DER_SYNPW
ID DER_SYNPW Reviewed; 455 AA.
AC A5GJ79;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=SynWH7803_0568;
OS Synechococcus sp. (strain WH7803).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32051;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH7803;
RG Genoscope;
RL Submitted (MAY-2006) 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; CT971583; CAK22994.1; -; Genomic_DNA.
DR RefSeq; WP_011932480.1; NC_009481.1.
DR AlphaFoldDB; A5GJ79; -.
DR SMR; A5GJ79; -.
DR STRING; 32051.SynWH7803_0568; -.
DR EnsemblBacteria; CAK22994; CAK22994; SynWH7803_0568.
DR KEGG; syx:SynWH7803_0568; -.
DR eggNOG; COG1160; Bacteria.
DR HOGENOM; CLU_016077_6_2_3; -.
DR OMA; KFRFLEY; -.
DR OrthoDB; 263682at2; -.
DR Proteomes; UP000001566; 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; IPR003593; AAA+_ATPase.
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 SMART; SM00382; AAA; 2.
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..455
FT /note="GTPase Der"
FT /id="PRO_1000011769"
FT DOMAIN 4..169
FT /note="EngA-type G 1"
FT DOMAIN 178..353
FT /note="EngA-type G 2"
FT DOMAIN 354..439
FT /note="KH-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 120..123
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 184..191
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 231..235
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 296..299
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
SQ SEQUENCE 455 AA; 50671 MW; BF211DEF023E3BA5 CRC64;
MARPVVAIIG RPNVGKSTLV NRLCHSREAI VHDEPGVTRD RTYQDGYWGD RDFKVVDTGG
LVFDDDSEFL PEIREQAALA LEEASVALVI VDGQQGVTAS DEAIAEFLRG QRCPALLAVN
KCESPEQGLA MAAEFWSLGL GEPYPISAIH GAGTAELLDQ VLTYLPPKSE EGDSEEPIQL
AIIGRPNVGK SSLLNAICGE QRAIVSPIRG TTRDTIDTSL VRENRPWRLV DTAGIRRRRS
VNYGPEFFGI NRSFKAIERS DVCVLVIDAL DGVTEQDQRL AGRIEEDGRA CVVVVNKWDA
VEKDSHTMTA MEKELRAKLY FLDWAPMLFT SALTGQRVDS IFALAALAVE QHRRRVSTSV
VNEVLKEALS WRSPPTTRGG RQGRLYYGTQ VASRPPSFTL FVNDPKLFGD TYRRYVERQI
REGLGFDGTP LKLFWRGKQQ RDAERDLARQ QNRQG
