ID A0A348AHP7_9FIRM Unreviewed; 626 AA.
AC A0A348AHP7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 28-JAN-2026, entry version 29.
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:BBB90595.1};
GN ORFNames=MAMMFC1_01249 {ECO:0000313|EMBL:BBB90595.1};
OS Methylomusa anaerophila.
OC Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
OC Sporomusaceae; Methylomusa.
OX NCBI_TaxID=1930071 {ECO:0000313|EMBL:BBB90595.1, ECO:0000313|Proteomes:UP000276437};
RN [1] {ECO:0000313|EMBL:BBB90595.1, ECO:0000313|Proteomes:UP000276437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMFC1 {ECO:0000313|EMBL:BBB90595.1,
RC ECO:0000313|Proteomes:UP000276437};
RX PubMed=29458677; DOI=10.1099/ijsem.0.002635;
RA Amano N., Yamamuro A., Miyahara M., Kouzuma A., Abe T., Watanabe K.;
RT "Methylomusa anaerophila gen. nov., sp. nov., an anaerobic methanol-
RT utilizing bacterium isolated from a microbial fuel cell.";
RL Int. J. Syst. Evol. Microbiol. 68:1118-1122(2018).
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; AP018449; BBB90595.1; -; Genomic_DNA.
DR RefSeq; WP_126307398.1; NZ_AP018449.1.
DR AlphaFoldDB; A0A348AHP7; -.
DR KEGG; mana:MAMMFC1_01249; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000276437; 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 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:BBB90595.1};
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:UP000276437}.
FT DOMAIN 1..173
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 626 AA; 68722 MW; BD54D5A74CD7A173 CRC64;
MKYMIIGTAG HVDHGKSAII KALTGTDTDR LKEEKLRGIS IDLGFASLNL GDDMIAGIVD
VPGHERFLKN MLAGSGGIDL VMLVIAADEG IMPQTREHLA MLQLLGIRQG VVVINKIDKV
DEEWLELIES ETRGFLAGTF LEAAKYIHVS AITGAGLDTL KNTLAQLAKT VPARNGSAPF
RLWIDRVFTV KGYGVVVTGS VLSGSAKSGD TMILYPAGKL VRVRGFESHG RKTEVIYAGQ
RAAINISGVD MEEIFRGMAL SSPERGEISN LWDITVEWLQ EVASGTRVRL HLGTGEFLGR
VYQYKDTSNK YMRLILEAPL AASLGDKGIL RLYSPQYLLG GATLLAPGKA SRKFGPELAE
LEQAIAAGNT EGMIWGRLAG AHKIQGVEDI RRQAGYLTDI TVAAAVAGLE KDEKLVNLKE
GYIARPVLEQ MTKQMLAVLK EYHRSQPDRG GMGKDILRQK LKLDEKTFER LLEYWHAHSG
IIMTGGDIAL AAHAAKHGDW KQDLTAKAEA ALAGIGLTDI DILLLGEKLA LPFEKAKAAH
EILTRAGILI KVGDMFVYRK TIQYIAQLIQ KHFQVYSTLS VAELRDMLNT SRKVAVPLME
YFDMHKYTIR DGDLRHATRK ILDLSE
//
