ID E8MZI8_ANATU Unreviewed; 630 AA.
AC E8MZI8;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 28-JAN-2026, entry version 71.
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:BAJ64536.1};
GN OrderedLocusNames=ANT_25100 {ECO:0000313|EMBL:BAJ64536.1};
OS Anaerolinea thermophila (strain DSM 14523 / JCM 11388 / NBRC 100420 /
OS UNI-1).
OC Bacteria; Bacillati; Chloroflexota; Anaerolineae; Anaerolineales;
OC Anaerolineaceae; Anaerolinea.
OX NCBI_TaxID=926569 {ECO:0000313|EMBL:BAJ64536.1, ECO:0000313|Proteomes:UP000008922};
RN [1] {ECO:0000313|EMBL:BAJ64536.1, ECO:0000313|Proteomes:UP000008922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14523 / JCM 11388 / NBRC 100420 / UNI-1
RC {ECO:0000313|Proteomes:UP000008922};
RA Narita-Yamada S., Kishi E., Watanabe Y., Takasaki K., Ankai A., Oguchi A.,
RA Fukui S., Takahashi M., Yashiro I., Hosoyama A., Sekiguchi Y., Hanada S.,
RA Fujita N.;
RT "Whole genome sequence of Anaerolinea thermophila UNI-1.";
RL Submitted (DEC-2010) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP012029; BAJ64536.1; -; Genomic_DNA.
DR RefSeq; WP_013560891.1; NC_014960.1.
DR AlphaFoldDB; E8MZI8; -.
DR STRING; 926569.ANT_25100; -.
DR KEGG; atm:ANT_25100; -.
DR eggNOG; COG3276; Bacteria.
DR HOGENOM; CLU_023030_3_0_0; -.
DR InParanoid; E8MZI8; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000008922; Chromosome.
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; 3.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:BAJ64536.1};
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:UP000008922}.
FT DOMAIN 1..173
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 630 AA; 70175 MW; 2AFF9061161BA66F CRC64;
MRVIGTAGHV DHGKSTLVAA LTGIHPDRLK EEQEREMTID LGFAWMTLPS GESVGIVDVP
GHRDFIENML AGVGGIDAAL FVVAVDEGIM PQTREHLAIL DLLQIPAGVI ALTKADLAPD
AEWLDWVRAD VQHAVHGTVL ENAPIVPVSA RTGEGLAQLV SALEACLAQQ PPRPDLKRPR
LPIDRVFTIS GFGTIVTGTL LDGSFRVGED VEILPGGLRG RIRGLQTHKT KEQTAVPGSR
TAINISGVNV DEVRRGQVVA HPGTYQPTQV LDVHFRLLPD LSLPLRHSSE VKLFLGSAEV
IARVRLLGKE VLNPGEEGWL QLVLREPVVA VRGDRYILRR PSPAETLGGG EVLDPHPPKL
YRRFDTAVLQ RLQALREGNP EEIVLEALQR AGIAPLKEAL SHTRMSSERL APALQYLLEK
ESVVLLEEGV PSPESDLLAT TREKWQMECD RLQKEMQAFH SRFSLRRGIP REELKSRLKM
PARVFNACLR RWVQEGRLRE EGTSLALPAF KVQFTPQQQM LIDRLLNRFA SAPFTPPSVR
EAQTEVGEEI YQALVESGRL VQVSPDVVFR KEDYDTMLDW VKRHFQHSPT LTVIEFRDAL
NTTRKYALGF LEHLDTIGVT VREGDYRKLR
//
