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Database: UniProt
Entry: V8R682_9PSED
LinkDB: V8R682_9PSED
Original site: V8R682_9PSED 
ID   V8R682_9PSED            Unreviewed;       638 AA.
AC   V8R682;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   ORFNames=PMO01_13780 {ECO:0000313|EMBL:ETF07158.1};
OS   Pseudomonas moraviensis R28-S.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1395516 {ECO:0000313|EMBL:ETF07158.1};
RN   [1] {ECO:0000313|EMBL:ETF07158.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R28-S {ECO:0000313|EMBL:ETF07158.1};
RX   PubMed=24558233;
RA   Hunter S.S., Yano H., Loftie-Eaton W., Hughes J., De Gelder L.,
RA   Stragier P., De Vos P., Settles M.L., Top E.M.;
RT   "Draft Genome Sequence of Pseudomonas moraviensis R28-S.";
RL   Genome Announc. 2:e00035-14(2014).
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:ETF07158.1}.
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DR   EMBL; AYMZ01000006; ETF07158.1; -; Genomic_DNA.
DR   RefSeq; WP_024013043.1; NZ_CM002330.1.
DR   AlphaFoldDB; V8R682; -.
DR   PATRIC; fig|1395516.4.peg.2801; -.
DR   eggNOG; COG3276; Bacteria.
DR   HOGENOM; CLU_023030_2_0_6; -.
DR   Proteomes; UP000024771; 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: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:ETF07158.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:ETF07158.1}.
FT   DOMAIN          1..170
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   638 AA;  70117 MW;  6111094C89E99D1E CRC64;
     MIVGTAGHID HGKTSLLQAL TGQTGDRRPQ ERERGMTIDL GYLYAELAAG AGLTGFIDVP
     GHEKFTHNML AGAQGIDLVL LVVAADDGVM PQTREHLAIV ELLGIPRALV AITKCDRAGA
     GRVEEVQRQV LDLLAPGPFA DAPIFTVSSV NGQGVGELRA ALLRAHNEVQ ARGCEGGFRL
     AIDRAFSVPG AGIVVTGTAL SGTVAVGDKL VLGPAGKSVR IRGLHAQNQA AEQAFAGQRV
     ALNLSGDRLE LAQIHRGQWL LADWLHAPTQ RIDIDFQLLP GERTFEHFHP VHLHLGTQDV
     IARVALLQGP RLSPGERMFA QLLINAPVQA VKGDRLILRD SSAQRTLGGG TVLDPFAPAR
     QRRSPERLAQ LQTLALSVSL EQALPALLNH SPGGLEPQRL ERQFNRPRAQ WTLAENIRLI
     DTRQGPLLFN VQRWGQLKFT LLEQLARFHE QEPDQMGPDR DRLRRFSALA LERSTFISLL
     DELLNAGSIL ASGPWLHLPD HQVRLNADDE ILWQQLQPLF EQAGFDPPWV RDAAKMLGED
     DASVRLLLRK LARLGLMHQV VRDLFISDIV LRQMAALLLK LAEENPAIEV TTFRDALGLG
     RKRCIQYLEY FDRLGLTRRL GESRQIRPDN ALANACAP
//
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