ID Q931D5_RHIME Unreviewed; 666 AA.
AC Q931D5;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 28-JAN-2026, entry version 137.
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:AAK64665.1};
GN ORFNames=SMa0015 {ECO:0000313|EMBL:AAK64665.1};
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymA {ECO:0000313|EMBL:AAK64665.1,
OG ECO:0000313|Proteomes:UP000001976}.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834 {ECO:0000313|EMBL:AAK64665.1, ECO:0000313|Proteomes:UP000001976};
RN [1] {ECO:0000313|EMBL:AAK64665.1, ECO:0000313|Proteomes:UP000001976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021 {ECO:0000313|EMBL:AAK64665.1,
RC ECO:0000313|Proteomes:UP000001976};
RC PLASMID=Plasmid pSymA {ECO:0000313|Proteomes:UP000001976};
RX PubMed=11481432; DOI=10.1073/pnas.161294798;
RA Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F.,
RA Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L.,
RA Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C.,
RA Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A.,
RA Long S.R.;
RT "Nucleotide sequence and predicted functions of the entire Sinorhizobium
RT meliloti pSymA megaplasmid.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).
RN [2] {ECO:0000313|Proteomes:UP000001976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021 {ECO:0000313|Proteomes:UP000001976};
RC PLASMID=Plasmid pSymA {ECO:0000313|Proteomes:UP000001976};
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
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; AE006469; AAK64665.1; -; Genomic_DNA.
DR PIR; G95262; G95262.
DR RefSeq; WP_010967006.1; NC_003037.1.
DR AlphaFoldDB; Q931D5; -.
DR EnsemblBacteria; AAK64665; AAK64665; SMa0015.
DR KEGG; sme:SMa0015; -.
DR PATRIC; fig|266834.11.peg.7; -.
DR HOGENOM; CLU_023030_3_0_5; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000001976; Plasmid pSymA.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-EC.
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; 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; 3.
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; 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: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; 3.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:AAK64665.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Plasmid {ECO:0000313|EMBL:AAK64665.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000001976}.
FT DOMAIN 1..170
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 639..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 666 AA; 72432 MW; CE9B3E079C947061 CRC64;
MIVGTAGHID HGKTTLVKAL TGVDTDRLKE EKARGITIDL GFAYARFAKD AVTGFVDVPG
HERFIHTMLA GAGGIDYAML VVAADDGIKP QTLEHLAILD LLGVSRGLVA ITKADLADPA
RLENLTDEIG AVLSSTSLRD AEILPVSVAA GQGIELLKER LAAAECATAA SAVGGRFRLA
VDRSFTLSGA GTVVTGTVLS GSVGVGDQVT VSPAGRSARV RSIHAQNQRA ERGFAGQRCA
LNLAGEGISK DAITRGDMVV DPHLHAPSDR LDADLSVLES ETKPIGEWFS ARFHHASAET
GIRIVPLEGP LLPGERRRVQ LVLDRPIAAA VGDRFILRDV SARRTIGGGR LLDLRAPARK
RRSPERLSYL QAASLSHAGE ALAALLDVPP FLVDLDVFAR DRALSEAELQ NAIRSASAEV
IEGSAVRHAL SKRQRAAFSD EVQRVLSAFH VENPDLQGIG RERLRLQVTP RLPPPAFLVA
LRAEQTAGRL VLEGAFVRLP GHEVRLSEKE EELYARILPH LEGEERFRPP RVRDFAEALG
VDEREIRRIL KLCARLGRVD QIRHDHFFTR QTTAEMVAII RQVAANAERG EFSAGLFRDR
VNNGRKVAIE ILEFFDRQGV TIRHGDVRRV NPHRLDLYEG PVPEADEGRG SSPVERPDFK
FYRAGS
//
