ID A0A4P7CID1_9PAST Unreviewed; 616 AA.
AC A0A4P7CID1;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, 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:QBQ63865.1};
GN ORFNames=EXH44_06260 {ECO:0000313|EMBL:QBQ63865.1};
OS Actinobacillus indolicus.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Pasteurellales; Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=51049 {ECO:0000313|EMBL:QBQ63865.1, ECO:0000313|Proteomes:UP000294444};
RN [1] {ECO:0000313|EMBL:QBQ63865.1, ECO:0000313|Proteomes:UP000294444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AIFJ1607 {ECO:0000313|EMBL:QBQ63865.1,
RC ECO:0000313|Proteomes:UP000294444};
RA Che Y., Zhou L.;
RL Submitted (MAR-2019) 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}.
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DR EMBL; CP038145; QBQ63865.1; -; Genomic_DNA.
DR RefSeq; WP_162856708.1; NZ_CP038145.1.
DR AlphaFoldDB; A0A4P7CID1; -.
DR KEGG; aio:EXH44_06260; -.
DR Proteomes; UP000294444; 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; IPR005225; Small_GTP-bd.
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 NCBIfam; TIGR00231; small_GTP; 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:QBQ63865.1};
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:UP000294444}.
FT DOMAIN 1..166
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 616 AA; 69737 MW; 363D0D9F8686D163 CRC64;
MIIVTAGHVD HGKTSLLHAL TGTHTAHLPE EKKRGLTIDL GYAYLPIEND ILGFIDVPGH
QKFLSNMLAG LGGIQHALLV VSADEGIKPQ TEEHLAILRL LNFKQIIVVL TKADRAEATR
ITQLIEQLKQ RYPFLASAHF FATSAQTGEG IEPLKQYLIS LNHQSTQIDK PFRYAIDRVF
NVKGAGLVVT GTAVAGKVAI GDEFYLSSGQ KVRIKNIHAQ NNEASIGVAG QRLALNIANV
EKEQIERGDW ITQQDPQFAC DRITVRLTTA QALKENNVVH LYHFASHTTA KLNLLDRSQC
LADDTAIAEL ILDTPLHIAL EDKLILRSGD DSQTLAGAEV IEIHSPKRHK RSEARLSYLS
QLANCTSYQE RIALYLQHKA VNLTQLLWAE QIFIRDLEKL SEKSDYYLNA NHLFNGAFKT
QIQQHIVAKL EEYHQQHSDQ LGVTKARLHR MTALDQAELL IFALIDDLIA NKTLAQTRGW
IHTPTHRIEF SDAELQIWAE IRPLFERTNQ ALWVRDIASE LSIDETEMRN LLYKAGKLGY
LVPIVKDRFL LHEQISAFAQ LIKNFIEQHG EISVNQLRDE IQYGRKVTVQ LIEYFDRSGF
LRRKGNVHLL RDKETY
//
