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Database: UniProt
Entry: A0A853H1K5_9BURK
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ID   A0A853H1K5_9BURK        Unreviewed;       642 AA.
AC   A0A853H1K5;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   28-JAN-2026, entry version 19.
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:NYT85115.1};
GN   ORFNames=H0A62_05825 {ECO:0000313|EMBL:NYT85115.1};
OS   Pollutimonas harenae.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Alcaligenaceae; Pollutimonas.
OX   NCBI_TaxID=657015 {ECO:0000313|EMBL:NYT85115.1, ECO:0000313|Proteomes:UP000554144};
RN   [1] {ECO:0000313|EMBL:NYT85115.1, ECO:0000313|Proteomes:UP000554144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25667 {ECO:0000313|EMBL:NYT85115.1,
RC   ECO:0000313|Proteomes:UP000554144};
RA   Szabo A., Felfoldi T.;
RT   "Taxonomic revisions and descriptions of new bacterial species based on
RT   genomic comparisons in the high-G+C-content subgroup of the family
RT   Alcaligenaceae.";
RL   Submitted (JUL-2020) 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:NYT85115.1}.
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DR   EMBL; JACCEV010000001; NYT85115.1; -; Genomic_DNA.
DR   RefSeq; WP_130037360.1; NZ_JACCEV010000001.1.
DR   AlphaFoldDB; A0A853H1K5; -.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000554144; 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; 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; 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; IPR031157; G_TR_CS.
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   PRINTS; PR00315; ELONGATNFCT.
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; 3.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Elongation factor {ECO:0000313|EMBL:NYT85115.1};
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:UP000554144}.
FT   DOMAIN          1..171
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   642 AA;  70450 MW;  14AEDD6CAFA6A561 CRC64;
     MIVGTAGHID HGKTTLVRAL TGVDTDRLKE EKARGISIEL GYAYTPLPND DVLGFIDVPG
     HERLIHTMAA GASGIDFGLL VVAADDGIMP QTLEHLAILS ILGISRGAIA ITKADRVDEA
     RLHDVQEAVV QLTKDTFLQN AAVFFVSATT DDDAGLHELR THLHAMAQTV AARNAAGLFR
     LAVDRVFTLK GQGTVVTGTV HDGVLALDDD TLDIRLMPAG QKLRVRSIHA QNQASQEARA
     GQRCALNLGG IDKSAITRGD WIADARCFVP SRNIDVELSL LPDSSSAVRA WSPLHIHLGA
     SHFLAHAVPL SCAALAAGET GWIQLVFDQA ICAMPGDRYL VRDAQARHTI GGGVVLDPNA
     PQRKRRSPER LAWLQAVSNH HAGAGLPGLL QQAPWGLDEY HVLRLTRRNP DEKPLPAGTL
     WISARGGQST RSLILQSHWN ALISQTLQTI ASFHKHWPDE PGIDAARLRR MAWPTLPEAM
     WLALSEHLTS TNQLARNGPW LHLPEHAVGL TAKEIELAGH LLPLLHAGRF DPPWVRDLAV
     QLNEDEQSVR QTLLKLLRRG DVYQVVRDLF YHREQIIQLA GLITAMGGNE GVNAAQFRDK
     TGLGRKRAIQ ILEFFDRAGY TRRLRDHHVL RKNGADFWHQ LS
//
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