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Database: UniProt
Entry: W0V624_9BURK
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Original site: W0V624_9BURK 
ID   W0V624_9BURK            Unreviewed;       646 AA.
AC   W0V624;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   28-JAN-2026, entry version 54.
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:CDG82717.1};
GN   ORFNames=GJA_2082 {ECO:0000313|EMBL:CDG82717.1};
OS   Janthinobacterium agaricidamnosum NBRC 102515 = DSM 9628.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=1349767 {ECO:0000313|EMBL:CDG82717.1, ECO:0000313|Proteomes:UP000027604};
RN   [1] {ECO:0000313|EMBL:CDG82717.1, ECO:0000313|Proteomes:UP000027604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 102515 / DSM 9628 {ECO:0000313|Proteomes:UP000027604};
RX   PubMed=25883287; DOI=10.1128/genomeA.00277-15;
RA   Graupner K., Lackner G., Hertweck C.;
RT   "Genome Sequence of Mushroom Soft-Rot Pathogen Janthinobacterium
RT   agaricidamnosum.";
RL   Genome Announc. 3:e00277-e00277(2015).
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; HG322949; CDG82717.1; -; Genomic_DNA.
DR   RefSeq; WP_038491512.1; NZ_BCTH01000028.1.
DR   AlphaFoldDB; W0V624; -.
DR   STRING; 1349767.GJA_2082; -.
DR   KEGG; jag:GJA_2082; -.
DR   PATRIC; fig|1349767.4.peg.3846; -.
DR   eggNOG; COG3276; Bacteria.
DR   HOGENOM; CLU_023030_2_0_4; -.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000027604; Chromosome I.
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; 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; IPR031157; G_TR_CS.
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   InterPro; IPR048931; WHD_2nd_SelB_bact.
DR   NCBIfam; TIGR00475; selB; 1.
DR   PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR   PANTHER; PTHR43721:SF9; GTP-BINDING PROTEIN 1; 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; PF21214; WHD_2nd_SelB_bact; 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; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Elongation factor {ECO:0000313|EMBL:CDG82717.1};
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:UP000027604}.
FT   DOMAIN          1..172
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   646 AA;  69122 MW;  5150DACC2747ED9A CRC64;
     MIVGTAGHID HGKTTLTRAL TGVHTDRLKE EQARGISIEL GYAYLPLADG TVLGVIDVPG
     HEKFIRTMAA GVTGIDFALL VVAADDGVMP QTREHLAILR LLGVVRGAVA LTKIDRVDGE
     RAAQVELDIR ALLADTALAG APVFGVAATR DGDPGVAALL AHLSRQARDL PRRDERRLFR
     LGVDRVFTLP GQGTIVTGTA LAGRVKVGDT LQLAPGGQTS RVRSIHAQNR AADSGLAGQR
     LALNLGGIAR EDIERGNWMV APALAACSER IDAELTLLPD CGLTLKPWSP LHVHLGAAHQ
     VARVVMLDGE QLAPGQRGRV QLVFDTPLHA VPGDRFVVRN PQATLTVGGG LVLDPFGPAR
     KRRSPARHAW LDALAAFIAH DDYAALLALS PSGLRLSLLL RLSQLPAEHI ALPPDTRKIG
     LRGDDTLLLS PASFEVLGQR IVQALDGFHQ RAPDEAGPEL WRLKRIVDSD MEDALWSALV
     ADLLERGDLR QRGASLHLPS HSVELRPEEQ AVAGRLLAAL EQGAFDPPWV RDLGRQFALE
     EGETRRLLRK LAKAGQVSQI VPDLFYHPAA LARLAQLVAS LAAGAEQAGA QPGAGAVGAA
     AFRDACGLGR KRAIQVLEFF DRVGYTRRVG NGHLLRPHAA WSYRAA
//
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