ID A0AAU8PHE2_DESK7 Unreviewed; 642 AA.
AC A0AAU8PHE2;
DT 27-NOV-2024, integrated into UniProtKB/TrEMBL.
DT 27-NOV-2024, sequence version 1.
DT 28-JAN-2026, entry version 6.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN OrderedLocusNames=Desku_1546 {ECO:0000313|EMBL:AEG15127.1};
OS Desulfofundulus kuznetsovii (strain DSM 6115 / VKM B-1805 / 17)
OS (Desulfotomaculum kuznetsovii).
OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulfofundulus.
OX NCBI_TaxID=760568 {ECO:0000313|EMBL:AEG15127.1, ECO:0000313|Proteomes:UP000009229};
RN [1] {ECO:0000313|Proteomes:UP000009229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6115 / VKM B-1805 / 17 {ECO:0000313|Proteomes:UP000009229};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Lu M., Saunders E., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Nazina T., Ivanova A.,
RA Parshina S., Kuever J., Muyzer G., Plugge C., Stams A., Woyke T.;
RT "Complete sequence of Desulfotomaculum kuznetsovii DSM 6115.";
RL Submitted (MAY-2011) 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; CP002770; AEG15127.1; -; Genomic_DNA.
DR RefSeq; WP_013822642.1; NC_015573.1.
DR AlphaFoldDB; A0AAU8PHE2; -.
DR KEGG; dku:Desku_1546; -.
DR Proteomes; UP000009229; Chromosome.
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 FunFam; 3.40.50.300:FF:001064; Selenocysteine-specific translation elongation factor; 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; 2.
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; 3.
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:AEG15127.1};
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:UP000009229}.
FT DOMAIN 1..172
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 642 AA; 72198 MW; FCD4B863DC8EAF94 CRC64;
MTYLIIGTAG HVDHGKTMLV KALTGVDTDR LKEEKERGIS IELGFASLTL PSGRQAGIVD
VPGHERFIKN MLAGVGGIDL VLLVIAADEG IMPQTKEHMD IIHLLQIPRG VVVLSKVDLV
DREWLDLVRE EVVDFLKGTT LEGAPVVEVS SVTGQGLDEL LRTIDLVAQE VKEKPATGHV
RLPVDRVFSI TGFGTVATGT LWSGILRAGD ALEIMPRKIA SRVRTLQVHG RKVEEARAGQ
RVAVNLTGVE VEEVPRGSVL ATPGSLTPSY RLDVRFVLLG TARPLKNRSR VRLHLGTAEI
MCRVILLDRD ELAPEETALA QLELEEPAVA VQGDRFVVRS YSPVRTIGGG RIIDPVAPKH
RRLRAEVIES LLTREKGTPE ELLLQQLNSH RTILTAEELV KASGLDEKTV KDTLLSLVEK
KQVRPIPSEN QVYYLLQEVY LQWAENMRLI LQEYHRDFPL REGFPKEEMR SRLLAGLNSK
QFQSLLQVME EDGLVKLYTQ DIALPEFTPR PNHKQEQQIK HLLEMYREAN YQPPAWGEAA
RRAGLEGPAA QEILQYLLKK GLLVRVADDL YFHPDCVDRA RQALVDYLRE KGEITVGETR
DLLQTSRKYA LPLLEYFDRE KTTRRVEDKR VLTRAEKQKN RS
//
