ID A0A3D8PH61_9RHOB Unreviewed; 355 AA.
AC A0A3D8PH61;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 28-JAN-2026, entry version 28.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
DE Flags: Fragment;
GN Name=selB {ECO:0000313|EMBL:RDW14578.1};
GN ORFNames=DIE28_01575 {ECO:0000313|EMBL:RDW14578.1};
OS Paracoccus thiocyanatus.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Paracoccaceae; Paracoccus.
OX NCBI_TaxID=34006 {ECO:0000313|EMBL:RDW14578.1, ECO:0000313|Proteomes:UP000256679};
RN [1] {ECO:0000313|EMBL:RDW14578.1, ECO:0000313|Proteomes:UP000256679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SST {ECO:0000313|EMBL:RDW14578.1,
RC ECO:0000313|Proteomes:UP000256679};
RA Ghosh W., Rameez M.J., Roy C.;
RT "Whole genome sequencing of Paracoccus thiocyanatus SST.";
RL Submitted (MAY-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:RDW14578.1}.
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DR EMBL; QFCQ01000005; RDW14578.1; -; Genomic_DNA.
DR RefSeq; WP_115754376.1; NZ_QFCQ01000005.1.
DR AlphaFoldDB; A0A3D8PH61; -.
DR Proteomes; UP000256679; 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 Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR057335; Beta-barrel_SelB.
DR InterPro; IPR050055; EF-Tu_GTPase.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR027417; P-loop_NTPase.
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 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 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 PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:RDW14578.1};
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:UP000256679}.
FT DOMAIN 1..170
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 355
FT /evidence="ECO:0000313|EMBL:RDW14578.1"
SQ SEQUENCE 355 AA; 36825 MW; 8D7A716889FC9713 CRC64;
MIVGTAGHID HGKSALVRSL TGIETDRLAE EQARGITIEL GFAYADLGGG GVTGFVDVPG
HEKFVHTMLA GAGGIDLALL VVAADDGIMP QTREHLAILD LLGISRGMVA LTKSDLAPPD
RIAALTAEIA ELLAPTGLAG APVFPVSSLT GAGIDALRAA LVQAEAQTAA RAAEARFRMA
IDRSFTLAGA GTVVTGTVLS GRIAPGDHLV ISPRGLPARV RDIRAQNRKA EAGLAGQRCA
LNLAGDGVTR EAIHRGDVAL DPMLHAPTQR IDVMLRVLGS EPKPLATWFP ARLHLGAAET
GARIVPLEGP LAPGEEGLAQ LVLDRPLAAI LGERFILRDV SARRTIGGGR LIDLR
//
