ID A4N0E8_HAEIF Unreviewed; 619 AA.
AC A4N0E8;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=CGSHi22121_01032 {ECO:0000313|EMBL:EDJ87871.1};
OS Haemophilus influenzae 22.1-21.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=374927 {ECO:0000313|EMBL:EDJ87871.1, ECO:0000313|Proteomes:UP000004131};
RN [1] {ECO:0000313|EMBL:EDJ87871.1, ECO:0000313|Proteomes:UP000004131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22.1-21 {ECO:0000313|EMBL:EDJ87871.1,
RC ECO:0000313|Proteomes:UP000004131};
RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA Ehrlich G.D.;
RT "Characterization and modeling of the Haemophilus influenzae core and
RT supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(2007).
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; AAZD01000005; EDJ87871.1; -; Genomic_DNA.
DR AlphaFoldDB; A4N0E8; -.
DR Proteomes; UP000004131; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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; IPR004161; EFTu-like_2.
DR InterPro; IPR015190; Elong_fac_SelB-wing-hlx_typ-2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR048931; SelB_WH_3rd.
DR InterPro; IPR015191; SelB_WHD4.
DR InterPro; IPR005225; Small_GTP-bd_dom.
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; PF21214; bact_SelB_WH_2nd; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF09106; SelB-wing_2; 1.
DR Pfam; PF09107; SelB-wing_3; 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 Elongation factor {ECO:0000313|EMBL:EDJ87871.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:EDJ87871.1}.
FT DOMAIN 1..167
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 619 AA; 70065 MW; 4F268ACFC5874CFD CRC64;
MIIVTSGHVD HGKTALLKAL TGKNTAHLPE EKKRGMTIDL GYAYLPLENK VLGFIDVPGH
EKFLSNMQAG LGGVHYAMLI VAADEGVATQ TKEHLAILRQ LQFHEIIVVI TKADRTNSEQ
IESLIQEIKQ NYSFLRGANY FVTSAETGQG ISELRHYLAN LPELSDTQKP FRYAIDRVFN
VKGAGTVVTG TAFSGTVKVN DELYLSTGQK VRVKAIHAQN TSSEQGIAGQ RLALNLNADL
DRTSMKRGDW LLQNEPLPPT DRISVQILAE VPLNESQPVH IYHGASRTTG KLTLLQGKNA
AKNDRTLAEI ILDSPLFLAF GDKLILRSGD TKTLIAGARV LEINSPKRHK RTEVRLNFLA
NLALAENASQ RIALTLQHNA TTACQLMWME QLTETQLDQA LSERGAVRHQ DWCFNTNYIQ
EKTQQILTAL NTYHEQHNDQ LGVSKARLYR MTALNQPENL INHFIDEMLE EGRLQQTRGW
LHLPEHKIQF SQEEQKRWGN VLNEFEKAQG QAIWVRDMAN ALAIDESIMR NFMYKAGKLG
YLTPIVKDRF FLTETIYAYA RLIKQIAEEQ GKVSVNEVRD KLNFGRKLTV QLMEYFDRMG
FLRRKGNDHI LRDKNVFDL
//
