ID A0A2A6RD54_9CHLR Unreviewed; 620 AA.
AC A0A2A6RD54;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 28-JAN-2026, 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 Name=selB {ECO:0000313|EMBL:PDV98896.1};
GN ORFNames=CJ255_21805 {ECO:0000313|EMBL:PDV98896.1};
OS Candidatus Viridilinea mediisalina.
OC Bacteria; Bacillati; Chloroflexota; Chloroflexia; Chloroflexales;
OC Chloroflexineae; Oscillochloridaceae; Candidatus Viridilinea.
OX NCBI_TaxID=2024553 {ECO:0000313|EMBL:PDV98896.1, ECO:0000313|Proteomes:UP000220527};
RN [1] {ECO:0000313|Proteomes:UP000220527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kir15-3F {ECO:0000313|Proteomes:UP000220527};
RA Grouzdev D.S., Gaisin V.A., Rysina M.S., Gorlenko V.M.;
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:PDV98896.1}.
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DR EMBL; NQWI01000253; PDV98896.1; -; Genomic_DNA.
DR RefSeq; WP_097646176.1; NZ_NQWI01000253.1.
DR AlphaFoldDB; A0A2A6RD54; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000220527; 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 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; 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; 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; 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; 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; 2.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:PDV98896.1};
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:UP000220527}.
FT DOMAIN 1..171
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 620 AA; 66977 MW; 579009C379C8298F CRC64;
MYIIGTAGHV DHGKSTLVKS LTGIDPDRWA EEQRREMTID LGFAWFTLPS GRLVSLVDVP
GHERFIKNML AGVGGFDAAM LVVAADEAVM PQTIEHLAIL DLLEVRHGLV VLTKADLVDA
PWLDLVREEV SERLRGTSLA HAPLVAVSAR SGAGLNELRQ TLDAVLDATP ARSHARGHPR
LPVDRAFTMG GFGTVVTGTL LDGPLALGAE LEILPVGRKA RVRGLQIHGQ KTEVALPGNR
VAVNLAGIHH SEVGRGAVLA PPGALRPTHM LDLHLRVLAD APAPILQNSA LDLFSGASEV
PCRVTLLDAE QLDPGAQGWV QLRLAAPIAL RRGDRCILRV ASPSRTVAGG LVVDTHPARH
RRFRADVLAQ LETLARGEPA DLLLQALACG MPQTYAEAAT RSGLPEAELG PLAAQGVAAG
QIVLLNSQSN DPHMISTGAW EQLCTQLQEH LRAHHQRFPL RRGIPREELR QKLQLNPRSL
SAVLHQAAQQ ALIATNETSV WLQGHNPHPD AAGQHALAAA LEAMARSPYS PPAPKLDGEL
LAWALEQHLF VRVAPEVFFL PATYAELVAW VRQTIINQGS ISLGNIRDHF GSSRKYALAL
LEHLDERKIT RREGEARVLV
//
