ID A0A2A7UWL8_COMTR Unreviewed; 640 AA.
AC A0A2A7UWL8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 28-JAN-2026, entry version 32.
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:PEH89581.1};
GN ORFNames=CRM82_14110 {ECO:0000313|EMBL:PEH89581.1};
OS Comamonas terrigena.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Comamonadaceae; Comamonas.
OX NCBI_TaxID=32013 {ECO:0000313|EMBL:PEH89581.1, ECO:0000313|Proteomes:UP000220246};
RN [1] {ECO:0000313|Proteomes:UP000220246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_394 {ECO:0000313|Proteomes:UP000220246};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (SEP-2017) 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:PEH89581.1}.
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DR EMBL; PDEA01000001; PEH89581.1; -; Genomic_DNA.
DR RefSeq; WP_066532430.1; NZ_PDEA01000001.1.
DR AlphaFoldDB; A0A2A7UWL8; -.
DR STRING; 1219032.GCA_001515545_00176; -.
DR GeneID; 80801754; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000220246; 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: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; 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:PEH89581.1};
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:UP000220246}.
FT DOMAIN 1..173
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 640 AA; 69095 MW; D977933C2D700C95 CRC64;
MIIGTAGHID HGKTTLVRAL TGVETDRLKE EKARGISIEL GYAYSPLPNG DVLGIIDVPG
HEKFVHTMAA GAVGIDHALL VVAADDGVMP QTIEHLEILQ LLGVKHGTVA LTKVDRVLPE
RLDDVRAEIQ AILSVTALAG SPIFATHAVQ ADDPGVAALR DHLQVQAQLM PARAQDGLFR
LAVDRVFTLP GQGTVVTGTV FNGRVNVGDQ LLHSATAQSV RVRSIHAQNQ ASDTGVAGQR
CALNLAGIAK EDIQRGDWIL DGRLLQATDR IDIRLHLLAE APPLAQWTPV HVHMGTHKGT
AHVALLQDQP IEPGTEVRAQ LVLDAPVFAL PGDRLILRNA QATRTIAGGM VVDPYAPARK
RRSAERTAYL DALEQLVATA SPAALIAQAP HGLPLSQLTR LTGRALDGAA LPGTLRLPMA
DGDALLLDAA RWQPLRARVL DTLERFHAKN PDEPGINAAR LRRMALPGLV HNQHDALWAG
LVEALLQDGS ITASGAWLHL PGHSVQLTAA EQTLSEQLLP LLHAGRYDPP WVRDLAADTG
TGEDAVRQLL RKLARQGQLF QVVKDLFYSA ARMDELADIV QQLAAQAAHG EVEARAFRDA
TGLGRKRAIQ IIECFDRLGY TRRVRDAHVL RPDAQWNRSR
//
