ID Q7VKC3_HAEDU Unreviewed; 622 AA.
AC Q7VKC3;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 28-JAN-2026, entry version 124.
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:AAP96709.1};
GN OrderedLocusNames=HD_1993 {ECO:0000313|EMBL:AAP96709.1};
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Pasteurellales; Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412 {ECO:0000313|EMBL:AAP96709.1, ECO:0000313|Proteomes:UP000001022};
RN [1] {ECO:0000313|Proteomes:UP000001022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724 {ECO:0000313|Proteomes:UP000001022};
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) 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 ---------------------------------------------------------------------------
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; AE017143; AAP96709.1; -; Genomic_DNA.
DR RefSeq; WP_010945730.1; NC_002940.2.
DR AlphaFoldDB; Q7VKC3; -.
DR STRING; 233412.HD_1993; -.
DR KEGG; hdu:HD_1993; -.
DR eggNOG; COG3276; Bacteria.
DR HOGENOM; CLU_023030_2_0_6; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000001022; 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; cd03696; SelB_II; 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; 2.
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; 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 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:AAP96709.1};
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:UP000001022}.
FT DOMAIN 1..173
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 622 AA; 70429 MW; D0B866C6992F0D9E CRC64;
MIFVTAGHVN HGKTSLLQAL TGMNTAHLPE EKKRGLTIDL GYAYLAIEDE MAKVERLGFI
DVPGHQKFMS NMLAGLGGIQ HALLVVSAEE GIKPQTEEHI EILRLLKFEQ IAVIVTKSDR
ANMSQMLALI AQLRTRYPFL HTSPCFYTST VTGAGIDELK QYLINCATQN SQTAKPFRYA
IDRIFNIKGA GLVVTGTAIA GQVKVGDELY LSNGESVRVK AIHAQNCIAE RGSAGQRLAL
NLANVEKEQL QRGNWLSALD PKFATDRISI QLTASTDLRE NQVVHLYHFA SHTMGKLNLL
DAKQAVRNEQ RLAEIILDQP LHIAFNDKLM IRSGDDRQTL AGARVLEINA PKRYKRTTER
LIYLNQLANT HECAERIALY SQSKAVAVDR LLWLEQLCLS DLAEMGFDTD KKWIVSDVYK
TRVQQAIVTK LTDYHQQHND QLGVAKARLY RMAALAEPEQ LVLALIDELI ETKQLAQTRG
WVHLPDHRIE FSAQELHVWQ QIKPLFEAKR EALWVRDVAN TLLIDETVMR DLLYKAGKLG
YLMPIVKDRF FLHEHIVEFA QIIKQFIANH GAISVNQLRD QLGFGRKMTV QLIEYFDRCG
FLRRKSNLHL LRDADIFSSS TH
//
