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Database: UniProt
Entry: A4N601_HAEIF
LinkDB: A4N601_HAEIF
Original site: A4N601_HAEIF 
ID   A4N601_HAEIF            Unreviewed;       619 AA.
AC   A4N601;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   ORFNames=CGSHi22421_09945 {ECO:0000313|EMBL:EDJ90361.1};
OS   Haemophilus influenzae R3021.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=375432 {ECO:0000313|EMBL:EDJ90361.1, ECO:0000313|Proteomes:UP000003798};
RN   [1] {ECO:0000313|EMBL:EDJ90361.1, ECO:0000313|Proteomes:UP000003798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R3021 {ECO:0000313|EMBL:EDJ90361.1,
RC   ECO:0000313|Proteomes:UP000003798};
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; AAZE01000016; EDJ90361.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4N601; -.
DR   Proteomes; UP000003798; 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; cd04450; DEP_RGS7-like; 1.
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; 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   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:EDJ90361.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:EDJ90361.1}.
FT   DOMAIN          1..167
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   619 AA;  69946 MW;  766B3D5F38D063C0 CRC64;
     MIIVTSGHVD HGKTALLKAL TGTSTAHLPE EKKRGMTIDL GYAYLPLENK VLGFIDVPGH
     EKFLSNMLAG LGGVHYAMLI VAADGGVAVQ TKEHLAILRQ LQFHEIIVVI TKADRTNPEQ
     IESLIQEIKQ NYSFLRGANY FVTSAETGQG INELRHYLAN LPELSDTQKP FRYAIDRVFN
     VKGAGTVVTG TAFSGTVKVN DEIYLSTGQK VRIKAIHAQN TSSEQGIAGQ RLALNLNADL
     DRTPMKRGDW LLQNEPLPPT DRISVQILAE VPLNESQPVH IYHGASRTTG KLTLLQGKNT
     AKNDRTLAEI ILDSPLFLAF GDKLILRSGD TKTLIAGAQV LEINSPKRHK RTEVRLNFLA
     NLALAENASQ RIALTLLHNA TTVRQLMWTE QLTSSQLDKA LAERGAVRYQ DWCFNTNYVQ
     EKTQQILTAL NTYHEQHNDQ LGVSKARLYR MATLNQPENL IHHFIDEMLD DGRLQQTRGW
     IHLPEHKIQF NTEEKSRWTD VLNEFEKANG QAIWVRDMAN ALAIDESIMR NFMYKAGKLG
     YLTPIVKDRF FLTETLYAYA RLIKQIAEEK GKVSVNEVRD KLNFGRKLTV QLMEYFDRMG
     FLRRKGNDHI LRDKNVFDL
//
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