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Database: UniProt
Entry: W1SDF8_9BACI
LinkDB: W1SDF8_9BACI
Original site: W1SDF8_9BACI 
ID   W1SDF8_9BACI            Unreviewed;       627 AA.
AC   W1SDF8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   ORFNames=BAVI_19334 {ECO:0000313|EMBL:ETI67100.1};
OS   Neobacillus vireti LMG 21834.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX   NCBI_TaxID=1131730 {ECO:0000313|EMBL:ETI67100.1, ECO:0000313|Proteomes:UP000018877};
RN   [1] {ECO:0000313|EMBL:ETI67100.1, ECO:0000313|Proteomes:UP000018877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21834 {ECO:0000313|EMBL:ETI67100.1,
RC   ECO:0000313|Proteomes:UP000018877};
RX   PubMed=24708037; DOI=10.1111/1462-2920.12478;
RA   Mania D., Heylen K., van Spanning R.J., Frostegard A.;
RT   "The nitrate-ammonifying and nosZ-carrying bacterium Bacillus vireti is a
RT   potent source and sink for nitric and nitrous oxide under high nitrate
RT   conditions.";
RL   Environ. Microbiol. 16:3196-3210(2014).
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:ETI67100.1}.
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DR   EMBL; ALAN01000105; ETI67100.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1SDF8; -.
DR   STRING; 220686.AA980_03785; -.
DR   PATRIC; fig|1131730.3.peg.4056; -.
DR   eggNOG; COG3276; Bacteria.
DR   OrthoDB; 9804504at2; -.
DR   Proteomes; UP000018877; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; 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; IPR005225; Small_GTP-bd_dom.
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; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF09106; SelB-wing_2; 1.
DR   Pfam; PF09107; SelB-wing_3; 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   Elongation factor {ECO:0000313|EMBL:ETI67100.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:ETI67100.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018877}.
FT   DOMAIN          3..174
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   627 AA;  71246 MW;  63709B29F9F138C3 CRC64;
     MEKRYFTIGM AGHIDHGKTS LTKALTNVDT DRLKEEKERQ ISIELGFAPL YEDDEIQISV
     IDVPGHERFI RQMIAGVAGI DLVVLVVAAD EGVMPQTREH LDILKFLGVK NGLVAISKID
     RVDEEFIELV KDDIFEELTG TVFEDAPFVL VDSLSNKGIN EIKELIIQTL KDQEMRDVKG
     AFRLPIDQVF TVKGQGTVVR GTVYEGSVEE GQPLKIMPKG LEVRARQIQV HHKPAEKAYA
     GQRTAINLSN VSKEDLERGA VLVSSEHFIV TKTLDVAIRM VEDLEHLVKQ RMPIKLHIGT
     AEVMGRIVFF DRNEIKEENG EVLCQLRLEE EILTKRGDRF ILRRPSPQET IGGGWVIDPR
     GNKYRFGNDT IEELEKKKAG TPKERITAAL IEAKSLPLNE LIKRTALDEA TLMEHLADAE
     FVLYNGKERT LQLLIESLEE DIFDRLQDYH LAHSMKPGVN KAELLQTMQK RFPKSLLDYV
     VENGIANGIF KRKEQFVSLA GFVPNVPKSW AKRTENMLEE LKSDGLMVRY LKDYFSGAGI
     PETLEFDLKR FLEDQELLVQ LDDQFAYHGE VFNGAVDKLR SQTGTEFEVG DAKDVLGLSR
     KYMIPFLEKL DAKGFTKRVE NKRVWKL
//
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