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Database: UniProt
Entry: L0A5P7_DEIPD
LinkDB: L0A5P7_DEIPD
Original site: L0A5P7_DEIPD 
ID   L0A5P7_DEIPD            Unreviewed;       678 AA.
AC   L0A5P7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Small GTP-binding protein domain protein {ECO:0000313|EMBL:AFZ68345.1};
GN   OrderedLocusNames=Deipe_2884 {ECO:0000313|EMBL:AFZ68345.1};
OS   Deinococcus peraridilitoris (strain DSM 19664 / LMG 22246 / CIP 109416 /
OS   KR-200).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=937777 {ECO:0000313|EMBL:AFZ68345.1, ECO:0000313|Proteomes:UP000010467};
RN   [1] {ECO:0000313|Proteomes:UP000010467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19664 / LMG 22246 / CIP 109416 / KR-200
RC   {ECO:0000313|Proteomes:UP000010467};
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., Lu M.,
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., Pukall R., Steenblock K., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Complete sequence of chromosome of Deinococcus peraridilitoris DSM
RT   19664.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP003382; AFZ68345.1; -; Genomic_DNA.
DR   RefSeq; WP_015236647.1; NC_019793.1.
DR   AlphaFoldDB; L0A5P7; -.
DR   STRING; 937777.Deipe_2884; -.
DR   KEGG; dpd:Deipe_2884; -.
DR   PATRIC; fig|937777.3.peg.2899; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_0; -.
DR   OrthoDB; 9801591at2; -.
DR   Proteomes; UP000010467; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro.
DR   CDD; cd04170; EF-G_bact; 1.
DR   CDD; cd16262; EFG_III; 1.
DR   CDD; cd01434; EFG_mtEFG1_IV; 1.
DR   CDD; cd03713; EFG_mtEFG_C; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.240; -; 1.
DR   Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR041095; EFG_II.
DR   InterPro; IPR009022; EFG_III.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR047872; EFG_IV.
DR   InterPro; IPR035649; EFG_V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43261:SF6; ELONGATION FACTOR G-LIKE PROTEIN; 1.
DR   PANTHER; PTHR43261; TRANSLATION ELONGATION FACTOR G-RELATED; 1.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF14492; EFG_III; 1.
DR   Pfam; PF03764; EFG_IV; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 1.
DR   SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010467}.
FT   DOMAIN          1..272
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   678 AA;  73663 MW;  74F3321BB291798B CRC64;
     MRVRNVSVVG HSGVGKTSLT EALLFRTGAI KRLGHVEDGT TASDHTEAER RRGISISTSV
     ERVEFDQTTI NLLDAPGYAD FVREIRGAIR AADSSLVLLS AVSGVEVGTE RVWATLDNFN
     MPRIVVVNKM DRERADFFTA LADVRSSLKG PSAAAYLPIG QEHDFRGVVD LLGRRAYVFT
     DGQSSEMDVP SGLTDVVEEY RAQLVEAIIE TDDELTERYL SDETIDDETL HDVFLRAVHG
     GLLYPVLPLS ATKLIGVECL LKLMARGLRS PEERGALTGI NGEKREPRRE APASARVWRT
     SIDPFVGKIA FVRVWSGVLR PGETLRNTTH GVDVRPAHLY TLNGKELVEV SELEAGTIGA
     ITKMSDLHTG DSLADPAQPI DYGALQLPDP VVSAAIHALT RSDEDKLGNA ITKLLEEDPT
     WRFERSVETG ETLLSGMGDT HLEIAVEKLA QLGVNVRATV PKIPYRETVR AVGEAQGKHK
     KQSGGHGQYG DCWLRLSPTG EDFEFASEVV GGVVPGKYIP SIEKGVLEAR QKGVVAGYPV
     QNVRVVVYGG SYHEVDSSDI AFKTAAGIAF RAAMEKARPC LLEPVMLLRV RVPSQYTGDV
     IGDLQTRRAR VQGMDPEGTV ITISALVPLA EIQQYSAALR SMTGDRGAYS LKPSGYAEVP
     AHLTEAIIQA RKAEMAHG
//
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