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DER_TOLAT
ID   DER_TOLAT               Reviewed;         498 AA.
AC   C4LC41;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=GTPase Der {ECO:0000255|HAMAP-Rule:MF_00195};
DE   AltName: Full=GTP-binding protein EngA {ECO:0000255|HAMAP-Rule:MF_00195};
GN   Name=der {ECO:0000255|HAMAP-Rule:MF_00195}; Synonyms=engA;
GN   OrderedLocusNames=Tola_0892;
OS   Tolumonas auensis (strain DSM 9187 / TA4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Tolumonas.
OX   NCBI_TaxID=595494;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9187 / TA4;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S.,
RA   Beller H.;
RT   "Complete sequence of Tolumonas auensis DSM 9187.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: GTPase that plays an essential role in the late steps of
CC       ribosome biogenesis. {ECO:0000255|HAMAP-Rule:MF_00195}.
CC   -!- SUBUNIT: Associates with the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00195}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC       GTPase superfamily. EngA (Der) GTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00195}.
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DR   EMBL; CP001616; ACQ92520.1; -; Genomic_DNA.
DR   RefSeq; WP_012729119.1; NC_012691.1.
DR   AlphaFoldDB; C4LC41; -.
DR   SMR; C4LC41; -.
DR   STRING; 595494.Tola_0892; -.
DR   EnsemblBacteria; ACQ92520; ACQ92520; Tola_0892.
DR   KEGG; tau:Tola_0892; -.
DR   eggNOG; COG1160; Bacteria.
DR   HOGENOM; CLU_016077_5_1_6; -.
DR   OMA; KFRFLEY; -.
DR   OrthoDB; 263682at2; -.
DR   Proteomes; UP000009073; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_00195; GTPase_Der; 1.
DR   InterPro; IPR031166; G_ENGA.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR016484; GTP-bd_EngA.
DR   InterPro; IPR032859; KH_dom-like.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   Pfam; PF14714; KH_dom-like; 1.
DR   Pfam; PF01926; MMR_HSR1; 2.
DR   PIRSF; PIRSF006485; GTP-binding_EngA; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR03594; GTPase_EngA; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 2.
DR   PROSITE; PS51712; G_ENGA; 2.
PE   3: Inferred from homology;
KW   GTP-binding; Nucleotide-binding; Reference proteome; Repeat;
KW   Ribosome biogenesis.
FT   CHAIN           1..498
FT                   /note="GTPase Der"
FT                   /id="PRO_1000204049"
FT   DOMAIN          3..166
FT                   /note="EngA-type G 1"
FT   DOMAIN          212..385
FT                   /note="EngA-type G 2"
FT   DOMAIN          386..470
FT                   /note="KH-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         9..16
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         56..60
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         118..121
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         218..225
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         265..269
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         330..333
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
SQ   SEQUENCE   498 AA;  55705 MW;  6B33460256CF8174 CRC64;
     MTPVVALVGR PNVGKSTLFN RLTRSRDALV ADFPGLTRDR KYGQAVVDDM NFIVVDTGGI
     DGSEEGIEVK MAEQSLQAID ESDVVLFMVD ARAGVTSADI GIANHLRRQK KKVFLVANKT
     DGLDGDVHCA DFYSLALGEV YQIAASHGRG VTSLLEKALA PFFEELTGKS AEEEAADEDA
     AYWAAFEGTD VTEEDESDEE LTGEDRYADL PIKFAIIGRP NVGKSTLTNR MLGEDRVIVY
     DLPGTTRDSI YIPLERDDQH YIVIDTAGVR KKKKIYETVE KFSVVKTLQA IEDANVVLLL
     IDAREGVSDQ DLSLLGFTLH SGRSIVIAVN KWDGLDQDTK EKIKEDLERR LGFVDFARVH
     FISALHGSGV GNLFDSIQEA YRSATKRIST SMLTRIMNMA AEDHQPPLVR GRRVKLKYAH
     AGGYNPPRII IHGNQVKDLP ESYKRYLINY YRKSLKIMGT PIHIEFQEGD NPFEGRRNKL
     TQTQIRKRRR MMSFVKKG
 
 
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