ID A0A1G9CZ17_9FIRM Unreviewed; 631 AA.
AC A0A1G9CZ17;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 28-JAN-2026, entry version 30.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=SAMN05660472_01598 {ECO:0000313|EMBL:SDK56927.1};
OS Natronincola ferrireducens.
OC Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
OC Natronincolaceae; Natronincola.
OX NCBI_TaxID=393762 {ECO:0000313|EMBL:SDK56927.1, ECO:0000313|Proteomes:UP000198718};
RN [1] {ECO:0000313|EMBL:SDK56927.1, ECO:0000313|Proteomes:UP000198718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18346 {ECO:0000313|EMBL:SDK56927.1,
RC ECO:0000313|Proteomes:UP000198718};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNFP01000002; SDK56927.1; -; Genomic_DNA.
DR RefSeq; WP_090553106.1; NZ_FNFP01000002.1.
DR AlphaFoldDB; A0A1G9CZ17; -.
DR STRING; 393762.SAMN05660472_01598; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000198718; 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; IPR031157; G_TR_CS.
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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:SDK56927.1};
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:UP000198718}.
FT DOMAIN 1..174
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 631 AA; 71717 MW; 5983A59E6FBB8EBB CRC64;
MKNIVIGTAG HIDHGKTTLI KALTGRSTDR LKEEKKRGIS IELGFTHFDL PSGRRAGIID
VPGHEKFIKH MLAGVGGMDI VLLVVAADEG VMPQTKEHLD ILSLLNIKKG IIVITKESLV
DEEWLQLIKE DIRQKVKSTF LENAKMMVVD SVGGTGIKEL ITIIDQLTDE TESRNINAPV
RMPIDRVFTI TGFGTVVTGT LVEGKITVED TLEILPQKIK VRIRNIQVHG NSVETAYAGQ
RVAINLANIK KEDIERGYVL AQVNSMETTM MIDVRIKTLK DVSRVIQNRD RVRLYHGSTE
IFGRIMLLEK QELSPGESDF VQLRLEESIA VKKGDHIVVR FYSPIETIGG AIVIDNNPQK
HKRFDKRVIQ ELAIKEKGTP EDILEKHIER YSNQFPDAAY LAKTTVQQID EVKKLVTHLV
AVNRVLLLNN TNVLHQSYYT EIKEKALGLL KEYHKSNPLR QGMMKEEFKG KLIPNNAGKS
GDALLALLEK DEIIKVLGKY IALYDFEISF NKAQIQIKSI LEENYLKEPF ATPRLEDVIK
SMEFKKQEIE QVLESMMAKE LMKISSDIVL HEKAYQKSKD LLIQYIEKHG SISLAEFRDL
LNTSRKYAVA LLEYFDNNRV TKRLEDRRTL Y
//
