVEALRHRLG LPDRALVEAL VRPPLVSRGG RISSGAMGVP EDLVLAVDRA
FEGLADRPFT APEANRLTEL GLGGRQLGAA VRAGLVVQLG GTVILRAGAP RQAARVLAGL
PDPFTVSEAR QALGTSRRVA VPLLELLDST GVTRQMPGDR RIVAAAPGD
//
