ID A0A1W1H655_9BACT Unreviewed; 639 AA.
AC A0A1W1H655;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 28-JAN-2026, entry version 30.
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:SLM27916.1};
GN ORFNames=MTBBW1_120037 {ECO:0000313|EMBL:SLM27916.1};
OS Desulfamplus magnetovallimortis.
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
OC Desulfobacterales; Desulfobacteraceae; Desulfamplus.
OX NCBI_TaxID=1246637 {ECO:0000313|EMBL:SLM27916.1, ECO:0000313|Proteomes:UP000191931};
RN [1] {ECO:0000313|EMBL:SLM27916.1, ECO:0000313|Proteomes:UP000191931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRJEB14757 {ECO:0000313|EMBL:SLM27916.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-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; FWEV01000024; SLM27916.1; -; Genomic_DNA.
DR RefSeq; WP_080798873.1; NZ_LT828540.1.
DR AlphaFoldDB; A0A1W1H655; -.
DR STRING; 1246637.MTBBW1_120037; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000191931; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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; 2.
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; IPR015190; Elong_fac_SelB-wing-hlx_typ-2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015191; SelB_WHD4.
DR InterPro; IPR005225; Small_GTP-bd.
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 NCBIfam; TIGR00231; small_GTP; 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 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:SLM27916.1};
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:UP000191931}.
FT DOMAIN 1..176
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 639 AA; 71446 MW; C1EEC6B296EE9264 CRC64;
MKQIILGTAG HIDHGKTSLI RALTGIETDR LKEEIKRGIT IELGFASITL SDGNVIGIVD
VPGHEKFVKN MVAGASGIDL VSMVIAADEG VMPQTREHME ICTLMGIKHG FIAMTKIDLV
DEDLMELAMD DVREFTRGTF LEDAPVVPVS STKNLGLDLF RSTLEKICNE IPERPYSPIF
RLPVDRVFSM KGFGTVITGT LASGKIDVGE NIMVFPSRVT SKVRGIQVHG KSVESASSGT
RTAINFQGLD RENVNRGDIL STPDTLKPSY MVDAHLHFLS SNTKPAKART RVRFHSGTSE
IMGNVILLDR EELMPGSLAP VQIRLENPIC VMHGDHFVIR SYSPVRTIGG GHILNPFPGK
HKLFNQEIID GLNGLLDNDP QQNISFFSKM GRHNGVSFGE LRLMTPLPDK KLDGILQKML
ASRSLVLSDK EKRTYIHGEI FDALSNDVLK LLSAYHEENP LKEGISKEEL KSKFRAFKSK
DSKLFPLVTS RLVKDGNIVQ EGNTIRLATH KVALQVDLKA VKEKIAKIYE RDGLTPPFFR
TICSELEVDP KIARDVLQML IDEKRIVKTK DDLYFDIQAI KKIEAQLLEF LTRENEITTP
QFKDMTGISR KYVIPLIEYF DAINFTIRVG DTRQLRKKI
//
