ID A0A1I7GXX9_9GAMM Unreviewed; 646 AA.
AC A0A1I7GXX9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 28-JAN-2026, entry version 30.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=SAMN04487955_103318 {ECO:0000313|EMBL:SFU53116.1};
OS Halomonas korlensis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Oceanospirillales; Halomonadaceae; Halomonas.
OX NCBI_TaxID=463301 {ECO:0000313|EMBL:SFU53116.1, ECO:0000313|Proteomes:UP000198693};
RN [1] {ECO:0000313|Proteomes:UP000198693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6981 {ECO:0000313|Proteomes:UP000198693};
RA Varghese N., Submissions S.;
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; FPBP01000003; SFU53116.1; -; Genomic_DNA.
DR RefSeq; WP_089794032.1; NZ_FPBP01000003.1.
DR AlphaFoldDB; A0A1I7GXX9; -.
DR STRING; 463301.SAMN04487955_103318; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000198693; 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:SFU53116.1};
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:UP000198693}.
FT DOMAIN 1..169
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 646 AA; 70265 MW; C6D78B363FF6418C CRC64;
MIVGTAGHVD HGKTALIQQL TGIDTDRLKE EKARGLTIEA GFAYPEADTE LDLGFVDVPG
HERFIHNMLA GSAGIDTVLL VVAADDGVMP QTIEHVQILQ LLGLTNGIVA LTKIDLVDEA
RSAEVQREIA ALLADTPLAG APIYPLSSRS GEGVAALRDA LWSMAAAPRQ APVQGQFRLA
IDRAFSKPGA GLVVTGTALS GRVRQGDPVR LVASGRTARV RRLRRQHRPS DQARQGDRVA
LNLAGAGIER DDVQRGDWVV ADALETPALK RLDIHLQLLD GTAVMAHWTP VHVHLGVTRV
MGRVALLEGP RLAPGGRMLS QLVLDRPVHA CLGDRFVIRD QGGHATLGGG VVLDGNPPRR
GQRAPTRLAW LAALAEAVAD ASRKGPPIEL RRPLQVALDA RPDGLDLAAI AWHTNTPLDA
LVAIVESLEG RVVVAQHEVR AFSHQAIEAL ETRMLDIVAA NHQREPAMPG TERARLNRQA
MPGIPGAVFR PLLKALIDAG RLERQGPFVA LPGHRAGLDA ADETLWQRLA PLLAATPFQP
PRVRDMARDE GLDEQRLRAA LTACARLGRL YQVRKDHFYL DTAVRDMAAI IQRLEAQHGT
VRCADFRDRI ATGRKLAIHI LEFFDSLGYT RRVRDERVIR QADLWH
//
