ID A0A369ZRM5_9PAST Unreviewed; 622 AA.
AC A0A369ZRM5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 28-JAN-2026, entry version 26.
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:RDF08908.1};
GN ORFNames=DPV92_07760 {ECO:0000313|EMBL:RDF08908.1};
OS Haemophilus paraphrohaemolyticus.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Pasteurellales; Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=736 {ECO:0000313|EMBL:RDF08908.1, ECO:0000313|Proteomes:UP000253945};
RN [1] {ECO:0000313|EMBL:RDF08908.1, ECO:0000313|Proteomes:UP000253945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C2014016342 {ECO:0000313|EMBL:RDF08908.1,
RC ECO:0000313|Proteomes:UP000253945};
RA Nichols M., Topaz N., Wang X., Wang X., Boxrud D.;
RT "Draft Genome Sequences for a Diverse set of 7 Haemophilus Species.";
RL Submitted (MAY-2018) 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:RDF08908.1}.
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DR EMBL; QEQF01000008; RDF08908.1; -; Genomic_DNA.
DR RefSeq; WP_111354383.1; NZ_QEQF01000008.1.
DR AlphaFoldDB; A0A369ZRM5; -.
DR STRING; 736.B0184_03785; -.
DR Proteomes; UP000253945; Unassembled WGS sequence.
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:RDF08908.1};
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:UP000253945}.
FT DOMAIN 1..171
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 622 AA; 70454 MW; E4B959059C7718F9 CRC64;
MIVVTAGHVD HGKTALLQAL TGTNTAHLPE EKKRGLTIDL GYAYLPIETP HGKHDILGFI
DVPGHQRFLS NMLAGVGGIQ HALLAVSAEE GIKPQTEEHL EILKLLRFSH IMLVITKADR
AKASRIEQLI YTIQNHYPFL VEAPVFVTSA HTGQGIEALK NHLIMLNEQA KSATDKPFRY
AIDRVFNVKG AGLVVTGTAV AGQVKIGDEF YLTSDQKVRV KGIHAQNSPS EIGLAGQRLA
LNIANVEKEQ VQRGDWITEL APHFATDRIT VRLNVIQPLK ESTVAHLYHF ASHVTGKVSL
LNTKQAVENG DYFAEILLDE PLHIAVNDRL IIRSGDDRQT LGSAEVLEIH SPKRYKRSEA
RLSFVNELAK TTACDDFTAR LALMLQNRAL TLDFLLWAEQ RFASQLPENT DAIVYDKWIF
SCKFKQQIQQ RMVEKLTEYH ANHQDQLGLS KARLYRMAVL EQPEGLALQW LNELVAEGVL
AQTRGWVHLP EHRIEFSDRE LQIWQQIRPL FEATNQALWV REIATELNLD ETDTRNLLYK
AGKLGYAVPI VKDRFLFAEQ IQQFASWIKA FVQTHGEISV NQLRDELQYG RKLTVQLMEY
FDRTGFLRRK GNVHLLRDAE SF
//
