ID A0A7X3SI01_9FIRM Unreviewed; 637 AA.
AC A0A7X3SI01;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 28-JAN-2026, entry version 20.
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:MXP74923.1};
GN ORFNames=GN277_05880 {ECO:0000313|EMBL:MXP74923.1};
OS Sporofaciens musculi.
OC Bacteria; Bacillati; Bacillota; Clostridia; Lachnospirales;
OC Lachnospiraceae; Sporofaciens.
OX NCBI_TaxID=2681861 {ECO:0000313|EMBL:MXP74923.1, ECO:0000313|Proteomes:UP000460412};
RN [1] {ECO:0000313|EMBL:MXP74923.1, ECO:0000313|Proteomes:UP000460412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCA-9-b2 {ECO:0000313|EMBL:MXP74923.1,
RC ECO:0000313|Proteomes:UP000460412};
RA Rasmussen T.S., Streidl T., Hitch T.C.A., Wortmann E., Deptula P.,
RA Hansen M., Nielsen D.S., Clavel T., Vogensen F.K.;
RT "Sporaefaciens musculi gen. nov., sp. nov., a novel bacterium isolated from
RT the caecum of an obese mouse.";
RL Submitted (DEC-2019) 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:MXP74923.1}.
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DR EMBL; WUQX01000001; MXP74923.1; -; Genomic_DNA.
DR RefSeq; WP_159750250.1; NZ_WUQX01000001.1.
DR AlphaFoldDB; A0A7X3SI01; -.
DR Proteomes; UP000460412; 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:MXP74923.1};
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:UP000460412}.
FT DOMAIN 1..173
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 637 AA; 72208 MW; C007ACDAEBB309E9 CRC64;
MKNIIVGTAG HIDHGKTTLI KALTGRNTDR WEEEQRRGIT IDLGFTYFDL PCGDRVGIID
VPGHERFINN MVAGVVGMDL VLLVIAADEG IMPQTREHVD ILNLLGIEKS IIVLNKCDLV
DEEWLELVEE EIKEELEGTF LENSPAVRVS AATGEGLKDL INLIERMTSD EVVEKDVQTI
PRLPVDRAFT LSGFGTIITG TLVSGTISKE DTLQMYPVGK ECKIRSIQVH GRDKEECFAG
QRVAINLSNV KKKEIKRGCV LAPKNSMKNT DLLDVKIRIL DSSVRVLTNH MRLHFFTGTS
EVLCRAVLLD KEEIGPAESG FVQLRLEEEV AVRRGDKFVV RFYSPMETIG GGVILEPNPR
VKRRFQQEVI EELERKESGS TADVIELHVK GHGDTLITLA ELAKLTALSL DEVREDVENL
ESQGIVCVFP MRKDTYVWHS DSRRGAEQTL KSVLKAYEER FPYRYGMKKA EVLAAHFQKI
KPNVFERILD LLIDDGCLKR VDEFLCTPEY EVRKDTTYDK VSKLLLDTFT KAKYDFVRYS
EIEFKGVDRM TADDILNILL EEQKIVKVTD DMFTLKEYME SAKEAIQKKL LEDPLITIAQ
VRDLFETSRK SAKPILEYMD SIKVTKKTGA ESERIAF
//
