ID L0KAL9_HALHC Unreviewed; 637 AA.
AC L0KAL9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 28-JAN-2026, entry version 57.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN OrderedLocusNames=Halha_2180 {ECO:0000313|EMBL:AGB42061.1};
OS Halobacteroides halobius (strain ATCC 35273 / DSM 5150 / MD-1).
OC Bacteria; Bacillati; Bacillota; Clostridia; Halanaerobiales;
OC Halobacteroidaceae; Halobacteroides.
OX NCBI_TaxID=748449 {ECO:0000313|EMBL:AGB42061.1, ECO:0000313|Proteomes:UP000010880};
RN [1] {ECO:0000313|Proteomes:UP000010880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35273 / DSM 5150 / MD-1
RC {ECO:0000313|Proteomes:UP000010880};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Gu W.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "The complete genome of Halobacteroides halobius DSM 5150.";
RL Submitted (FEB-2012) 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; CP003359; AGB42061.1; -; Genomic_DNA.
DR RefSeq; WP_015327775.1; NC_019978.1.
DR AlphaFoldDB; L0KAL9; -.
DR STRING; 748449.Halha_2180; -.
DR KEGG; hhl:Halha_2180; -.
DR PATRIC; fig|748449.3.peg.2094; -.
DR eggNOG; COG3276; Bacteria.
DR HOGENOM; CLU_023030_3_0_9; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000010880; Chromosome.
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; 3.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:AGB42061.1};
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:UP000010880}.
FT DOMAIN 2..174
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 637 AA; 72095 MW; B022CFB3DE83D332 CRC64;
MSKNLIIGTA GHVDHGKTTL IKALTGQDTD RLDEENERGV SIELGFSHLE LNDDLQVGII
DVPGHEKFIK NMLAGAGGVD LGLLVVAADE IIMQQTREHL EILDLLNVKQ GLIAVTKSDL
VDDEWLNLVI YEIKEAVKDT FLEGTSVIPV SAVEETGIDK LKEEIEEVIA DIPTKDKTGN
TYFPIDRVFS LTGHGTIVTG TLLKGQIKEG AKLRIYPSGI DVRVRSLQVH EKGVETAYPG
QRVGINLSGV DTKEVDRGDV LATKESLVKT EYLDARLEML SSAPLILKHG DRIRLHLGAE
EVLGRVYLLD NEELYPGEEG LVQFRLEEEV VANFKERYVI RRYSPMTTIG GGQILESNPI
RHRKFEEDTI KALKIKEVGS SKERIELALK RNTSKPLSIE ELIQITSLST KQLSNKLASL
VEDGRVVELA TGRESSWLHQ SHIQQLREEI ISYLQDYHQQ YHLRWGIDKE ELRTKLSLRL
DSNQYDLLLA DLKQTNKIEE QDAKLSLENF EVEFNLEEEK IKEEILTSFN AQGFQPPRLE
KVISDFANED LATEIVDFLI TNNKLVKVAE NLYLHHQVLD KAKSLLREYL IKEGQISLAQ
FRDLLNSSRK YALPLLDYFD KQGVTKREGD IRHLEDK
//
