ID A0A7I9VPW7_9BACT Unreviewed; 648 AA.
AC A0A7I9VPW7;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 21.
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:GEJ58454.1};
GN ORFNames=AMYX_31950 {ECO:0000313|EMBL:GEJ58454.1};
OS Anaeromyxobacter diazotrophicus.
OC Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=2590199 {ECO:0000313|EMBL:GEJ58454.1, ECO:0000313|Proteomes:UP000503640};
RN [1] {ECO:0000313|Proteomes:UP000503640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R267 {ECO:0000313|Proteomes:UP000503640};
RA Masuda Y., Yamanaka H., Xu Z.X., Shiratori Y., Aono T., Amachi S.,
RA Senoo K., Itoh H.;
RT "Diazotrophic Anaeromyxobacter Isolates from Soils.";
RL Appl. Environ. Microbiol. 86:e00956-e00920(2020).
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:GEJ58454.1}.
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; BJTG01000008; GEJ58454.1; -; Genomic_DNA.
DR RefSeq; WP_176067028.1; NZ_BJTG01000008.1.
DR AlphaFoldDB; A0A7I9VPW7; -.
DR Proteomes; UP000503640; 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; 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; IPR005225; Small_GTP-bd.
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; 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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000503640}.
FT DOMAIN 1..176
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 648 AA; 67852 MW; E07C12B71745643C CRC64;
MKRIVLGTAG HIDHGKTALV KALTGVDTDR LREEKRRGIT IELGFAHLAL PDGTVAGVVD
VPGHERFVRA MAAGAGGIDL VVLVVAADEG VMPQTREHLD ICRLLGVPRG VVAITKSDLL
PELGADWLPL LEADVRAAAK GTFLEEAALV PVSARTGEGL PALVAEVARL AREVPERPAD
GPLFLPVDRA FSLKGFGTVV TGTLLSGAVA VEDEVVLSPP AQGQGRLRVR SVQVHGQPVQ
RALAGQRTAV NLPGVEAQTI SRGQALVHAG VVPLSHALDV ELTLLAAAPK PLRHRAKLLL
HVGTAQVQAA VSLLDRAELA PGATALAQLR LASPAAALPG QRFILRGFAV LEGRGKTLAG
GRVLAVAVRR RRRGRPAEVE QLEALAKGDV EARLTAVLAS AGPAGLAADA LLGRTGLSPK
ALQGALERLG AKGGAVLFDR EKRAYVAGEV ARGLAARLVE AVKAFHASHP LATGISREEL
RGRLPPVTDA RLFARLLAQL VEKGELVTEA DQVRLPTHRA ASGAAGGALK ATVTAALVKG
GLTPPWLSEL PGLAGAAPEE VAAVLKLLLA EGAAVRVSSE LYYDAGAIHG LRERLVAHLA
VRREITTQEF KELVGATRKH VIPLAEYFDR EKVTLRVGDK RVLRGEGR
//
