ID A0A5C1AIP2_9BACT Unreviewed; 643 AA.
AC A0A5C1AIP2;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 28-JAN-2026, entry version 27.
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:QEL18113.1};
GN ORFNames=PX52LOC_05127 {ECO:0000313|EMBL:QEL18113.1};
OS Limnoglobus roseus.
OC Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia; Gemmatales;
OC Gemmataceae; Limnoglobus.
OX NCBI_TaxID=2598579 {ECO:0000313|EMBL:QEL18113.1, ECO:0000313|Proteomes:UP000324974};
RN [1] {ECO:0000313|Proteomes:UP000324974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX52 {ECO:0000313|Proteomes:UP000324974};
RA Kulichevskaya I.S., Naumoff D.G., Miroshnikov K., Ivanova A.,
RA Philippov D.A., Hakobyan A., Rijpstra I.C., Sinninghe Damste J.S.,
RA Liesack W., Dedysh S.N.;
RT "Limnoglobus roseus gen. nov., sp. nov., a novel freshwater planctomycete
RT with a giant genome from the family Gemmataceae.";
RL Submitted (AUG-2019) 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}.
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DR EMBL; CP042425; QEL18113.1; -; Genomic_DNA.
DR RefSeq; WP_149112646.1; NZ_CP042425.1.
DR AlphaFoldDB; A0A5C1AIP2; -.
DR KEGG; lrs:PX52LOC_05127; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000324974; Chromosome.
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:UniProtKB-KW.
DR GO; GO:0001514; P:selenocysteine incorporation; IEA:InterPro.
DR CDD; cd04171; SelB; 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; 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; PF09107; WHD_3rd_SelB; 1.
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:QEL18113.1};
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:UP000324974}.
FT DOMAIN 1..173
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 643 AA; 69807 MW; F03379E08572DC69 CRC64;
MRDLILGTAG HIDHGKTALV KALTGIDCDR LPEEKRRGIT IDIGFAQLSL GGFDLGVVDV
PGHEKFVKNM LAGATGIDLA LLVVAADDAV MPQTREHLAI LNALGVERGV IALTKADLVD
DTARELAILD VRELVRGSFL QDAPIIPTSA VAGTGVRELK AAIAAACEKL PPRPDAGWFR
LAIDRSFVVQ GHGTVVTGSA TAGSVRVGDE LDWHKGDGTS ERVRVRGLNR HNQSTDELHR
GQRAALNLAG VPHDAVQRGQ ELATPGILVP SKVLTVRLQN LTLPERPLKH RLPVRLHVGT
ADVPATLSLL DTNLVRPGEW VFAQLFLDES VTAVWGQPFV LRDSSAEHTL GGGQVLQPTG
KKLRRRHVES LERVEQLATD EPLHRTTAAA WFAGFQGFEA NDLVRMAALP CSEIEPTILK
LLADDALVEM TLGLNRKHFL HRDRVRELGE LILDVLRDLH AAHPLHTNHA RPMVLARLDY
VGNESLVQAV TDRMIGSKQI VGDSKRIARA DFKPRLSVNQ RKLKDKIVDD HRRGGCSPPD
PASFANAAGG NAGALKEIFE VAVAEGHLVR IAADFFLHAD EEAKARQVVA DGLRTSEGLT
LAEIRDLLGT TRKYAVPLCE YLDRAGVTRR QGDLRMLAGQ TAE
//
