ID A0A1M6RTB8_9FIRM Unreviewed; 638 AA.
AC A0A1M6RTB8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 28-JAN-2026, entry version 34.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=SAMN02745243_02769 {ECO:0000313|EMBL:SHK35680.1};
OS Hespellia stercorisuis DSM 15480.
OC Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
OC Lachnospiraceae; Hespellia.
OX NCBI_TaxID=1121950 {ECO:0000313|EMBL:SHK35680.1, ECO:0000313|Proteomes:UP000184301};
RN [1] {ECO:0000313|EMBL:SHK35680.1, ECO:0000313|Proteomes:UP000184301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15480 {ECO:0000313|EMBL:SHK35680.1,
RC ECO:0000313|Proteomes:UP000184301};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQZY01000044; SHK35680.1; -; Genomic_DNA.
DR RefSeq; WP_073111483.1; NZ_FQZY01000044.1.
DR AlphaFoldDB; A0A1M6RTB8; -.
DR STRING; 1121950.SAMN02745243_02769; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000184301; 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 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; 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:SHK35680.1};
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:UP000184301}.
FT DOMAIN 1..173
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 638 AA; 72543 MW; AD18B8D241121D92 CRC64;
MKNIIIGTAG HIDHGKTTLI KALTGRNTDR WEEEQRRGIT IDLGFTYFDT KSGDRVGIID
VPGHEKFINN MVAGVVGMDL VMLVVAADEG IMPQTREHID ILGLLGMQKS ILVLNKCDLV
DDEWIELVEE DIKEELKDTF LENAPIVHVS AATGQGLDEL KDTIDHLMKD EVVAKDTKTI
PRLPIDRVFT LSGFGTIITG TLISGTISKE DVLEMYPIER ECKIRSIQVH GKDQDVCEAG
QRVAINLSNV KKKEISRGCV IAARNSMKNT DMLDVKLTVL NDSMRIVTNH ERLHLYTGTS
EILCRAVLLD KDEIGPGESG LVQLRLEEQI ALKRGDRFVV RFYSPMETIG GGVVLEPNPT
RKKRFDANAI EELKRKESGS LADIMELHIK EHGDTMITLN ELAKTMAHSV DELQEYLEEL
KESGAIYVFS MKKDIYLWHK ESEFALRQKI ERDLTKYHEK YPFRFGMKKA EIHMTYLKKV
KPNVFDAYID FLVAENAVCR KEEFLYLPDF TVCKDDAYKA IEKIITEAFE KAGYDFVRFS
EIEFGKTSGD KADDVLNIMI VEKTVTRIND EMFTMSHLMD EAKEKIQQHL QKENLITIAQ
VRDMFSTSRK SAKPILEYMD SIKVTKKVGA ESERVAYL
//
