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Database: UniProt
Entry: A0A4Q9G5C6_9RHOB
LinkDB: A0A4Q9G5C6_9RHOB
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ID   A0A4Q9G5C6_9RHOB        Unreviewed;       673 AA.
AC   A0A4Q9G5C6;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   28-JAN-2026, entry version 29.
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:TBN43813.1};
GN   ORFNames=EYE42_01360 {ECO:0000313|EMBL:TBN43813.1};
OS   Paracoccus subflavus.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rhodobacterales; Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=2528244 {ECO:0000313|EMBL:TBN43813.1, ECO:0000313|Proteomes:UP000293520};
RN   [1] {ECO:0000313|EMBL:TBN43813.1, ECO:0000313|Proteomes:UP000293520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GY0581 {ECO:0000313|EMBL:TBN43813.1,
RC   ECO:0000313|Proteomes:UP000293520};
RA   Zhang G.;
RT   "Paracoccus subflavus sp. nov., isolated from marine sediment of the
RT   Pacific Ocean.";
RL   Submitted (FEB-2019) 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:TBN43813.1}.
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DR   EMBL; SISK01000001; TBN43813.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Q9G5C6; -.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000293520; 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   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   InterPro; IPR048931; WHD_2nd_SelB_bact.
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; 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; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Elongation factor {ECO:0000313|EMBL:TBN43813.1};
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:UP000293520}.
FT   DOMAIN          1..168
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          646..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   673 AA;  71735 MW;  2A55BE7928967152 CRC64;
     MIVGTAGHID HGKTALVKAL TGTDADRLAE EKARGITIDL GFAYADLGGG SVTGFVDVPG
     HERLIHTMLA GAGGIDMALL VVAADDGVMP QTREHMAILD LLGIGRGIVA LTKADLADDA
     RRQAVAAEIR ETLADTVLAD APILPVSSLT GEGLDALRAA LIDAETQTVA RRADGPMRLA
     VDRSFTLSGA GTVVTGTMLT GRVALGDQVV VSPTGLPARV RAIHAQNRPA AEGVAGQRCA
     LNLAGEAISK GAIHRGHVVL SPALHAPTDR IDAWLTVLPG EPKPIGTWFP ARLHSHAVEA
     GARIVPLADP IRPGRGGPVQ IVLDRPIAAA VHDRFILRDV SASRTIGGGR FLDLRPPARK
     RRSPERLALI GAAQADDPAK ALAAMLTVTS VDLPGFARDR SLSVPAIAAT VAAADAVTIG
     DLAIGRDALA RLRDGLTTAL AHFHEDNPDL PGMGRERLRL MLQPRMPKDA FLAFLRTEAD
     AGRALPDGAF VRLPGHEVRL TPEDEALWQR IGPALLGEMR FRPPRVRDLA TDFGIDERDV
     RRVLKLTQRL GRTDQIAHDH FFARAVTAEM VAIIHDVAAQ AENGWFTAPA FRDRVQNGRK
     VAIEILDFFD RHGLTLRRGD LRRINPHRAD LFGDLGRESS PVGRPVFKTG WGSEPVPGGF
     DSHSLPPESQ GQE
//
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