ID A0A942YVG2_9BACI Unreviewed; 628 AA.
AC A0A942YVG2;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 16.
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:MBS4211501.1};
GN ORFNames=KHA99_03390 {ECO:0000313|EMBL:MBS4211501.1};
OS Neobacillus rhizophilus.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Neobacillus.
OX NCBI_TaxID=2833579 {ECO:0000313|EMBL:MBS4211501.1, ECO:0000313|Proteomes:UP000679749};
RN [1] {ECO:0000313|EMBL:MBS4211501.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FJAT-49825 {ECO:0000313|EMBL:MBS4211501.1};
RA Liu G.;
RT "Novel Bacillus species.";
RL Submitted (MAY-2021) 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:MBS4211501.1}.
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DR EMBL; JAGYPF010000001; MBS4211501.1; -; Genomic_DNA.
DR RefSeq; WP_213116011.1; NZ_JAGYPF010000001.1.
DR AlphaFoldDB; A0A942YVG2; -.
DR Proteomes; UP000679749; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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; IPR005225; Small_GTP-bd.
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 NCBIfam; TIGR00231; small_GTP; 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 Elongation factor {ECO:0000313|EMBL:MBS4211501.1};
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:UP000679749}.
FT DOMAIN 3..174
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 628 AA; 71893 MW; 6D0D7EB9AA445F51 CRC64;
MEKRYFTIGM AGHIDHGKTS LTKALTNVDT DRLKEEKERQ ISIELGFAPL YEDEEIQISV
IDVPGHERFI RQMIAGVAGI DLVVLVVAAD EGVMPQTKEH LEILKFLGVK NGIIAITKID
RVDEEFIELV KDDILAELQG TVFEAAPFVL IDSLSKKGIE EIKQLIIKKL KEQEMRDAKG
AFRLPIDQVF TVKGQGTVVR GTVYEGTVEE GQALKVMPKG LEVRARQIQV HHKPSPKAYA
GQRAAINLSG VSKEDLERGE VLVSSEHFIV TRIIDVAIRV VEELEHLIKQ RMPIKLHIGT
AEVMGRIVFF DRNEIKEENG EILCQLRLEE EILTKRGDRF ILRRPSPTET IGGGWVIDPR
GNKYRFGEQT IGELEKKKVG TPKERITAAL LEAKSLTLPE LIKRTALDEE TLSEHLQNDE
FVLFNGKEYT LQQLIQSIEE DIYDRLQDFH QQNSMKQGIN KAEILQSMQK KFSKSLLDYV
VENAISKKVF YRREQFVWLA EFSPHVPKNW AKRTENLLAE LKKDELKVRY LKDYLSAAGI
PDTLEGDLRR FLEDQELIVL LDDQFAYHGD VFKEAVYQLQ SATGLEFEVG EAKEVLELSR
KYMIPFLEKL DAKGYTKRVE NKRVWKNK
//
