ID A0A1H8E269_9RHOB Unreviewed; 635 AA.
AC A0A1H8E269;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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 ORFNames=SAMN04489859_1001148 {ECO:0000313|EMBL:SEN13535.1};
OS Paracoccus alcaliphilus.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Paracoccaceae; Paracoccus.
OX NCBI_TaxID=34002 {ECO:0000313|EMBL:SEN13535.1, ECO:0000313|Proteomes:UP000199054};
RN [1] {ECO:0000313|EMBL:SEN13535.1, ECO:0000313|Proteomes:UP000199054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8512 {ECO:0000313|EMBL:SEN13535.1,
RC ECO:0000313|Proteomes:UP000199054};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FODE01000001; SEN13535.1; -; Genomic_DNA.
DR RefSeq; WP_090610126.1; NZ_CP067124.1.
DR AlphaFoldDB; A0A1H8E269; -.
DR STRING; 34002.SAMN04489859_1001148; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000199054; 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; 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; IPR005225; Small_GTP-bd.
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; 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; 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:SEN13535.1};
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:UP000199054}.
FT DOMAIN 1..171
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 635 AA; 68493 MW; F2789A7F4084C96B CRC64;
MIVGTAGHID HGKTALIKAL TGTDTDRLAE EKSRGITIDL GFAYADLGGG AITGFVDVPG
HERLIHTMLA GAGGIDLALL IVAADDGVMP QTREHLAILD LLGITRGIVA LTKADLADDV
RLAEVETQLR QLLAPTGLRD APVFPVSSLT GSGIDALRKA VVQAEAETTA RQDAGLFRLA
VDRSFTLQGT GTVVTGTVLG GRVAIGDIVT VSPRGLTARV RGIHAQNQPA AEGLAGQRCA
LNLAGEAITK EAIHRGDVVL SPELHAPTDR IDAILDVLPT EAKPIGTWFP ARLHSHAVEA
GARIVPLGDP LRPGASGPVQ IVLDRPISAA VGDRFILRDT SSSRTIGGGR LLDLRGPARK
RRTPQRLALI SAAAHPDPAQ ALAALLKVAP VDIAGFARDR SLTTTQIHAV LEQSDAVEIG
GLALSAPTHR QLRDDLTDTL RRWHEEQPDL PGLGRERTRL ALQPRLPKEA FLAFLRDEAA
QGRIRLDGAF LRLPDHEVQL SPEDEALFAR ILPALTGDMR FRPPRVRDFA TEFGIDEGTI
RRVLKLTQKT GRTDQIAHDH FFAREVTAEM VSILHELAAE SPDGWFGAPA FRDRVQNGRK
VAIEILDFFD RHGLTLRRGD LRRLNPHRQD LFTKL
//
