ID A0A1M7GDQ1_9RHOB Unreviewed; 642 AA.
AC A0A1M7GDQ1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=SAMN05444389_10479 {ECO:0000313|EMBL:SHM14512.1};
OS Paracoccus solventivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=53463 {ECO:0000313|EMBL:SHM14512.1, ECO:0000313|Proteomes:UP000184444};
RN [1] {ECO:0000313|EMBL:SHM14512.1, ECO:0000313|Proteomes:UP000184444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6637 {ECO:0000313|EMBL:SHM14512.1,
RC ECO:0000313|Proteomes:UP000184444};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FRCK01000004; SHM14512.1; -; Genomic_DNA.
DR RefSeq; WP_073065063.1; NZ_FRCK01000004.1.
DR AlphaFoldDB; A0A1M7GDQ1; -.
DR STRING; 53463.SAMN05444389_10479; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000184444; 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 CDD; cd03696; SelB_II; 1.
DR CDD; cd15491; selB_III; 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; 3.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR015190; Elong_fac_SelB-wing-hlx_typ-2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR048931; SelB_WH_3rd.
DR InterPro; IPR015191; SelB_WHD4.
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 PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR Pfam; PF21214; bact_SelB_WH_2nd; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF09106; SelB-wing_2; 1.
DR Pfam; PF09107; SelB-wing_3; 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; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Elongation factor {ECO:0000313|EMBL:SHM14512.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:SHM14512.1}.
FT DOMAIN 1..174
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 642 AA; 68320 MW; 842363621766037F CRC64;
MIVGTAGHID HGKTALVRAL TGTDADRLAE EKSRGITIEL GFAYADLGDG TDGGDVTGFV
DVPGHERFVH TMLAGAGGID LALLVVAADD GVMPQTREHL AILDLLGVHR GIVALSKADL
ADDERRADVT AQIAATLDGT GLAGAPVLPV SSVTGEGIEA LRRALAQAAA ATAARALDRR
FRLSVDRSFA LKGSGTVVTG TVLSGQVSVG DTITVSPRGL AARVRAIHAQ NRPVQTGIAG
QRCALNLAGD GVARDAIHRG DMVLDPALHA PSDRIDATLR VLGSEPHPIG TWFPARLHSG
AAEVGARIVP LAEALMPGAE GLVQLVLDAP LAASVGDRYI LRDVSARRTI GGGVFLDLRA
PARRRRTPER MLQLDAATQP EPEQALRGML AAPPFLADLD AFIRDRALGP EAAARLAAAA
VVLQSGATQV ALSAATHRGL VAGMLDALAR FHEDAPEMQG PGREKLRLGL TPRLPKEAFA
ALLAERIAAG EIVAEGAFLR LPSHIVRLSE DDEALYARIL PELSGELRFR PPRVRDMATA
WDIPEEDVRR VLRMAARQGR VDQIRRDHFY LRTTTAEMVG IIAAVQQDAP DGWVTAAAFR
DRIETGRKLA IEILDFYDRQ GVTLRRGDLR RINPHRADLY GS
//
