ID A0A6G8QAB5_9ACTN Unreviewed; 619 AA.
AC A0A6G8QAB5;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
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:QIN83399.1};
GN ORFNames=GBA63_12700 {ECO:0000313|EMBL:QIN83399.1};
OS Rubrobacter tropicus.
OC Bacteria; Bacillati; Actinomycetota; Rubrobacteria; Rubrobacterales;
OC Rubrobacteraceae; Rubrobacter.
OX NCBI_TaxID=2653851 {ECO:0000313|EMBL:QIN83399.1, ECO:0000313|Proteomes:UP000501452};
RN [1] {ECO:0000313|EMBL:QIN83399.1, ECO:0000313|Proteomes:UP000501452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 52909 {ECO:0000313|EMBL:QIN83399.1,
RC ECO:0000313|Proteomes:UP000501452};
RA Chen R.W.;
RT "Rubrobacter sp nov SCSIO 52090 isolated from a deep-sea sediment in the
RT South China Sea.";
RL Submitted (OCT-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; CP045119; QIN83399.1; -; Genomic_DNA.
DR RefSeq; WP_166176647.1; NZ_CP045119.1.
DR AlphaFoldDB; A0A6G8QAB5; -.
DR KEGG; rub:GBA63_12700; -.
DR Proteomes; UP000501452; 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; cd15491; selB_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
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; 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 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; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:QIN83399.1};
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:UP000501452}.
FT DOMAIN 11..173
FT /note="Tr-type G"
FT /evidence="ECO:0000259|Pfam:PF00009"
FT DOMAIN 201..266
FT /note="Translation elongation factor EFTu-like"
FT /evidence="ECO:0000259|Pfam:PF03144"
FT DOMAIN 283..362
FT /note="Selenocysteine-specific elongation factor beta-
FT barrel"
FT /evidence="ECO:0000259|Pfam:PF25461"
FT DOMAIN 567..611
FT /note="Elongation factor SelB fourth winged-helix"
FT /evidence="ECO:0000259|Pfam:PF09107"
SQ SEQUENCE 619 AA; 65589 MW; D64D55784D4113D1 CRC64;
MGEPADGRIA LTIGTAGHVD HGKTTLVRRM TGTDTDRLEE EHRRGISIVP GYAELVLPGG
RRASLVDVPG HERFVKNMVS GATGVDAFLL VVAADDGVMP QTREHLDVLR VLGVERGVVA
LTKTDAVDEE TAELAALDAE DLLESVGISA PVIPASGKTG EGVEELLRAL DGLAAQGHED
HVGGRLARLP VDRVFVLKGI GVVATGTLWS GEIRTGDTLY TSRGHRPRVR SIQNHGHPAE
VAHPGARTAL DLTGIDASQL EAGDVLLSRP IPESRAFDAR LRLLEGARPL AHGARVRLHH
GTRATNARVR LSGTDGLQPG ESAFARLRPE EPLILLPGDR FVLRAMSPQV TIGGGTVLDP
APAGRRPEPG WLEALERGDV SRTIPLVLAR YPARGMSAEE LALAVSVSPK RAQEVSDGAP
EISKVGSVYA SAEAVSAAKD RLHQALRSRA KEHPESPEVS VAEARSAMQL ESPLADALLE
DLAGAEVRVT GTGVSLPGAG EVSAELEEAA RRLLAELDAS GAEPPAPGPS PELRLLLKRD
EAVDLGGGLF ASRDTADLIL EDIKTVCREE GEISLSGLRD RLGTSRRYAQ AWLEFSDASG
VTSRTGDVRV LTRRHRGPM
//
