ID A0A810QHT0_9FIRM Unreviewed; 639 AA.
AC A0A810QHT0;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 20.
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:BCK85667.1};
GN ORFNames=MM59RIKEN_29860 {ECO:0000313|EMBL:BCK85667.1};
OS Pusillibacter faecalis.
OG Plasmid pMM59_01 {ECO:0000313|EMBL:BCK85667.1,
OG ECO:0000313|Proteomes:UP000679848}.
OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
OC Oscillospiraceae; Pusillibacter.
OX NCBI_TaxID=2714358 {ECO:0000313|EMBL:BCK85667.1, ECO:0000313|Proteomes:UP000679848};
RN [1] {ECO:0000313|EMBL:BCK85667.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MM59 {ECO:0000313|EMBL:BCK85667.1};
RC PLASMID=pMM59_01 {ECO:0000313|EMBL:BCK85667.1};
RA Kitahara M., Shigeno Y., Shime M., Matsumoto Y., Nakamura S., Motooka D.,
RA Fukuoka S., Nishikawa H., Benno Y.;
RT "New species isolated from human feces.";
RL Submitted (SEP-2020) 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; AP023421; BCK85667.1; -; Genomic_DNA.
DR RefSeq; WP_213543727.1; NZ_AP023421.1.
DR AlphaFoldDB; A0A810QHT0; -.
DR KEGG; pfaa:MM59RIKEN_29860; -.
DR Proteomes; UP000679848; Plasmid pMM59_01.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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:InterPro.
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; 1.10.10.2770; -; 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; 1.
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 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; 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; 2.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Plasmid {ECO:0000313|EMBL:BCK85667.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000679848}.
FT DOMAIN 1..177
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 639 AA; 69823 MW; DBB804CE57E8714D CRC64;
MKHVVIGTAG HVDHGKTELI RALTGIDTDR LPEEKARGLT IEPGFAHLDF EDGSQSGIVD
VPGHEKFIHH MLCGAAGMDF VMLVVAADEG WMPQTAEHLE ILSLLGLREG LVVLTKADLV
NADRLLAAER EAREQVRGTF LDGKPVTAVS ARTGHGIPGL RSLLQNMVQR VQERNPLLSF
RLPIDRVFTV EGFGTVVTGT LLEGRIRCRG VAELAPSGRA TRVRGLQVHG RDVWEAEAGQ
RVAVNLAGVK KRELHRGDTL VAPGSLPASL TADVRLQLLP SSRRTIRTGT QVHLYHGASA
YLARVVLLEC GVLHPGESAY AQLRLAEPFA ARCGDRFVIR FLSPLETIGG GVILDPLPCR
HKRGDPAVLS ALTVLEKGDG AQRILQVLAA GGMPALAELS KALALPPDSL NSELRPLLSR
GEVLEPLPHR YLSAAALEQF RIRCCGILER YHTAQPLHSG IRPAELRQKA LASLDADAAN
AVLSMLVQLG ELQRAGERYA LPGFQVRLTR RQSTIRETLL ALCEKSSAKA VKSEDLLRGF
SLRDQADCRQ VLESLLTGGE LIPLTQGLLC SAAEMRRCRQ TAEAWFTAHE TLTLAQFRDL
LGSSRDYALL VLEFWDRQGL TQREGNARRL VSDSFFTWE
//
