DER_COXBR
ID DER_COXBR Reviewed; 443 AA.
AC A9NDV6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=COXBURSA331_A1390;
OS Coxiella burnetii (strain RSA 331 / Henzerling II).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=360115;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 331 / Henzerling II;
RA Seshadri R., Samuel J.E.;
RT "Genome sequencing of phylogenetically and phenotypically diverse Coxiella
RT burnetii isolates.";
RL Submitted (NOV-2007) 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; CP000890; ABX78377.1; -; Genomic_DNA.
DR RefSeq; WP_005770802.1; NC_010117.1.
DR AlphaFoldDB; A9NDV6; -.
DR SMR; A9NDV6; -.
DR KEGG; cbs:COXBURSA331_A1390; -.
DR HOGENOM; CLU_016077_6_2_6; -.
DR OMA; KFRFLEY; -.
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; Repeat; Ribosome biogenesis.
FT CHAIN 1..443
FT /note="GTPase Der"
FT /id="PRO_1000077656"
FT DOMAIN 3..167
FT /note="EngA-type G 1"
FT DOMAIN 176..349
FT /note="EngA-type G 2"
FT DOMAIN 350..434
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 119..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 182..189
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 229..233
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 294..297
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
SQ SEQUENCE 443 AA; 49707 MW; 040B36345FD487EF CRC64;
MLPVIAIVGR PNVGKSTLFN YLTKSRAALV ADVPGVTRDR QYGETTIDSQ RLLLVDTGGL
VDTENKEVAP LAETQVEQAI DESDCILFLV DAKAGLVPAD EIIAERLRKK GKKIFLAVNK
ADRARAAVVQ SDFYKLGFGE PYVIAAASGR GVKDLMTQVL ENLPEEKEVI EKEVGIKIAM
IGRPNVGKST LINRLLGEER VIVYDQPGTT RDSIYIPFAR NDENYTLIDT AGIRRRAKIQ
DYVEKFSMIK SLQAMHAADV VIFLLDARQG VTEQDLRLLN RIVEAGVSLI IAVNKWDGLN
IEERDNVRNA IDRRMPFVDF ARRYFISALH GTGVGKLFRA IQESYQSIQQ ELTTGQLTRA
LEKAVAEHEP PLVKGRRIRL RYAHLGARHP LTIVVHGKQT KSLPQSYSRY LANYFRKTFN
FIGVPVHIKL KTDPNPYEGQ EER