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Database: UniProt
Entry: A0A938XNG9_9FIRM
LinkDB: A0A938XNG9_9FIRM
Original site: A0A938XNG9_9FIRM 
ID   A0A938XNG9_9FIRM        Unreviewed;       635 AA.
AC   A0A938XNG9;
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   ORFNames=JOC47_000558 {ECO:0000313|EMBL:MBM7555733.1};
OS   Halanaerobacter jeridensis.
OC   Bacteria; Bacillati; Bacillota; Clostridia; Halanaerobiales;
OC   Halobacteroidaceae; Halanaerobacter.
OX   NCBI_TaxID=706427 {ECO:0000313|EMBL:MBM7555733.1, ECO:0000313|Proteomes:UP000774000};
RN   [1] {ECO:0000313|EMBL:MBM7555733.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 23230 {ECO:0000313|EMBL:MBM7555733.1};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JAN-2021) 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:MBM7555733.1}.
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DR   EMBL; JAFBDQ010000002; MBM7555733.1; -; Genomic_DNA.
DR   RefSeq; WP_204700453.1; NZ_JAFBDQ010000002.1.
DR   AlphaFoldDB; A0A938XNG9; -.
DR   Proteomes; UP000774000; 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; 1.10.10.2770; -; 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; 1.
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   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; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Elongation factor {ECO:0000313|EMBL:MBM7555733.1};
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:UP000774000}.
FT   DOMAIN          2..174
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   COILED          440..502
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   635 AA;  71404 MW;  9CB160A21B36DB7E CRC64;
     MAENLIIGTA GHVDHGKTTL IGALTGENTD RLEEEQERGL SIDLGFSRLN FDNGLQAGII
     DVPGHEKFIK NMLAGAGGVD IGLLVVAADE AIMEQTREHL AILELLNVEQ GVIAVTKSDK
     VDSEWLELVI DEIKEFVEDT FLEDAAVIPV SGIEETGIED LKEELGHLMQ QLPDKDKEAN
     VYFPIDRVFS IGGHGTVVTG TLMQGQIQLE DELEIYPSQL KARVRGLQVH EKDVEVAQPG
     QRIGINLSGV DKDEIERGDV LAAQDSLVKT EYLDARLELI ESAPLVLEHG ERIRLHLGAK
     EVIGRVYLLD SEELLPGEEG LVQFRLEDTV VANFKERYVL RRYSPMTTIG GGKILEANPA
     QHRKNDEAVI KALQIKEEGT TAERIKLALQ REEDKALTVD DLVTRTSLAQ EQIREELMGL
     QSRNEVIELD VGTESSLLHS DDYQQLMEEI IANLKDYHQE YHLRLGMPKE ELRTKLSLAL
     TANEYDRLLD DLKEQEVIEE KQAKISLADF AVKLTADEKK IKAEIEEKFA QNKYLPPKLD
     GLISSYSDEQ VAEEISNLLI NNGELIKVAH NIYFDYQAVK EAKELLINYL KKNETIDVAQ
     FRDLLDSSRK YALPLLEYFD QRGVTKREGD IRRLS
//
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