ID B0S2I5_FINM2 Unreviewed; 625 AA.
AC B0S2I5;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 28-JAN-2026, entry version 95.
DE SubName: Full=Selenocysteine-specific elongation factor {ECO:0000313|EMBL:BAG08575.1};
GN OrderedLocusNames=FMG_1157 {ECO:0000313|EMBL:BAG08575.1};
OS Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508)
OS (Peptostreptococcus magnus).
OC Bacteria; Bacillati; Bacillota; Tissierellia; Tissierellales;
OC Peptoniphilaceae; Finegoldia.
OX NCBI_TaxID=334413 {ECO:0000313|EMBL:BAG08575.1, ECO:0000313|Proteomes:UP000001319};
RN [1] {ECO:0000313|EMBL:BAG08575.1, ECO:0000313|Proteomes:UP000001319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29328 / DSM 20472 / WAL 2508
RC {ECO:0000313|Proteomes:UP000001319};
RX PubMed=18263572; DOI=10.1093/dnares/dsm030;
RA Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K.,
RA Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.;
RT "Complete genome sequence of Finegoldia magna, an anaerobic opportunistic
RT pathogen.";
RL DNA Res. 15:39-47(2008).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; AP008971; BAG08575.1; -; Genomic_DNA.
DR RefSeq; WP_012290859.1; NC_010376.1.
DR AlphaFoldDB; B0S2I5; -.
DR STRING; 334413.FMG_1157; -.
DR KEGG; fma:FMG_1157; -.
DR eggNOG; COG3276; Bacteria.
DR HOGENOM; CLU_023030_3_0_9; -.
DR Proteomes; UP000001319; 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; 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; 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; 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:BAG08575.1};
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:UP000001319}.
FT DOMAIN 1..171
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 625 AA; 71607 MW; 5BFD7EB9C64C8082 CRC64;
MDFIIGTSGH IDHGKTTLIK ALTGNSTDRL PEEKKRGISI DLGFSYFDLP SGQRAGIIDV
PGHEKFVKNM MTGTFGMDMI LLCIDCKEGV MPQTVEHLDI LRFLNKTEGI VVLTKRDLAT
DEETEKTVEQ VKELVKGTFL ENCPICEVDS ISKRGIDNLI QMIDSESKKL KQKHAERDYR
MNIDRKFNVK GIGTVVTGTL LDGDIHKGES FIYPIEKDIN IKNIQVHNKN VNVAHPSQRV
ALNINLNLDE IDRGFVIAKK NSLKAFNMID VRLTLLESAS PLNHWDRVRL FHGTKEIFGR
VVPLDKQVIQ PGTQALVQIR LEEKIYAKTS DPFILRQFSP QVTIGGGIII DGSVRKHKLF
DEEIIENLKI KEEGKIKDII LNYLQDEIFP TKIDDLVFYS SESKDKVLKE LDGLKQEDKV
VIRNDKVLEK EAYLKLLGKL KMFVISFHKT NPLLPGINKE ELLKKLQLDD DRPFFNYMIK
DLIDQEVLIE ESGIVSSTGH KVKLSDEDEK IRKKMLQDIC QNQFDKLLKI DNVVHNQKDK
TILGILLQKD VVILRDNFLI SKKCYDKFIK TVDDHFNKNK TLNVKELKDM LNISRKSAIT
LLETLDIKGY TKRIENDRVK VKDFK
//
