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Database: UniProt
Entry: A0A2K1Q366_9GAMM
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Original site: A0A2K1Q366_9GAMM 
ID   A0A2K1Q366_9GAMM        Unreviewed;       643 AA.
AC   A0A2K1Q366;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   28-JAN-2026, entry version 26.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   ORFNames=Lysil_1118 {ECO:0000313|EMBL:PNS09489.1};
OS   Solilutibacter silvestris.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Lysobacterales; Lysobacteraceae; Solilutibacter.
OX   NCBI_TaxID=1645665 {ECO:0000313|EMBL:PNS09489.1, ECO:0000313|Proteomes:UP000236220};
RN   [1] {ECO:0000313|EMBL:PNS09489.1, ECO:0000313|Proteomes:UP000236220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM20-91 {ECO:0000313|EMBL:PNS09489.1,
RC   ECO:0000313|Proteomes:UP000236220};
RA   Zhang D.-C., Albuquerque L., Franca L., Froufe H.J.C., Barroso C., Egas C.,
RA   Da Costa M., Margesin R.;
RT   "Lysobacter sylvestris genome.";
RL   Submitted (AUG-2017) 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:PNS09489.1}.
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DR   EMBL; NPZB01000001; PNS09489.1; -; Genomic_DNA.
DR   RefSeq; WP_103074535.1; NZ_NPZB01000001.1.
DR   AlphaFoldDB; A0A2K1Q366; -.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000236220; 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; 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; IPR057335; Beta-barrel_SelB.
DR   InterPro; IPR050055; EF-Tu_GTPase.
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   InterPro; IPR048931; WHD_2nd_SelB_bact.
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; PF09106; WHD_2nd_SelB; 1.
DR   Pfam; PF21214; WHD_2nd_SelB_bact; 1.
DR   Pfam; PF09107; WHD_3rd_SelB; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Elongation factor {ECO:0000313|EMBL:PNS09489.1};
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:UP000236220}.
FT   DOMAIN          1..177
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   643 AA;  69931 MW;  AAEDD5123340CF2A CRC64;
     MIVGTAGHID HGKTSLVRAL TGIDTDRLKE EKARGISIEL GYAYVPIEAD TAEDSATILG
     FVDVPGHERF VHTMVAGATG IDFALLVIAA DDGVMPQTRE HLAILELLGV RHGAIALTKV
     DRVDQQRVAD VEAEIATLLA KSPLRESLLF ACNSTSTDDP GITALRDHLH AVAASPRHDA
     GNDLRDELFR MPVDRVFTLP GHGTMVTGAI HGGQIETSAT PRLMPAGTTV RVRSIHAQNR
     ASARAVAGQR CALNLAAIAC EDIARGDWIA DPRAFVATTR VDVRLRLSVD APPLRNWTPL
     HIHWGTMDRL AHAVVLDDGD GERGALVQLV FAAPVCAMCG DRFIARDSGA NTTIGGGIVL
     DPNPPQRRRR SPARLAWLSA LEQLAAGDGI APLLQEAPTG VAMSALVRYC RRPAERIALP
     EDMLRIATRD DTFIILATHW QALRAKVVVA VSEWHVRHPD EPGIDSGRLQ RSTLPNLAPG
     LWQALLHDLQ ANGTLQRLGA WWCLPGHDSA PPEHERALLQ RLVPLLHAGG FDPPWVRTLA
     TQTGEDEEKT RGILRRAAAR GELFQVVPDL FYDPRRIAEL AATLAALVQD GGATDAAAFR
     DAIGLGRKRS IQILEFFNRV GYTRRVGDTH RPRDDMRWNA NQT
//
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