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Database: UniProt
Entry: A0A1I2ZH54_9GAMM
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ID   A0A1I2ZH54_9GAMM        Unreviewed;       642 AA.
AC   A0A1I2ZH54;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   28-JAN-2026, entry version 27.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   ORFNames=SAMN04487959_103107 {ECO:0000313|EMBL:SFH36829.1};
OS   Modicisalibacter xianhensis.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Oceanospirillales; Halomonadaceae; Modicisalibacter.
OX   NCBI_TaxID=442341 {ECO:0000313|EMBL:SFH36829.1, ECO:0000313|Proteomes:UP000199040};
RN   [1] {ECO:0000313|EMBL:SFH36829.1, ECO:0000313|Proteomes:UP000199040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6848 {ECO:0000313|EMBL:SFH36829.1,
RC   ECO:0000313|Proteomes:UP000199040};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOPY01000003; SFH36829.1; -; Genomic_DNA.
DR   RefSeq; WP_092843903.1; NZ_FOPY01000003.1.
DR   AlphaFoldDB; A0A1I2ZH54; -.
DR   STRING; 442341.SAMN04487959_103107; -.
DR   Proteomes; UP000199040; 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; 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; 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; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Elongation factor {ECO:0000313|EMBL:SFH36829.1};
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:UP000199040}.
FT   DOMAIN          1..172
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   642 AA;  70654 MW;  6F97D97AA04A234D CRC64;
     MIVGTAGHVD HGKTALIQRL TGIDTDRLKE EKARGLTIEA GFAYPEVEPG MELGFVDVPG
     HEKFIHNMMA GSAGIDSVLL VVAADDGVMP QTVEHVQILS LLGLSRGRVA LTKCDLVDAA
     RLARVESEIR QLLSATPLAE ASIYRVSSHT GEGVGALRDA LWTEAAQRHE LPAWGAFRLA
     VDRVFTKTGA GLVVTGTAVS GTVHEGDMLR LEPSGIRARV RSLRRQHRES EQARQGDRVA
     LNLVGSGVER DAIVRGGWVV DESLETPPLQ RVDVDITLLD NVTALKHWTP VHVHLGVARL
     TGRVSLLEGQ RLEPGGRMLG QLALDRPVHA CLGDRFVIRD HGGQMTLGGG TVLDGDPPRR
     GQRAPKRLTW LTALAECAAG GSPYDIVRPL ETGLSLWPEG LDLDKLVRNF NSDQQDLAAR
     VEAMGGQVIS AQGHVWAFSR QGLEAVKART LETLQHNHVN EPSMLGTERE RLRRQVMPGL
     PGAFFRPLLN AMIEVGHIER HGPFLALPGH QVALDEADER LWQQVQPLLA DTPFEPPRVR
     DMAAKQELDE QAIRQALMAC ARLGRVYQVR KDHFYEAMAV ERLAGIIKRL DAEHGAARAA
     DFRDHIGTGR KLAIQILEFF DRLGFTRRVR DDHIVLRHDM FE
//
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