ID J2X0W4_9PSED Unreviewed; 635 AA.
AC J2X0W4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=PMI35_06149 {ECO:0000313|EMBL:EJN18380.1};
OS Pseudomonas sp. GM78.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144337 {ECO:0000313|EMBL:EJN18380.1, ECO:0000313|Proteomes:UP000007302};
RN [1] {ECO:0000313|EMBL:EJN18380.1, ECO:0000313|Proteomes:UP000007302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM78 {ECO:0000313|EMBL:EJN18380.1,
RC ECO:0000313|Proteomes:UP000007302};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJN18380.1}.
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DR EMBL; AKJF01000205; EJN18380.1; -; Genomic_DNA.
DR RefSeq; WP_008065518.1; NZ_AKJF01000205.1.
DR AlphaFoldDB; J2X0W4; -.
DR PATRIC; fig|1144337.3.peg.5954; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000007302; Unassembled WGS sequence.
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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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; IPR004161; EFTu-like_2.
DR InterPro; IPR015190; Elong_fac_SelB-wing-hlx_typ-2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR048931; SelB_WH_3rd.
DR InterPro; IPR015191; SelB_WHD4.
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 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; PF21214; bact_SelB_WH_2nd; 1.
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; 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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Elongation factor {ECO:0000313|EMBL:EJN18380.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:EJN18380.1}.
FT DOMAIN 1..172
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 635 AA; 69800 MW; 54FB02642F27FE17 CRC64;
MIVGTAGHID HGKTALLEAL TGQAGDRRRE ERERGMTIDL GYLYTALEPG AALTGFIDVP
GHERFTHNML AGAHGIDLVL LVVAADDGVM PQTREHLAIV ELLGIPRAIV AITKCDRVEP
SRVQAVREQI ATLLAPGSYA EAPLIALSSV TGEGVQTLRQ ALLMAQSEVR QRSQDGGFRL
AIDRAFSVPG AGIVVTGTAL SGQVTVGDSL VLGPLGKTVR VRGLHAQNQP ANVAVAGQRV
ALNLSAERLA LSQIHRGQWL SAPWLHAPTQ RLDIDLQLLP GESRAFEHFE PVHVHLGTRD
VTGRVALLEG SSLAPGQRMF AQLLVNAPVQ AVLGDRLILR DQSAQRTLGG GKVLDPFAPS
RHRRSPERLA QLVALAASTR LEDVLPGLLA NSDSGLDPQQ LERQFNRPRD TWVLPGDIRL
IETRQAPVLF SASRWQALQD ELQQHLARFH EQEPDHMGPD RDRLCRFAGS TLDRPVFISL
LEQLLANGRI VASGPWLHLP GHQVRLSDEE QALWQKLQPR FDAAGFDPPW VRDLGHDEAT
VRALLRKMAR LGLLHAVVRD LFYTDTMIRR LAAMLLQLAD DNPVIEVAAF RDAVGLGRKR
SIQILEYFDR LGLTRRVGDR RQIRADNALA RRSRD
//
