ID A0A1I4R4X4_9PSEU Unreviewed; 581 AA.
AC A0A1I4R4X4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=SAMN05421805_101384 {ECO:0000313|EMBL:SFM46973.1};
OS Saccharopolyspora antimicrobica.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=455193 {ECO:0000313|EMBL:SFM46973.1, ECO:0000313|Proteomes:UP000199398};
RN [1] {ECO:0000313|EMBL:SFM46973.1, ECO:0000313|Proteomes:UP000199398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CPCC 201259 {ECO:0000313|EMBL:SFM46973.1,
RC ECO:0000313|Proteomes:UP000199398};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOUP01000001; SFM46973.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4R4X4; -.
DR STRING; 455193.SAMN05421805_101384; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000199398; Unassembled WGS sequence.
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 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; IPR004161; EFTu-like_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015191; SelB_WHD4.
DR InterPro; IPR005225; Small_GTP-bd_dom.
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 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; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF09107; SelB-wing_3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Elongation factor {ECO:0000313|EMBL:SFM46973.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Protein biosynthesis {ECO:0000313|EMBL:SFM46973.1}.
FT DOMAIN 1..169
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 581 AA; 61729 MW; 66FEC0C91C552048 CRC64;
MHVIATAGHV DHGKSTLVRR LTGTDPDRWA EERRRGLTID LGFAWTRLAD GCTAAFVDVP
GHERFVPNML AGIGPVPAVL FVVAADEGWM PQSDEHLDAL DALGVRHGVL AVTRSDLADP
AAATEQAVAR LAGTALAGIP AVQVSGATGA GVDALRGELD ALFHRLPPPD PDADVRLWID
RVFTVRGAGT VVTGTLAAGT LRIGDQLRLH PAGITCTVRG LQALGSPESQ VGAVARVAVN
LRGVDCAQAR RGDALLTPDR WLTTEVFDVR IHPAPTSWPA ELVLHIGSAA TTVRVRPLGP
VHARLTSRLP LPLRIGDRAL LRDPGGHRIH GGLHVLDVRP PALTRRGAAR ARAAELAAMS
TSPDGRAELD RRRVIRADEL RAMGASPPGA GRWLISEEHR AELAARLVEL LARHEQDDPL
AGGMPVEAAR RALDLPDTAL VAEVAATAGI ALRAGQLRHE HPQLPGNVHR AVAAVREALL
DHPFRAPTAA ELAALGLGDR ELAAAARVGE LLRVAPGLVL LPDAEQQAVD RLTPLPEPFT
LSQARQALDT SRRVAVPLLE LLAHRGRTRR LPDGTHRVVP Q
//
