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Database: UniProt
Entry: A0A2M8S4H0_9PAST
LinkDB: A0A2M8S4H0_9PAST
Original site: A0A2M8S4H0_9PAST 
ID   A0A2M8S4H0_9PAST        Unreviewed;       619 AA.
AC   A0A2M8S4H0;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   28-JAN-2026, entry version 24.
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:PJG86043.1};
GN   ORFNames=CVP05_02425 {ECO:0000313|EMBL:PJG86043.1};
OS   Conservatibacter flavescens.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pasteurellales; Pasteurellaceae; Conservatibacter.
OX   NCBI_TaxID=28161 {ECO:0000313|EMBL:PJG86043.1, ECO:0000313|Proteomes:UP000229329};
RN   [1] {ECO:0000313|EMBL:PJG86043.1, ECO:0000313|Proteomes:UP000229329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7_4 {ECO:0000313|EMBL:PJG86043.1,
RC   ECO:0000313|Proteomes:UP000229329};
RA   Christensen H.;
RT   "Reclassification of Bisgaard taxon 7 as Conservatibacter flavescens gen.
RT   nov., sp. nov.";
RL   Submitted (NOV-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:PJG86043.1}.
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DR   EMBL; PHHA01000003; PJG86043.1; -; Genomic_DNA.
DR   RefSeq; WP_100287975.1; NZ_PHHA01000003.1.
DR   AlphaFoldDB; A0A2M8S4H0; -.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000229329; Unassembled WGS sequence.
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   FunFam; 1.10.10.10:FF:000350; Selenocysteine-specific translation elongation factor; 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; 2.
DR   InterPro; IPR057335; Beta-barrel_SelB.
DR   InterPro; IPR050055; EF-Tu_GTPase.
DR   InterPro; IPR015190; Elong_fac_SelB-wing-hlx_typ-2.
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; PF09106; WHD_2nd_SelB; 1.
DR   Pfam; PF21214; WHD_2nd_SelB_bact; 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; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Elongation factor {ECO:0000313|EMBL:PJG86043.1};
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:UP000229329}.
FT   DOMAIN          1..167
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   619 AA;  70390 MW;  58B72D54BA3CAB77 CRC64;
     MIIVTSGHVD HGKTALIQAL TGTNTAHLPE EKKRGMTIDL GYAYLPVGDK VLGFIDVPGH
     EKFLANMLAG LGGIRYAMLI VAADEGIKPQ TQEHLTILRL LQIEQIIVVI TKADRAGSTQ
     IDTLEHQLQQ YYPFLDSAKF FITSAQTGQG IEPLRDYLCQ LPNLAQRNKP FRYAIDRVFT
     VKGAGTVVTG TAFSGEVNID DELYLSTGEK VRVKNIHAQN VASKQGLAGQ RLALNISADL
     NRTQIERGDW LLTEEPLVAT DRVTLWLEAE SHLNENQPVH IYHAASRTVG KLNLLTGKSF
     QPYEQGLAEL ILDKPLFLAY GDKLILRSGD AKSVIAGAKV VEIYSPKRHK RSEERLNFLK
     KLVQADTAEQ RIQLYLQQRA IPIKQIAWTE QLNSTQLADI LRQNGDLHYQ DWCFNEEFVG
     QQKMKILTAL SNYHAQHGDQ LGLSKARLYR IAAINQPEKL IYHFIDQMLL QKELEQTRGW
     IHTPDHKIQF SNEEAELWQQ TEQQFIQYQG QALWVRELGN TLAVEESIMR NFLYKAGKLG
     YLTPIVKDRF MLTETIYQYA KLIKKIIAKQ GSISVNQLRD ELNFGRKVTV QLIEYYDRCG
     FLRRKGNQHI LRDGDVFDL
//
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