ID A0A0P6XQZ5_9CHLR Unreviewed; 636 AA.
AC A0A0P6XQZ5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=ADM99_01365 {ECO:0000313|EMBL:KPL74753.1};
OS Leptolinea tardivitalis.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Leptolinea.
OX NCBI_TaxID=229920 {ECO:0000313|EMBL:KPL74753.1, ECO:0000313|Proteomes:UP000050430};
RN [1] {ECO:0000313|EMBL:KPL74753.1, ECO:0000313|Proteomes:UP000050430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YMTK-2 {ECO:0000313|EMBL:KPL74753.1,
RC ECO:0000313|Proteomes:UP000050430};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Genome sequence of Leptolinea tardivitalis DSM 16556.";
RL Submitted (JUL-2015) 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:KPL74753.1}.
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DR EMBL; LGCK01000002; KPL74753.1; -; Genomic_DNA.
DR RefSeq; WP_062423232.1; NZ_LGCK01000002.1.
DR AlphaFoldDB; A0A0P6XQZ5; -.
DR STRING; 229920.ADM99_01365; -.
DR PATRIC; fig|229920.5.peg.3087; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000050430; 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:InterPro.
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; IPR004161; EFTu-like_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015191; SelB_WHD4.
DR InterPro; IPR005225; Small_GTP-bd_dom.
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; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 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; 2.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000050430}.
FT DOMAIN 1..173
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 636 AA; 71507 MW; D0F74D9717743ADA CRC64;
MKVIGTAGHV DHGKSTLVSV LTGMDPDRLK EEKTRQMTID LGFAWMNLPS GETIGFVDVP
GHIDFVDNMI SGVGGIDAVV LVIAADEGVM PQTREHLEIL DLLAINYGVI ALTKCDLVTD
NEWLEIVTED IRKSVKNTFL ESSPIIPISA KTKAGIPELI EAIENVISGI KNRRDISRPR
LSVDRVFTIK GFGTVVTGTL MDGMLHTGDE ICILPKGIIS RIRGLQSLKR NVDQVFPGSR
VAINIQGIDA STVERGDMIT GGQASRPSKR IDAHVTVLSE SLKSLKHNDQ VKVHLFAASR
MGRIRLLGAE EINPGSEGYI QIEFSDPIPV EIGDRIILRN PSLSLTIGGG EIMRVDVPQK
YKRFDENNLK TLARIFHGTL DEKILGIADQ NFIFSTKDLY ARIPESPEII RIEIERLIDS
RKIIDLLSKE TNFDKKAFIT TENWTEFRKK MMNLLDGYHT KNPMSDGISK IELQQSLKIN
KDLLEILLNH ALYLKLIIKK NEHLQLPNYS IQFSADQIGK IEELFKIWDQ RPYKPPDEME
ITEVVGKKVF NALVADGKII RVSTDIYFRD SEIEKMTNFV IQTISKKNEI TVAEFRDYFK
STRKYALAFL EYLDRSGVTL RDGDVRRLGK INKLPG
//
