ID A0AA41X3G3_9BACI Unreviewed; 625 AA.
AC A0AA41X3G3;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 28-JAN-2026, entry version 11.
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:MCP8968032.1};
GN ORFNames=NK662_05695 {ECO:0000313|EMBL:MCP8968032.1};
OS Ectobacillus ponti.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Ectobacillus.
OX NCBI_TaxID=2961894 {ECO:0000313|EMBL:MCP8968032.1, ECO:0000313|Proteomes:UP001156102};
RN [1] {ECO:0000313|EMBL:MCP8968032.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SYSU M60031 {ECO:0000313|EMBL:MCP8968032.1};
RA Li W.-J., Deng Q.-Q.;
RL Submitted (JUL-2022) 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:MCP8968032.1}.
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DR EMBL; JANCLT010000002; MCP8968032.1; -; Genomic_DNA.
DR RefSeq; WP_254757933.1; NZ_JANCLT010000002.1.
DR AlphaFoldDB; A0AA41X3G3; -.
DR Proteomes; UP001156102; Unassembled WGS sequence.
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: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; 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; 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; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:MCP8968032.1};
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:UP001156102}.
FT DOMAIN 2..172
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 605..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 625 AA; 68585 MW; F43416748756D781 CRC64;
MQKHFTVGLA GHVDHGKTTL TKALTGVDTD RLKEEKERQI SIEPGFAPLH LEQGIVSIVD
VPGHERFIRQ MIAGVSGIDL MLLVVAADEG VMPQTREHLD ILKLLGVGQG IVVMTKVHAM
PEDLRELVEE EIREALQGTV FADAPILQVD SLDGTGIVEV KSAIAARLAE TKERNHTVPF
RMSIDQVFTI KGSGTVVRGT VTEGIVREGE HLSLLPVGTE VRVRQVQVHG QAQTEARAGQ
RAALNLAGLG KDEVARGDVL AAPDTCPVTE VVDVRVDWLA EVQHGIKQRS LVKCHMGTAE
VMAKVVFFDR NEAEGGQEGV LCQLRLEQPV ASKRGDHFIL RRPSPVETLG GGTVIDPQGG
KYRFGQETVE QLARKLEGTP MERIQAVLQR EKLLEKRELL ALASITEAEL EEANLIAISA
AFTSQAVAAE AAAALQAEVG AYHENHPMRP GISKAQLLER VPYPKRLLEQ VLPQACEVIG
QHVALHNFIP HFPGKWAKRM ERALETLRQD GFEAKLWDVY MKEAGIPQPE AEELSHYLLR
TGQLYLLDKQ PVSAEVLQDG IAKLRAASGA SFSIQEAKDV LGLSRKTAIP FLELLDNLGL
TERKENRREW RESHEGAFAP AAARP
//
