GenomeNet

Database: UniProt
Entry: I4EUX5_9ACTN
LinkDB: I4EUX5_9ACTN
Original site: I4EUX5_9ACTN 
ID   I4EUX5_MODI5            Unreviewed;       579 AA.
AC   I4EUX5;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   28-JAN-2026, entry version 63.
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:CCH87188.1};
GN   OrderedLocusNames=MODMU_1749 {ECO:0000313|EMBL:CCH87188.1};
OS   Modestobacter italicus (strain DSM 44449 / CECT 9708 / BC 501).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Modestobacter.
OX   NCBI_TaxID=2732864 {ECO:0000313|EMBL:CCH87188.1, ECO:0000313|Proteomes:UP000006461};
RN   [1] {ECO:0000313|EMBL:CCH87188.1, ECO:0000313|Proteomes:UP000006461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC 501 {ECO:0000313|Proteomes:UP000006461};
RX   PubMed=22887672; DOI=10.1128/JB.01029-12;
RA   Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA   Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA   Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT   "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT   a Representative Actinobacterium That Thrives on Calcareous Stone
RT   Surfaces.";
RL   J. Bacteriol. 194:4773-4774(2012).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FO203431; CCH87188.1; -; Genomic_DNA.
DR   AlphaFoldDB; I4EUX5; -.
DR   STRING; 477641.MODMU_1749; -.
DR   KEGG; mmar:MODMU_1749; -.
DR   PATRIC; fig|477641.3.peg.1647; -.
DR   eggNOG; COG3276; Bacteria.
DR   HOGENOM; CLU_023030_1_1_11; -.
DR   OMA; HYAMLIV; -.
DR   Proteomes; UP000006461; Chromosome.
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   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; 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; IPR004535; Transl_elong_SelB.
DR   InterPro; IPR036388; WH-like_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; PF09107; WHD_3rd_SelB; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Elongation factor {ECO:0000313|EMBL:CCH87188.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006461}.
FT   DOMAIN          1..168
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   579 AA;  60487 MW;  2F809FAEFD6A7E0F CRC64;
     MIATAGHVDH GKSALVRALT GMEPDRWEEE RRRGLTIDLG FAWTTLPSGR RVAVVDVPGH
     ERFIGNMLAG VGSVPTALVV VAADDGWSAQ TAEHVAVLDA LGVRAGLLAV TKADLADPAP
     VLADARERLA GTSLGRLPAV AVSARTGAGL PELTAALERV LAGLPAPDPA APVRLWVDRA
     FTIRGAGTVV TGTLAAGTLT AGDRLDLGGR TVTVRGLQSL GAPVETAVAT ARVALNLRGV
     AVEEISRGDA LLTPDAFRRT ADLDVTLVAP VEGTLPAEAV VHIGSATVAA RVRPLDGTAV
     RLRLAHELPL RVGDRLLLRD PGVRRVLGAD VRDVDPPELR RRGAARSRAA ELAEQPAGAE
     GAAADLARRR FVRRADFVAM GWPVPAGTTT VGPWLVAPGL ADELAARVPQ VVARYRQLRP
     LEPGPPLAVL RSALELPDVE LVPAVVRAPL ELREGRVVAA DPGLPAAVQR AVDGIRARLA
     AEPFAAPEAG DLVAAGLGTR ELAAAVRAEQ LVRIADGVYL APGVAEVARA RLAGLPSPFT
     LSEARQAWGT TRRVAVPLAE WLDARGITVR LPDNTRRLR
//
DBGET integrated database retrieval system