ID A0A418ZSJ8_9RHOB Unreviewed; 630 AA.
AC A0A418ZSJ8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JAN-2026, entry version 27.
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:RJL00506.1};
GN ORFNames=D3P06_13350 {ECO:0000313|EMBL:RJL00506.1};
OS Paracoccus aestuarii.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Paracoccaceae; Paracoccus.
OX NCBI_TaxID=453842 {ECO:0000313|EMBL:RJL00506.1, ECO:0000313|Proteomes:UP000285530};
RN [1] {ECO:0000313|EMBL:RJL00506.1, ECO:0000313|Proteomes:UP000285530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19484 {ECO:0000313|EMBL:RJL00506.1,
RC ECO:0000313|Proteomes:UP000285530};
RA Jurado V., Gutierrez-Patricio S., Gonzalez-Pimentel J.L., Laiz L.,
RA 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:RJL00506.1}.
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DR EMBL; QZEV01000078; RJL00506.1; -; Genomic_DNA.
DR RefSeq; WP_119887016.1; NZ_CP067171.1.
DR AlphaFoldDB; A0A418ZSJ8; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000285530; 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 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:RJL00506.1};
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:UP000285530}.
FT DOMAIN 1..169
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 630 AA; 66700 MW; E9C4584015DFBCC0 CRC64;
MIVGTAGHID HGKTALVRAL TGTDADRLAE EKARGITIDL GFAYAALGGG GVTGFVDVPG
HERLIHTMLA GAGGIDLALL VVACDDGVMP QTREHLAILD LLGLSRGLVA MTKADLADAD
RRAQVTAQIR EALAGGGLAD APIIPVSSVT GEGIAVLRNA LIRAEGAQAR RATDAGFRLA
VDRSFTLQGA GTVITGTVLS GRVAVGDAVT LGPSGIAARV RAIHAQSRPA TEGLAGQRCA
LNLAGEAVSK DAIHRGDIVQ APALHAPTDR IDAVLTVLPS EPKPIGTWFP ARMHSHAAEA
GARIVPLGDP IPPGGSGPVQ IVLDRPLAAT IGDRFILRDV SASRTIGGGH LLDLRPPARK
RRTPERLALI AAAGAPDPLA AMLAVAPVDL GVFARDRAMP PDQARAALAR AGGTVLAGLA
LSPAQLEALR TGIAAQLAAF HADNPDLPGL GRERLRLSLT PRLPKDPWLA LLRAEAEAGR
ILPDGAFLRL PGHEVRLSPD DEAIWDRIQP ALLGDLRYRP PRVRDFATEF GADEKDIRRI
LRLTQRLGRT DQIAHDHFFA RRVTADMVAI LRDVAAATDD GWFTAPQFRD RVRNGRKVAI
EILDFFDRHG VTLRRGDLRR LNPHRLDLFG
//
