ID D4CL33_9FIRM Unreviewed; 640 AA.
AC D4CL33;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
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:EFE92044.1};
GN ORFNames=GCWU000341_01231 {ECO:0000313|EMBL:EFE92044.1};
OS Oribacterium sp. oral taxon 078 str. F0262.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Oribacterium.
OX NCBI_TaxID=608534 {ECO:0000313|EMBL:EFE92044.1, ECO:0000313|Proteomes:UP000004602};
RN [1] {ECO:0000313|EMBL:EFE92044.1, ECO:0000313|Proteomes:UP000004602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0262 {ECO:0000313|EMBL:EFE92044.1,
RC ECO:0000313|Proteomes:UP000004602};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2010) 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:EFE92044.1}.
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DR EMBL; ACIQ02000013; EFE92044.1; -; Genomic_DNA.
DR RefSeq; WP_009214705.1; NZ_GG729934.1.
DR AlphaFoldDB; D4CL33; -.
DR STRING; 608534.GCWU000341_01231; -.
DR eggNOG; COG3276; Bacteria.
DR HOGENOM; CLU_023030_3_0_9; -.
DR Proteomes; UP000004602; 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; 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_dom.
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; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF09106; SelB-wing_2; 1.
DR Pfam; PF09107; SelB-wing_3; 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; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Elongation factor {ECO:0000313|EMBL:EFE92044.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:EFE92044.1}.
FT DOMAIN 1..174
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 640 AA; 72707 MW; AB82F01BF4294B48 CRC64;
MKHIIIGTAG HIDHGKTTLI RALTGRNTDR LKEEQNRGIT IELGFTWFDM KDGTRCGVID
VPGHEKFINN MVAGVVGMDL VLMVVAADEG IMPQTREHLD ILELLGIKKC ILVLNKCDLV
EEEWISMMEE EIRGELKGTI LDHAPLARVS AATGEGIDAL KDLILQMVTE DVPEKDVNGI
PRLPIDRVFS LPGFGTIITG TLLSGRISRG DSLSIYPEGL SCKVRNIQVH DRDTDICEAG
QRVALNLSNV KKSDLKRGSV IAPSGSMENT TLIDVKLSVL RDSRRSIRNR ERLHLFTGTS
ELLCRAVLLD RDEIPPGETG PAQLLLEEEL VVKRGDRFVV RFYSPLETIG GGVVLEPNPR
KKKRFSEEAI AELSRKESGS LADVCELNIR AENDTLINLR ELAKNMSHSE EELKPCLSEL
RDRGLIYEFV LRKDSYYWHR DNAFIIEQEI QRALRSFYEK HPYRYGIRKA EIQSVYMKSV
KLNVFDACME KLCADGSLQL REEYLCLPGR EIPKDERFRD LESLITEQLE KAGYEFLRFS
ELSRKNYSDE LMLDVIHVLM DEGKLVRIGG EELEMYTMKH FMDSAKEAVK KHFETNELLT
ISEIRDMFAT SRKCAKPIIL YMDSQKITKK LGAETERVAY
//
