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Database: UniProt
Entry: A0A327KTJ2_9HYPH
LinkDB: A0A327KTJ2_9HYPH
Original site: A0A327KTJ2_9HYPH 
ID   A0A327KTJ2_9BRAD        Unreviewed;       705 AA.
AC   A0A327KTJ2;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   28-JAN-2026, entry version 32.
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:RAI41274.1};
GN   ORFNames=CH338_03700 {ECO:0000313|EMBL:RAI41274.1};
OS   Rhodoplanes elegans.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Nitrobacteraceae; Rhodoplanes.
OX   NCBI_TaxID=29408 {ECO:0000313|EMBL:RAI41274.1, ECO:0000313|Proteomes:UP000248863};
RN   [1] {ECO:0000313|EMBL:RAI41274.1, ECO:0000313|Proteomes:UP000248863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11907 {ECO:0000313|EMBL:RAI41274.1,
RC   ECO:0000313|Proteomes:UP000248863};
RA   Lasarre B., Mckinlay J.B.;
RT   "Draft Genome Sequences of Select Purple Nonsulfur Bacteria.";
RL   Submitted (JUL-2017) 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:RAI41274.1}.
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DR   EMBL; NPEU01000021; RAI41274.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A327KTJ2; -.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000248863; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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; 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; 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: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; 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:RAI41274.1};
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:UP000248863}.
FT   DOMAIN          1..168
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          646..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..663
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..686
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   705 AA;  74946 MW;  4C5BA8F6B1A35A09 CRC64;
     MIVGTAGHID HGKTSLVRAL TGVDTDRLKE EKARGISIDL GFAYVPTPDG GVLGFVDVPG
     HERFVHTMVA GASGIDLVLL VVAGDDGVMP QTREHLAIVD LLGIRTGIVA LTKSDMVPPE
     RRAEATAEIA AALAGTGLAD APIVPVSSVT GEGIEALRAQ LFDAARAFGR REAGDKKFRL
     AVDRSFTLAG TGTVVTGTVL SGRVTVGDRV TVSPSGLSAR VRSIHAQNRP AGEGVAGDRC
     ALNLAGDQIS KEAIRRGDMV LDPTLHAPAD RIDVTLRLLP GEAKPPTQWM PVRLHHASAE
     VGARIVLLGD APPAPGREGR VQLVLETPIA AAAGDRFVLR DVSASRTIGG GRFLDLRGPA
     RKRRTPERVA QLDALALDDP GAALAALLAR PPAHVELTGF ARDHALADDA LARLVETLGI
     VRIADKDLLI GLAAPTWEAL TRDVVARLDA FHADNPDLPG VGLERLRLQI EPRLPAPAFR
     SVLQGLARAG AAVLDGAWVR RPGHAVRLSE AEELIWQRIA PTLGGAERFK PPRVRDLAGL
     FAIDEVLVRR VLRLTARTGR VDEVAHDHYF LRGTVAEMVT IARDLADQPS GVFTAAQFRD
     RLDNGRKVAI QILEFFDRHG VTLRRGDLRR MNKHRLDLFG SLPAGDAQAG EAAGAEPDAT
     AADADQHGRE SSPVGRPDFK SGRGREPVSG GFDSHSLPPS IRSAR
//
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