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Database: UniProt
Entry: A0A1T4KFK2_9FUSO
LinkDB: A0A1T4KFK2_9FUSO
Original site: A0A1T4KFK2_9FUSO 
ID   A0A1T4KFK2_9FUSO        Unreviewed;       630 AA.
AC   A0A1T4KFK2;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   28-JAN-2026, entry version 33.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   ORFNames=SAMN02745174_00405 {ECO:0000313|EMBL:SJZ41125.1};
OS   Cetobacterium ceti.
OC   Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia; Fusobacteriales;
OC   Fusobacteriaceae; Cetobacterium.
OX   NCBI_TaxID=180163 {ECO:0000313|EMBL:SJZ41125.1, ECO:0000313|Proteomes:UP000191153};
RN   [1] {ECO:0000313|EMBL:SJZ41125.1, ECO:0000313|Proteomes:UP000191153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700028 {ECO:0000313|EMBL:SJZ41125.1,
RC   ECO:0000313|Proteomes:UP000191153};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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; FUWX01000005; SJZ41125.1; -; Genomic_DNA.
DR   RefSeq; WP_078692952.1; NZ_FUWX01000005.1.
DR   AlphaFoldDB; A0A1T4KFK2; -.
DR   STRING; 180163.SAMN02745174_00405; -.
DR   OrthoDB; 9804504at2; -.
DR   Proteomes; UP000191153; 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; 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   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; PF09107; WHD_3rd_SelB; 1.
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:SJZ41125.1};
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:UP000191153}.
FT   DOMAIN          1..173
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   630 AA;  71825 MW;  5C890CA9E22B4A13 CRC64;
     MKNLVIGTAG HIDHGKTTLI KHLTGVDTDT LPEEAKRGMT INLGFTYFQL SSGEKIGIVD
     VPGHEKFIKN MVAGATGLDF ILFIVACDDG IMPQTIEHGN IIELLNINHG ITVLTKRDLV
     SKERVEEVKK SIKETFVHGA IKSFPIVEVS PKDEKSYDHL RGLIEKELNH LNKRKRENSF
     FKMAIDRVFS VKGFGTVVTG TSAQGVIHKG DSLMIYPQMI NVKVKGIENH GNKVEFLEAG
     HRCALNLTGV ETSEIKRGSL LAPEKALFVT DKIDCFFTLL NNKKNIKNNH RIRLHIGTTE
     IIGRIKLLER DTLEPGQSSL IQLELEKSIV CNMGDIGVIR NYSPMDTIGG IKIISPQGKN
     TKRYNEEYIA SLKSLLGNEE EKILETLKKF NNNLATLDDI SINLGKYISL ETLLENPKII
     NFQEGDNFKF IHMDNFNNLK NKVHEYLINF YKENNLKKGV SRSEIKNKIF QSYTLKDFNL
     IIKLLENDFI DTSEDVIALK GYSVKLTKEQ KLIKDDILKI YKNMEFSPNS IKEIQQNFIN
     KNDFSIMHNY LKEKGLLIPL TKENFVLKGF FQESQSRLID YAKINEKITL GEFKNIIGTS
     RKFALLFLDK FDEIGFTKRI DDYRILRKEN
//
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