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Database: UniProt
Entry: A0A845QT39_9CLOT
LinkDB: A0A845QT39_9CLOT
Original site: A0A845QT39_9CLOT 
ID   A0A845QT39_9CLOT        Unreviewed;       635 AA.
AC   A0A845QT39;
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:NBI05705.1};
GN   ORFNames=D3Z33_02400 {ECO:0000313|EMBL:NBI05705.1};
OS   Senegalia massiliensis.
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Senegalia.
OX   NCBI_TaxID=1720316 {ECO:0000313|EMBL:NBI05705.1, ECO:0000313|Proteomes:UP000467132};
RN   [1] {ECO:0000313|EMBL:NBI05705.1, ECO:0000313|Proteomes:UP000467132}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=583 {ECO:0000313|EMBL:NBI05705.1,
RC   ECO:0000313|Proteomes:UP000467132};
RA   Liu C.;
RT   "Murine metabolic-syndrome-specific gut microbial biobank.";
RL   Submitted (AUG-2018) 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:NBI05705.1}.
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DR   EMBL; QXXA01000004; NBI05705.1; -; Genomic_DNA.
DR   RefSeq; WP_160196201.1; NZ_QXXA01000004.1.
DR   AlphaFoldDB; A0A845QT39; -.
DR   OrthoDB; 9804504at2; -.
DR   Proteomes; UP000467132; 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; cd03696; SelB_II; 1.
DR   CDD; cd15491; selB_III; 1.
DR   FunFam; 3.40.50.300:FF:001064; Selenocysteine-specific translation elongation factor; 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; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015191; SelB_WHD4.
DR   InterPro; IPR005225; Small_GTP-bd.
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   NCBIfam; TIGR00231; small_GTP; 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; 2.
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:NBI05705.1};
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:UP000467132}.
FT   DOMAIN          1..174
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   635 AA;  72764 MW;  48B15E8BDB497D8F CRC64;
     MKNVIIGTAG HIDHGKTTLI KALTGRDTDN LKQEKDRGIS IELGFTYFDL PSGRRAGIID
     VPGHEKFIKN MLAGVSGMDV VILVVAADEG MMPQTIEHLN ILNLLNIKKG IIALTKTDTV
     DNEWIELVKE DIYESVENTF LKDAKIIEVS STKLEGIDEL SRQIDYLTSE IENRDSKNIP
     RLPIDRVFTL TGFGTIITGT LLQGSLKVSD EVEIYPKGLK ARIRSVQVHG EDTDIALAGQ
     RVAINLVGVK KSEIEKGNII SYPDSMVNTR MIDVKLNLLE NSPWIIENRT RLRLYLGTEE
     ILCRAILLDK ENLTPGESGY VQLRLENITS SKIGDRFIVR FYSPMTTVGG GIVLDNNPTK
     KKRFKSDIIK ELKARETGNK EKILEESIKE KSRSFPSTKD LSIELVTTES EIKNNTNKLT
     QNQKIIKFTM SDGEHYIHID YFEYIKMEII EFLQKYHEKN SLKKGILKEE IKSKYFSNIK
     PKLSELFIDK LIYDNIIKQD NLYISLNNFQ IKYNEKEKSI KDNIYDLILK DKFNPPKINE
     LIKILQHKEE EVLKVIDSCI QQEGIILLDE DIIISKQAYD NSLDIIRDYL NKNSSISLGE
     FRDLLNTSRK FAMALLEDFD RNKFTKRIED KRIIY
//
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