ID A0A6L6J6F1_9RHOB Unreviewed; 625 AA.
AC A0A6L6J6F1;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
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:MTH66357.1};
GN ORFNames=GL284_19040 {ECO:0000313|EMBL:MTH66357.1};
OS Paracoccus shanxieyensis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Paracoccaceae; Paracoccus.
OX NCBI_TaxID=2675752 {ECO:0000313|EMBL:MTH66357.1, ECO:0000313|Proteomes:UP000478740};
RN [1] {ECO:0000313|EMBL:MTH66357.1, ECO:0000313|Proteomes:UP000478740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK608 {ECO:0000313|EMBL:MTH66357.1,
RC ECO:0000313|Proteomes:UP000478740};
RA Dong K.;
RL Submitted (NOV-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:MTH66357.1}.
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DR EMBL; WMII01000029; MTH66357.1; -; Genomic_DNA.
DR RefSeq; WP_155046073.1; NZ_WMIH01000029.1.
DR AlphaFoldDB; A0A6L6J6F1; -.
DR Proteomes; UP000478740; 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; ELONGATION FACTOR TU-RELATED; 1.
DR PANTHER; PTHR43721:SF11; SELENOCYSTEINE-SPECIFIC ELONGATION FACTOR; 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:MTH66357.1};
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:UP000478740}.
FT DOMAIN 1..170
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 625 AA; 67272 MW; 1FFA390C30606EF4 CRC64;
MIVGTAGHID HGKTALVKAL TGVDADRLAE EKARGITIDL GFAYADLGGG AITGFIDVPG
HEKFVHTMLA GAGGIDLALL VIAADDGIMP QTREHLAILD LLGIGRGIVA LTKADLADAD
RLATLGTDIH DLLAGTTLAG SRVIPVSSLS GAGIDVLRDA LAQAEAATLA RATDRRFRMA
IDRSFTISGA GTVVTGTVLS GRVQVGDQIT ISPLGAAARV RGIHAQNRKA DAGLAGQRCA
LNLTGPTHHD IHRGDVALDP LLDAPTQRID VLLRVLASEP KALTTWFPAR LHLGASEIGA
RIVPLQGPLQ PGDTGLAQIV LDRPVAATVQ DRFILRDVSA RRTIGGGSLI DLRPPARRRS
RPERLAVLAA MQDSLPKLAD LALVDLDAHA RDHALVASDT TGVALLPGTH QALSPRLLAA
LRQKMQDELA TYHAENPDLQ GMGREPLRMI LTPRIAKPDF TAFLRAEAAA GLIALDGAFI
RLPQHLPRLS DTDETILAQI LPMLRGDARF RPPRVRDLAH DLSADEAEIR RILRMAARQG
RIDQIAHDHF FTRDTTIEMI RILRELPQQD GWFTAPDFRD RTQNGRKVAI QILDFFDKLG
LTLRRGDLRR INPHRMDLFA ADGSD
//
