ID A0A344PHR2_9RHOB Unreviewed; 667 AA.
AC A0A344PHR2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-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:AXC48917.1};
GN ORFNames=DRW48_03675 {ECO:0000313|EMBL:AXC48917.1};
OS Paracoccus suum.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Paracoccaceae; Paracoccus.
OX NCBI_TaxID=2259340 {ECO:0000313|EMBL:AXC48917.1, ECO:0000313|Proteomes:UP000252023};
RN [1] {ECO:0000313|Proteomes:UP000252023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2-6 {ECO:0000313|Proteomes:UP000252023};
RA Heo J., Kim S.-J., Kwon S.-W.;
RT "Genome sequencing of Paracoccus sp. SC2-6.";
RL Submitted (JUL-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}.
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DR EMBL; CP030918; AXC48917.1; -; Genomic_DNA.
DR RefSeq; WP_114075236.1; NZ_CP030918.1.
DR AlphaFoldDB; A0A344PHR2; -.
DR KEGG; pars:DRW48_03675; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000252023; Chromosome.
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 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:AXC48917.1};
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:UP000252023}.
FT DOMAIN 1..170
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 637..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 667 AA; 70205 MW; 69EA310E978D1019 CRC64;
MIVGTAGHID HGKTALVLAL TGTDTDRLAE EKARGITIAL GFAYTDLGNG RITGFVDVPG
HKRLVHAMVA GAGGINLGLL VVAADDGIMP QTREHLAILD LLGVPRLVVA LTKADRVPAA
RITAVTAEIN ALLAPTSLTG APALPVSALT GEGIAALRAI LAAQDVAPPQ QGRGFRLAVD
RSFTLSGAGT VVTGTVHSGS IAAGASVVVS PTGLAARVRE LRAENQAVAT AVAGQRVALN
LAGPAITREA IRRGDEIVDP SLHAPTARID ATLRLLASEI APLRSGAQVH LHTATAEAVA
RVVPLGAAAL PGGPAAWVQL VLDRPIATSW GRRYILRDAS GQRTLGGGQF IDLRPPARKR
ATAARRAALM ASLPPVPAEA LSAQLELPGG SVDLDNFIRD RALTPGEGDA ALQATATVTI
GVAPQRLVLS AATIHSLRTA MSKRLQMFHV EHPDLPGIAA ERLRLSLTPR LPASAFATLL
KAEAARGALH LKGGFVALPS HAPTLTPPDE ALFTRIAPAL LGEGRFRPPR VRDFATELSE
DEDNLRRILR LAARMGRVDQ IARDHFFDRA VTSEMVQIAR ALSEAAPTGW FAAPAFRDQL
RNGRKVAIEI LDFFDRHRIT YRRGDLRRIN PLRADLFAAE QPSDDTTTRA PDGGESSPVG
RPDFKSG
//
