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Database: UniProt
Entry: A0A923HIC9_9BURK
LinkDB: A0A923HIC9_9BURK
Original site: A0A923HIC9_9BURK 
ID   A0A923HIC9_9BURK        Unreviewed;       644 AA.
AC   A0A923HIC9;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   28-JAN-2026, entry version 15.
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:MBC3864279.1};
GN   ORFNames=H8K32_19440 {ECO:0000313|EMBL:MBC3864279.1};
OS   Undibacterium jejuense.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Oxalobacteraceae; Undibacterium.
OX   NCBI_TaxID=1344949 {ECO:0000313|EMBL:MBC3864279.1, ECO:0000313|Proteomes:UP000634011};
RN   [1] {ECO:0000313|EMBL:MBC3864279.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KACC 12607 {ECO:0000313|EMBL:MBC3864279.1};
RA   Lu H.;
RT   "Novel species isolated from subtropical streams in China.";
RL   Submitted (AUG-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:MBC3864279.1}.
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DR   EMBL; JACOFV010000027; MBC3864279.1; -; Genomic_DNA.
DR   RefSeq; WP_186914221.1; NZ_JACOFV010000027.1.
DR   AlphaFoldDB; A0A923HIC9; -.
DR   Proteomes; UP000634011; 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; 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; ELONGATION FACTOR TU-RELATED; 1.
DR   PANTHER; PTHR43721:SF11; SELENOCYSTEINE-SPECIFIC ELONGATION FACTOR; 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:MBC3864279.1};
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:UP000634011}.
FT   DOMAIN          1..171
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   644 AA;  71309 MW;  B917BB2CE5BAC14D CRC64;
     MIVGTAGHID HGKTTLSRAL TGVDTDRLKE EKARGISIEL GYAYTPLPNG DVLGLVDVPG
     HEKLIHTMAA GASGIDYALL VIAADDGVMP QTREHLTILE LLGIQRGVVA LTKIDRVDAD
     RISAVKKEIQ HLLATSSFAD ATIFCTQAHI ENDPGVAELK AHLMKVAQAL TQKEHQRLFR
     LAIDRVFNLS GKGLFIAGTA SAGAVAIGDT ITLAPSGKTV RVRSIHAQNR PVDIAYAGQR
     LAMNIVGVEK DEVERGHWAT ATAMAECSER IDVDLQLLDN AGLSLKPWSQ VHVHLGASHR
     IARVLMLDGD SIEPGCQARA QLVFEVPVHS VPGDRFVIRN AQAQRTIGGG RVLDPFGPAR
     KRRSLERKQW LDALSNYLDT NDHNALVDGS AMGIRRSLLT RLTQLPVEQL QYHDDVIQIA
     LRGDDVIILP HAVLIALREK IVVALRAFHT NFPDETGPQN PRLKRIVAPE IDEMVWRTLI
     DKLVQTEVLI AQGPWLRLPE HSIELEPEQQ RLADVLLNAL LASQFDPPWV RDLAKAHQLN
     EETVRSLLRK LALRGQVYQI VRDLYCHPQR IAELAKLAEA VASTLELNSP YRQISAADFR
     DASGMGRKRA IQFLEFFDRV GYTRRLRDVH VLRTDSLWQA ANMQ
//
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