ID A0A0W7YSR0_9BURK Unreviewed; 641 AA.
AC A0A0W7YSR0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 28-JAN-2026, entry version 43.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=AS359_04500 {ECO:0000313|EMBL:KUF37972.1};
OS Comamonas kerstersii.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Comamonadaceae; Comamonas.
OX NCBI_TaxID=225992 {ECO:0000313|EMBL:KUF37972.1, ECO:0000313|Proteomes:UP000053300};
RN [1] {ECO:0000313|EMBL:KUF37972.1, ECO:0000313|Proteomes:UP000053300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12322-1 {ECO:0000313|EMBL:KUF37972.1,
RC ECO:0000313|Proteomes:UP000053300};
RA Ming D., Wang M., Hu S., Zhou Y., Jiang T.;
RT "Complete genome sequence of a multi-drug resistant strain Acidovorax sp.
RT 12322-1.";
RL Submitted (DEC-2015) 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}.
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:KUF37972.1}.
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; LPXH01000041; KUF37972.1; -; Genomic_DNA.
DR RefSeq; WP_058880581.1; NZ_LPXH01000041.1.
DR AlphaFoldDB; A0A0W7YSR0; -.
DR STRING; 225992.B5M06_13015; -.
DR Proteomes; UP000053300; Unassembled WGS sequence.
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; cd03696; SelB_II; 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; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 3.
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; 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 InterPro; IPR048931; WHD_2nd_SelB_bact.
DR NCBIfam; TIGR00475; selB; 1.
DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR PANTHER; PTHR43721:SF11; SELENOCYSTEINE-SPECIFIC ELONGATION FACTOR; 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; PF21214; WHD_2nd_SelB_bact; 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; 3.
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:KUF37972.1};
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:UP000053300}.
FT DOMAIN 1..175
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 641 AA; 70577 MW; 666D005091FE056A CRC64;
MIIGTAGHID HGKTTLVRAL TGVETDRLKE EKARGISIEL GYAYVPLPNG DVMGIIDVPG
HERFVHTMAA GAVGIDHALL VVAADDGVMP QTLEHLEILQ LLGVKKGTVA LTKVDRVLPE
RIADVRAEIE AILSVTALAD SPIFETAASQ PEDPGVAHLR AHLEVQAQMM HARPQDGLFR
LAVDRVFTLP GQGTVVTGTV FNGKVAVGDV LHHSSSGKEV RVRSIHAQNQ AAEAGVAGQR
CALNLAGIAK EDIIRGDWIA DARVLQATDR IDIRMHLLAE APRMQQWTTV HVHIGTQRCT
AHIALLQDEP IEPGTEAVVQ LVLDEPVFAI PGDRLILRNA QATRTIAGGM VLDPYAPARK
RRSAERFAYL QALEQLIATG SPEALIAHSS YGVSLSQLRR LSGHALDALQ LPGVQRIGQT
DEDAILIDAA RWKQLQQQVM DTITHFHEKY PDEPGINAAR LRRMAWPGLI HAQHDRLWRA
LIDQLLAEKH LSSSGAWLHL PGHSVQLTAN EQTLAEQLLP KLQEGRFDPP WVRDLANDTG
TSEELVRQLL RKLARQGQLF QVVKDLFYTA ANMDELARII KTLADATPNG EVMAREFRDA
TGLGRKRAIQ IIECFDRLGY TRRVRDAHIL RPDAQWHSHK T
//