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Database: UniProt
Entry: A0A419A8B9_9RHOB
LinkDB: A0A419A8B9_9RHOB
Original site: A0A419A8B9_9RHOB 
ID   A0A419A8B9_9RHOB        Unreviewed;       671 AA.
AC   A0A419A8B9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   28-JAN-2026, entry version 26.
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:RJL18167.1};
GN   ORFNames=D3P05_08030 {ECO:0000313|EMBL:RJL18167.1};
OS   Paracoccus siganidrum.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rhodobacterales; Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1276757 {ECO:0000313|EMBL:RJL18167.1, ECO:0000313|Proteomes:UP000283587};
RN   [1] {ECO:0000313|Proteomes:UP000283587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26381 {ECO:0000313|Proteomes:UP000283587};
RA   Jurado V., Gutierrez-Patricio S., Gonzalez-Pimentel J.L., Miller A.Z.,
RA   Laiz L., Saiz-Jimenez C.;
RT   "Paracoccus onubensis nov. sp. a moderate halophilic bacterium isolated
RT   from Gruta de las Maravillas (Aracena, Spain).";
RL   Submitted (SEP-2018) 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}.
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:RJL18167.1}.
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DR   EMBL; QZEW01000027; RJL18167.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A419A8B9; -.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000283587; Unassembled WGS sequence.
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   FunFam; 3.40.50.300:FF:001064; Selenocysteine-specific translation elongation factor; 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:RJL18167.1};
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:UP000283587}.
FT   DOMAIN          1..171
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          643..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   671 AA;  71101 MW;  1B72801E15DCB63A CRC64;
     MIVGTAGHID HGKTALVKAL TGTDADRLAE EKARGITIDL GFAYADLGGG GITGFVDVPG
     HERLIHTMLA GAGGIDLALM VVAADDGVMP QTREHLAILD LLGIARGIVA LTKADLVDAA
     RRQQVAAQIR EALAPTGLRD APVIPVSALT GEGIADLRAA LAAAEAQTTA RHASGPFRLA
     VDRSFTLAGA GTVVTGTVLT GRIGLGDSVT ISPQGIAARI RAIHAQNRPA DQGLAGQRCA
     LNLAGEAVTK QAIGRGDVVL TPGLHAPTDR IDAQLAVLGT EPKPVGTWFP ARLHSHAVEL
     GARIVPLGDP LHPGTSGPVQ IVLERPIAAA VGDRFILRDS SASRTIGGGH FLDLRAPARK
     RRTPERLALI AAADHADPAE ALAALLSVTP VGIAAFARDR SLSEDDMTAA LDRVGAVSIG
     GLALSVEAHQ ALREGLTATL AAFHADNPDL PGMGREKCRL MLRPRLPKQP WLALLHREAA
     DGRIVLDGAF LRLPGHEVRL SPEDEALFAR ILPALRGDTR FRPPRVRDFA AEFGIDEAEI
     RRVLKLTQKL GRTDQIAQDH FFAREVTAEM VAIIRDVAGA TADGWFTAPA FRDRVQNGRK
     VAIEILDFFD RHGVTLRRGD LRRINPHRAD LFGTHGWESS PVGRPDFNSG WGSEPVPGGF
     DSHSLPPARR E
//
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