ID A6TQL3_ALKMQ Unreviewed; 631 AA.
AC A6TQL3;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 28-JAN-2026, entry version 102.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN OrderedLocusNames=Amet_2324 {ECO:0000313|EMBL:ABR48481.1};
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
OC Natronincolaceae; Alkaliphilus.
OX NCBI_TaxID=293826 {ECO:0000313|EMBL:ABR48481.1, ECO:0000313|Proteomes:UP000001572};
RN [1] {ECO:0000313|Proteomes:UP000001572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF {ECO:0000313|Proteomes:UP000001572};
RX PubMed=27811105; DOI=10.1128/genomea.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
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}.
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DR EMBL; CP000724; ABR48481.1; -; Genomic_DNA.
DR RefSeq; WP_012063456.1; NC_009633.1.
DR AlphaFoldDB; A6TQL3; -.
DR STRING; 293826.Amet_2324; -.
DR KEGG; amt:Amet_2324; -.
DR eggNOG; COG3276; Bacteria.
DR HOGENOM; CLU_023030_3_0_9; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000001572; 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; 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; 2.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:ABR48481.1};
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:UP000001572}.
FT DOMAIN 1..174
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 631 AA; 71450 MW; 3343C692A92020F4 CRC64;
MENIVIGTAG HIDHGKTTLI KALTGRETDR LKEEKKRGIS IELGFTYFDL PSGKRAGIID
VPGHEKFIRN MLAGVGGMDI VLLVVAADEG VMPQTKEHLD IISVLNIKKG IIVITKAGLV
DEEWLELVKA DIKERVKDTF LRDADMMAVD SVNQIGIKEL VEKIDHLTNE TGPRDTNSPA
RMPIDRVFTI TGFGTVVTGT LGQGKITVED TMEILPAKQK VRIRNIQVHG KSVKTAYAGQ
RVAINLANVK KEEIERGFIL AQIDSLEATM MIDAKFNMLK DAQRIIKNRD RVRIYHGSAE
VLARVSLLGT DELLPGESSF VQFRLEELTA IKKDDPLVIR LYSPMETLGG AIVIDGNPQK
HKRFDQKVIE DLALREKGTL KEVIEKQVER YSNEYPDISF ISKTMGLQLT EVKEQIQLLE
QEDKVVFLGS GHVLHQKYFG DLKEKSLTLL SSYHEGNPLR KGMLKEELIS RLFTTKFNKV
ADSFLQKLFE AGEIKIYQKY VAMSTFQVKF NEQHQKIRAL LEKAYGEQFY NPPRLEDVTK
QLPFDNEIIN QVIEAIMDEV LIKISSDITL HMDAYKEAKN KLSDHIEKNG KITLSEFRDL
LDTSRKFAVA ILEHFDNHKI TKRLGDTRVL M
//
