ID A0A494X778_9BURK Unreviewed; 650 AA.
AC A0A494X778;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, 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 Name=selB {ECO:0000313|EMBL:RKP46575.1};
GN ORFNames=D7S86_24035 {ECO:0000313|EMBL:RKP46575.1};
OS Pararobbsia silviterrae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Pararobbsia.
OX NCBI_TaxID=1792498 {ECO:0000313|EMBL:RKP46575.1, ECO:0000313|Proteomes:UP000270342};
RN [1] {ECO:0000313|EMBL:RKP46575.1, ECO:0000313|Proteomes:UP000270342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHC34 {ECO:0000313|EMBL:RKP46575.1,
RC ECO:0000313|Proteomes:UP000270342};
RA Gao Z.-H., Qiu L.-H.;
RT "Robbsia sp. DHC34, isolated from soil.";
RL Submitted (OCT-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RKP46575.1}.
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DR EMBL; RBZU01000014; RKP46575.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A494X778; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000270342; 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; IPR031157; G_TR_CS.
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; 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; 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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Elongation factor {ECO:0000313|EMBL:RKP46575.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:RKP46575.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000270342}.
FT DOMAIN 1..171
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 650 AA; 70226 MW; 615A9429F8FA53A1 CRC64;
MIVGTAGHID HGKTTLVRAL TGVDTDRLKE EKARGISIEL GYAYAPLENG DVLGFIDVPG
HERFIHTMAA GACGIDHALI VVAADDGVMP QTREHLAILE LLGVTQGFVA LTKIDRVDDA
RCDAVRHEIA ALLAPTPFAH APVFAVQATA PGDPGVAALD RALRARATES RARRDDALFR
LAIDRVFTLA GHGTIVTGTV FSGSVRVGDT LRLVPDGAAV RVRGIHAQNR AAEHGHAGQR
CALNLASIDK DRMRRGDAMV DDRLAALSAR VDTDLSLLGD AASPLTHWSP VHVHIGTLHA
LAHVALLDDA PLAPGKTARA QLVFETPVCV VPGMRFVIRN AQASATIGGG RVLDPFGPAR
KRRGAQRRVW LDAIAAWLDA QRIEPLLDAS PFGLPSRLAS HLTGRAVERL ALPPGVRLVS
DADERVLILG GHWDALAERV LAALRAFHTR APDEIGPDAA RLRRIVAQTW PDGVWRALLD
ALAQAGGIRR SGPWLHLPDH VPALDDAERT QGDDVLARVR AGRFDPPWVR EIGTASGLGE
DRARRIMQRL AQRAELHQIV RDLFYDPAAI AELAALARSV ATSPGDRVTA AAFRDATGLG
RKRAIQVLEF FDRLGYTRFH RDAHWIRAPR GVHPFEQPER AQAAQPSFRS
//
