ID A0A7S7SIH8_PALFE Unreviewed; 616 AA.
AC A0A7S7SIH8;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 18.
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:QOY85703.1};
GN ORFNames=IRI77_23120 {ECO:0000313|EMBL:QOY85703.1};
OS Paludibaculum fermentans.
OC Bacteria; Pseudomonadati; Acidobacteriota; Terriglobia; Bryobacterales;
OC Bryobacteraceae; Paludibaculum.
OX NCBI_TaxID=1473598 {ECO:0000313|EMBL:QOY85703.1, ECO:0000313|Proteomes:UP000593892};
RN [1] {ECO:0000313|EMBL:QOY85703.1, ECO:0000313|Proteomes:UP000593892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P105 {ECO:0000313|EMBL:QOY85703.1,
RC ECO:0000313|Proteomes:UP000593892};
RA Dedysh S.N., Beletsky A.V., Kulichevskaya I.S., Mardanov A.V., Ravin N.V.;
RT "Complete genome sequence of Paludibaculum fermentans P105T, a
RT facultatively anaerobic acidobacterium capable of dissimilatory Fe(III)
RT reduction.";
RL Submitted (OCT-2020) 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; CP063849; QOY85703.1; -; Genomic_DNA.
DR RefSeq; WP_194447373.1; NZ_CP063849.1.
DR AlphaFoldDB; A0A7S7SIH8; -.
DR KEGG; pfer:IRI77_23120; -.
DR Proteomes; UP000593892; 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; 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; 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; 2.
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:QOY85703.1};
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:UP000593892}.
FT DOMAIN 1..171
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 616 AA; 66390 MW; 04229136CAA19463 CRC64;
MKNIIVGTAG HIDHGKTTLV RALTGIDTDR LEEEKRRGIT IDLGFAHMEH AGIRFGFVDV
PGHERFVKNM LAGAGGIDMV LLVIGADESI KPQTREHFDI CRLLDIRQGL VVLTKSDAVD
EEILELARME AAEFVAGSFL EGAPIVAVSG VTGAGLPALR EAMTAMAART KGRDTTAPFR
LPIDRSFTLK GFGTVVTGTL TAGQLNVEQE VEVHPGGRRL RVRGVQVHGG AVDKAYAGQR
TAVNLAGVEA SELSRGMVLT PPDLFLPTQA LDCSFTLLPG AQALKHRAPI HFHAGTAEVE
AQVRMLRGTE PLQPGSTGFV RLLLNEPLLL LPGDRFIARM FSPVITIGGG VVLDNAPPLR
MKKPLVLDRL ALLEGAPLPV RMSLFAQEDP AGCTVAALAA RVGATPEALH AAAAQAGLVF
VRAAEPRFIA QAALETCAAG LRLALAGFHK QNPLLRGMPR TSASVPAFLL DTLLGSMKDV
VAEEDLLRLG SHRLQLKGEE DEASGRIEAL FRDAGLSVPA VNEVLAKSGV DANRARTLLQ
ILLKDKKLVR ISTDLIYHAE ALIYLKELLT PRKGVRFGVA EFKDWTGVSR KYAIPLLEFL
DRERVTRREG DQRMIL
//
