ID   SELB_DESBA              Reviewed;         634 AA.
AC   Q46497;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Selenocysteine-specific elongation factor;
DE   AltName: Full=SelB translation factor;
GN   Name=selB;
OS   Desulfomicrobium baculatum (Desulfovibrio baculatus).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfomicrobiaceae; Desulfomicrobium.
OX   NCBI_TaxID=899;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 1743;
RX   PubMed=8893853; DOI=10.1006/jmbi.1996.0525;
RA   Kromayer M., Wilting R., Tormay P., Boeck A.;
RT   "Domain structure of the prokaryotic selenocysteine-specific elongation
RT   factor SelB.";
RL   J. Mol. Biol. 262:413-420(1996).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. SelB subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU01059}.
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; X99911; CAA68184.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q46497; -.
DR   SMR; Q46497; -.
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:InterPro.
DR   GO; GO:0001514; P:selenocysteine incorporation; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR015190; Elong_fac_SelB-wing-hlx_typ-2.
DR   InterPro; IPR015191; Elong_fac_SelB-wing-hlx_typ-3.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
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   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF09106; SelB-wing_2; 1.
DR   Pfam; PF09107; SelB-wing_3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF46785; SSF46785; 3.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF50465; SSF50465; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00475; selB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..634
FT                   /note="Selenocysteine-specific elongation factor"
FT                   /id="PRO_0000091473"
FT   DOMAIN          1..173
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          9..16
FT                   /note="G1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          37..41
FT                   /note="G2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          59..62
FT                   /note="G3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          114..117
FT                   /note="G4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   REGION          149..151
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   BINDING         9..16
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         59..63
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         114..117
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   634 AA;  70128 MW;  7616465454A67219 CRC64;
     MPVIMGTAGH IDHGKTSLIK ALTGINCDRL AEEQKRGITI ELGFAYLDLT PEVRLGIIDV
     PGHERFVKNM VSGAAGIDFV LLVIAADEGI MPQTREHLEI CSLLGIRAGL VALTKTDMVE
     EDWLELVHEE VQTYLAGSFL EGAPIVPVSA HTGAGLEELK GYIAELSSTF APDRRSDLFR
     LPVDRVFTMK GHGTVVTGTS ISGALRLGEE IEIVPSGHRS KVRGLQVHGT AAEVARAGER
     TAVNLYGLEV AELERGEVLA HPQTLFPSPV WDVEMTCLSS SPNPLKHRTE VHFHHGSREI
     LAKLFFLDRD KLEPGETAVC QVRFPRPLPG VYGDRCIVRS FSPLQTVAGG RIINPLGRKV
     RRHSKDMETL STLGAATGEE LLLAQLRLAG RGGLTVAELR IMTDMESKLL DKTLQILGGK
     QLAFQFDRDD KRFVGADVLD GLAGACLEYL GEYHRREPMR QGLSRAELIS GFGRGMHPKL
     VHFLVERLVK SGQVLLEADI LRLPGHVVSL ASDQSGLRTL METTYVQAGL MPPTTKAFLE
     ENGLTAKDVA QMFRLLMEEG VLIKVSEEFY YAKTAMDEII GRVRSFFESN QEMGPQDFRD
     LTELTRKFAI PVLEYLDKEK ITMRIGDKRQ IRKR