SELB_METJA
ID SELB_METJA Reviewed; 469 AA.
AC Q57918;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Selenocysteine-specific elongation factor;
DE AltName: Full=SelB translation factor;
GN Name=selB; OrderedLocusNames=MJ0495;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION.
RX PubMed=10860743; DOI=10.1006/jmbi.2000.3756;
RA Rother M., Wilting R., Commans S., Boeck A.;
RT "Identification and characterisation of the selenocysteine-specific
RT translation factor SelB from the archaeon Methanococcus jannaschii.";
RL J. Mol. Biol. 299:351-358(2000).
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:0000269|PubMed:10860743}.
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}.
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DR EMBL; L77117; AAB98485.1; -; Genomic_DNA.
DR PIR; G64361; G64361.
DR AlphaFoldDB; Q57918; -.
DR SMR; Q57918; -.
DR STRING; 243232.MJ_0495; -.
DR EnsemblBacteria; AAB98485; AAB98485; MJ_0495.
DR KEGG; mja:MJ_0495; -.
DR eggNOG; arCOG01564; Archaea.
DR HOGENOM; CLU_019148_1_0_2; -.
DR InParanoid; Q57918; -.
DR OMA; FGHIDHG; -.
DR PhylomeDB; Q57918; -.
DR Proteomes; UP000000805; 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; IBA:GO_Central.
DR GO; GO:0001514; P:selenocysteine incorporation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 2.40.10.190; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR038661; L35A_sf.
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 Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00475; selB; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..469
FT /note="Selenocysteine-specific elongation factor"
FT /id="PRO_0000091477"
FT DOMAIN 7..181
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 16..23
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 48..52
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 69..72
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 123..126
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 159..161
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 16..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 69..73
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 123..126
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 469 AA; 51849 MW; F3C1863CAAF04A92 CRC64;
MVISMEMKNV NVGLFGHIDH GKTQLAKQLT EIASTSALDK PKESQKRGIT IDLGFSSFTL
DRYRITLVDA PGHSELIRTA IGAGNIIDAA LLVVDAKEGP KTQTGEHLLV LDLLNIPTIV
VINKIDIAND EEIKRTEMFM KQILNSTINL KNSKIIKISA KTGEGIGELK KELKNLLDSL
DIKRDINSYL KMPIDHAFKI KGVGTVVTGT IHKGKVEVGD NLRILPINHE VKVKSIQCFK
QDVSIAYAGD RVGMALMGVE PESLFRGCIL TSEDTKLKVV DKFIAKVKIL ELFKYNLAPK
MKVHINIGLL TVPATIIPYK IEKINDKEEP IILEEIKGGD SCYCIFKLEE RVVVDEGDKI
LIMRLDLPPT TLRICGFGEV IDFGEVEVKK IVVKEGKVVK KKDKIYIEGL ASSKTAGEKL
IGGKVYIPDK NIWGVIKGTF GTKGALIAEF DEEVNGGEKV VLKRVRKWG
